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1. The matricellular protein CCN5 prevents anti-VEGF drug-induced epithelial-mesenchymal transition of retinal pigment epithelium

Author: Sora Im, Min Ho Song, Muthukumar Elangovan, Kee Min Woo, and Woo Jin Park
Subjects: Medicine, Science
Abstract: Abstract Age-related macular degeneration (AMD) is one of the major causes of blindness in the elderly worldwide. Anti-vascular endothelial growth factor (VEGF) drugs have been widely used to treat the neovascular type of AMD (nAMD). However, VEGF acts not only as a pro-angiogenic factor but also as an anti-apoptotic factor in the eyes. In this study, we found that anti-VEGF drugs, including bevacizumab (Bev), ranibizumab (Ran), and aflibercept (Afl), induced epithelial-mesenchymal transition (EMT) in ARPE-19 cells in vitro, accompanied by the induction of CCN2, a potent pro-fibrotic factor. Similarly, intravitreal injection of Afl into mouse eyes resulted in EMT in the retinal pigmented epithelium (RPE). Co-treatment with CCN5, an anti-fibrotic factor that down-regulates CCN2 expression, significantly attenuated the adverse effects of the anti-VEGF drugs both in vitro and in vivo. Inhibition of the VEGF signaling pathway with antagonists of VEGF receptors, SU5416 and ZM323881, induced EMT and up-regulated CCN2 in ARPE-19 cells. Additionally, knock-down of CCN2 with siRNA abolished the adverse effects of the anti-VEGF drugs in ARPE-19 cells. Collectively, these results suggest that anti-VEGF drugs induce EMT in RPE through the induction of CCN2 and that co-treatment with CCN5 attenuates the adverse effects of anti-VEGF drugs in mouse eyes.
Published: 2024
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2. Therapeutic effects of a novel synthetic α-secretase

Author: Sung Bin Kim, Bo-Ram Mun, Sung Yoon Kim, Muthukumar Elangovan, Euy Jun Park, Won-Seok Choi, and Woo Jin Park
Subjects: Alzheimer’s disease, amyloid-β clearance, amyloid-β degrading enzyme, synthetic α-secretase, nuclear inclusion a, Neurosciences. Biological psychiatry. Neuropsychiatry, RC321-571
Abstract: Excessive accumulation of amyloid-β (Aβ) has been associated with the pathogenesis of Alzheimer’s disease (AD). Clinical studies have further proven that elimination of Aβ can be a viable therapeutic option. In the current study, we conceptualized a fusion membrane protein, referred to as synthetic α-secretase (SAS), that can cleave amyloid precursor protein (APP) and Aβ specifically at the α-site. In mammalian cells, SAS indeed cleaved APP and Aβ at the α-site. Overexpression of SAS in the hippocampus was achieved by direct injection of recombinant adeno-associated virus serotype 9 (AAV9) that expresses SAS (AAV9-SAS) into the bilateral ventricles of mouse brains. SAS enhanced the non-amyloidogenic processing of APP, thus reducing the levels of soluble Aβ and plaques in the 5xFAD mice. In addition, SAS significantly attenuated the cognitive deficits in 5xFAD mice, as demonstrated by novel object recognition and Morris water maze tests. Unlike other Aβ-cleaving proteases, SAS has highly strict substrate specificity. We propose that SAS can be an efficient modality to eliminate excessive Aβ from diseased brains.
Published: 2024
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3. Modified mRNA-Mediated CCN5 Gene Transfer Ameliorates Cardiac Dysfunction and Fibrosis without Adverse Structural Remodeling

Author: Min Ho Song, Jimeen Yoo, Do-A Kwon, Elena Chepurko, Sunghye Cho, Anthony Fargnoli, Roger J. Hajjar, Woo Jin Park, Lior Zangi, and Dongtak Jeong
Subjects: modified mRNA (modRNA), CCN5, myocardial infarction (MI), cardiac fibrosis, heart failure (HF), left ventricular rupture, Biology (General), QH301-705.5, Chemistry, QD1-999
Abstract: Modified mRNAs (modRNAs) are an emerging delivery method for gene therapy. The success of modRNA-based COVID-19 vaccines has demonstrated that modRNA is a safe and effective therapeutic tool. Moreover, modRNA has the potential to treat various human diseases, including cardiac dysfunction. Acute myocardial infarction (MI) is a major cardiac disorder that currently lacks curative treatment options, and MI is commonly accompanied by fibrosis and impaired cardiac function. Our group previously demonstrated that the matricellular protein CCN5 inhibits cardiac fibrosis (CF) and mitigates cardiac dysfunction. However, it remains unclear whether early intervention of CF under stress conditions is beneficial or more detrimental due to potential adverse effects such as left ventricular (LV) rupture. We hypothesized that CCN5 would alleviate the adverse effects of myocardial infarction (MI) through its anti-fibrotic properties under stress conditions. To induce the rapid expression of CCN5, ModRNA-CCN5 was synthesized and administrated directly into the myocardium in a mouse MI model. To evaluate CCN5 activity, we established two independent experimental schemes: (1) preventive intervention and (2) therapeutic intervention. Functional analyses, including echocardiography and magnetic resonance imaging (MRI), along with molecular assays, demonstrated that modRNA-mediated CCN5 gene transfer significantly attenuated cardiac fibrosis and improved cardiac function in both preventive and therapeutic models, without causing left ventricular rupture or any adverse cardiac remodeling. In conclusion, early intervention in CF by ModRNA-CCN5 gene transfer is an efficient and safe therapeutic modality for treating MI-induced heart failure.
Published: 2024
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4. Circular RNA circSMAD4 regulates cardiac fibrosis by targeting miR-671-5p and FGFR2 in cardiac fibroblasts

Author: Anna Jeong, Yongwoon Lim, Taewon Kook, Duk-Hwa Kwon, Young Kuk Cho, Juhee Ryu, Yun-Gyeong Lee, Sera Shin, Nakwon Choe, Yong Sook Kim, Hye Jung Cho, Jeong Chul Kim, Yoonjoo Choi, Su-Jin Lee, Hyung-Seok Kim, Hae Jin Kee, Kwang-Il Nam, Youngkeun Ahn, Myung Ho Jeong, Woo Jin Park, Young-Kook Kim, and Hyun Kook
Subjects: MT: Non-coding RNAs, circular RNA, transverse aortic constriction, cardiac fibrosis, circSMAD4, miR-671-5p, Therapeutics. Pharmacology, RM1-950
Abstract: Heart failure is a leading cause of death and is often accompanied by activation of quiescent cardiac myofibroblasts, which results in cardiac fibrosis. In this study, we aimed to identify novel circular RNAs that regulate cardiac fibrosis. We applied transverse aortic constriction (TAC) for 1, 4, and 8 weeks in mice. RNA sequencing datasets were obtained from cardiac fibroblasts isolated by use of a Langendorff apparatus and then further processed by use of selection criteria such as differential expression and conservation in species. CircSMAD4 was upregulated by TAC in mice or by transforming growth factor (TGF)-β1 in primarily cultured human cardiac fibroblasts. Delivery of si-circSMAD4 attenuated myofibroblast activation and cardiac fibrosis in mice treated with isoproterenol (ISP). si-circSmad4 significantly reduced cardiac fibrosis and remodeling at 8 weeks. Mechanistically, circSMAD4 acted as a sponge against the microRNA miR-671-5p in a sequence-specific manner. miR-671-5p was downregulated during myofibroblast activation and its mimic form attenuated cardiac fibrosis. miR-671-5p mimic destabilized fibroblast growth factor receptor 2 (FGFR2) mRNA in a sequence-specific manner and interfered with the fibrotic action of FGFR2. The circSMAD4-miR-671-5p-FGFR2 pathway is involved in the differentiation of cardiac myofibroblasts and thereby the development of cardiac fibrosis.
Published: 2023
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5. Artificial Intelligence-Based Anomaly Detection Technology over Encrypted Traffic: A Systematic Literature Review

Author: Il Hwan Ji, Ju Hyeon Lee, Min Ji Kang, Woo Jin Park, Seung Ho Jeon, and Jung Taek Seo
Subjects: cyber security, anomaly detection, encrypted traffic, Chemical technology, TP1-1185
Abstract: As cyber-attacks increase in unencrypted communication environments such as the traditional Internet, protected communication channels based on cryptographic protocols, such as transport layer security (TLS), have been introduced to the Internet. Accordingly, attackers have been carrying out cyber-attacks by hiding themselves in protected communication channels. However, the nature of channels protected by cryptographic protocols makes it difficult to distinguish between normal and malicious network traffic behaviors. This means that traditional anomaly detection models with features from packets extracted a deep packet inspection (DPI) have been neutralized. Recently, studies on anomaly detection using artificial intelligence (AI) and statistical characteristics of traffic have been proposed as an alternative. In this review, we provide a systematic review for AI-based anomaly detection techniques over encrypted traffic. We set several research questions on the review topic and collected research according to eligibility criteria. Through the screening process and quality assessment, 30 research articles were selected with high suitability to be included in the review from the collected literature. We reviewed the selected research in terms of dataset, feature extraction, feature selection, preprocessing, anomaly detection algorithm, and performance indicators. As a result of the literature review, it was confirmed that various techniques used for AI-based anomaly detection over encrypted traffic were used. Some techniques are similar to those used for AI-based anomaly detection over unencrypted traffic, but some technologies are different from those used for unencrypted traffic.
Published: 2024
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6. Circular RNA circSmoc1-2 regulates vascular calcification by acting as a miR-874-3p sponge in vascular smooth muscle cells

Author: Juhee Ryu, Nakwon Choe, Duk-Hwa Kwon, Sera Shin, Yeong-Hwan Lim, Gwangho Yoon, Ji Hye Kim, Hyung Seok Kim, In-Kyu Lee, Youngkeun Ahn, Woo Jin Park, Hyun Kook, and Young-Kook Kim
Subjects: Circular RNA, circSmoc1-2, miRNA-874-3p, Adam19, vascular calcification, vascular smooth muscle cells, Therapeutics. Pharmacology, RM1-950
Abstract: Vascular calcification (VC), or calcium deposition inside the blood vessels, is common in patients with atherosclerosis, cardiovascular disease, and chronic kidney disease. Although several treatments are available to reduce calcification, the incidence of VC continues to rise. Recently, there have been several reports describing the regulation of circular RNAs (circRNAs) in various diseases. However, the role of circRNAs in VC has not yet been fully explored. Here, we investigated the function of circSmoc1-2, one of the circRNAs generated from the Smoc1 gene, which is downregulated in response to VC. CircSmoc1-2 is localized primarily to the cytoplasm and is resistant to exonuclease digestion. Inhibition of circSmoc1-2 worsens VC, while overexpression of circSmoc1-2 reduces VC, suggesting that circSmoc1-2 can prevent calcification. We went on to investigate the mechanism of circSmoc1-2 as a microRNA sponge and noted that miR-874-3p, the predicted target of circSmoc1-2, promotes VC, while overexpression of circSmoc1-2 reduces VC by suppressing miR-874-3p. Additionally, we identified the potential mRNA target of miR-874-3p as Adam19. In conclusion, we revealed that the circSmoc1-2/miR-874-3p/Adam19 axis regulates VC, suggesting that circSmoc1-2 may be a novel therapeutic target in the treatment of VC.
Published: 2022
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7. Regulation of MDM2 E3 ligase-dependent vascular calcification by MSX1/2

Author: Duk-Hwa Kwon, Nakwon Choe, Sera Shin, Juhee Ryu, Nacksung Kim, Gwang Hyeon Eom, Kwang-Il Nam, Hyung Seok Kim, Youngkeun Ahn, Young-Kook Kim, Woo Jin Park, Susan M. Mendrysa, and Hyun Kook
Subjects: Medicine, Biochemistry, QD415-436
Abstract: Vascular disease: Driver of deposition of calcium salts identified The identification of a signaling pathway involved in triggering vascular calcification, the deposition of calcium phosphate crystals in blood vessels, could inform new therapeutic interventions for related cardiovascular complications. Vascular calcification causes significant complications in patients with metabolic syndrome, renal failure, or cardiovascular disease. In their previous work, Hyun Kook and Duk-Hwa Kwon at Chonnam National University Medical School, Jeollanamdo, Republic of Korea, and coworkers demonstrated that the E3 ligase activity of a protein called MDM2 induces calcification. Now, following further mouse trials, the team have identified an upstream signaling pathway involving several development proteins such as MSX1 and MSX2 which activate MDM2. The activation of this signaling axis leads to the degradation of a key protein that would otherwise prevent calcification. The results may provide a platform for novel therapies targeting the condition.
Published: 2021
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8. miR-27a-3p Targets ATF3 to Reduce Calcium Deposition in Vascular Smooth Muscle Cells

Author: Nakwon Choe, Duk-Hwa Kwon, Juhee Ryu, Sera Shin, Hye Jung Cho, Hosouk Joung, Gwang Hyeon Eom, Youngkeun Ahn, Woo Jin Park, Kwang-Il Nam, Young-Kook Kim, and Hyun Kook
Subjects: vascular calcification, vascular smooth muscle cells, miRNA, miR-27a-3p, activating transcription factor 3, Therapeutics. Pharmacology, RM1-950
Abstract: Vascular calcification, the ectopic deposition of calcium in blood vessels, develops in association with various metabolic diseases and atherosclerosis and is an independent predictor of morbidity and mortality associated with these diseases. Herein, we report that reduction of microRNA-27a-3p (miR-27a-3p) causes an increase in activating transcription factor 3 (ATF3), a novel osteogenic transcription factor, in vascular smooth muscle cells. Both microRNA (miRNA) and mRNA microarrays were performed with rat vascular smooth muscle cells, and reciprocally regulated pairs of miRNA and mRNA were selected after bioinformatics analysis. Inorganic phosphate significantly reduced the expression of miR-27a-3p in A10 cells. The transcript level was also reduced in vitamin D3-administered mouse aortas. miR-27a-3p mimic reduced calcium deposition, whereas miR-27a-3p inhibitor increased it. The Atf3 mRNA level was upregulated in a cellular vascular calcification model, and miR-27a-3p reduced the Atf3 mRNA and protein levels. Transfection with Atf3 could recover the miR-27a-3p-induced reduction of calcium deposition. Our results suggest that reduction of miR-27a-3p may contribute to the development of vascular calcification by de-repression of ATF3.
Published: 2020
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9. Matricellular Protein CCN5 Gene Transfer Ameliorates Cardiac and Skeletal Dysfunction in mdx/utrn (±) Haploinsufficient Mice by Reducing Fibrosis and Upregulating Utrophin Expression

Author: Min Ho Song, Jimeen Yoo, Jae Gyun Oh, Hyun Kook, Woo Jin Park, and Dongtak Jeong
Subjects: CCN5, DMD, cardiomyopathy, utrophin, AAV9, Diseases of the circulatory (Cardiovascular) system, RC666-701
Abstract: Duchenne muscular dystrophy (DMD) is a genetic disorder characterized by progressive muscle degeneration due to dystrophin gene mutations. Patients with DMD initially experience muscle weakness in their limbs during adolescence. With age, patients develop fatal respiratory and cardiac dysfunctions. During the later stages of the disease, severe cardiac fibrosis occurs, compromising cardiac function. Previously, our research showed that the matricellular protein CCN5 has antifibrotic properties. Therefore, we hypothesized that CCN5 gene transfer would ameliorate cardiac fibrosis and thus improve cardiac function in DMD-induced cardiomyopathy. We utilized mdx/utrn (±) haploinsufficient mice that recapitulated the DMD-disease phenotypes and used an adeno-associated virus serotype-9 viral vector for CCN5 gene transfer. We evaluated the onset of cardiac dysfunction using echocardiography and determined the experimental starting point in 13-month-old mice. Two months after CCN5 gene transfer, cardiac function was significantly enhanced, and cardiac fibrosis was ameliorated. Additionally, running performance was improved in CCN5 gene-transfected mice. Furthermore, in silico gene profiling analysis identified utrophin as a novel transcriptional target of CCN5. This was supplemented by a utrophin promoter assay and RNA-seq analysis, which confirmed that CCN5 was directly associated with utrophin expression. Our results showed that CCN5 may be a promising therapeutic molecule for DMD-induced cardiac and skeletal dysfunction.
Published: 2022
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10. Suppression of choroidal neovascularization and epithelial-mesenchymal transition in retinal pigmented epithelium by adeno-associated virus-mediated overexpression of CCN5 in mice.

Author: Sora Im, Jung Woo Han, Euy Jun Park, Ji Hong Bang, Hee Jeong Shin, Hun Soo Chang, Kee Min Woo, Woo Jin Park, and Tae Kwann Park
Subjects: Medicine, Science
Abstract: Choroidal neovascularization (CNV) is a defining characteristic feature of neovascular age-related macular degeneration (nAMD) that frequently results in irreversible vision loss. The current strategies for the treatment of nAMD are mainly based on neutralizing vascular endothelial growth factor (VEGF). However, anti-VEGF therapies are often associated with subretinal fibrosis that eventually leads to damages in macula. In this study, we tested whether an anti-fibrotic and anti-angiogenic protein CCN5 can potentially be an effective and safe therapeutic modality in a mouse model of CNV. Laser photocoagulation was utilized to induce CNV, which was followed by intravitreal injection of recombinant adeno-associated virus serotype 2 encoding CCN5 (rAAV2-CCN5). Our data demonstrated that rAAV2-CCN5, but not a control viral vector, rAAV2-VLP, prominently attenuated both CNV lesions and angiogenesis. Aflibercept, which was utilized as a positive control, exhibited similar effects on CNV lesions and angiogenesis in our experimental settings. Upon laser photocoagulation, retinal pigmented epithelium (RPE) cells underwent significant morphological changes including cellular enlargement and loss of hexagonality. rAAV2-CCN5 significantly normalized these morphological defects. Laser photocoagulation also led to fibrotic deformation in RPE cells through inducing epithelial-mesenchymal transition (EMT), which was completely blocked by rAAV2-CCN5. In a striking contrast, aflibercept as well as rAAV2-VLP failed to exhibit any effects on EMT. Collectively, this study suggest that CCN5 might provide a potential novel strategy for the treatment of nAMD with a capability to inhibit CNV and fibrosis simaultaneously.
Published: 2022
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11. The matricellular protein CCN5 induces apoptosis in myofibroblasts through SMAD7-mediated inhibition of NFκB.

Author: Mai Tuyet Nguyen, Min-Ah Lee, Young-Kook Kim, Hyun Kook, Dongtak Jeong, Seung Pil Jang, Tae Hwan Kwak, and Woo Jin Park
Subjects: Medicine, Science
Abstract: We previously showed that the matricellular protein CCN5 reverses established cardiac fibrosis (CF) through inducing apoptosis in myofibroblasts (MyoFBs) but not in cardiomyocytes or fibroblasts (FBs). In this study, we set out to elucidate the molecular mechanisms underlying CCN5-mediated selective apoptosis of MyoFBs. We first observed that the apoptotic protein p53 and the anti-apoptotic protein NFκB are simultaneously induced in MyoFBs. When the expression level of p53 was suppressed using a siRNA, CCN5 did not induce apoptosis in MyoFBs. By contrast, when NFκB signaling was inhibited using IKK VII, an IκB inhibitor, MyoFBs underwent apoptosis even in the absence of CCN5. SMAD7 is one of the downstream targets of CCN5 and it was previously shown to potentiate apoptosis in epithelial cells through inhibition of NFκB. In accordance with these reports, when the expression of SMAD7 was suppressed using a siRNA, NFκB signaling was enhanced, and CCN5 did not induce apoptosis. Lastly, we used a luciferase reporter construct to show that CCN5 positively regulated SMAD7 expression at the transcriptional level. Collectively, our data suggest that a delicate balance between the two mutually antagonistic proteins p53 and NFκB is maintained for MyoFBs to survive, and CCN5 tips the balance in favor of the apoptotic protein p53. This study provides insight into the anti-fibrotic activity of CCN5 during the regression of CF.
Published: 2022
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12. The TSP-1 domain of the matricellular protein CCN5 is essential for its nuclear localization and anti-fibrotic function.

Author: Min Ho Song, Yongjoon Jo, Young-Kook Kim, Hyun Kook, Dongtak Jeong, and Woo Jin Park
Subjects: Medicine, Science
Abstract: The matricellular protein CCN5 exerts anti-fibrotic activity in hearts partly by inducing reverse trans-differentiation of myofibroblasts (MyoFBs) to fibroblasts (FBs). CCN5 consists of three structural domains: an insulin-like growth factor binding protein (IGFBP), a von Willebrand factor type C (VWC), and a thrombospondin type 1 (TSP-1). In this study, we set out to elucidate the roles of these domains in the context of the reverse trans-differentiation of MyoFBs to FBs. First, human cardiac FBs were trans-differentiated to MyoFBs by treatment with TGF-β; this was then reversed by treatment with recombinant human CCN5 protein or various recombinant proteins comprising individual or paired CCN5 domains. Subcellular localization of these recombinant proteins was analyzed by immunocytochemistry, cellular fractionation, and western blotting. Anti-fibrotic activity was also evaluated by examining expression of MyoFB-specific markers, α-SMA and fibronectin. Our data show that CCN5 is taken up by FBs and MyoFBs mainly via clathrin-mediated endocytosis, which is essential for the function of CCN5 during the reverse trans-differentiation of MyoFBs. Furthermore, we showed that the TSP-1 domain is essential and sufficient for endocytosis and nuclear localization of CCN5. However, the TSP-1 domain alone is not sufficient for the anti-fibrotic function of CCN5; either the IGFBP or VWC domain is needed in addition to the TSP-1 domain.
Published: 2022
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13. Anti-Ischemic Effects of PIK3IP1 Are Mediated through Its Interactions with the ETA-PI3Kγ-AKT Axis

Author: Jei Hyoung Park, Kyoung Jin Nho, Ji Young Lee, Yung Joon Yoo, Woo Jin Park, Chunghee Cho, and Do Han Kim
Subjects: myocardial infarction, ROS, PI3Kγ, PIK3IP1, endothelin receptor A, AKT, Cytology, QH573-671
Abstract: Oxidative stress, caused by the accumulation of reactive oxygen species (ROS) during acute myocardial infarction (AMI), is one of the main factors leading to myocardial cell damage and programmed cell death. Phosphatidylinositol-3-kinase-AKT (PI3K-AKT) signaling is essential for regulating cell proliferation, differentiation, and apoptosis. Phosphoinositide-3-kinase (PI3K)-interacting protein 1 (PIK3IP1) is an intrinsic inhibitor of PI3K in various tissues, but its functional role during AMI remains unknown. In this study, the anti-ischemic role of PIK3IP1 in an in vitro AMI setting was evaluated using H9c2 cells. The MTT assay demonstrated that cell viability decreased significantly via treatment with H2O2 (200–500 μM). The TUNEL assay results revealed substantial cellular apoptosis following treatment with 200 μM H2O2. Under the same conditions, the expression levels of hypoxia-inducible factor (HIF-1α), endothelin-1 (ET-1), bcl-2-like protein 4 (BAX), and cleaved caspase-3 were elevated, whereas those of PIK3IP1, LC3II, p53, and Bcl-2 decreased significantly. PIK3IP1 overexpression inhibited H2O2-induced and PI3K-mediated apoptosis; however, PIK3IP1 knockdown reversed this effect, suggesting that PIK3IP1 functions as an anti-apoptotic molecule. To identify both the upstream and downstream molecules associated with PIK3IP1, ET-1 receptor type-specific antagonists (BQ-123 and BQ-788) and PI3K subtype-specific antagonists (LY294002 and IPI-549) were used to determine the participating isoforms. Co-immunoprecipitation was performed to identify the binding partners of PIK3IP1. Our results demonstrated that ROS-induced cardiac cell death may occur through the ETA-PI3Kγ-AKT axis, and that PIK3IP1 inhibits binding with both ETA and PI3Kγ. Taken together, these findings reveal that PIK3IP1 plays an anti-ischemic role by reducing the likelihood of programmed cell death via interaction with the ETA-PI3Kr-AKT axis.
Published: 2022
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14. The matricellular protein CCN5 inhibits fibrotic deformation of retinal pigment epithelium.

Author: Aeri Yoon, Sora Im, Juyeon Lee, Daeho Park, Dong Hyun Jo, Jin Hyoung Kim, Jeong Hun Kim, and Woo Jin Park
Subjects: Medicine, Science
Abstract: Retinal pigment epithelium (RPE) plays an essential role in maintaining retinal function, and its defect is thought to be critically implicated in various ocular disorders. This study demonstrated that the matricellular protein CCN5 was down-regulated in ARPE-19 cells treated with the pro-fibrotic agent transforming growth factor (TGF)-β. A recombinant adenovirus expressing CCN5 (AdCCN5) was used to restore the level of CCN5 in these cells. AdCCN5 prevented TGF-β-induced fibrotic changes, including disruption of tight junctions, up-regulation of mesenchymal marker proteins, and down-regulation of epithelial marker proteins. In addition, AdCCN5 prevented TGF-β-induced functional defects, including increased migratory activity and reduced phagocytic activity. Notably, AdCCN5 reversed morphological and functional defects pre-established by TGF-β prior to viral infection. The CCN5 level was down-regulated in RPE of 18-month-old Ccl2-/- mice, which exhibited retinal defects. Restoration of the CCN5 level via intravitreal injection of a recombinant adeno-associated virus expressing CCN5 (AAV9-CCN5) normalized the altered expression of mesenchymal, epithelial, and functional marker proteins, as assessed by western blotting and immunohistochemistry. Taken together, these data suggest that down-regulation of CCN5 is associated with fibrotic deformation of RPE under pathological conditions and that restoration of the CCN5 level effectively promotes recovery of deformed RPE.
Published: 2018
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15. CCN5 knockout mice exhibit lipotoxic cardiomyopathy with mild obesity and diabetes.

Author: Jihwa Kim, Sanghyun Joo, Gwang Hyeon Eom, Seung Hoon Lee, Min-Ah Lee, Miyoung Lee, Ki Woo Kim, Do Han Kim, Hyun Kook, Tae Hwan Kwak, and Woo Jin Park
Subjects: Medicine, Science
Abstract: Obesity is associated with various human disorders, such as type 2 diabetes, cardiovascular diseases, hypertension, and cancers. In this study, we observed that knockout (KO) of CCN5, which encodes a matricellular protein, caused mild obesity in mice. The CCN5 KO mice also exhibited mild diabetes characterized by high fasting glucose levels and impaired insulin and glucose tolerances. Cardiac hypertrophy, ectopic lipid accumulation, and impaired lipid metabolism in hearts were observed in the CCN5 KO mice, as determined using histology, quantitative RT-PCR, and western blotting. Fibrosis was significantly greater in hearts from the CCN5 KO mice both in interstitial and perivascular regions, which was accompanied by higher expression of pro-fibrotic and pro-inflammatory genes. Both systolic and diastolic functions were significantly impaired in hearts from the CCN5 KO mice, as assessed using echocardiography. Taken together, these results indicate that CCN5 KO leads to lipotoxic cardiomyopathy with mild obesity and diabetes in mice.
Published: 2018
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16. Identification of long noncoding RNAs involved in muscle differentiation.

Author: Yeong-Hwan Lim, Duk-Hwa Kwon, Jaetaek Kim, Woo Jin Park, Hyun Kook, and Young-Kook Kim
Subjects: Medicine, Science
Abstract: Long noncoding RNAs (lncRNAs) are a large class of regulatory RNAs with diverse roles in cellular processes. Thousands of lncRNAs have been discovered; however, their roles in the regulation of muscle differentiation are unclear because no comprehensive analysis of lncRNAs during this process has been performed. In the present study, by combining diverse RNA sequencing datasets obtained from public database, we discovered lncRNAs that could behave as regulators in the differentiation of smooth or skeletal muscle cells. These analyses confirmed the roles of previously reported lncRNAs in this process. Moreover, we discovered dozens of novel lncRNAs whose expression patterns suggested their possible involvement in the phenotypic switch of vascular smooth muscle cells. The comparison of lncRNA expression change suggested that many lncRNAs have common roles during the differentiation of smooth and skeletal muscles, while some lncRNAs may have opposite roles in this process. The expression change of lncRNAs was highly correlated with that of their neighboring genes, suggesting that they may function as cis-acting lncRNAs. Furthermore, within the lncRNA sequences, there were binding sites for miRNAs with expression levels inversely correlated with the expression of corresponding lncRNAs during differentiation, suggesting a possible role of these lncRNAs as competing endogenous RNAs. The lncRNAs identified in this study will be a useful resource for future studies of gene regulation during muscle differentiation.
Published: 2018
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17. Tauroursodeoxycholic acid (TUDCA) attenuates pressure overload-induced cardiac remodeling by reducing endoplasmic reticulum stress.

Author: Shilpa Rani, Pradeep Kumar Sreenivasaiah, Jin Ock Kim, Mi Young Lee, Wan Seok Kang, Yong Sook Kim, Youngkeun Ahn, Woo Jin Park, Chunghee Cho, and Do Han Kim
Subjects: Medicine, Science
Abstract: Pressure overload in the heart induces pathological hypertrophy and is associated with cardiac dysfunction. Apoptosis and fibrosis signaling initiated by the endoplasmic reticulum stress (ERS) is known to contribute to these maladaptive effects. The aim of this study was to investigate whether reduction of ERS by a known chemical chaperone, tauroursodeoxycholic acid (TUDCA) can attenuate pressure overload-induced cardiac remodeling in a mouse model of transverse aortic constriction (TAC). Oral administration of TUDCA at a dose of 300 mg/kg body weight (BW) in the TUDCA-TAC group reduced ERS markers (GRP78, p-PERK, and p-eIf2α), compared to the Vehicle (Veh)-TAC group. TUDCA administration, for 4 weeks after TAC significantly reduced cardiac hypertrophy as shown by the reduced heart weight (HW) to BW ratio, and expression of hypertrophic marker genes (ANF, BNP, and α-SKA). Masson's trichrome staining showed that myocardial fibrosis and collagen deposition were also significantly reduced in the TUDCA-TAC group. We also found that TUDCA significantly decreased expression of TGF-β signaling proteins and collagen isoforms. TUDCA administration also reduced cardiac apoptosis and the related proteins in the TUDCA-TAC group. Microarray analysis followed by gene ontology (GO) and pathway analysis demonstrated that extracellular matrix genes responsible for hypertrophy and fibrosis, and mitochondrial genes responsible for apoptosis and fatty acid metabolism were significantly altered in the Veh-TAC group, but the alterations were normalized in the TUDCA-TAC group, suggesting potential of TUDCA in treatment of heart diseases related to pressure-overload.
Published: 2017
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18. SERCA2a: a prime target for modulation of cardiac contractility during heart failure

Author: Woo Jin Park and Jae Gyun Oh
Subjects: Inhibitor-1, Phospholamban, PKCα, Protein phosphatase 1, SERCA2a, Biology (General), QH301-705.5, Biochemistry, QD415-436
Abstract: Heart failure is one of the leading causes of sudden death indeveloped countries. While current therapies are mostly aimedat mitigating associated symptoms, novel therapies targetingthe subcellular mechanisms underlying heart failure areemerging. Failing hearts are characterized by reduced contractileproperties caused by impaired Ca2+ cycling between thesarcoplasm and sarcoplasmic reticulum (SR). Sarcoplasmic/endoplasmic reticulum Ca2+ATPase 2a (SERCA2a) mediatesCa2+ reuptake into the SR in cardiomyocytes. Of note, theexpression level and/or activity of SERCA2a, translating to thequantity of SR Ca2+ uptake, are significantly reduced in failinghearts. Normalization of the SERCA2a expression level bygene delivery has been shown to restore hampered cardiacfunctions and ameliorate associated symptoms in pre-clinicalas well as clinical studies. SERCA2a activity can be regulated atmultiple levels of a signaling cascade comprised of phospholamban,protein phosphatase 1, inhibitor-1, and PKCα.SERCA2 activity is also regulated by post-translational modificationsincluding SUMOylation and acetylation. In this review,we will highlight the molecular mechanisms underlying theregulation of SERCA2a activity and the potential therapeuticmodalities for the treatment of heart failure. [BMB Reports2013; 46(5): 237-243]
Published: 2013
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19. Cytokine-Like 1 Regulates Cardiac Fibrosis via Modulation of TGF-β Signaling.

Author: Jooyeon Kim, Jihwa Kim, Seung Hee Lee, Sacha V Kepreotis, Jimeen Yoo, Jang-Soo Chun, Roger J Hajjar, Dongtak Jeong, and Woo Jin Park
Subjects: Medicine, Science
Abstract: Cytokine-like 1 (Cytl1) is a secreted protein that is involved in diverse biological processes. A comparative modeling study indicated that Cytl1 is structurally and functionally similar to monocyte chemoattractant protein 1 (MCP-1). As MCP-1 plays an important role in cardiac fibrosis (CF) and heart failure (HF), we investigated the role of Cytl1 in a mouse model of CF and HF. Cytl1 was upregulated in the failing mouse heart. Pressure overload-induced CF was significantly attenuated in cytl1 knock-out (KO) mice compared to that from wild-type (WT) mice. By contrast, adeno-associated virus (AAV)-mediated overexpression of cytl1 alone led to the development of CF in vivo. The endothelial-mesenchymal transition (EndMT) and the transdifferentiation of fibroblasts (FBs) to myofibroblasts (MFBs) have been suggested to contribute considerably to CF. Adenovirus-mediated overexpression of cytl1 was sufficient to induce these two critical CF-related processes in vitro, which were completely abrogated by co-treatment with SB-431542, an antagonist of TGF-β receptor 1. Cytl1 induced the expression of TGF-β2 both in vivo and in vitro. Antagonizing the receptor for MCP-1, C-C chemokine receptor type 2 (CCR2), with CAS 445479-97-0 did not block the pro-fibrotic activity of Cytl1 in vitro. Collectively, our data suggest that Cytl1 plays an essential role in CF likely through activating the TGF-β-SMAD signaling pathway. Although the receptor for Cyt1l remains to be identified, Cytl1 provides a novel platform for the development of anti-CF therapies.
Published: 2016
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20. A Decoy Peptide Targeted to Protein Phosphatase 1 Attenuates Degradation of SERCA2a in Vascular Smooth Muscle Cells.

Author: Seung Pil Jang, Jae Gyun Oh, Dong Hoon Kang, Ju Young Kang, Sang Won Kang, Roger J Hajjar, and Woo Jin Park
Subjects: Medicine, Science
Abstract: Neointimal growth in the injured vasculature is largely facilitated by the proliferation of vascular smooth muscle cells (VSMC), which associates with reduced sarco/endoplasmic reticulum Ca2+-ATPase (SERCA2a) activity. The gene transfer-mediated restoration of the SERCA2a level thus attenuates neointimal growth and VSMC proliferation. We previously reported that a peptide targeted to protein phosphatase 1, ψPLB-SE, normalizes SERCA2a activity in cardiomyocytes. In this study, we found that ψPLB-SE attenuated neointimal growth in balloon-injured rat carotid arteries, and the proliferation and migration of VSMC cultured in high-serum media (synthetic conditions). In parallel, ψPLB-SE inhibited the degradation of SERCA2a in the injured carotid arteries and VSMC under synthetic conditions. The calpain inhibitor MDL28170 also attenuated SERCA2a degradation and VSMC proliferation under synthetic conditions, indicating that calpain degrades SERCA2a. The Ca2+ ionophore A23187 induced SERCA2a degradation in VSMC, which was blocked by either ψPLB-SE or MDL28170. Additionally, ψPLB-SE normalized the cytosolic Ca2+ level in VSMC that was increased by either A23187 or synthetic stimulation. Collectively, these data indicate that ψPLB-SE corrects the abnormal Ca2+ handling by activating SERCA2a, which further protects SERCA2a from calpain-dependent degradation in VSMC. We conclude that ψPLB-SE may form the basis of a therapeutic strategy for vascular proliferative disorders.
Published: 2016
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21. Cucurbitacin I Attenuates Cardiomyocyte Hypertrophy via Inhibition of Connective Tissue Growth Factor (CCN2) and TGF- β/Smads Signalings.

Author: Moon Hee Jeong, Shang-Jin Kim, Hara Kang, Kye Won Park, Woo Jin Park, Seung Yul Yang, and Dong Kwon Yang
Subjects: Medicine, Science
Abstract: Cucurbitacin I is a naturally occurring triterpenoid derived from Cucurbitaceae family plants that exhibits a number of potentially useful pharmacological and biological activities. However, the therapeutic impact of cucurbitacin I on the heart has not heretofore been reported. To evaluate the functional role of cucurbitacin I in an in vitro model of cardiac hypertrophy, phenylephrine (PE)-stimulated cardiomyocytes were treated with a sub-cytotoxic concentration of the compound, and the effects on cell size and mRNA expression levels of ANF and β-MHC were investigated. Consequently, PE-induced cell enlargement and upregulation of ANF and β-MHC were significantly suppressed by pretreatment of the cardiomyocytes with cucurbitacin I. Notably, cucurbitacin I also impaired connective tissue growth factor (CTGF) and MAPK signaling, pro-hypertrophic factors, as well as TGF-β/Smad signaling, the important contributing factors to fibrosis. The protective impact of cucurbitacin I was significantly blunted in CTGF-silenced or TGF-β1-silenced hypertrophic cardiomyocytes, indicating that the compound exerts its beneficial actions through CTGF. Taken together, these findings signify that cucurbitacin I protects the heart against cardiac hypertrophy via inhibition of CTGF/MAPK, and TGF- β/Smad-facilitated events. Accordingly, the present study provides new insights into the defensive capacity of cucurbitacin I against cardiac hypertrophy, and further suggesting cucurbitacin I's utility as a novel therapeutic agent for the management of heart diseases.
Published: 2015
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22. Pik3ip1 modulates cardiac hypertrophy by inhibiting PI3K pathway.

Author: Hong Ki Song, Jiyeon Kim, Jong Sub Lee, Kyoung Jin Nho, Hae Chang Jeong, Jihwa Kim, Youngkeun Ahn, Woo Jin Park, and Do Han Kim
Subjects: Medicine, Science
Abstract: Cardiac hypertrophy is an adaptive response to various physiological and pathological stimuli. Phosphoinositide-3 kinase (PI3K) is a highly conserved lipid kinase involved in physiological cardiac hypertrophy (PHH). PI3K interacting protein1 (Pik3ip1) shares homology with the p85 regulatory subunit of PI3K and is known to interact with the p110 catalytic subunit of PI3K, leading to attenuation of PI3K activity in liver and immune cells. However, the role of Pik3ip1 in the heart remains unknown. In the present study, the effects of Pik3ip1 on cardiac hypertrophy were examined. We found that the expression level of Pik3ip1 was markedly higher in cardiomyocytes than in fibroblasts. The interaction of Pik3ip1 with the p110a subunit of PI3K in the heart was identified by immunoprecipitation using neonatal rat cardiomyocytes (NRCM). Approximately 35% knockdown of Pik3ip1 was sufficient to induce myocardial hypertrophy. Pik3ip1 deficiency was shown to lead to activation of PI3K/protein kinase B (AKT)/ mammalian target of rapamycin (mTOR) signaling pathway, increasing protein synthesis and cell size. However, adenovirus-mediated overexpression of Pik3ip1 attenuated PI3K-mediated cardiac hypertrophy. Pik3ip1 was upregulated by PHH due to swimming training, but not by pathological cardiac hypertrophy (PAH) due to pressure-overload, suggesting that Pik3ip1 plays a compensatory negative role for PHH. Collectively, our results elucidate the mechanisms for the roles of Pik3ip1 in PI3K/AKT signaling pathway.
Published: 2015
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23. Intracellular cleavage of amyloid β by a viral protease NIa prevents amyloid β-mediated cytotoxicity.

Author: Baehyun Shin, Hyejin Oh, Sang Min Park, Hye-Eun Han, Michael Ye, Woo Keun Song, and Woo Jin Park
Subjects: Medicine, Science
Abstract: Nuclear inclusion a (NIa) of turnip mosaic virus is a cytosolic protease that cleaves amyloid β (Aβ) when heterologously overexpressed. Lentivirus-mediated expression of NIa in the brains of APP(sw)/PS1 mice significantly reduces cerebral Aβ levels and plaque depositions, and improves behavioral deficits. Here, the effects of NIa and neprilysin (NEP), a well-known Aβ-cleaving protease, on oligomeric Aβ-induced cell death were evaluated. NIa cleaved monomeric and oligomeric Aβ at a similar rate, whereas NEP only cleaved monomeric Aβ. Oligomeric Aβ-induced cytotoxicity and mitochondrial dysfunction were significantly ameliorated by NIa, but not by NEP. Endocytosed fluorescently-labeled Aβ localized to mitochondria, and this was significantly reduced by NIa, but not by NEP. These data suggest that NIa may exerts its protective roles by degrading Aβ and thus preventing mitochondrial deposition of Aβ.
Published: 2014
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24. β-Lapachone ameliorates lipotoxic cardiomyopathy in acyl CoA synthase transgenic mice.

Author: Moon Hee Jeong, Nguyen Khoi Song Tran, Tae Hwan Kwak, Byung Keon Park, Chul Soon Lee, Tae-Sik Park, Young-Hoon Lee, Woo Jin Park, and Dong Kwon Yang
Subjects: Medicine, Science
Abstract: Lipotoxic cardiomyopathy is caused by myocardial lipid accumulation and often occurs in patients with diabetes and obesity. This study investigated the effects of β-lapachone (β-lap), a natural compound that activates Sirt1 through elevation of the intracellular NAD+ level, on acyl CoA synthase (ACS) transgenic (Tg) mice, which have lipotoxic cardiomyopathy. Oral administration of β-lap to ACS Tg mice significantly attenuated heart failure and inhibited myocardial accumulation of triacylglycerol. Electron microscopy and measurement of mitochondrial complex II protein and mitochondrial DNA revealed that administration of β-lap restored mitochondrial integrity and biogenesis in ACS Tg hearts. Accordingly, β-lap administration significantly increased the expression of genes associated with mitochondrial biogenesis and fatty acid metabolism that were down-regulated in ACS Tg hearts. β-lap also restored the activities of Sirt1 and AMP-activated protein kinase (AMPK), the two key regulators of metabolism, which were suppressed in ACS Tg hearts. In H9C2 cells, β-lap-mediated elevation of AMPK activity was retarded when the level of Sirt1 was reduced by transfection of siRNA against Sirt1. Taken together, these results indicate that β-lap exerts cardioprotective effects against cardiac lipotoxicity through the activation of Sirt1 and AMPK. β-lap may be a novel therapeutic agent for the treatment of lipotoxic cardiomyopathy.
Published: 2014
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25. SPIN90 knockdown attenuates the formation and movement of endosomal vesicles in the early stages of epidermal growth factor receptor endocytosis.

Author: Hyejin Oh, Hwan Kim, Kyung-Hwun Chung, Nan Hyung Hong, Baehyun Shin, Woo Jin Park, Youngsoo Jun, Sangmyung Rhee, and Woo Keun Song
Subjects: Medicine, Science
Abstract: The finding that SPIN90 colocalizes with epidermal growth factor (EGF) in EEA1-positive endosomes prompted us to investigate the role of SPIN90 in endocytosis of the EGF receptor (EGFR). In the present study, we demonstrated that SPIN90 participates in the early stages of endocytosis, including vesicle formation and trafficking. Stable HeLa cells with knockdown of SPIN90 displayed significantly higher levels of surface EGFR than control cells. Analysis of the abundance and cellular distribution of EGFR via electron microscopy revealed that SPIN90 knockdown cells contain residual EGFR at cell membranes and fewer EGFR-containing endosomes, both features that reflect reduced endosome formation. The delayed early endosomal targeting capacity of SPIN90 knockdown cells led to increased EGFR stability, consistent with the observed accumulation of EGFR at the membrane. Small endosome sizes and reduced endosome formation in SPIN90 knockdown cells, observed using fluorescent confocal microscopy, strongly supported the involvement of SPIN90 in endocytosis of EGFR. Overexpression of SPIN90 variants, particularly the SH3, PRD, and CC (positions 643 - 722) domains, resulted in aberrant morphology of Rab5-positive endosomes (detected as small spots located near the cell membrane) and defects in endosomal movement. These findings clearly suggest that SPIN90 participates in the formation and movement of endosomes. Consistent with this, SPIN90 knockdown enhanced cell proliferation. The delay in EGFR endocytosis effectively increased the levels of endosomal EGFR, which triggered activation of ERK1/2 and cell proliferation via upregulation of cyclin D1. Collectively, our findings suggest that SPIN90 contributes to the formation and movement of endosomal vesicles, and modulates the stability of EGFR protein, which affects cell cycle progression via regulation of the activities of downstream proteins, such as ERK1/2, after EGF stimulation.
Published: 2013
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26. Pharmacological activation of Sirt1 ameliorates polyglutamine-induced toxicity through the regulation of autophagy.

Author: Bae Hyun Shin, Yunki Lim, Hye Jin Oh, Sang Min Park, Sun-Kyung Lee, Joohong Ahnn, Do Han Kim, Woo Keun Song, Tae Hwan Kwak, and Woo Jin Park
Subjects: Medicine, Science
Abstract: Intracellular accumulation of polyglutamine (polyQ)-expanded Huntingtin (Htt) protein is a hallmark of Huntington's disease (HD). This study evaluated whether activation of Sirt1 by the anti-cancer agent, β-lapachone (β-lap), induces autophagy in human neuroblastoma SH-SY5Y cells, thereby reducing intracellular levels of polyQ aggregates and their concomitant cytotoxicity. Treatment of cells with β-lap markedly diminished the cytotoxicity induced by forced expression of Htt exon 1 containing a pathogenic polyQ stretch fused to green fluorescent protein (HttEx1(97Q)-GFP). β-lap increased autophagy in SH-SY5Y cells, as evidenced by the increased formation of LC3-II and autolysosomes. Furthermore, β-lap reduced HttEx1(97Q)-GFP aggregation, which was significantly prevented by co-incubation with 3-methyladenine, an inhibitor of autophagy. β-lap increased Sirt1 activity, as shown by the increased deacetylation of the Sirt1 substrates, PARP-1 and Atg5, and the nuclear translocation of FOXO1. Both the induction of autophagy and attenuation of HttEx1(97Q)-GFP aggregation by β-lap were significantly prevented by co-incubation with sirtinol, a general sirtuin inhibitor or by co-transfection with shRNA against Sirt1. The pro-autophagic actions of β-lap were further investigated in a transgenic Caenorhabditis elegans (C. elegans) line that expressed Q67 fused to cyanine fluorescent protein (Q67). Notably, β-lap reduced the number of Q67 puncta and restored Q67-induced defects in motility, which were largely prevented by pre-treatment with RNAi against sir-2.1, the C. elegans orthologue of Sirt1. Collectively, these data suggest that β-lap induces autophagy through activation of Sirt1, which in turn leads to a reduction in polyQ aggregation and cellular toxicity. Thus, β-lap provides a novel therapeutic opportunity for the treatment of HD.
Published: 2013
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27. Cardiomyocyte specific deletion of Crif1 causes mitochondrial cardiomyopathy in mice.

Author: Juhee Shin, Seok Hong Lee, Min-Chul Kwon, Dong Kwon Yang, Ha-Rim Seo, Jaetaek Kim, Yoon-Young Kim, Sun-Kyoung Im, Evan Dale Abel, Kyong-Tai Kim, Woo Jin Park, and Young-Yun Kong
Subjects: Medicine, Science
Abstract: Mitochondria are key organelles dedicated to energy production. Crif1, which interacts with the large subunit of the mitochondrial ribosome, is indispensable for the mitochondrial translation and membrane insertion of respiratory subunits. To explore the physiological function of Crif1 in the heart, Crif1(f/f) mice were crossed with Myh6-cre/Esr1 transgenic mice, which harbor cardiomyocyte-specific Cre activity in a tamoxifen-dependent manner. The tamoxifen injections were given at six weeks postnatal, and the mutant mice survived only five months due to hypertrophic heart failure. In the mutant cardiac muscles, mitochondrial mass dramatically increased, while the inner structure was altered with lack of cristae. Mutant cardiac muscles showed decreased rates of oxygen consumption and ATP production, suggesting that Crif1 plays a critical role in the maintenance of both mitochondrial structure and respiration in cardiac muscles.
Published: 2013
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28. AAV-mediated knock-down of HRC exacerbates transverse aorta constriction-induced heart failure.

Author: Chang Sik Park, Hyeseon Cha, Eun Jeong Kwon, Dongtak Jeong, Roger J Hajjar, Evangelia G Kranias, Chunghee Cho, Woo Jin Park, and Do Han Kim
Subjects: Medicine, Science
Abstract: Histidine-rich calcium binding protein (HRC) is located in the lumen of sarcoplasmic reticulum (SR) that binds to both triadin (TRN) and SERCA affecting Ca(2+) cycling in the SR. Chronic overexpression of HRC that may disrupt intracellular Ca(2+) homeostasis is implicated in pathogenesis of cardiac hypertrophy. Ablation of HRC showed relatively normal phenotypes under basal condition, but exhibited a significantly increased susceptibility to isoproterenol-induced cardiac hypertrophy. In the present study, we characterized the functions of HRC related to Ca(2+) cycling and pathogenesis of cardiac hypertrophy using the in vitro siRNA- and the in vivo adeno-associated virus (AAV)-mediated HRC knock-down (KD) systems, respectively.AAV-mediated HRC-KD system was used with or without C57BL/6 mouse model of transverse aortic constriction-induced failing heart (TAC-FH) to examine whether HRC-KD could enhance cardiac function in failing heart (FH). Initially we expected that HRC-KD could elicit cardiac functional recovery in failing heart (FH), since predesigned siRNA-mediated HRC-KD enhanced Ca(2+) cycling and increased activities of RyR2 and SERCA2 without change in SR Ca(2+) load in neonatal rat ventricular cells (NRVCs) and HL-1 cells. However, AAV9-mediated HRC-KD in TAC-FH was associated with decreased fractional shortening and increased cardiac fibrosis compared with control. We found that phospho-RyR2, phospho-CaMKII, phospho-p38 MAPK, and phospho-PLB were significantly upregulated by HRC-KD in TAC-FH. A significantly increased level of cleaved caspase-3, a cardiac cell death marker was also found, consistent with the result of TUNEL assay.Increased Ca(2+) leak and cytosolic Ca(2+) concentration due to a partial KD of HRC could enhance activity of CaMKII and phosphorylation of p38 MAPK, causing the mitochondrial death pathway observed in TAC-FH. Our results present evidence that down-regulation of HRC could deteriorate cardiac function in TAC-FH through perturbed SR-mediated Ca(2+) cycling.
Published: 2012
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29. An engineered viral protease exhibiting substrate specificity for a polyglutamine stretch prevents polyglutamine-induced neuronal cell death.

Author: Saravanan Sellamuthu, Bae Hyun Shin, Hye-Eun Han, Sang Min Park, Hye Jin Oh, Seong-Hwan Rho, Yong Jae Lee, and Woo Jin Park
Subjects: Medicine, Science
Abstract: BACKGROUND: Polyglutamine (polyQ)-induced protein aggregation is the hallmark of a group of neurodegenerative diseases, including Huntington's disease. We hypothesized that a protease that could cleave polyQ stretches would intervene in the initial events leading to pathogenesis in these diseases. To prove this concept, we aimed to generate a protease possessing substrate specificity for polyQ stretches. METHODOLOGY/PRINCIPAL FINDINGS: Hepatitis A virus (HAV) 3C protease (3CP) was subjected to engineering using a yeast-based method known as the Genetic Assay for Site-specific Proteolysis (GASP). Analysis of the substrate specificity revealed that 3CP can cleave substrates containing glutamine at positions P5, P4, P3, P1, P2', or P3', but not substrates containing glutamine at the P2 or P1' positions. To accommodate glutamine at P2 and P1', key residues comprising the active sites of the S2 or S1' pockets were separately randomized and screened. The resulting sets of variants were combined by shuffling and further subjected to two rounds of randomization and screening using a substrate containing glutamines from positions P5 through P3'. One of the selected variants (Var26) reduced the expression level and aggregation of a huntingtin exon1-GFP fusion protein containing a pathogenic polyQ stretch (HttEx1(97Q)-GFP) in the neuroblastoma cell line SH-SY5Y. Var26 also prevented cell death and caspase 3 activation induced by HttEx1(97Q)-GFP. These protective effects of Var26 were proteolytic activity-dependent. CONCLUSIONS/SIGNIFICANCE: These data provide a proof-of-concept that proteolytic cleavage of polyQ stretches could be an effective modality for the treatment of polyQ diseases.
Published: 2011
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30. The nuclear inclusion a (NIa) protease of turnip mosaic virus (TuMV) cleaves amyloid-β.

Author: Hye-Eun Han, Saravanan Sellamuthu, Bae Hyun Shin, Yong Jae Lee, Sungmin Song, Ji-Seon Seo, In-Sun Baek, Jeomil Bae, Hannah Kim, Yung Joon Yoo, Yong-Keun Jung, Woo Keun Song, Pyung-Lim Han, and Woo Jin Park
Subjects: Medicine, Science
Abstract: BACKGROUND: The nuclear inclusion a (NIa) protease of turnip mosaic virus (TuMV) is responsible for the processing of the viral polyprotein into functional proteins. NIa was previously shown to possess a relatively strict substrate specificity with a preference for Val-Xaa-His-Gln↓, with the scissile bond located after Gln. The presence of the same consensus sequence, Val(12)-His-His-Gln(15), near the presumptive α-secretase cleavage site of the amyloid-β (Aβ) peptide led us to hypothesize that NIa could possess activity against Aβ. METHODOLOGY/PRINCIPAL FINDINGS: Western blotting results showed that oligomeric as well as monomeric forms of Aβ can be degraded by NIa in vitro. The specific cleavage of Aβ was further confirmed by mass spectrometry analysis. NIa was shown to exist predominantly in the cytoplasm as observed by immunofluorescence microscopy. The overexpression of NIa in B103 neuroblastoma cells resulted in a significant reduction in cell death caused by both intracellularly generated and exogenously added Aβ. Moreover, lentiviral-mediated expression of NIa in APP(sw)/PS1 transgenic mice significantly reduced the levels of Aβ and plaques in the brain. CONCLUSIONS/SIGNIFICANCE: These results indicate that the degradation of Aβ in the cytoplasm could be a novel strategy to control the levels of Aβ, plaque formation, and the associated cell death.
Published: 2010
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31. miR-27a-3p Targets ATF3 to Reduce Calcium Deposition in Vascular Smooth Muscle Cells

Author: Woo Jin Park, Hyun Kook, Gwang Hyeon Eom, Kwang Il Nam, Young Kook Kim, Hye Jung Cho, Nakwon Choe, Sera Shin, Juhee Ryu, Duk-Hwa Kwon, Youngkeun Ahn, and Hosouk Joung
Subjects: 0301 basic medicine, Vascular smooth muscle, Activating transcription factor, chemistry.chemical_element, Calcium, 03 medical and health sciences, 0302 clinical medicine, Downregulation and upregulation, Drug Discovery, microRNA, vascular smooth muscle cells, Transcription factor, miRNA, ATF3, Chemistry, lcsh:RM1-950, Transfection, Cell biology, 030104 developmental biology, lcsh:Therapeutics. Pharmacology, vascular calcification, 030220 oncology & carcinogenesis, Molecular Medicine, Original Article, activating transcription factor 3, miR-27a-3p
Abstract: Vascular calcification, the ectopic deposition of calcium in blood vessels, develops in association with various metabolic diseases and atherosclerosis and is an independent predictor of morbidity and mortality associated with these diseases. Herein, we report that reduction of microRNA-27a-3p (miR-27a-3p) causes an increase in activating transcription factor 3 (ATF3), a novel osteogenic transcription factor, in vascular smooth muscle cells. Both microRNA (miRNA) and mRNA microarrays were performed with rat vascular smooth muscle cells, and reciprocally regulated pairs of miRNA and mRNA were selected after bioinformatics analysis. Inorganic phosphate significantly reduced the expression of miR-27a-3p in A10 cells. The transcript level was also reduced in vitamin D3-administered mouse aortas. miR-27a-3p mimic reduced calcium deposition, whereas miR-27a-3p inhibitor increased it. The Atf3 mRNA level was upregulated in a cellular vascular calcification model, and miR-27a-3p reduced the Atf3 mRNA and protein levels. Transfection with Atf3 could recover the miR-27a-3p-induced reduction of calcium deposition. Our results suggest that reduction of miR-27a-3p may contribute to the development of vascular calcification by de-repression of ATF3., Graphical Abstract, Vascular calcification causes stiffness of blood vessels, which causes secondary damage to the cardiovascular system. A reduction in the microRNA miR-27a-3p leads to an increase in the transcription factor ATF3, which induces calcium deposition. This miR-27a-3p/ATF signaling pathway may provide a novel therapeutic target for vascular calcification.
Published: 2020

32. Recent Advances in Anti-Aging Medicine

Author: Da Hye Son, Woo Jin Park, and Yongjae Lee
Subjects: Aging, Hormone Replacement Therapy, medicine.medical_treatment, Calorie restriction, Calorie Restriction, 030209 endocrinology & metabolism, Review Article, Gut flora, Bioinformatics, 03 medical and health sciences, 0302 clinical medicine, medicine, Vitamin D and neurology, 030212 general & internal medicine, Hormone replacement therapy, Vitamin D, biology, business.industry, Prebiotic, biology.organism_classification, Metformin, Sirtuin, Pegvisomant, biology.protein, Family Practice, business, medicine.drug
Abstract: A rapidly aging population in Korea has led to increased attention in the field of anti-aging medicine. The purpose of anti-aging medicine is to slow, stop, or reverse the aging process and its associated effects, such as disability and frailty. Anti-aging medicine is emerging as a growing industry, but many supplements or protocols are available that do not have scientific evidence to support their claims. In this review, the mechanisms of action and the clinical implications of anti-aging interventions were examined and explained. Calorie restriction mimetics define compounds that imitate the outcome of calorie restriction, including an activator of AMP protein kinase (metformin), inhibitor of growth hormone/insulin-like growth factor-1 axis (pegvisomant), inhibitor of mammalian target of rapamycin (rapamycin), and activator of the sirtuin pathway (resveratrol). Hormonal replacement has also been widely used in the elderly population to improve their quality of life. Manipulating healthy gut microbiota through prebiotic/probiotics or fecal microbiota transplantation has significant potential in anti-aging medicine. Vitamin D is expected to be a primary anti-aging medicine in the near future due to its numerous positive effects in the elderly population.
Published: 2019

33. Dry age-related macular degeneration like pathology in aged 5XFAD mice: Ultrastructure and microarray analysis

Author: Young-Jun Park, Kihwang Lee, Woo Jin Park, Hyoung Oh Jun, Young Hoon Lee, Jin Hyoung Kim, Jeong Hun Kim, Sung Wook Park, and Sora Im
Subjects: 0301 basic medicine, medicine.medical_specialty, Pathology, Aging, Amyloid β, genetic structures, retinal pigment epithelium, Mice, Inbred Strains, Mice, Transgenic, Lipofuscin, 03 medical and health sciences, Macular Degeneration, Research Paper: Gerotarget (Focus on Aging), Microscopy, Electron, Transmission, Alzheimer Disease, Ophthalmology, transmission electron microscopy, medicine, Animals, Humans, age-related macular degeneration, Oligonucleotide Array Sequence Analysis, Retinal pigment epithelium, Amyloid beta-Peptides, business.industry, Microarray analysis techniques, Gerotarget, Gene Expression Profiling, Macular degeneration, medicine.disease, eye diseases, Disease Models, Animal, 030104 developmental biology, Choroidal neovascularization, medicine.anatomical_structure, Oncology, Ultrastructure, amyloid β, sense organs, Bruch Membrane, medicine.symptom, business, microarray, Biomedical sciences
Abstract: // Sung Wook Park 1 , 2 , Sora Im 3 , Hyoung Oh Jun 2 , Kihwang Lee 4 , Young-Jun Park 5 , Jin Hyoung Kim 2 , Woo Jin Park 3 , Young-Hoon Lee 6 and Jeong Hun Kim 1,2,7 1 Department of Biomedical Sciences, Seoul National University College of Medicine, Daehak-Ro, Jongno-Gu, Seoul, Republic of Korea 2 Fight Against Angiogenesis-Related Blindness Laboratory, Biomedical Research Institute, Seoul National University Hospital, Daehak-Ro, Jongno-Gu, Seoul, Republic of Korea 3 Department of Life Sciences, Life Sciences Concentration Gwangju Institute of Science and Technology Cheomdan-Gwagiro, Buk-Gu, Gwangju, Republic of Korea 4 Department of Ophthalmology, Ajou University School of Medicine, World Cup-Ro, Yeongtong-Gu, Suwon-Si, Gyeonggi-Do, Republic of Korea 5 Immunotherapy Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea 6 Department of Oral Anatomy, School of Dentistry, Chonbuk National University, Deokjin-Gu, Jeonju-Si, Jeollabuk-Do, Republic of Korea 7 Institute of Oral Biosciences, Chonbuk National University, Deokjin-Gu, Jeonju-Si, Jeollabuk-Do, Republic of Korea Correspondence to Jeong Hun Kim, email: // Keywords : amyloid β, age-related macular degeneration, transmission electron microscopy, retinal pigment epithelium, microarray, Gerotarget Received : September 02, 2016 Accepted : March 29, 2017 Published : April 08, 2017 Abstract Age-related macular degeneration (AMD) is a leading cause of blindness in the elderly. The two types of AMD are: dry and wet AMD. While laser-induced choroidal neovascularization has been used extensively in the studies of wet AMD, there is no established mouse model that fully recapitulates the cardinal features of dry AMD. A lack of appropriate mouse model for dry AMD has hampered the translational research on the pathogenesis of the disease and the development of therapeutic agents. We hypothesized that 5XFAD mice, an animal model for the study of Alzheimer’s disease, can be used as a mouse model for dry AMD with regard to the amyloid beta (Aβ) related pathology. In this study, the ultrastructure of the retinal pigment epithelium (RPE) of 5XFAD mice was analyzed using transmission electron microscopy. Of importance, the aged 5XFAD mice show ultrastructural changes in the RPE and Bruch’s membrane (BM) that are compatible with the cardinal features of human dry AMD, including a loss of apical microvilli and basal infolding of the RPE, increased BM thickness, basal laminar and linear deposits, and accumulation of lipofuscin granules and undigested photoreceptor outer segment-laden phagosomes. In microarray-based analysis, the RPE complex of the aged 5XFAD mice shows differential gene expression profiles consistent with dry AMD in the inflammation response, immune reaction pathway, and decreased retinol metabolism. Taken together, we suggest that aged 5XFAD mice can be used as a mouse model of dry AMD to study Aβ related pathology and develop a new therapeutic approaches.
Published: 2017

34. Role of SIRT1 in Modulating Acetylation of the Sarco-Endoplasmic Reticulum Ca(2+)-ATPase in Heart Failure

Author: Junichi Sadoshima, Yoichi Sunagawa, Changwon Kho, Koji Hasegawa, Tatsuya Morimoto, Dongtak Jeong, Vadim Chepurko, Roger J. Hajjar, Ahyoung Lee, Tae Hwan Kwak, Woo Jin Park, Dong Kwon Yang, Soo Hyun Eom, Yung Joon Yoo, Peter Vangheluwe, Przemek A. Gorski, Hyun Kook, Seung Pil Jang, Zee-Yong Park, Do Han Kim, Jae Gyun Oh, and Philyoung Lee
Subjects: Cardiac function curve, Male, mice, Physiology, Swine, SUMO protein, Mice, Transgenic, Article, Cell Line, Sarcoplasmic Reticulum Calcium-Transporting ATPases, chemistry.chemical_compound, Adenosine Triphosphate, Sirtuin 1, medicine, Animals, Humans, Myocytes, Cardiac, Cells, Cultured, Heart Failure, Mice, Knockout, lysine, biology, Endoplasmic reticulum, Lysine, Acetylation, medicine.disease, Cell biology, Mice, Inbred C57BL, endoplasmic reticulum, chemistry, Heart failure, biology.protein, cardiovascular system, Cardiology and Cardiovascular Medicine, Adenosine triphosphate, Reticulum, E1A-Associated p300 Protein, Protein Processing, Post-Translational, circulatory and respiratory physiology
Abstract: Rationale: SERCA2a, sarco-endoplasmic reticulum Ca 2+ -ATPase, is a critical determinant of cardiac function. Reduced level and activity of SERCA2a are major features of heart failure. Accordingly, intensive efforts have been made to develop efficient modalities for SERCA2a activation. We showed that the activity of SERCA2a is enhanced by post-translational modification with SUMO1 (small ubiquitin-like modifier 1). However, the roles of other post-translational modifications on SERCA2a are still unknown. Objective: In this study, we aim to assess the role of lysine acetylation on SERCA2a function and determine whether inhibition of lysine acetylation can improve cardiac function in the setting of heart failure. Methods and Results: The acetylation of SERCA2a was significantly increased in failing hearts of humans, mice, and pigs, which is associated with the reduced level of SIRT1 (sirtuin 1), a class III histone deacetylase. Downregulation of SIRT1 increased the SERCA2a acetylation, which in turn led to SERCA2a dysfunction and cardiac defects at baseline. In contrast, pharmacological activation of SIRT1 reduced the SERCA2a acetylation, which was accompanied by recovery of SERCA2a function and cardiac defects in failing hearts. Lysine 492 (K492) was of critical importance for the regulation of SERCA2a activity via acetylation. Acetylation at K492 significantly reduced the SERCA2a activity, presumably through interfering with the binding of ATP to SERCA2a. In failing hearts, acetylation at K492 appeared to be mediated by p300 (histone acetyltransferase p300), a histone acetyltransferase. Conclusions: These results indicate that acetylation/deacetylation at K492, which is regulated by SIRT1 and p300, is critical for the regulation of SERCA2a activity in hearts. Pharmacological activation of SIRT1 can restore SERCA2a activity through deacetylation at K492. These findings might provide a novel strategy for the treatment of heart failure.
Published: 2019

35. Partial loss of interleukin 2 receptor gamma function in pigs provides mechanistic insights for the study of human immunodeficiency syndrome

Author: Clifton N. Murphy, Woo-Jin Park, Deug-Nam Kwon, Jin-Hoi Kim, Kiho Lee, Melissa Samuel, Jeong Tae Do, Chankyu Park, Alana N. Brown, Kwang-Wook Park, Yun-Jung Choi, Randall S. Prather, Seong-Keun Cho, Hyuk Song, and Animal and Poultry Sciences
Subjects: 0301 basic medicine, GENES, Swine, CD3, Spleen, Interleukin Receptor Common gamma Subunit, somatic cell nuclear transfer, 03 medical and health sciences, Gene Knockout Techniques, 0302 clinical medicine, TALEN, Pathology Section, medicine, Animals, Humans, IL-2 receptor, Immunodeficiency, Severe combined immunodeficiency, biology, business.industry, LIVESTOCK, Cell Biology, X-SCID, medicine.disease, Molecular biology, IL2RG, Research Paper: Pathology, Disease Models, Animal, 030104 developmental biology, medicine.anatomical_structure, KNOCKOUT, Oncology, Immunology, CELLS, biology.protein, CHAIN, Severe Combined Immunodeficiency, Stem cell, business, immunodeficiency, CD8, 030215 immunology
Abstract: // Yun-Jung Choi 1,* , Kiho Lee 2,3,* , Woo-Jin Park 1 , Deug-Nam Kwon 1 , Chankyu Park 1 , Jeong Tae Do 1 , Hyuk Song 1 , Seong-Keun Cho 5 , Kwang-Wook Park 6 , Alana N. Brown 3,4 , Melissa S. Samuel 3,4 , Clifton N. Murphy 3,4 , Randall S. Prather 3,4 and Jin-Hoi Kim 1 1 Animal Biotechnology to Stem Cell and Regenerative Biotechnology, Humanized Pig Research Center (SRC), Konkuk University, Seoul, Republic of Korea 2 Department of Animal and Poultry Sciences, Virginia Tech, Blacksburg, VA, USA 3 Division of Animal Science, National Swine Resource and Research Center, University of Missouri, Columbia, MO, USA 4 National Swine Resource and Research Center, University of Missouri, Columbia, MO, USA 5 Department of Animal Science, Pusan National University, Miryang, Gyeongnam, Republic of Korea 6 Department of Animal Science and Technology, Sunchon National University, Suncheon, Jeonnam, Republic of Korea * These authors have contributed equally to this work Correspondence to: Randall S. Prather, email: // Jin-Hoi Kim, email: // Keywords : IL2RG, X-SCID, immunodeficiency, somatic cell nuclear transfer, TALEN, Pathology Section Received : May 08, 2016 Accepted : July 13, 2016 Published : July 24, 2016 Abstract In this study, we described the phenotype of monoallelic interleukin 2 receptor gamma knockout ( mIL2RG +/Δ69-368 KO) pigs. Approximately 80% of mIL2RG +/Δ69-368 KO pigs (8/10) were athymic, whereas 20% (2/10) presented a rudimentary thymus. The body weight of IL2RG +/Δ69-368 KO pigs developed normally. Immunological analysis showed that mIL2RG +/Δ69-368 KO pigs possessed CD25 + CD44- or CD25-CD44 + cells, whereas single (CD4 or CD8) or double (CD4/8) positive cells were lacking in mIL2RG +/Δ69-368 KO pigs. CD3 + cells in the thymus of mIL2RG +/Δ69-368 KO pigs contained mainly CD44 + cells and/or CD25 + cells, which included FOXP3 + cells. These observations demonstrated that T cells from mIL2RG +/Δ69-368 KO pigs were able to develop to the DN3 stage, but failed to transition toward the DN4 stage. Whole-transcriptome analysis of thymus and spleen, and subsequent pathway analysis revealed that a subset of genes differentially expressed following the loss of IL2RG might be responsible for both impaired T-cell receptor and cytokine-mediated signalling. However, comparative analysis of two mIL2RG +/Δ69-368 KO pigs revealed little variability in the down- and up-regulated gene sets. In conclusion, mIL2RG +/Δ69-368 KO pigs presented a T-B+NK- SCID phenotype, suggesting that pigs can be used as a valuable and suitable biomedical model for human SCID research.
Published: 2016

36. Integrated Quantitative Phosphoproteomics and Cell-Based Functional Screening Reveals Specific Pathological Cardiac Hypertrophy-Related Phosphorylation Sites.

Author: Hye Kyeong Kwon, Hyunwoo Choi, Sung-Gyoo Park, Woo Jin Park, Do Han Kim, and Zee-Yong Park
Abstract: Cardiac hypertrophic signaling cascades resulting in heart failure diseases are mediated by protein phosphorylation. Recent developments in mass spectrometry-based phosphoproteomics have led to the identification of thousands of differentially phosphorylated proteins and their phosphorylation sites. However, functional studies of these differentially phosphorylated proteins have not been conducted in a large-scale or high-throughput manner due to a lack of methods capable of revealing the functional relevance of each phosphorylation site. In this study, an integrated approach combining quantitative phosphoproteomics and cell-based functional screening using phosphorylation competition peptides was developed. A pathological cardiac hypertrophy model, junctate-1 transgenic mice and control mice, were analyzed using label-free quantitative phosphoproteomics to identify differentially phosphorylated proteins and sites. A cell-based functional assay system measuring hypertrophic cell growth of neonatal rat ventricle cardiomyocytes (NRVMs) following phenylephrine treatment was applied, and changes in phosphorylation of individual differentially phosphorylated sites were induced by incorporation of phosphorylation competition peptides conjugated with cell-penetrating peptides. Cell-based functional screening against 18 selected phosphorylation sites identified three phosphorylation sites (Ser-98, Ser-179 of Ldb3, and Ser-1146 of palladin) displaying near-complete inhibition of cardiac hypertrophic growth of NRVMs. Changes in phosphorylation levels of Ser-98 and Ser-179 in Ldb3 were further confirmed in NRVMs and other pathological/physiological hypertrophy models, including transverse aortic constriction and swimming models, using site-specific phospho-antibodies. Our integrated approach can be used to identify functionally important phosphorylation sites among differentially phosphorylated sites, and unlike conventional approaches, it is easily applicable for large-scale and/or high-throughput analyses. [ABSTRACT FROM AUTHOR]
Published: 2021
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37. Connexin43 and zonula occludens-1 are targets of Akt in cardiomyocytes that correlate with cardiac contractile dysfunction in Akt deficient hearts

Author: Tae Jin Lee, Young Kook Kim, Hyun Min Kim, Sangmi Ock, E. D. Abel, Woo Jin Park, Kyu Sang Park, Jaetaek Kim, Wang Soo Lee, and Hyun Kook
Subjects: 0301 basic medicine, medicine.medical_specialty, Programmed cell death, Cardiac fibrosis, AKT1, AKT2, 030204 cardiovascular system & hematology, Article, Muscle hypertrophy, 03 medical and health sciences, Mice, 0302 clinical medicine, Internal medicine, Natriuretic Peptide, Brain, medicine, Animals, Myocytes, Cardiac, Molecular Biology, Protein kinase B, Mice, Knockout, Chemistry, Myocardium, medicine.disease, Brain natriuretic peptide, Fibrosis, Myocardial Contraction, Rats, 030104 developmental biology, Endocrinology, Heart failure, Connexin 43, embryonic structures, Zonula Occludens-1 Protein, Molecular Medicine, Cardiomyopathies, Proto-Oncogene Proteins c-akt, hormones, hormone substitutes, and hormone antagonists, Atrial Natriuretic Factor
Abstract: While deletion of Akt1 results in a smaller heart size and Akt2(−/−) mice are mildly insulin resistant, Akt1(−/−)/Akt2(−/−) mice exhibit perinatal lethality, indicating a large degree of functional overlap between the isoforms of the serine/threonine kinase Akt. The present study aimed to determine the cooperative contribution of Akt1 and Akt2 on the structure and contractile function of adult hearts. To generate an inducible, cardiomyocyte-restricted Akt2 knockout (KO) model, Akt2(flox/flox) mice were crossed with tamoxifen-inducible MerCreMer transgenic (MCM) mice and germline Akt1(−/−) mice to generate the following genotypes:Akt1(+/+); Akt2(flox/flox) (WT), Akt2(flox/flox); α-MHC-MCM (iAkt2 KO), Akt1(−/−), and Akt1(−/−); Akt2(flox/flox); α-MHC-MCM mice (Akt1(−/−)/iAkt2 KO). At 28 days after the first tamoxifen injection, Akt1(−/−)/iAkt2 KO mice developed contractile dysfunction paralleling increased atrial and brain natriuretic peptide (ANP and BNP) levels, and repressed mitochondrial gene expression. Neither cardiac fibrosis nor apoptosis were detected in Akt1(−/−)/iAkt2 KO hearts. To explore potential molecular mechanisms for contractile dysfunction, we investigated myocardial microstructure before the onset of heart failure. At 3 days after the first tamoxifen injection, Akt1(−/−)/iAkt2 KO hearts showed decreased expression of connexin43 (Cx43) and connexin-interacting protein zonula occludens-1 (ZO-1). Furthermore, Akt1/2 silencing significantly decreased both Cx43 and ZO-1 expression in cultured neonatal rat cardiomyocytes in concert with reduced beating frequency. Akt1 and Akt2 are required to maintain cardiac contraction. Loss of Akt signaling disrupts gap junction protein, which might precipitate early contractile dysfunction prior to heart failure in the absence of myocardial remodeling, such as hypertrophy, fibrosis, or cell death.
Published: 2018

38. RAGE mediated intracellular Aβ uptake contributes to the breakdown of tight junction in retinal pigment epithelium

Author: Minho Moon, Jeong Hun Kim, Sang Min Park, Kyu Hyung Park, Woo Jin Park, Sung Wook Park, Jin Hyoung Kim, and Kihwang Lee
Subjects: Gerontology, Male, Programmed cell death, Amyloid beta, MAP Kinase Signaling System, p38 mitogen-activated protein kinases, tight junction, Receptor for Advanced Glycation End Products, Retinal Pigment Epithelium, Endocytosis, RAGE (receptor), Tight Junctions, Macular Degeneration, Mice, Research Paper: Gerotarget (Focus on Aging), medicine, endocytosis, Animals, Humans, age-related macular degeneration, Cells, Cultured, Retinal pigment epithelium, Amyloid beta-Peptides, biology, Tight junction, business.industry, Gerotarget, eye diseases, Mice, Inbred C57BL, medicine.anatomical_structure, Oncology, biology.protein, Cancer research, amyloid β, sense organs, business, Intracellular, Signal Transduction
Abstract: // Sung Wook Park 1,2 , Jin Hyoung Kim 1 , Sang Min Park 3 , Minho Moon 4 , Kihwang Lee 5 , Kyu Hyung Park 6,7 , Woo Jin Park 3 and Jeong Hun Kim 1,2,6 1 Fight against Angiogenesis-Related Blindness Laboratory, Biomedical Research Institute, Seoul National University Hospital, Jongno-gu, Seoul, Korea 2 Department of Biomedical Sciences, College of Medicine, Seoul National University, Daehak-ro, Jongno-gu, Seoul, Korea 3 Department of Life Sciences, Life Sciences Concentration GIST (Gwangju Institute of Science and Technology), Cheomdan-gwagiro, Buk-gu, Gwangju, Korea 4 Department of Biochemistry, College of Medicine, Konyang University, Seo-gu, Daejeon, Korea 5 Department of Ophthalmology, Ajou University School of Medicine, Yeongtong-gu, Suwon-si, Gyeonggi-do, Korea 6 Department of Ophthalmology, College of Medicine, Seoul National University, Daehak-ro, Jongno-gu, Seoul, Korea 7 Department of Ophthalmology, Seoul National University Bundang Hospital, Gumiro, Bundang-gu, Seongnam, Gyeonggi-do, Korea Correspondence to: Jeong Hun Kim, email: // Keywords : amyloid β, age-related macular degeneration, endocytosis, tight junction, receptor for advanced glycation end products,Gerotarget Received : September 10, 2015 Accepted : September 22, 2015 Published : September 29, 2015 Abstract Intracellular amyloid beta (Aβ) has been implicated in neuronal cell death in Alzheimer’s disease (AD). Intracellular Aβ also contributes to tight junction breakdown of retinal pigment epithelium (RPE) in age-related macular degeneration (AMD). Although Aβ is predominantly secreted from neuronal cells, the mechanism of Aβ transport into RPE remains to be fully elucidated. In this study, we demonstrated that intracellular Aβ was found concomitantly with the breakdown of tight junction in RPE after subretinal injection of Aβ into the mouse eye. We also presented evidence that receptor for advanced glycation end products (RAGE) contributed to endocytosis of Aβ in RPE. siRNA-mediated knockdown of RAGE prevented intracellular Aβ accumulation as well as subsequent tight junction breakdown in RPE. In addition, we found that RAGE-mediated p38 MAPK signaling contributed to endocytosis of Aβ. Blockade of RAGE/p38 MAPK signaling inhibited Aβ endocytosis, thereby preventing tight junction breakdown in RPE. These results implicate that intracellular Aβ contributes to the breakdown of tight junction in RPE via the RAGE/p38 MAPK-mediated endocytosis. Thus, we suggest that RAGE could be a potential therapeutic target for intracellular Aβ induced outer BRB breakdown in AMD.
Published: 2015

39. Analysis of Latency Performance of Bluetooth Low Energy (BLE) Networks

Author: Wooseong Cho, Kijun Han, Keuchul Cho, Jihoon Seo, Moonki Hong, Gisu Park, and Woo-Jin Park
Subjects: Computer science, computer.internet_protocol, Distributed computing, Internet of Things, Latency (audio), lcsh:Chemical technology, Biochemistry, Article, Analytical Chemistry, law.invention, Bluetooth low energy, Bluetooth, Bluetooth 4.0, law, Wireless, lcsh:TP1-1185, Sensitivity (control systems), Electrical and Electronic Engineering, Instrumentation, Bluetooth Low Energy, business.industry, Atomic and Molecular Physics, and Optics, Range (mathematics), Embedded system, business, computer, discovery, Communication channel
Abstract: Bluetooth Low Energy (BLE) is a short-range wireless communication technology aiming at low-cost and low-power communication. The performance evaluation of classical Bluetooth device discovery have been intensively studied using analytical modeling and simulative methods, but these techniques are not applicable to BLE, since BLE has a fundamental change in the design of the discovery mechanism, including the usage of three advertising channels. Recently, there several works have analyzed the topic of BLE device discovery, but these studies are still far from thorough. It is thus necessary to develop a new, accurate model for the BLE discovery process. In particular, the wide range settings of the parameters introduce lots of potential for BLE devices to customize their discovery performance. This motivates our study of modeling the BLE discovery process and performing intensive simulation. This paper is focused on building an analytical model to investigate the discovery probability, as well as the expected discovery latency, which are then validated via extensive experiments. Our analysis considers both continuous and discontinuous scanning modes. We analyze the sensitivity of these performance metrics to parameter settings to quantitatively examine to what extent parameters influence the performance metric of the discovery processes.
Published: 2014

40. A Decoy Peptide Targeted to Protein Phosphatase 1 Attenuates Degradation of SERCA2a in Vascular Smooth Muscle Cells

Author: Ju Young Kang, Roger J. Hajjar, Sang Won Kang, Jae Gyun Oh, Woo Jin Park, Dong Hoon Kang, and Seung Pil Jang
Subjects: Male, Proteomics, 0301 basic medicine, Vascular smooth muscle, Gene Transfer, lcsh:Medicine, Synthetic Biotechnology, Stimulation, Peptide, Immunostaining, Smooth Muscle Cells, 030204 cardiovascular system & hematology, Biochemistry, Muscle, Smooth, Vascular, Rats, Sprague-Dawley, 0302 clinical medicine, Animal Cells, Protein Phosphatase 1, Calpain Inhibitors, Medicine and Health Sciences, Enzyme Inhibitors, lcsh:Science, Peptide sequence, Aorta, Staining, chemistry.chemical_classification, Multidisciplinary, biology, Calpain, Chemistry, Chemical Synthesis, Arteries, Carotid Arteries, cardiovascular system, Engineering and Technology, Synthetic Biology, Anatomy, Cellular Types, Research Article, Biotechnology, circulatory and respiratory physiology, Biosynthetic Techniques, Muscle Tissue, Research and Analysis Methods, Sarcoplasmic Reticulum Calcium-Transporting ATPases, 03 medical and health sciences, Genetics, Animals, Humans, Protease Inhibitors, Amino Acid Sequence, Synthetic Peptides, Peptide Synthesis, Cell Proliferation, Muscle Cells, Endoplasmic reticulum, Calcium-Binding Proteins, lcsh:R, Biology and Life Sciences, Protein phosphatase 1, Cell Biology, Molecular biology, Peptide Fragments, Rats, Cytosol, Biological Tissue, 030104 developmental biology, Specimen Preparation and Treatment, Proteolysis, Cardiovascular Anatomy, Enzymology, biology.protein, Blood Vessels, lcsh:Q, Peptides
Abstract: Neointimal growth in the injured vasculature is largely facilitated by the proliferation of vascular smooth muscle cells (VSMC), which associates with reduced sarco/endoplasmic reticulum Ca2+-ATPase (SERCA2a) activity. The gene transfer-mediated restoration of the SERCA2a level thus attenuates neointimal growth and VSMC proliferation. We previously reported that a peptide targeted to protein phosphatase 1, psi PLB-SE, normalizes SERCA2a activity in cardiomyocytes. In this study, we found that psi PLB-SE attenuated neointimal growth in balloon-injured rat carotid arteries, and the proliferation and migration of VSMC cultured in high-serum media (synthetic conditions). In parallel, psi PLB-SE inhibited the degradation of SERCA2a in the injured carotid arteries and VSMC under synthetic conditions. The calpain inhibitor MDL28170 also attenuated SERCA2a degradation and VSMC proliferation under synthetic conditions, indicating that calpain degrades SERCA2a. The Ca2+ ionophore A23187 induced SERCA2a degradation in VSMC, which was blocked by either psi PLB-SE or MDL28170. Additionally, psi PLB-SE normalized the cytosolic Ca2+ level in VSMC that was increased by either A23187 or synthetic stimulation. Collectively, these data indicate that psi PLB-SE corrects the abnormal Ca2+ handling by activating SERCA2a, which further protects SERCA2a from calpain-dependent degradation in VSMC. We conclude that psi PLB-SE may form the basis of a therapeutic strategy for vascular proliferative disorders.
Published: 2016

41. Cytokine-Like 1 Regulates Cardiac Fibrosis via Modulation of TGF-β Signaling

Author: Dongtak Jeong, Sacha V. Kepreotis, Jang-Soo Chun, Woo Jin Park, Jimeen Yoo, Jooyeon Kim, Seung Hee Lee, Jihwa Kim, and Roger J. Hajjar
Subjects: 0301 basic medicine, Male, CCR2, Cell signaling, Cardiac fibrosis, Endomyocardial fibrosis, Myocardial Infarction, Receptor, Transforming Growth Factor-beta Type I, lcsh:Medicine, Smad Proteins, Constriction, Pathologic, Signal transduction, Biochemistry, Monocytes, Chemokine receptor, Mice, White Blood Cells, 0302 clinical medicine, Animal Cells, Medicine and Health Sciences, Receptor, Myofibroblasts, lcsh:Science, Aorta, Coronary Arteries, Mice, Knockout, Transdifferentiation, Multidisciplinary, Chemistry, Signaling cascades, Heart, Arteries, Endomyocardial Fibrosis, Cell biology, 030220 oncology & carcinogenesis, Benzamides, Hyperexpression Techniques, Anatomy, Cellular Types, Research Article, Cell Physiology, Receptors, CCR2, Immune Cells, Immunology, Cardiology, Myocardial Reperfusion Injury, Dioxoles, Protein Serine-Threonine Kinases, Research and Analysis Methods, 03 medical and health sciences, Transforming Growth Factor beta2, Downregulation and upregulation, medicine, Gene Expression and Vector Techniques, Animals, Humans, Receptors, Cytokine, Molecular Biology Techniques, Molecular Biology, Heart Failure, Molecular Biology Assays and Analysis Techniques, Blood Cells, Biology and life sciences, lcsh:R, Proteins, Fibroblasts, medicine.disease, Disease Models, Animal, 030104 developmental biology, Gene Expression Regulation, TGF-beta signaling cascade, Cell Transdifferentiation, Cardiovascular Anatomy, Blood Vessels, lcsh:Q, Receptors, Transforming Growth Factor beta, Collagens
Abstract: Cytokine-like 1 (Cytl1) is a secreted protein that is involved in diverse biological processes. A comparative modeling study indicated that Cytl1 is structurally and functionally similar to monocyte chemoattractant protein 1 (MCP-1). As MCP-1 plays an important role in cardiac fibrosis (CF) and heart failure (HF), we investigated the role of Cytl1 in a mouse model of CF and HF. Cytl1 was upregulated in the failing mouse heart. Pressure overload-induced CF was significantly attenuated in cytl1 knock-out (KO) mice compared to that from wild-type (WT) mice. By contrast, adeno-associated virus (AAV)-mediated overexpression of cytl1 alone led to the development of CF in vivo. The endothelial-mesenchymal transition (EndMT) and the transdifferentiation of fibroblasts (FBs) to myofibroblasts (MFBs) have been suggested to contribute considerably to CF. Adenovirus-mediated overexpression of cytl1 was sufficient to induce these two critical CF-related processes in vitro, which were completely abrogated by co-treatment with SB-431542, an antagonist of TGF-β receptor 1. Cytl1 induced the expression of TGF-β2 both in vivo and in vitro. Antagonizing the receptor for MCP-1, C-C chemokine receptor type 2 (CCR2), with CAS 445479-97-0 did not block the pro-fibrotic activity of Cytl1 in vitro. Collectively, our data suggest that Cytl1 plays an essential role in CF likely through activating the TGF-β-SMAD signaling pathway. Although the receptor for Cyt1l remains to be identified, Cytl1 provides a novel platform for the development of anti-CF therapies.
Published: 2016

42. Expression of the plant viral protease NIa in the brain of a mouse model of Alzheimer's disease mitigates Aβ pathology and improves cognitive function

Author: Hannah Kim, Woo Jin Park, Daehan Choi, Hye Eun Han, Pyung Lim Han, Tae Kyung Kim, and Jung-Eun Lee
Subjects: Pathology, medicine.medical_specialty, Clinical Biochemistry, maze learning, Gene Expression, Mice, Transgenic, Plaque, Amyloid, Water maze, Disease, Biology, Biochemistry, Marble burying, Amyloid beta-Protein Precursor, Mice, Viral Proteins, Cognition, Alzheimer Disease, Memory, Scissoring, mental disorders, Consensus sequence, medicine, Avoidance Learning, Presenilin-1, Animals, Molecular Biology, Amyloid beta-Peptides, disease models, animal, Brain, amyloid β-peptides, medicine.disease, endopeptidases, Mice, Inbred C57BL, Viral protease, Molecular Medicine, Original Article, Alzheimer's disease, Cognition Disorders
Abstract: The plant viral protease, NIa, has a strict substrate specificity for the consensus sequence of Val-Xaa-His-Gln, with a scissoring property after Gln. We recently reported that NIa efficiently cleaved the amyloid-β (Aβ) peptide, which contains the sequence Val-His-His-Gln in the vicinity of the cleavage site by α-secretase, and that the expression of NIa using a lentiviral system in the brain of AD mouse model reduced plaque deposition levels. In the present study, we investigated whether exogenous expression of NIa in the brain of AD mouse model is beneficial to the improvement of cognitive deficits. To address this question, Lenti-NIa was intracerebrally injected into the brain of Tg-APPswe/ PS1dE9 (Tg-APP/PS1) mice at 7 months of age and behavioral tests were performed 15-30 days afterwards. The results of the water maze test indicated that Tg-APP/PS1 mice which had been injected with Lenti-GFP showed an increased latency in finding the hidden-platform and markedly enhanced navigation near the maze-wall, and that such behavioral deficits were significantly reversed in Tg-APP/PS1 mice injected with Lenti-NIa. In the passive avoidance test, Tg-APP/PS1 mice exhibited a severe deficit in their contextual memory retention, which was reversed by NIa expression. In the marble burying test, Tg-APP/PS1 mice buried marbles fewer than non-transgenic mice, which was also significantly improved by NIa. After behavioral tests, it was verified that the Tg-APP/PS1 mice with Lenti-NIa injection had reduced Aβ levels and plaque deposition when compared to Tg-APP/PS1 mice. These results showed that the plant viral protease, NIa, not only reduces Aβ pathology, but also improves behavioral deficits.
Published: 2012

43. Cucurbitacin I Attenuates Cardiomyocyte Hypertrophy via Inhibition of Connective Tissue Growth Factor (CCN2) and TGF- β/Smads Signalings

Author: Kye Won Park, Hara Kang, Shang-Jin Kim, Seung Yul Yang, Dong Kwon Yang, Woo Jin Park, and Moon Hee Jeong
Subjects: MAPK/ERK pathway, Cell signaling, medicine.medical_specialty, Cardiotonic Agents, Cell Survival, medicine.medical_treatment, Science, Primary Cell Culture, Smad Proteins, SMAD, Biology, Pharmacology, Rats, Sprague-Dawley, Transforming Growth Factor beta1, Ventricular Myosins, Phenylephrine, Downregulation and upregulation, Fibrosis, Internal medicine, medicine, Animals, Myocytes, Cardiac, RNA, Small Interfering, Multidisciplinary, Growth factor, Connective Tissue Growth Factor, medicine.disease, Triterpenes, Rats, CTGF, Endocrinology, Animals, Newborn, Gene Expression Regulation, Medicine, Mitogen-Activated Protein Kinases, Atrial Natriuretic Factor, Transforming growth factor, Research Article, Signal Transduction
Abstract: Cucurbitacin I is a naturally occurring triterpenoid derived from Cucurbitaceae family plants that exhibits a number of potentially useful pharmacological and biological activities. However, the therapeutic impact of cucurbitacin I on the heart has not heretofore been reported. To evaluate the functional role of cucurbitacin I in an in vitro model of cardiac hypertrophy, phenylephrine (PE)-stimulated cardiomyocytes were treated with a sub-cytotoxic concentration of the compound, and the effects on cell size and mRNA expression levels of ANF and beta-MHC were investigated. Consequently, PE-induced cell enlargement and upregulation of ANF and beta-MHC were significantly suppressed by pretreatment of the cardiomyocytes with cucurbitacin I. Notably, cucurbitacin I also impaired connective tissue growth factor (CTGF) and MAPK signaling, pro-hypertrophic factors, as well as TGF-beta/Smad signaling, the important contributing factors to fibrosis. The protective impact of cucurbitacin I was significantly blunted in CTGF-silenced or TGF-beta 1-silenced hypertrophic cardiomyocytes, indicating that the compound exerts its beneficial actions through CTGF. Taken together, these findings signify that cucurbitacin I protects the heart against cardiac hypertrophy via inhibition of CTGF/MAPK, and TGF-beta/Smad-facilitated events. Accordingly, the present study provides new insights into the defensive capacity of cucurbitacin I against cardiac hypertrophy, and further suggesting cucurbitacin I's utility as a novel therapeutic agent for the management of heart diseases.
Published: 2015

44. Long-range angular correlations on the near and away side in p–Pb collisions at root s(NN)= 5.02 TeV

Author: Betty Abelev, Jaroslav Adam, Dagmar Adamova, Andrew Marshall Adare, Madan Aggarwal, Gianluca Aglieri Rinella, Michelangelo Agnello, Andras Gabor Agocs, Zubayer Ahammed, Nazeer Ahmad, Arshad Ahmad, Sul Ah Ahn, Sang Un Ahn, Muhammad Ajaz, Alexander Akindinov, Dmitry Aleksandrov, Bruno Alessandro, Andrea Alici, Anton Alkin, Erick Jonathan Almaraz Avina, Johan Alme, Torsten Alt, Valerio Altini, Sedat Altinpinar, Igor Altsybeev, Cristian Andrei, Anton Andronic, Venelin Anguelov, Jonas Anielski, Christopher Daniel Anson, Tome Anticic, Federico Antinori, Pietro Antonioli, Laurent Bernard Aphecetche, Harald Appelshauser, Nicolas Arbor, Andreas Arend, Nestor Armesto, Roberta Arnaldi, Tomas Robert Aronsson, Ionut Cristian Arsene, Mesut Arslandok, Andzhey Asryan, Andre Augustinus, Ralf Peter Averbeck, Terry Awes, Juha Heikki Aysto, Mohd Danish Azmi, Matthias Jakob Bach, Angela Badala, Yong Wook Baek, Raphaelle Marie Bailhache, Renu Bala, Rinaldo Baldini Ferroli, Alberto Baldisseri, Fernando Baltasar Dos Santos Pedrosa, Jaroslav Ban, Rama Chandra Baral, Roberto Barbera, Francesco Barile, Gergely Gabor Barnafoldi, Lee Stuart Barnby, Valerie Barret, Jerzy Gustaw Bartke, Nicole Bastid, Sumit Basu, Bastian Bathen, Guillaume Batigne, Boris Batyunya, Christoph Heinrich Baumann, Ian Gardner Bearden, Hans Beck, Nirbhay Kumar Behera, Iouri Belikov, Rene Bellwied, Ernesto Belmont Moreno, Gyula Bencedi, Stefania Beole, Ionela Berceanu, Alexandru Bercuci, Yaroslav Berdnikov, Daniel Berenyi, Anais Annick Erica Bergognon, Dario Berzano, Latchezar Betev, Anju Bhasin, Ashok Kumar Bhati, Jihyun Bhom, Livio Bianchi, Nicola Bianchi, Jaroslav Bielcik, Jana Bielcikova, Ante Bilandzic, Sandro Bjelogrlic, Francesco Blanco, F. Blanco, Dmitry Blau, Christoph Blume, Marco Boccioli, Stefan Boettger, Alexey Bogdanov, Hans Boggild, Mikhail Bogolyubsky, Laszlo Boldizsar, Marek Bombara, Julian Book, Herve Borel, Alexander Borissov, Francesco Bossu, Michiel Botje, Elena Botta, Ermes Braidot, Peter Braun Munzinger, Marco Bregant, Timo Gunther Breitner, Theo Alexander Broker, Tyler Allen Browning, Michal Broz, Rene Brun, Elena Bruna, Giuseppe Eugenio Bruno, Dmitry Budnikov, Henner Buesching, Stefania Bufalino, Predrag Buncic, Oliver Busch, Edith Zinhle Buthelezi, Diego Caballero Orduna, Davide Caffarri, Xu Cai, Helen Louise Caines, Ernesto Calvo Villar, Paolo Camerini, Veronica Canoa Roman, Giovanni Cara Romeo, Wisla Carena, Francesco Carena, Nelson Carlin Filho, Federico Carminati, Amaya Ofelia Casanova Diaz, Javier Ernesto Castillo Castellanos, Juan Francisco Castillo Hernandez, Ester Anna Rita Casula, Vasile Catanescu, Costanza Cavicchioli, Cesar Ceballos Sanchez, Jan Cepila, Piergiaio Cerello, Beomsu Chang, Sylvain Chapeland, Jean Luc Fernand Charvet, Sukalyan Chattopadhyay, Subhasis Chattopadhyay, Isha Chawla, Michael Gerard Cherney, Cvetan Cheshkov, Brigitte Cheynis, Vasco Miguel Chibante Barroso, David Chinellato, Peter Chochula, Marek Chojnacki, Subikash Choudhury, Panagiotis Christakoglou, Christian Holm Christensen, Peter Christiansen, Tatsuya Chujo, Suh Urk Chung, Corrado Cicalo, Federico Cindolo, Jean Willy Andre Cleymans, Fabrizio Coccetti, Fabio Colamaria, Domenico Colella, Alberto Collu, Gustavo Conesa Balbastre, Zaida Conesa del Valle, Megan Elizabeth Connors, Giacomo Contin, Jesus Guillermo Contreras, Thomas Michael Cormier, Yasser Corrales Morales, Pietro Cortese, Ismael Cortes Maldonado, Mauro Rogerio Cosentino, Filippo Costa, Manuel Enrique Cotallo, Elisabetta Crescio, Philippe Crochet, Emilia Cruz Alaniz, Rigoberto Cruz Albino, Eleazar Cuautle, Leticia Cunqueiro, Andrea Dainese, Hans Hjersing Dalsgaard, Andrea Danu, Indranil Das, Debasish Das, Supriya Das, Kushal Das, Ajay Kumar Dash, Sadhana Dash, Sudipan De, Gabriel de Barros, Annalisa De Caro, Giacinto de Cataldo, Jan de Cuveland, Alessandro De Falco, Daniele De Gruttola, Hugues Delagrange, Andrzej Deloff, Nora De Marco, Ervin Denes, Salvatore De Pasquale, Airton Deppman, Ginevra DʼErasmo, Raoul Stefan de Rooij, Miguel Angel Diaz Corchero, Domenico Di Bari, Thomas Dietel, Carmelo Di Giglio, Sergio Di Liberto, Antonio Di Mauro, Pasquale Di Nezza, Roberto Divia, Oeystein Djuvsland, Alexandru Florin Dobrin, Tadeusz Antoni Dobrowolski, Benjamin Donigus, Olja Dordic, Olga Driga, Anand Kumar Dubey, Andrea Dubla, Laurent Ducroux, Pascal Dupieux, A. K. Dutta Majumdar, Domenico Elia, David Philip Emschermann, Heiko Engel, Barbara Erazmus, Hege Austrheim Erdal, Bruno Espagnon, Magali Danielle Estienne, Shinichi Esumi, David Evans, Gyulnara Eyyubova, Daniela Fabris, Julien Faivre, Alessandra Fantoni, Markus Fasel, Roger Worsley Fearick, Dominik Fehlker, Linus Feldkamp, Daniel Felea, Alessandro Feliciello, Bo Fenton Olsen, Grigory Feofilov, Arturo Fernandez Tellez, Alessandro Ferretti, Andrea Festanti, Jan Figiel, Marcel Figueredo, Sergey Filchagin, Dmitry Finogeev, Fiorella Fionda, Enrichetta Maria Fiore, Emmanuel Floratos, Michele Floris, Siegfried Valentin Foertsch, Panagiota Foka, Sergey Fokin, Enrico Fragiacomo, Andrea Francescon, Ulrich Michael Frankenfeld, Ulrich Fuchs, Christophe Furget, Mario Fusco Girard, Jens Joergen Gaardhoje, Martino Gagliardi, Alberto Gago, Mauro Gallio, Dhevan Raja Gangadharan, Paraskevi Ganoti, Jose Garabatos, Edmundo Garcia Solis, Irakli Garishvili, Jochen Gerhard, Marie Germain, Claudio Geuna, Mihaela Gheata, Andrei Geae Gheata, Bruno Ghidini, Premomoy Ghosh, Paola Gianotti, Martin Robert Girard, Paolo Giubellino, Ewa Gladysz Dziadus, Peter Glassel, Ramon Gomez, Elena Gonzalez Ferreiro, Laura Helena Gonzalez Trueba, Pedro Gonzalez Zamora, Sergey Gorbunov, Ankita Goswami, Sven Gotovac, Lukasz Kamil Graczykowski, Robert Grajcarek, Alessandro Grelli, Costin Grigoras, Alina Gabriela Grigoras, Vladislav Grigoriev, Ara Grigoryan, Smbat Grigoryan, Boris Grinyov, Nevio Grion, Philippe Gros, Jan Fiete Grosse Oetringhaus, Jean Yves Grossiord, Raffaele Grosso, Fedor Guber, Rachid Guernane, Maxime Rene Joseph Guilbaud, Kristjan Herlache Gulbrandsen, Hrant Gulkanyan, Taku Gunji, Anik Gupta, Ramni Gupta, Rudiger Haake, Oystein Senneset Haaland, Cynthia Marie Hadjidakis, Maria Haiduc, Hideki Hamagaki, Gergoe Hamar, Byounghee Han, Luke David Hanratty, Alexander Hansen, Zuzana Harmanova, John William Harris, Matthias Hartig, Austin Harton, Despoina Hatzifotiadou, Shinichi Hayashi, Arsen Hayrapetyan, Stefan Thomas Heckel, Markus Ansgar Heide, Haavard Helstrup, Andrei Ionut Herghelegiu, Gerardo Antonio Herrera Corral, Norbert Herrmann, Benjamin Andreas Hess, Kristin Fanebust Hetland, Bernard Hicks, Boris Hippolyte, Yasuto Hori, Peter Zahariev Hristov, Ivana Hrivnacova, Meidana Huang, Thomas Humanic, Dae Sung Hwang, Raphaelle Ichou, Radiy Ilkaev, Iryna Ilkiv, Motoi Inaba, Elisa Incani, Pier Giaio Innocenti, Gian Michele Innocenti, Mikhail Ippolitov, Muhammad Irfan, Cristian Geae Ivan, Vladimir Ivanov, Andrey Ivanov, Marian Ivanov, Oleksii Ivanytskyi, Adam Wlodzimierz Jacholkowski, Peter Jacobs, Haeng Jin Jang, Malgorzata Anna Janik, Rudolf Janik, Sandun Jayarathna, Satyajit Jena, Deeptanshu Manu Jha, Raul Tonatiuh Jimenez Bustamante, Peter Graham Jones, Hyung Taik Jung, Anton Jusko, Alexei Kaidalov, Sebastian Kalcher, Peter Kalinak, Tuomo Esa Aukusti Kalliokoski, Alexander Philipp Kalweit, Ju Hwan Kang, Vladimir Kaplin, Ayben Karasu Uysal, Oleg Karavichev, Tatiana Karavicheva, Evgeny Karpechev, Andrey Kazantsev, Udo Wolfgang Kebschull, Ralf Keidel, Palash Khan, Shuaib Ahmad Khan, Mohisin Mohammed Khan, Kamal Hussain Khan, Alexei Khanzadeev, Yury Kharlov, Bjarte Kileng, Beomkyu Kim, Jin Sook Kim, Jonghyun Kim, Dong Jo Kim, Do Won Kim, Taesoo Kim, Se Yong Kim, Mimae Kim, Minwoo Kim, Stefan Kirsch, Ivan Kisel, Sergey Kiselev, Adam Ryszard Kisiel, Jennifer Lynn Klay, Jochen Klein, Christian Klein Bosing, Michael Kliemant, Alexander Kluge, Michael Linus Knichel, Anders Garritt Knospe, Markus Kohler, Thorsten Kollegger, Anatoly Kolojvari, Mikhail Kompaniets, Valery Kondratiev, Natalia Kondratyeva, Artem Konevskih, Vladimir Kovalenko, Marek Kowalski, Serge Kox, Greeshma Koyithatta Meethaleveedu, Jiri Kral, Ivan Kralik, Frederick Kramer, Adela Kravcakova, Tobias Krawutschke, Michal Krelina, Matthias Kretz, Marian Krivda, Filip Krizek, Miroslav Krus, Evgeny Kryshen, Mikolaj Krzewicki, Yury Kucheriaev, Thanushan Kugathasan, Christian Claude Kuhn, Paul Kuijer, Igor Kulakov, Jitendra Kumar, Podist Kurashvili, A. Kurepin, A. B. 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Yaldo, Yorito Yamaguchi, Hongyan Yang, Shiming Yang, Stanislav Yasnopolsky, JunGyu Yi, Zhongbao Yin, In Kwon Yoo, Jongik Yoon, Weilin Yu, Xianbao Yuan, Igor Yushmanov, Valentina Zaccolo, Cenek Zach, Chiara Zampolli, Sergey Zaporozhets, Andrey Zarochentsev, Petr Zavada, Nikolai Zaviyalov, Hanna Paulina Zbroszczyk, Pierre Zelnicek, Sorin Ion Zgura, Mikhail Zhalov, Haitao Zhang, Xiaoming Zhang, Fengchu Zhou, You Zhou, Daicui Zhou, Hongsheng Zhu, Jianhui Zhu, Jianlin Zhu, Xiangrong Zhu, Antonino Zichichi, Alice Zimmermann, Gennady Zinovjev, Yannick Denis Zoccarato, Mykhaylo Zynovyev, Maksym Zyzak, AGOSTINELLI, ANDREA, ARCELLI, SILVIA, BASILE, MAURIZIO, BELLINI, FRANCESCA, CIFARELLI, LUISA, FALCHIERI, DAVIDE, GUERZONI, BARBARA, SCIOLI, GILDA, Betty Abelev, Jaroslav Adam, Dagmar Adamova, Andrew Marshall Adare, Madan Aggarwal, Gianluca Aglieri Rinella, Michelangelo Agnello, Andras Gabor Agoc, Andrea Agostinelli, Zubayer Ahammed, Nazeer Ahmad, Arshad Ahmad, Sul-Ah Ahn, Sang Un Ahn, Muhammad Ajaz, Alexander Akindinov, Dmitry Aleksandrov, Bruno Alessandro, Andrea Alici, Anton Alkin, Erick Jonathan Almaraz Avina, Johan Alme, Torsten Alt, Valerio Altini, Sedat Altinpinar, Igor Altsybeev, Cristian Andrei, Anton Andronic, Venelin Anguelov, Jonas Anielski, Christopher Daniel Anson, Tome Anticic, Federico Antinori, Pietro Antonioli, Laurent Bernard Aphecetche, Harald Appelshauser, Nicolas Arbor, Silvia Arcelli, Andreas Arend, Nestor Armesto, Roberta Arnaldi, Tomas Robert Aronsson, Ionut Cristian Arsene, Mesut Arslandok, Andzhey Asryan, Andre Augustinu, Ralf Peter Averbeck, Terry Awe, Juha Heikki Aysto, Mohd Danish Azmi, Matthias Jakob Bach, Angela Badala, Yong Wook Baek, Raphaelle Marie Bailhache, Renu Bala, Rinaldo Baldini Ferroli, Alberto Baldisseri, Fernando Baltasar Dos Santos Pedrosa, Jaroslav Ban, Rama Chandra Baral, Roberto Barbera, Francesco Barile, Gergely Gabor Barnafoldi, Lee Stuart Barnby, Valerie Barret, Jerzy Gustaw Bartke, Maurizio Basile, Nicole Bastid, Sumit Basu, Bastian Bathen, Guillaume Batigne, Boris Batyunya, Christoph Heinrich Baumann, Ian Gardner Bearden, Hans Beck, Nirbhay Kumar Behera, Iouri Belikov, Francesca Bellini, Rene Bellwied, Ernesto Belmont-Moreno, Gyula Bencedi, Stefania Beole, Ionela Berceanu, Alexandru Bercuci, Yaroslav Berdnikov, Daniel Berenyi, Anais Annick Erica Bergognon, Dario Berzano, Latchezar Betev, Anju Bhasin, Ashok Kumar Bhati, Jihyun Bhom, Livio Bianchi, Nicola Bianchi, Jaroslav Bielcik, Jana Bielcikova, Ante Bilandzic, Sandro Bjelogrlic, Francesco Blanco, F. Blanco, Dmitry Blau, Christoph Blume, Marco Boccioli, Stefan Boettger, Alexey Bogdanov, Hans Boggild, Mikhail Bogolyubsky, Laszlo Boldizsar, Marek Bombara, Julian Book, Herve Borel, Alexander Borissov, Francesco Bossu, Michiel Botje, Elena Botta, Ermes Braidot, Peter Braun-Munzinger, Marco Bregant, Timo Gunther Breitner, Theo Alexander Broker, Tyler Allen Browning, Michal Broz, Rene Brun, Elena Bruna, Giuseppe Eugenio Bruno, Dmitry Budnikov, Henner Buesching, Stefania Bufalino, Predrag Buncic, Oliver Busch, Edith Zinhle Buthelezi, Diego Caballero Orduna, Davide Caffarri, Xu Cai, Helen Louise Caine, Ernesto Calvo Villar, Paolo Camerini, Veronica Canoa Roman, Giovanni Cara Romeo, Wisla Carena, Francesco Carena, Nelson Carlin Filho, Federico Carminati, Amaya Ofelia Casanova Diaz, Javier Ernesto Castillo Castellano, Juan Francisco Castillo Hernandez, Ester Anna Rita Casula, Vasile Catanescu, Costanza Cavicchioli, Cesar Ceballos Sanchez, Jan Cepila, Piergiaio Cerello, Beomsu Chang, Sylvain Chapeland, Jean-Luc Fernand Charvet, Sukalyan Chattopadhyay, Subhasis Chattopadhyay, Isha Chawla, Michael Gerard Cherney, Cvetan Cheshkov, Brigitte Cheyni, Vasco Miguel Chibante Barroso, David Chinellato, Peter Chochula, Marek Chojnacki, Subikash Choudhury, Panagiotis Christakoglou, Christian Holm Christensen, Peter Christiansen, Tatsuya Chujo, Suh-Urk Chung, Corrado Cicalo, Luisa Cifarelli, Federico Cindolo, Jean Willy Andre Cleyman, Fabrizio Coccetti, Fabio Colamaria, Domenico Colella, Alberto Collu, Gustavo Conesa Balbastre, Zaida Conesa del Valle, Megan Elizabeth Connor, Giacomo Contin, Jesus Guillermo Contrera, Thomas Michael Cormier, Yasser Corrales Morale, Pietro Cortese, Ismael Cortes Maldonado, Mauro Rogerio Cosentino, Filippo Costa, Manuel Enrique Cotallo, Elisabetta Crescio, Philippe Crochet, Emilia Cruz Alaniz, Rigoberto Cruz Albino, Eleazar Cuautle, Leticia Cunqueiro, Andrea Dainese, Hans Hjersing Dalsgaard, Andrea Danu, Indranil Da, Debasish Da, Supriya Da, Kushal Da, Ajay Kumar Dash, Sadhana Dash, Sudipan De, Gabriel de Barro, Annalisa De Caro, Giacinto de Cataldo, Jan de Cuveland, Alessandro De Falco, Daniele De Gruttola, Hugues Delagrange, Andrzej Deloff, Nora De Marco, Ervin Dene, Salvatore De Pasquale, Airton Deppman, Ginevra DʼErasmo, Raoul Stefan de Rooij, Miguel Angel Diaz Corchero, Domenico Di Bari, Thomas Dietel, Carmelo Di Giglio, Sergio Di Liberto, Antonio Di Mauro, Pasquale Di Nezza, Roberto Divia, Oeystein Djuvsland, Alexandru Florin Dobrin, Tadeusz Antoni Dobrowolski, Benjamin Donigu, Olja Dordic, Olga Driga, Anand Kumar Dubey, Andrea Dubla, Laurent Ducroux, Pascal Dupieux, A.K. Dutta Majumdar, Domenico Elia, David Philip Emschermann, Heiko Engel, Barbara Erazmu, Hege Austrheim Erdal, Bruno Espagnon, Magali Danielle Estienne, Shinichi Esumi, David Evan, Gyulnara Eyyubova, Daniela Fabri, Julien Faivre, Davide Falchieri, Alessandra Fantoni, Markus Fasel, Roger Worsley Fearick, Dominik Fehlker, Linus Feldkamp, Daniel Felea, Alessandro Feliciello, Bo Fenton-Olsen, Grigory Feofilov, Arturo Fernandez Tellez, Alessandro Ferretti, Andrea Festanti, Jan Figiel, Marcel Figueredo, Sergey Filchagin, Dmitry Finogeev, Fiorella Fionda, Enrichetta Maria Fiore, Emmanuel Florato, Michele Flori, Siegfried Valentin Foertsch, Panagiota Foka, Sergey Fokin, Enrico Fragiacomo, Andrea Francescon, Ulrich Michael Frankenfeld, Ulrich Fuch, Christophe Furget, Mario Fusco Girard, Jens Joergen Gaardhoje, Martino Gagliardi, Alberto Gago, Mauro Gallio, Dhevan Raja Gangadharan, Paraskevi Ganoti, Jose Garabato, Edmundo Garcia-Soli, Irakli Garishvili, Jochen Gerhard, Marie Germain, Claudio Geuna, Mihaela Gheata, Andrei Geae Gheata, Bruno Ghidini, Premomoy Ghosh, Paola Gianotti, Martin Robert Girard, Paolo Giubellino, Ewa Gladysz-Dziadu, Peter Glassel, Ramon Gomez, Elena Gonzalez Ferreiro, Laura Helena Gonzalez-Trueba, Pedro Gonzalez-Zamora, Sergey Gorbunov, Ankita Goswami, Sven Gotovac, Lukasz Kamil Graczykowski, Robert Grajcarek, Alessandro Grelli, Costin Grigora, Alina Gabriela Grigora, Vladislav Grigoriev, Ara Grigoryan, Smbat Grigoryan, Boris Grinyov, Nevio Grion, Philippe Gro, Jan Fiete Grosse-Oetringhau, Jean-Yves Grossiord, Raffaele Grosso, Fedor Guber, Rachid Guernane, Barbara Guerzoni, Maxime Rene Joseph Guilbaud, Kristjan Herlache Gulbrandsen, Hrant Gulkanyan, Taku Gunji, Anik Gupta, Ramni Gupta, Rudiger Haake, Oystein Senneset Haaland, Cynthia Marie Hadjidaki, Maria Haiduc, Hideki Hamagaki, Gergoe Hamar, Byounghee Han, Luke David Hanratty, Alexander Hansen, Zuzana Harmanova, John William Harri, Matthias Hartig, Austin Harton, Despoina Hatzifotiadou, Shinichi Hayashi, Arsen Hayrapetyan, Stefan Thomas Heckel, Markus Ansgar Heide, Haavard Helstrup, Andrei Ionut Herghelegiu, Gerardo Antonio Herrera Corral, Norbert Herrmann, Benjamin Andreas He, Kristin Fanebust Hetland, Bernard Hick, Boris Hippolyte, Yasuto Hori, Peter Zahariev Hristov, Ivana Hrivnacova, Meidana Huang, Thomas Humanic, Dae Sung Hwang, Raphaelle Ichou, Radiy Ilkaev, Iryna Ilkiv, Motoi Inaba, Elisa Incani, Pier Giaio Innocenti, Gian Michele Innocenti, Mikhail Ippolitov, Muhammad Irfan, Cristian Geae Ivan, Vladimir Ivanov, Andrey Ivanov, Marian Ivanov, Oleksii Ivanytskyi, Adam Wlodzimierz Jacholkowski, Peter Jacob, Haeng Jin Jang, Malgorzata Anna Janik, Rudolf Janik, Sandun Jayarathna, Satyajit Jena, Deeptanshu Manu Jha, Raul Tonatiuh Jimenez Bustamante, Peter Graham Jone, Hyung Taik Jung, Anton Jusko, Alexei Kaidalov, Sebastian Kalcher, Peter Kalinak, Tuomo Esa Aukusti Kalliokoski, Alexander Philipp Kalweit, Ju Hwan Kang, Vladimir Kaplin, Ayben Karasu Uysal, Oleg Karavichev, Tatiana Karavicheva, Evgeny Karpechev, Andrey Kazantsev, Udo Wolfgang Kebschull, Ralf Keidel, Palash Khan, Shuaib Ahmad Khan, Mohisin Mohammed Khan, Kamal Hussain Khan, Alexei Khanzadeev, Yury Kharlov, Bjarte Kileng, Beomkyu Kim, Jin Sook Kim, Jonghyun Kim, Dong Jo Kim, Do Won Kim, Taesoo Kim, Se Yong Kim, Mimae Kim, Minwoo Kim, Stefan Kirsch, Ivan Kisel, Sergey Kiselev, Adam Ryszard Kisiel, Jennifer Lynn Klay, Jochen Klein, Christian Klein-Bosing, Michael Kliemant, Alexander Kluge, Michael Linus Knichel, Anders Garritt Knospe, Markus Kohler, Thorsten Kollegger, Anatoly Kolojvari, Mikhail Kompaniet, Valery Kondratiev, Natalia Kondratyeva, Artem Konevskih, Vladimir Kovalenko, Marek Kowalski, Serge Kox, Greeshma Koyithatta Meethaleveedu, Jiri Kral, Ivan Kralik, Frederick Kramer, Adela Kravcakova, Tobias Krawutschke, Michal Krelina, Matthias Kretz, Marian Krivda, Filip Krizek, Miroslav Kru, Evgeny Kryshen, Mikolaj Krzewicki, Yury Kucheriaev, Thanushan Kugathasan, Christian Claude Kuhn, Paul Kuijer, Igor Kulakov, Jitendra Kumar, Podist Kurashvili, A. Kurepin, A.B. Kurepin, Alexey Kuryakin, Svetlana Kushpil, Vasily Kushpil, Henning Kvaerno, Min Jung Kweon, Youngil Kwon, Pedro Ladron de Guevara, Igor Lakomov, Rune Langoy, Sarah Louise La Pointe, Camilo Ernesto Lara, Antoine Xavier Lardeux, Paola La Rocca, Ramona Lea, Mateusz Lechman, Ki Sang Lee, Sung Chul Lee, Graham Richard Lee, Iosif Legrand, Joerg Walter Lehnert, Matthieu Laurent Lenhardt, Vito Lenti, Hermes Leon, Ildefonso Leon Monzon, Hermes Leon Varga, Peter Levai, Shuang Li, Jaen Lien, Roman Lietava, Svein Lindal, Volker Lindenstruth, Christian Lippmann, Michael Annan Lisa, Hans Martin Ljunggren, Per-Ivar Loenne, Vera Loggin, Vitaly Loginov, Daniel Lohner, Constantinos Loizide, Kai Krister Loo, Xavier Bernard Lopez, Ernesto Lopez Torre, Gunnar Lovhoiden, Xianguo Lu, Philipp Luettig, Marcello Lunardon, Jiebin Luo, Grazia Luparello, Cinzia Luzzi, Rongrong Ma, Ke Ma, Dilan Minthaka Madagodahettige-Don, Alla Maevskaya, Magnus Mager, Durga Prasad Mahapatra, Antonin Maire, Mikhail Malaev, Ivonne Alicia Maldonado Cervante, Ludmila Malinina, Dmitry MalʼKevich, Peter Malzacher, Alexander Mamonov, Loic Henri Antoine Manceau, Lalit Kumar Mangotra, Vladislav Manko, Franck Manso, Vito Manzari, Yaxian Mao, Massimiliano Marchisone, Jiri Mare, Giacomo Vito Margagliotti, Anselmo Margotti, Ana Maria Marin, Christina Markert, Marco Marquard, Irakli Martashvili, Nicole Alice Martin, Paolo Martinengo, Mario Ivan Martinez, Arnulfo Martinez Davalo, Gines Martinez Garcia, Yevgen Martynov, Alexis Jean-Michel Ma, Silvia Masciocchi, Massimo Masera, Alberto Masoni, Laure Marie Massacrier, Annalisa Mastroserio, Adam Tomasz Matyja, Christoph Mayer, Joel Mazer, Alessandra Maria Mazzoni, Franco Meddi, Arturo Alejandro Menchaca-Rocha, Jae Mercado Perez, Michal Mere, Yasuo Miake, Leonardo Milano, Jovan Milosevic, Andre Mischke, Aditya Nath Mishra, Dariusz Miskowiec, Ciprian Mihai Mitu, Sanshiro Mizuno, Jocelyn Mlynarz, Bedangadas Mohanty, Levente Molnar, Luis Manuel Montano Zetina, Marco Monteno, Esther 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Yvonne Chiara Pachmayer, Milos Pachr, Fatima Padilla, Paola Pagano, Guy Paic, Florian Painke, Carlos Pajare, Susanta Kumar Pal, Arvinder Singh Palaha, Armando Palmeri, Vardanush Papikyan, Giuseppe Pappalardo, Woo Jin Park, Annika Passfeld, Blahoslav Pastircak, Dmitri Ivanovich Patalakha, Vincenzo Paticchio, Biswarup Paul, Alexei Pavlinov, Tomasz Jan Pawlak, Thomas Peitzmann, Hugo Denis Antonio Pereira Da Costa, Elienos Pereira De Oliveira Filho, Dmitri Peresunko, Carlos Eugenio Perez Lara, Diego Perini, Davide Perrino, Wiktor Stanislaw Peryt, Alessandro Pesci, Vladimir Peskov, Yury Pestov, Vojtech Petracek, Michal Petran, Mariana Petri, Plamen Rumenov Petrov, Mihai Petrovici, Catia Petta, Stefano Piano, Miroslav Pikna, Philippe Pillot, Ombretta Pinazza, Lawrence Pinsky, Nora Pitz, Danthasinghe Piyarathna, Mirko Planinic, Mateusz Andrzej Ploskon, Jan Marian Pluta, Timur Pocheptsov, Sona Pochybova, Pedro Luis Manuel Podesta Lerma, Martin Poghosyan, Karel Polak, Boris Polichtchouk, Amalia Pop, Sarah Porteboeuf-Houssai, Vladimir Pospisil, Baba Potukuchi, Sidharth Kumar Prasad, Roberto Preghenella, Francesco Prino, Claude Andre Pruneau, Igor Pshenichnov, Giovanna Puddu, Valery Punin, Marian Puti, Jorn Henning Putschke, Emanuele Quercigh, Henrik Qvigstad, Alexandre Rachevski, Alphonse Rademaker, Tomi Samuli Raiha, Jan Rak, Andry Malala Rakotozafindrabe, Luciano Ramello, Abdiel Ramirez Reye, Rashmi Raniwala, Sudhir Raniwala, Sami Sakari Rasanen, Bogdan Theodor Rascanu, Deepika Rathee, Kenneth Francis Read, Jean-Sebastien Real, Krzysztof Redlich, Rosi Jan Reed, Attiq Ur Rehman, Patrick Reichelt, Martijn Reicher, Rainer Arno Ernst Renfordt, Anna Rita Reolon, Andrey Reshetin, Felix Vincenz Rettig, Jean-Pierre Revol, Klaus Johannes Reyger, Lodovico Riccati, Renato Angelo Ricci, Tuva Richert, Matthias Rudolph Richter, Petra Riedler, Werner Riegler, Francesco Riggi, Mario Rodriguez Cahuantzi, Alis Rodriguez Manso, Ketil Roed, David Rohr, Dieter Rohrich, Rosa Romita, Federico Ronchetti, Philippe Rosnet, Stefan Rossegger, Andrea Rossi, Christelle Sophie Roy, Pradip Kumar Roy, Antonio Juan Rubio Montero, Rinaldo Rui, Riccardo Russo, Evgeny Ryabinkin, Andrzej Rybicki, Sergey Sadovsky, Karel Safarik, Raghunath Sahoo, Pradip Kumar Sahu, Jogender Saini, Hiroaki Sakaguchi, Shingo Sakai, Dosatsu Sakata, Carlos Albert Salgado, Jai Salzwedel, Sanjeev Singh Sambyal, Vladimir Samsonov, Xitzel Sanchez Castro, Ladislav Sandor, Andres Sandoval, Masato Sano, Gianluca Santagati, Romualdo Santoro, Juho Jaako Sarkamo, Eugenio Scapparone, Fernando Scarlassara, Rolf Paul Scharenberg, Claudiu Cornel Schiaua, Rainer Martin Schicker, Christian Joachim Schmidt, Hans Rudolf Schmidt, Simone Schuchmann, Jurgen Schukraft, Tim Schuster, Yves Roland Schutz, Kilian Eberhard Schwarz, Kai Oliver Schweda, Gilda Scioli, Enrico Scomparin, Patrick Aaron Scott, Rebecca Scott, Gianfranco Segato, Ilya Selyuzhenkov, Serhiy Senyukov, Jeewon Seo, Sergio Serci, Eulogio Serradilla, Adrian Sevcenco, Alexandre Shabetai, Galina Shabratova, Ruben Shahoyan, Natasha Sharma, Satish Sharma, Rohini Sharma, Kenta Shigaki, Katherin Shtejer, Yury Sibiriak, Eva Sicking, Sabyasachi Siddhanta, Teodor Siemiarczuk, David Olle Rickard Silvermyr, Catherine Silvestre, Goran Simatovic, Giuseppe Simonetti, Rama Narayana Singaraju, Ranbir Singh, Subhash Singha, Vikas Singhal, Bikash Sinha, Tinku Sinha, Branislav Sitar, Mario Sitta, Bernhard Skaali, Kyrre Skjerdal, Radek Smakal, Nikolai Smirnov, Raimond Snelling, Carsten Sogaard, Ron Ariel Soltz, Hyungsuk Son, Jihye Song, Myunggeun Song, Csaba Soo, Francesca Soramel, Iwona Sputowska, Martha Spyropoulou-Stassinaki, Brijesh Kumar Srivastava, Johanna Stachel, Ionel Stan, Grzegorz Stefanek, Matthew Steinprei, Evert Anders Stenlund, Gideon Francois Steyn, Johannes Hendrik Stiller, Diego Stocco, Mikhail Stolpovskiy, Peter Strmen, Alexandre Alarcon do Passo Suaide, Martin Alfonso Subieta Vasquez, Toru Sugitate, Christophe Pierre Suire, Rishat Sultanov, Michal Sumbera, Tatjana Susa, Timothy Symon, Alejandro Szanto de Toledo, Imrich Szarka, Adam Szczepankiewicz, Artur Krzysztof Szostak, Maciej Szymanski, Jun Takahashi, Daniel Jesus Tapia Takaki, Attilio Tarantola Peloni, Alfonso Tarazona Martinez, Arturo Tauro, Guillermo Tejeda Munoz, Adriana Telesca, Cristina Terrevoli, Jochen Mathias Thader, Deepa Thoma, Raphael Noel Tieulent, Anthony Timmin, David Tlusty, Alberica Toia, Hisayuki Torii, Luca Toscano, Victor Trubnikov, David Christopher Truesdale, Wladyslaw Henryk Trzaska, Tomoya Tsuji, Alexandr Tumkin, Rosario Turrisi, Trine Spedstad Tveter, Jason Glyndwr Ulery, Kjetil Ullaland, Jochen Ulrich, Antonio Ura, Jozef Urban, Guido Marie Urciuoli, Gianluca Usai, Michal Vajzer, Martin Vala, Lizardo Valencia Palomo, Sara Vallero, Pierre Vande Vyvre, Marco van Leeuwen, Luigi Vannucci, Aurora Diozcora Varga, Raghava Varma, Maria Vasileiou, Andrey Vasiliev, Vladimir Vechernin, Misha Veldhoen, Massimo Venaruzzo, Ermanno Vercellin, Sergio Vergara, Renaud Vernet, Marta Verweij, Linda Vickovic, Giuseppe Viesti, Jussi Viinikainen, Zabulon Vilakazi, Orlando Villalobos Baillie, Yury Vinogradov, Alexander Vinogradov, Leonid Vinogradov, Tiziano Virgili, Yogendra Viyogi, Alexander Vodopianov, Sergey Voloshin, Kirill Voloshin, Giacomo Volpe, Barthelemy von Haller, Ivan Vorobyev, Danilo Vranic, Janka Vrlakova, Bogdan Vulpescu, Alexey Vyushin, Boris Wagner, Vladimir Wagner, Renzhuo Wan, Yaping Wang, Yifei Wang, Mengliang Wang, Dong Wang, Kengo Watanabe, Michael Weber, Johannes Wessel, Uwe Westerhoff, Jens Wiechula, Jon Wikne, Martin Rudolf Wilde, Grzegorz Andrzej Wilk, Alexander Wilk, Crispin William, Bernd Stefan Windelband, Leonidas Xaplanteris Karampatso, Chris G. Yaldo, Yorito Yamaguchi, Hongyan Yang, Shiming Yang, Stanislav Yasnopolsky, JunGyu Yi, Zhongbao Yin, In-Kwon Yoo, Jongik Yoon, Weilin Yu, Xianbao Yuan, Igor Yushmanov, Valentina Zaccolo, Cenek Zach, Chiara Zampolli, Sergey Zaporozhet, Andrey Zarochentsev, Petr Zavada, Nikolai Zaviyalov, Hanna Paulina Zbroszczyk, Pierre Zelnicek, Sorin Ion Zgura, Mikhail Zhalov, Haitao Zhang, Xiaoming Zhang, Fengchu Zhou, You Zhou, Daicui Zhou, Hongsheng Zhu, Jianhui Zhu, Jianlin Zhu, Xiangrong Zhu, Antonino Zichichi, Alice Zimmermann, Gennady Zinovjev, Yannick Denis Zoccarato, Mykhaylo Zynovyev, and Maksym Zyzak
Subjects: p–Pb collisions at the LHC, ALICE experiment, Angular correlation, Nuclear Experiment
Abstract: Angular correlations between charged trigger and associated particles are measured by the ALICE detector in p–Pb collisions at a nucleon–nucleon centre-of-mass energy of 5.02 TeV for transverse momentum ranges within 0.5 < pT,assoc < pT,trig < 4 GeV/c. The correlations are measured over two units of pseudorapidity and full azimuthal angle in different intervals of event multiplicity, and expressed as associated yield per trigger particle. Two long-range ridge-like structures, one on the near side and one on the away side, are observed when the per-trigger yield obtained in low-multiplicity events is subtracted from the one in high-multiplicity events. The excess on the near-side is qualitatively similar to that recently reported by the CMS Collaboration, while the excess on the away-side is reported for the first time. The two-ridge structure projected onto azimuthal angle is quantified with the second and third Fourier coefficients as well as by near-side and away-side yields and widths. The yields on the near side and on the away side are equal within the uncertainties for all studied event multiplicity and pT bins, and the widths show no significant evolution with event multiplicity or pT. These findings suggest that the near-side ridge is accompanied by an essentially identical away-side ridge.
Published: 2013

45. Long-range angular correlations on the near and away side in p–Pb collisions at √sNN = 5.02 TeV

Author: Betty Abelev, Jaroslav Adam, Dagmar Adamova, Andrew Marshall Adare, Madan Aggarwal, Gianluca Aglieri Rinella, Michelangelo Agnello, Andras Gabor Agocs, Andrea Agostinelli, Zubayer Ahammed, Nazeer Ahmad, Arshad Ahmad, Sul Ah Ahn, Sang Un Ahn, Muhammad Ajaz, Alexander Akindinov, Dmitry Aleksandrov, Bruno Alessandro, Andrea Alici, Anton Alkin, Erick Jonathan Almaraz Avina, Johan Alme, Torsten Alt, Valerio Altini, Sedat Altinpinar, Igor Altsybeev, Cristian Andrei, Anton Andronic, Venelin Anguelov, Jonas Anielski, Christopher Daniel Anson, Tome Anticic, Federico Antinori, Pietro Antonioli, Laurent Bernard Aphecetche, Harald Appelshauser, Nicolas Arbor, Silvia Arcelli, Andreas Arend, Nestor Armesto, Roberta Arnaldi, Tomas Robert Aronsson, Ionut Cristian Arsene, Mesut Arslandok, Andzhey Asryan, Andre Augustinus, Ralf Peter Averbeck, Terry Awes, Juha Heikki Aysto, Mohd Danish Azmi, Matthias Jakob Bach, Angela Badala, Yong Wook Baek, Raphaelle Marie Bailhache, Renu Bala, Rinaldo Baldini Ferroli, Alberto Baldisseri, Fernando Baltasar Dos Santos Pedrosa, Jaroslav Ban, Rama Chandra Baral, Roberto Barbera, Francesco Barile, Gergely Gabor Barnafoldi, Lee Stuart Barnby, Valerie Barret, Jerzy Gustaw Bartke, Maurizio Basile, Nicole Bastid, Sumit Basu, Bastian Bathen, Guillaume Batigne, Boris Batyunya, Christoph Heinrich Baumann, Ian Gardner Bearden, Hans Beck, Nirbhay Kumar Behera, Iouri Belikov, Francesca Bellini, Rene Bellwied, Ernesto Belmont Moreno, Gyula Bencedi, Stefania Beole, Ionela Berceanu, Alexandru Bercuci, Yaroslav Berdnikov, Daniel Berenyi, Anais Annick Erica Bergognon, Dario Berzano, Latchezar Betev, Anju Bhasin, Ashok Kumar Bhati, Jihyun Bhom, Livio Bianchi, Nicola Bianchi, Jaroslav Bielcik, Jana Bielcikova, Ante Bilandzic, Sandro Bjelogrlic, Francesco Blanco, F. Blanco, Dmitry Blau, Christoph Blume, Marco Boccioli, Stefan Boettger, Alexey Bogdanov, Hans Boggild, Mikhail Bogolyubsky, Laszlo Boldizsar, Marek Bombara, Julian Book, Herve Borel, Alexander Borissov, Francesco Bossu, Michiel Botje, Elena Botta, Ermes Braidot, Peter Braun Munzinger, Timo Gunther Breitner, Theo Alexander Broker, Tyler Allen Browning, Michal Broz, Rene Brun, Elena Bruna, Giuseppe Eugenio Bruno, Dmitry Budnikov, Henner Buesching, Stefania Bufalino, Predrag Buncic, Oliver Busch, Edith Zinhle Buthelezi, Diego Caballero Orduna, Davide Caffarri, Xu Cai, Helen Louise Caines, Ernesto Calvo Villar, Veronica Canoa Roman, Giovanni Cara Romeo, Wisla Carena, Francesco Carena, Nelson Carlin Filho, Federico Carminati, Amaya Ofelia Casanova Diaz, Javier Ernesto Castillo Castellanos, Juan Francisco Castillo Hernandez, Ester Anna Rita Casula, Vasile Catanescu, Costanza Cavicchioli, Cesar Ceballos Sanchez, Jan Cepila, Piergiaio Cerello, Beomsu Chang, Sylvain Chapeland, Jean Luc Fernand Charvet, Sukalyan Chattopadhyay, Subhasis Chattopadhyay, Isha Chawla, Michael Gerard Cherney, Cvetan Cheshkov, Brigitte Cheynis, Vasco Miguel Chibante Barroso, David Chinellato, Peter Chochula, Marek Chojnacki, Subikash Choudhury, Panagiotis Christakoglou, Christian Holm Christensen, Peter Christiansen, Tatsuya Chujo, Suh Urk Chung, Corrado Cicalo, Luisa Cifarelli, Federico Cindolo, Jean Willy Andre Cleymans, Fabrizio Coccetti, Fabio Colamaria, Domenico Colella, Alberto Collu, Gustavo Conesa Balbastre, Zaida Conesa del Valle, Megan Elizabeth Connors, Jesus Guillermo Contreras, Thomas Michael Cormier, Yasser Corrales Morales, Pietro Cortese, Ismael Cortes Maldonado, Mauro Rogerio Cosentino, Filippo Costa, Manuel Enrique Cotallo, Elisabetta Crescio, Philippe Crochet, Emilia Cruz Alaniz, Rigoberto Cruz Albino, Eleazar Cuautle, Leticia Cunqueiro, Andrea Dainese, Hans Hjersing Dalsgaard, Andrea Danu, Indranil Das, Debasish Das, Supriya Das, Kushal Das, Ajay Kumar Dash, Sadhana Dash, Sudipan De, Gabriel de Barros, Annalisa De Caro, Giacinto de Cataldo, Jan de Cuveland, Alessandro De Falco, Daniele De Gruttola, Hugues Delagrange, Andrzej Deloff, Nora De Marco, Ervin Denes, Salvatore De Pasquale, Airton Deppman, Ginevra DʼErasmo, Raoul Stefan de Rooij, Miguel Angel Diaz Corchero, Domenico Di Bari, Thomas Dietel, Carmelo Di Giglio, Sergio Di Liberto, Antonio Di Mauro, Pasquale Di Nezza, Roberto Divia, Oeystein Djuvsland, Alexandru Florin Dobrin, Tadeusz Antoni Dobrowolski, Benjamin Donigus, Olja Dordic, Olga Driga, Anand Kumar Dubey, Andrea Dubla, Laurent Ducroux, Pascal Dupieux, A. K. Dutta Majumdar, Domenico Elia, David Philip Emschermann, Heiko Engel, Barbara Erazmus, Hege Austrheim Erdal, Bruno Espagnon, Magali Danielle Estienne, Shinichi Esumi, David Evans, Gyulnara Eyyubova, Daniela Fabris, Julien Faivre, Davide Falchieri, Alessandra Fantoni, Markus Fasel, Roger Worsley Fearick, Dominik Fehlker, Linus Feldkamp, Daniel Felea, Alessandro Feliciello, Bo Fenton Olsen, Grigory Feofilov, Arturo Fernandez Tellez, Alessandro Ferretti, Andrea Festanti, Jan Figiel, Marcel Figueredo, Sergey Filchagin, Dmitry Finogeev, Fiorella Fionda, Enrichetta Maria Fiore, Emmanuel Floratos, Michele Floris, Siegfried Valentin Foertsch, Panagiota Foka, Sergey Fokin, Andrea Francescon, Ulrich Michael Frankenfeld, Ulrich Fuchs, Christophe Furget, Mario Fusco Girard, Jens Joergen Gaardhoje, Martino Gagliardi, Alberto Gago, Mauro Gallio, Dhevan Raja Gangadharan, Paraskevi Ganoti, Jose Garabatos, Edmundo Garcia Solis, Irakli Garishvili, Jochen Gerhard, Marie Germain, Claudio Geuna, Mihaela Gheata, Andrei Geae Gheata, Bruno Ghidini, Premomoy Ghosh, Paola Gianotti, Martin Robert Girard, Paolo Giubellino, Ewa Gladysz Dziadus, Peter Glassel, Ramon Gomez, Elena Gonzalez Ferreiro, Laura Helena Gonzalez Trueba, Pedro Gonzalez Zamora, Sergey Gorbunov, Ankita Goswami, Sven Gotovac, Lukasz Kamil Graczykowski, Robert Grajcarek, Alessandro Grelli, Costin Grigoras, Alina Gabriela Grigoras, Vladislav Grigoriev, Ara Grigoryan, Smbat Grigoryan, Boris Grinyov, Nevio Grion, Philippe Gros, Jan Fiete Grosse Oetringhaus, Jean Yves Grossiord, Raffaele Grosso, Fedor Guber, Rachid Guernane, Barbara Guerzoni, Maxime Rene Joseph Guilbaud, Kristjan Herlache Gulbrandsen, Hrant Gulkanyan, Taku Gunji, Anik Gupta, Ramni Gupta, Rudiger Haake, Oystein Senneset Haaland, Cynthia Marie Hadjidakis, Maria Haiduc, Hideki Hamagaki, Gergoe Hamar, Byounghee Han, Luke David Hanratty, Alexander Hansen, Zuzana Harmanova, John William Harris, Matthias Hartig, Austin Harton, Despoina Hatzifotiadou, Shinichi Hayashi, Arsen Hayrapetyan, Stefan Thomas Heckel, Markus Ansgar Heide, Haavard Helstrup, Andrei Ionut Herghelegiu, Gerardo Antonio Herrera Corral, Norbert Herrmann, Benjamin Andreas Hess, Kristin Fanebust Hetland, Bernard Hicks, Boris Hippolyte, Yasuto Hori, Peter Zahariev Hristov, Ivana Hrivnacova, Meidana Huang, Thomas Humanic, Dae Sung Hwang, Raphaelle Ichou, Radiy Ilkaev, Iryna Ilkiv, Motoi Inaba, Elisa Incani, Pier Giaio Innocenti, Gian Michele Innocenti, Mikhail Ippolitov, Muhammad Irfan, Cristian Geae Ivan, Vladimir Ivanov, Andrey Ivanov, Marian Ivanov, Oleksii Ivanytskyi, Adam Wlodzimierz Jacholkowski, Peter Jacobs, Haeng Jin Jang, Malgorzata Anna Janik, Rudolf Janik, Sandun Jayarathna, Satyajit Jena, Deeptanshu Manu Jha, Raul Tonatiuh Jimenez Bustamante, Peter Graham Jones, Hyung Taik Jung, Anton Jusko, Alexei Kaidalov, Sebastian Kalcher, Peter Kalinak, Tuomo Esa Aukusti Kalliokoski, Alexander Philipp Kalweit, Ju Hwan Kang, Vladimir Kaplin, Ayben Karasu Uysal, Oleg Karavichev, Tatiana Karavicheva, Evgeny Karpechev, Andrey Kazantsev, Udo Wolfgang Kebschull, Ralf Keidel, Palash Khan, Shuaib Ahmad Khan, Mohisin Mohammed Khan, Kamal Hussain Khan, Alexei Khanzadeev, Yury Kharlov, Bjarte Kileng, Beomkyu Kim, Jin Sook Kim, Jonghyun Kim, Dong Jo Kim, Do Won Kim, Taesoo Kim, Se Yong Kim, Mimae Kim, Minwoo Kim, Stefan Kirsch, Ivan Kisel, Sergey Kiselev, Adam Ryszard Kisiel, Jennifer Lynn Klay, Jochen Klein, Christian Klein Bosing, Michael Kliemant, Alexander Kluge, Michael Linus Knichel, Anders Garritt Knospe, Markus Kohler, Thorsten Kollegger, Anatoly Kolojvari, Mikhail Kompaniets, Valery Kondratiev, Natalia Kondratyeva, Artem Konevskih, Vladimir Kovalenko, Marek Kowalski, Serge Kox, Greeshma Koyithatta Meethaleveedu, Jiri Kral, Ivan Kralik, Frederick Kramer, Adela Kravcakova, Tobias Krawutschke, Michal Krelina, Matthias Kretz, Marian Krivda, Filip Krizek, Miroslav Krus, Evgeny Kryshen, Mikolaj Krzewicki, Yury Kucheriaev, Thanushan Kugathasan, Christian Claude Kuhn, Paul Kuijer, Igor Kulakov, Jitendra Kumar, Podist Kurashvili, A. Kurepin, A. B. Kurepin, Alexey Kuryakin, Svetlana Kushpil, Vasily Kushpil, Henning Kvaerno, Min Jung Kweon, Youngil Kwon, Pedro Ladron de Guevara, Igor Lakomov, Rune Langoy, Sarah Louise La Pointe, Camilo Ernesto Lara, Antoine Xavier Lardeux, Paola La Rocca, Mateusz Lechman, Ki Sang Lee, Sung Chul Lee, Graham Richard Lee, Iosif Legrand, Joerg Walter Lehnert, Matthieu Laurent Lenhardt, Vito Lenti, Hermes Leon, Ildefonso Leon Monzon, Hermes Leon Vargas, Peter Levai, Shuang Li, Jaen Lien, Roman Lietava, Svein Lindal, Volker Lindenstruth, Christian Lippmann, Michael Annan Lisa, Hans Martin Ljunggren, Per Ivar Loenne, Vera Loggins, Vitaly Loginov, Daniel Lohner, Constantinos Loizides, Kai Krister Loo, Xavier Bernard Lopez, Ernesto Lopez Torres, Gunnar Lovhoiden, Xianguo Lu, Philipp Luettig, Marcello Lunardon, Jiebin Luo, Grazia Luparello, Cinzia Luzzi, Rongrong Ma, Ke Ma, Dilan Minthaka Madagodahettige Don, Alla Maevskaya, Magnus Mager, Durga Prasad Mahapatra, Antonin Maire, Mikhail Malaev, Ivonne Alicia Maldonado Cervantes, Ludmila Malinina, Dmitry MalʼKevich, Peter Malzacher, Alexander Mamonov, Loic Henri Antoine Manceau, Lalit Kumar Mangotra, Vladislav Manko, Franck Manso, Vito Manzari, Yaxian Mao, Massimiliano Marchisone, Jiri Mares, Anselmo Margotti, Ana Maria Marin, Christina Markert, Marco Marquard, Irakli Martashvili, Nicole Alice Martin, Paolo Martinengo, Mario Ivan Martinez, Arnulfo Martinez Davalos, Gines Martinez Garcia, Yevgen Martynov, Alexis Jean Michel Mas, Silvia Masciocchi, Massimo Masera, Alberto Masoni, Laure Marie Massacrier, Annalisa Mastroserio, Adam Tomasz Matyja, Christoph Mayer, Joel Mazer, Alessandra Maria Mazzoni, Franco Meddi, Arturo Alejandro Menchaca Rocha, Jae Mercado Perez, Michal Meres, Yasuo Miake, Leonardo Milano, Jovan Milosevic, Andre Mischke, Aditya Nath Mishra, Dariusz Miskowiec, Ciprian Mihai Mitu, Sanshiro Mizuno, Jocelyn Mlynarz, Bedangadas Mohanty, Levente Molnar, Luis Manuel Montano Zetina, Marco Monteno, Esther Montes, Taebong Moon, Maurizio Morando, Denise Aparecida Moreira De Godoy, Sandra Moretto, Astrid Morreale, Andreas Morsch, Valeria Muccifora, Eugen Mudnic, Sanjib Muhuri, Maitreyee Mukherjee, Hans Muller, Marcelo Munhoz, Sean Murray, Luciano Musa, Jan Musinsky, Alfredo Musso, Basanta Kumar Nandi, Rosario Nania, Eugenio Nappi, Christine Nattrass, Tapan Kumar Nayak, Sergey Nazarenko, Alexander Nedosekin, Maria Nicassio, Mihai Niculescu, Bae Svane Nielsen, Takafumi Niida, Sergey Nikolaev, Vedran Nikolic, Sergey Nikulin, Vladimir Nikulin, Bjorn Steven Nilsen, Mads Stormo Nilsson, Francesco Noferini, Petr Nomokonov, Gerardus Nooren, Norbert Novitzky, Alexandre Nyanin, Anitha Nyatha, Casper Nygaard, Joakim Ingemar Nystrand, Alexander Ochirov, Helmut Oskar Oeschler, Saehanseul Oh, Sun Kun Oh, Janusz Oleniacz, Antonio Carlos Oliveira Da Silva, Chiara Oppedisano, Antonio Ortiz Velasquez, Anders Nils Erik Oskarsson, Piotr Krystian Ostrowski, Jacek Tomasz Otwinowski, Ken Oyama, Kyoichiro Ozawa, Yvonne Chiara Pachmayer, Milos Pachr, Fatima Padilla, Paola Pagano, Guy Paic, Florian Painke, Carlos Pajares, Susanta Kumar Pal, Arvinder Singh Palaha, Armando Palmeri, Vardanush Papikyan, Giuseppe Pappalardo, Woo Jin Park, Annika Passfeld, Blahoslav Pastircak, Dmitri Ivanovich Patalakha, Vincenzo Paticchio, Biswarup Paul, Alexei Pavlinov, Tomasz Jan Pawlak, Thomas Peitzmann, Hugo Denis Antonio Pereira Da Costa, Elienos Pereira De Oliveira Filho, Dmitri Peresunko, Carlos Eugenio Perez Lara, Diego Perini, Davide Perrino, Wiktor Stanislaw Peryt, Alessandro Pesci, Vladimir Peskov, Yury Pestov, Vojtech Petracek, Michal Petran, Mariana Petris, Plamen Rumenov Petrov, Mihai Petrovici, Catia Petta, Miroslav Pikna, Philippe Pillot, Ombretta Pinazza, Lawrence Pinsky, Nora Pitz, Danthasinghe Piyarathna, Mirko Planinic, Mateusz Andrzej Ploskon, Jan Marian Pluta, Timur Pocheptsov, Sona Pochybova, Pedro Luis Manuel Podesta Lerma, Martin Poghosyan, Karel Polak, Boris Polichtchouk, Amalia Pop, Sarah Porteboeuf Houssais, Vladimir Pospisil, Baba Potukuchi, Sidharth Kumar Prasad, Roberto Preghenella, Francesco Prino, Claude Andre Pruneau, Igor Pshenichnov, Giovanna Puddu, Valery Punin, Marian Putis, Jorn Henning Putschke, Emanuele Quercigh, Henrik Qvigstad, Alexandre Rachevski, Alphonse Rademakers, Tomi Samuli Raiha, Jan Rak, Andry Malala Rakotozafindrabe, Luciano Ramello, Abdiel Ramirez Reyes, Rashmi Raniwala, Sudhir Raniwala, Sami Sakari Rasanen, Bogdan Theodor Rascanu, Deepika Rathee, Kenneth Francis Read, Jean Sebastien Real, Krzysztof Redlich, Rosi Jan Reed, Attiq Ur Rehman, Patrick Reichelt, Martijn Reicher, Rainer Arno Ernst Renfordt, Anna Rita Reolon, Andrey Reshetin, Felix Vincenz Rettig, Jean Pierre Revol, Klaus Johannes Reygers, Lodovico Riccati, Renato Angelo Ricci, Tuva Richert, Matthias Rudolph Richter, Petra Riedler, Werner Riegler, Francesco Riggi, Mario Rodriguez Cahuantzi, Alis Rodriguez Manso, Ketil Roed, David Rohr, Dieter Rohrich, Rosa Romita, Federico Ronchetti, Philippe Rosnet, Stefan Rossegger, Andrea Rossi, Christelle Sophie Roy, Pradip Kumar Roy, Antonio Juan Rubio Montero, Riccardo Russo, Evgeny Ryabinkin, Andrzej Rybicki, Sergey Sadovsky, Karel Safarik, Raghunath Sahoo, Pradip Kumar Sahu, Jogender Saini, Hiroaki Sakaguchi, Shingo Sakai, Dosatsu Sakata, Carlos Albert Salgado, Jai Salzwedel, Sanjeev Singh Sambyal, Vladimir Samsonov, Xitzel Sanchez Castro, Ladislav Sandor, Andres Sandoval, Masato Sano, Gianluca Santagati, Romualdo Santoro, Juho Jaako Sarkamo, Eugenio Scapparone, Fernando Scarlassara, Rolf Paul Scharenberg, Claudiu Cornel Schiaua, Rainer Martin Schicker, Christian Joachim Schmidt, Hans Rudolf Schmidt, Simone Schuchmann, Jurgen Schukraft, Tim Schuster, Yves Roland Schutz, Kilian Eberhard Schwarz, Kai Oliver Schweda, Gilda Scioli, Enrico Scomparin, Patrick Aaron Scott, Rebecca Scott, Gianfranco Segato, Ilya Selyuzhenkov, Serhiy Senyukov, Jeewon Seo, Sergio Serci, Eulogio Serradilla, Adrian Sevcenco, Alexandre Shabetai, Galina Shabratova, Ruben Shahoyan, Natasha Sharma, Satish Sharma, Rohini Sharma, Kenta Shigaki, Katherin Shtejer, Yury Sibiriak, Eva Sicking, Sabyasachi Siddhanta, Teodor Siemiarczuk, David Olle Rickard Silvermyr, Catherine Silvestre, Goran Simatovic, Giuseppe Simonetti, Rama Narayana Singaraju, Ranbir Singh, Subhash Singha, Vikas Singhal, Bikash Sinha, Tinku Sinha, Branislav Sitar, Mario Sitta, Bernhard Skaali, Kyrre Skjerdal, Radek Smakal, Nikolai Smirnov, Raimond Snellings, Carsten Sogaard, Ron Ariel Soltz, Hyungsuk Son, Jihye Song, Myunggeun Song, Csaba Soos, Francesca Soramel, Iwona Sputowska, Martha Spyropoulou Stassinaki, Brijesh Kumar Srivastava, Johanna Stachel, Ionel Stan, Grzegorz Stefanek, Matthew Steinpreis, Evert Anders Stenlund, Gideon Francois Steyn, Johannes Hendrik Stiller, Diego Stocco, Mikhail Stolpovskiy, Peter Strmen, Alexandre Alarcon do Passo Suaide, Martin Alfonso Subieta Vasquez, Toru Sugitate, Christophe Pierre Suire, Rishat Sultanov, Michal Sumbera, Tatjana Susa, Timothy Symons, Alejandro Szanto de Toledo, Imrich Szarka, Adam Szczepankiewicz, Artur Krzysztof Szostak, Maciej Szymanski, Jun Takahashi, Daniel Jesus Tapia Takaki, Attilio Tarantola Peloni, Alfonso Tarazona Martinez, Arturo Tauro, Guillermo Tejeda Munoz, Adriana Telesca, Cristina Terrevoli, Jochen Mathias Thader, Deepa Thomas, Raphael Noel Tieulent, Anthony Timmins, David Tlusty, Alberica Toia, Hisayuki Torii, Luca Toscano, Victor Trubnikov, David Christopher Truesdale, Wladyslaw Henryk Trzaska, Tomoya Tsuji, Alexandr Tumkin, Rosario Turrisi, Trine Spedstad Tveter, Jason Glyndwr Ulery, Kjetil Ullaland, Jochen Ulrich, Antonio Uras, Jozef Urban, Guido Marie Urciuoli, Gianluca Usai, Michal Vajzer, Martin Vala, Lizardo Valencia Palomo, Sara Vallero, Pierre Vande Vyvre, Marco van Leeuwen, Luigi Vannucci, Aurora Diozcora Vargas, Raghava Varma, Maria Vasileiou, Andrey Vasiliev, Vladimir Vechernin, Misha Veldhoen, Ermanno Vercellin, Sergio Vergara, Renaud Vernet, Marta Verweij, Linda Vickovic, Giuseppe Viesti, Jussi Viinikainen, Zabulon Vilakazi, Orlando Villalobos Baillie, Yury Vinogradov, Alexander Vinogradov, Leonid Vinogradov, Tiziano Virgili, Yogendra Viyogi, Alexander Vodopianov, Sergey Voloshin, Kirill Voloshin, Giacomo Volpe, Barthelemy von Haller, Ivan Vorobyev, Danilo Vranic, Janka Vrlakova, Bogdan Vulpescu, Alexey Vyushin, Boris Wagner, Vladimir Wagner, Renzhuo Wan, Yaping Wang, Yifei Wang, Mengliang Wang, Dong Wang, Kengo Watanabe, Michael Weber, Johannes Wessels, Uwe Westerhoff, Jens Wiechula, Jon Wikne, Martin Rudolf Wilde, Grzegorz Andrzej Wilk, Alexander Wilk, Crispin Williams, Bernd Stefan Windelband, Leonidas Xaplanteris Karampatsos, Chris G. Yaldo, Yorito Yamaguchi, Hongyan Yang, Shiming Yang, Stanislav Yasnopolsky, JunGyu Yi, Zhongbao Yin, In Kwon Yoo, Jongik Yoon, Weilin Yu, Xianbao Yuan, Igor Yushmanov, Valentina Zaccolo, Cenek Zach, Chiara Zampolli, Sergey Zaporozhets, Andrey Zarochentsev, Petr Zavada, Nikolai Zaviyalov, Hanna Paulina Zbroszczyk, Pierre Zelnicek, Sorin Ion Zgura, Mikhail Zhalov, Haitao Zhang, Xiaoming Zhang, Fengchu Zhou, You Zhou, Daicui Zhou, Hongsheng Zhu, Jianhui Zhu, Jianlin Zhu, Xiangrong Zhu, Antonino Zichichi, Alice Zimmermann, Gennady Zinovjev, Yannick Denis Zoccarato, Mykhaylo Zynovyev, Maksym Zyzak, BREGANT, MARCO, CAMERINI, Paolo, CONTIN, GIACOMO, FRAGIACOMO, ENRICO, LEA, RAMONA, MARGAGLIOTTI, GIACOMO, PIANO, STEFANO, RUI, RINALDO, VENARUZZO, MASSIMO, Betty, Abelev, Jaroslav, Adam, Dagmar, Adamova, Andrew Marshall Adare, Madan, Aggarwal, Gianluca Aglieri Rinella, Michelangelo, Agnello, Andras Gabor Agocs, Andrea, Agostinelli, Zubayer, Ahammed, Nazeer, Ahmad, Arshad, Ahmad, Sul Ah Ahn, Sang Un Ahn, Muhammad, Ajaz, Alexander, Akindinov, Dmitry, Aleksandrov, Bruno, Alessandro, Andrea, Alici, Anton, Alkin, Erick Jonathan Almaraz Avina, Johan, Alme, Torsten, Alt, Valerio, Altini, Sedat, Altinpinar, Igor, Altsybeev, Cristian, Andrei, Anton, Andronic, Venelin, Anguelov, Jonas, Anielski, Christopher Daniel Anson, Tome, Anticic, Federico, Antinori, Pietro, Antonioli, Laurent Bernard Aphecetche, Harald, Appelshauser, Nicolas, Arbor, Silvia, Arcelli, Andreas, Arend, Nestor, Armesto, Roberta, Arnaldi, Tomas Robert Aronsson, Ionut Cristian Arsene, Mesut, Arslandok, Andzhey, Asryan, Andre, Augustinu, Ralf Peter Averbeck, Terry, Awe, Juha Heikki Aysto, Mohd Danish Azmi, Matthias Jakob Bach, Angela, Badala, Yong Wook Baek, Raphaelle Marie Bailhache, Renu, Bala, Rinaldo Baldini Ferroli, Alberto, Baldisseri, Fernando Baltasar Dos Santos Pedrosa, Jaroslav, Ban, Rama Chandra Baral, Roberto, Barbera, Francesco, Barile, Gergely Gabor Barnafoldi, Lee Stuart Barnby, Valerie, Barret, Jerzy Gustaw Bartke, Maurizio, Basile, Nicole, Bastid, Sumit, Basu, Bastian, Bathen, Guillaume, Batigne, Boris, Batyunya, Christoph Heinrich Baumann, Ian Gardner Bearden, Hans, Beck, Nirbhay Kumar Behera, Iouri, Belikov, Francesca, Bellini, Rene, Bellwied, Ernesto Belmont Moreno, Gyula, Bencedi, Stefania, Beole, Ionela, Berceanu, Alexandru, Bercuci, Yaroslav, Berdnikov, Daniel, Berenyi, Anais Annick Erica Bergognon, Dario, Berzano, Latchezar, Betev, Anju, Bhasin, Ashok Kumar Bhati, Jihyun, Bhom, Livio, Bianchi, Nicola, Bianchi, Jaroslav, Bielcik, Jana, Bielcikova, Ante, Bilandzic, Sandro, Bjelogrlic, Francesco, Blanco, Blanco, F., Dmitry, Blau, Christoph, Blume, Marco, Boccioli, Stefan, Boettger, Alexey, Bogdanov, Hans, Boggild, Mikhail, Bogolyubsky, Laszlo, Boldizsar, Marek, Bombara, Julian, Book, Herve, Borel, Alexander, Borissov, Francesco, Bossu, Michiel, Botje, Elena, Botta, Ermes, Braidot, Peter Braun Munzinger, Bregant, Marco, Timo Gunther Breitner, Theo Alexander Broker, Tyler Allen Browning, Michal, Broz, Rene, Brun, Elena, Bruna, Giuseppe Eugenio Bruno, Dmitry, Budnikov, Henner, Buesching, Stefania, Bufalino, Predrag, Buncic, Oliver, Busch, Edith Zinhle Buthelezi, Diego Caballero Orduna, Davide, Caffarri, Cai, Xu, Helen Louise Caines, Ernesto Calvo Villar, Camerini, Paolo, Veronica Canoa Roman, Giovanni Cara Romeo, Wisla, Carena, Francesco, Carena, Nelson Carlin Filho, Federico, Carminati, Amaya Ofelia Casanova Diaz, Javier Ernesto Castillo Castellanos, Juan Francisco Castillo Hernandez, Ester Anna Rita Casula, Vasile, Catanescu, Costanza, Cavicchioli, Cesar Ceballos Sanchez, Jan, Cepila, Piergiaio, Cerello, Beomsu, Chang, Sylvain, Chapeland, Jean Luc Fernand Charvet, Sukalyan, Chattopadhyay, Subhasis, Chattopadhyay, Isha, Chawla, Michael Gerard Cherney, Cvetan, Cheshkov, Brigitte, Cheyni, Vasco Miguel Chibante Barroso, David, Chinellato, Peter, Chochula, Marek, Chojnacki, Subikash, Choudhury, Panagiotis, Christakoglou, Christian Holm Christensen, Peter, Christiansen, Tatsuya, Chujo, Suh Urk Chung, Corrado, Cicalo, Luisa, Cifarelli, Federico, Cindolo, Jean Willy Andre Cleymans, Fabrizio, Coccetti, Fabio, Colamaria, Domenico, Colella, Alberto, Collu, Gustavo Conesa Balbastre, Zaida Conesa del Valle, Megan Elizabeth Connors, Contin, Giacomo, Jesus Guillermo Contreras, Thomas Michael Cormier, Yasser Corrales Morales, Pietro, Cortese, Ismael Cortes Maldonado, Mauro Rogerio Cosentino, Filippo, Costa, Manuel Enrique Cotallo, Elisabetta, Crescio, Philippe, Crochet, Emilia Cruz Alaniz, Rigoberto Cruz Albino, Eleazar, Cuautle, Leticia, Cunqueiro, Andrea, Dainese, Hans Hjersing Dalsgaard, Andrea, Danu, Indranil, Da, Debasish, Da, Supriya, Da, Kushal, Da, Ajay Kumar Dash, Sadhana, Dash, Sudipan, De, Gabriel de Barros, Annalisa De Caro, Giacinto de Cataldo, Jan de Cuveland, Alessandro De Falco, Daniele De Gruttola, Hugues, Delagrange, Andrzej, Deloff, Nora De Marco, Ervin, Dene, Salvatore De Pasquale, Airton, Deppman, Ginevra, Dʼerasmo, Raoul Stefan de Rooij, Miguel Angel Diaz Corchero, Domenico Di Bari, Thomas, Dietel, Carmelo Di Giglio, Sergio Di Liberto, Antonio Di Mauro, Pasquale Di Nezza, Roberto, Divia, Oeystein, Djuvsland, Alexandru Florin Dobrin, Tadeusz Antoni Dobrowolski, Benjamin, Donigu, Olja, Dordic, Olga, Driga, Anand Kumar Dubey, Andrea, Dubla, Laurent, Ducroux, Pascal, Dupieux, Dutta Majumdar, A. K., Domenico, Elia, David Philip Emschermann, Heiko, Engel, Barbara, Erazmu, Hege Austrheim Erdal, Bruno, Espagnon, Magali Danielle Estienne, Shinichi, Esumi, David, Evan, Gyulnara, Eyyubova, Daniela, Fabri, Julien, Faivre, Davide, Falchieri, Alessandra, Fantoni, Markus, Fasel, Roger Worsley Fearick, Dominik, Fehlker, Linus, Feldkamp, Daniel, Felea, Alessandro, Feliciello, Bo Fenton Olsen, Grigory, Feofilov, Arturo Fernandez Tellez, Alessandro, Ferretti, Andrea, Festanti, Jan, Figiel, Marcel, Figueredo, Sergey, Filchagin, Dmitry, Finogeev, Fiorella, Fionda, Enrichetta Maria Fiore, Emmanuel, Florato, Michele, Flori, Siegfried Valentin Foertsch, Panagiota, Foka, Sergey, Fokin, Fragiacomo, Enrico, Andrea, Francescon, Ulrich Michael Frankenfeld, Ulrich, Fuch, Christophe, Furget, Mario Fusco Girard, Jens Joergen Gaardhoje, Martino, Gagliardi, Alberto, Gago, Mauro, Gallio, Dhevan Raja Gangadharan, Paraskevi, Ganoti, Jose, Garabato, Edmundo Garcia Solis, Irakli, Garishvili, Jochen, Gerhard, Marie, Germain, Claudio, Geuna, Mihaela, Gheata, Andrei Geae Gheata, Bruno, Ghidini, Premomoy, Ghosh, Paola, Gianotti, Martin Robert Girard, Paolo, Giubellino, Ewa Gladysz Dziadus, Peter, Glassel, Ramon, Gomez, Elena Gonzalez Ferreiro, Laura Helena Gonzalez Trueba, Pedro Gonzalez Zamora, Sergey, Gorbunov, Ankita, Goswami, Sven, Gotovac, Lukasz Kamil Graczykowski, Robert, Grajcarek, Alessandro, Grelli, Costin, Grigora, Alina Gabriela Grigoras, Vladislav, Grigoriev, Ara, Grigoryan, Smbat, Grigoryan, Boris, Grinyov, Nevio, Grion, Philippe, Gro, Jan Fiete Grosse Oetringhaus, Jean Yves Grossiord, Raffaele, Grosso, Fedor, Guber, Rachid, Guernane, Barbara, Guerzoni, Maxime Rene Joseph Guilbaud, Kristjan Herlache Gulbrandsen, Hrant, Gulkanyan, Taku, Gunji, Anik, Gupta, Ramni, Gupta, Rudiger, Haake, Oystein Senneset Haaland, Cynthia Marie Hadjidakis, Maria, Haiduc, Hideki, Hamagaki, Gergoe, Hamar, Byounghee, Han, Luke David Hanratty, Alexander, Hansen, Zuzana, Harmanova, John William Harris, Matthias, Hartig, Austin, Harton, Despoina, Hatzifotiadou, Shinichi, Hayashi, Arsen, Hayrapetyan, Stefan Thomas Heckel, Markus Ansgar Heide, Haavard, Helstrup, Andrei Ionut Herghelegiu, Gerardo Antonio Herrera Corral, Norbert, Herrmann, Benjamin Andreas Hess, Kristin Fanebust Hetland, Bernard, Hick, Boris, Hippolyte, Yasuto, Hori, Peter Zahariev Hristov, Ivana, Hrivnacova, Meidana, Huang, Thomas, Humanic, Dae Sung Hwang, Raphaelle, Ichou, Radiy, Ilkaev, Iryna, Ilkiv, Motoi, Inaba, Elisa, Incani, Pier Giaio Innocenti, Gian Michele Innocenti, Mikhail, Ippolitov, Muhammad, Irfan, Cristian Geae Ivan, Vladimir, Ivanov, Andrey, Ivanov, Marian, Ivanov, Oleksii, Ivanytskyi, Adam Wlodzimierz Jacholkowski, Peter, Jacob, Haeng Jin Jang, Malgorzata Anna Janik, Rudolf, Janik, Sandun, Jayarathna, Satyajit, Jena, Deeptanshu Manu Jha, Raul Tonatiuh Jimenez Bustamante, Peter Graham Jones, Hyung Taik Jung, Anton, Jusko, Alexei, Kaidalov, Sebastian, Kalcher, Peter, Kalinak, Tuomo Esa Aukusti Kalliokoski, Alexander Philipp Kalweit, Ju Hwan Kang, Vladimir, Kaplin, Ayben Karasu Uysal, Oleg, Karavichev, Tatiana, Karavicheva, Evgeny, Karpechev, Andrey, Kazantsev, Udo Wolfgang Kebschull, Ralf, Keidel, Palash, Khan, Shuaib Ahmad Khan, Mohisin Mohammed Khan, Kamal Hussain Khan, Alexei, Khanzadeev, Yury, Kharlov, Bjarte, Kileng, Beomkyu, Kim, Jin Sook Kim, Jonghyun, Kim, Dong Jo Kim, Do Won Kim, Taesoo, Kim, Se Yong Kim, Mimae, Kim, Minwoo, Kim, Stefan, Kirsch, Ivan, Kisel, Sergey, Kiselev, Adam Ryszard Kisiel, Jennifer Lynn Klay, Jochen, Klein, Christian Klein Bosing, Michael, Kliemant, Alexander, Kluge, Michael Linus Knichel, Anders Garritt Knospe, Markus, Kohler, Thorsten, Kollegger, Anatoly, Kolojvari, Mikhail, Kompaniet, Valery, Kondratiev, Natalia, Kondratyeva, Artem, Konevskih, Vladimir, Kovalenko, Marek, Kowalski, Serge, Kox, Greeshma Koyithatta Meethaleveedu, Jiri, Kral, Ivan, Kralik, Frederick, Kramer, Adela, Kravcakova, Tobias, Krawutschke, Michal, Krelina, Matthias, Kretz, Marian, Krivda, Filip, Krizek, Miroslav, Kru, Evgeny, Kryshen, Mikolaj, Krzewicki, Yury, Kucheriaev, Thanushan, Kugathasan, Christian Claude Kuhn, Paul, Kuijer, Igor, Kulakov, Jitendra, Kumar, Podist, Kurashvili, Kurepin, A., Kurepin, A. B., Alexey, Kuryakin, Svetlana, Kushpil, Vasily, Kushpil, Henning, Kvaerno, Min Jung Kweon, Youngil, Kwon, Pedro Ladron de Guevara, Igor, Lakomov, Rune, Langoy, Sarah Louise La Pointe, Camilo Ernesto Lara, Antoine Xavier Lardeux, Paola La Rocca, Lea, Ramona, Mateusz, Lechman, Ki Sang Lee, Sung Chul Lee, Graham Richard Lee, Iosif, Legrand, Joerg Walter Lehnert, Matthieu Laurent Lenhardt, Vito, Lenti, Hermes, Leon, Ildefonso Leon Monzon, Hermes Leon Vargas, Peter, Levai, Shuang, Li, Jaen, Lien, Roman, Lietava, Svein, Lindal, Volker, Lindenstruth, Christian, Lippmann, Michael Annan Lisa, Hans Martin Ljunggren, Per Ivar Loenne, Vera, Loggin, Vitaly, Loginov, Daniel, Lohner, Constantinos, Loizide, Kai Krister Loo, Xavier Bernard Lopez, Ernesto Lopez Torres, Gunnar, Lovhoiden, Xianguo, Lu, Philipp, Luettig, Marcello, Lunardon, Jiebin, Luo, Grazia, Luparello, Cinzia, Luzzi, Rongrong, Ma, Ke, Ma, Dilan Minthaka Madagodahettige Don, Alla, Maevskaya, Magnus, Mager, Durga Prasad Mahapatra, Antonin, Maire, Mikhail, Malaev, Ivonne Alicia Maldonado Cervantes, Ludmila, Malinina, Dmitry, Malʼkevich, Peter, Malzacher, Alexander, Mamonov, Loic Henri Antoine Manceau, Lalit Kumar Mangotra, Vladislav, Manko, Franck, Manso, Vito, Manzari, Yaxian, Mao, Massimiliano, Marchisone, Jiri, Mare, Margagliotti, Giacomo, Anselmo, Margotti, Ana Maria Marin, Christina, Markert, Marco, Marquard, Irakli, Martashvili, Nicole Alice Martin, Paolo, Martinengo, Mario Ivan Martinez, Arnulfo Martinez Davalos, Gines Martinez Garcia, Yevgen, Martynov, Alexis Jean Michel Mas, Silvia, Masciocchi, Massimo, Masera, Alberto, Masoni, Laure Marie Massacrier, Annalisa, Mastroserio, Adam Tomasz Matyja, Christoph, Mayer, Joel, Mazer, Alessandra Maria Mazzoni, Franco, Meddi, Arturo Alejandro Menchaca Rocha, Jae Mercado Perez, Michal, Mere, Yasuo, Miake, Leonardo, Milano, Jovan, Milosevic, Andre, Mischke, Aditya Nath Mishra, Dariusz, Miskowiec, Ciprian Mihai Mitu, Sanshiro, Mizuno, Jocelyn, Mlynarz, Bedangadas, Mohanty, Levente, Molnar, Luis Manuel Montano Zetina, Marco, Monteno, Esther, Monte, Taebong, Moon, Maurizio, Morando, Denise Aparecida Moreira De Godoy, Sandra, Moretto, Astrid, Morreale, Andreas, Morsch, Valeria, Muccifora, Eugen, Mudnic, Sanjib, Muhuri, Maitreyee, Mukherjee, Hans, Muller, Marcelo, Munhoz, Sean, Murray, Luciano, Musa, Jan, Musinsky, Alfredo, Musso, Basanta Kumar Nandi, Rosario, Nania, Eugenio, Nappi, Christine, Nattra, Tapan Kumar Nayak, Sergey, Nazarenko, Alexander, Nedosekin, Maria, Nicassio, Mihai, Niculescu, Bae Svane Nielsen, Takafumi, Niida, Sergey, Nikolaev, Vedran, Nikolic, Sergey, Nikulin, Vladimir, Nikulin, Bjorn Steven Nilsen, Mads Stormo Nilsson, Francesco, Noferini, Petr, Nomokonov, Gerardus, Nooren, Norbert, Novitzky, Alexandre, Nyanin, Anitha, Nyatha, Casper, Nygaard, Joakim Ingemar Nystrand, Alexander, Ochirov, Helmut Oskar Oeschler, Saehanseul, Oh, Sun Kun Oh, Janusz, Oleniacz, Antonio Carlos Oliveira Da Silva, Chiara, Oppedisano, Antonio Ortiz Velasquez, Anders Nils Erik Oskarsson, Piotr Krystian Ostrowski, Jacek Tomasz Otwinowski, Ken, Oyama, Kyoichiro, Ozawa, Yvonne Chiara Pachmayer, Milos, Pachr, Fatima, Padilla, Paola, Pagano, Guy, Paic, Florian, Painke, Carlos, Pajare, Susanta Kumar Pal, Arvinder Singh Palaha, Armando, Palmeri, Vardanush, Papikyan, Giuseppe, Pappalardo, Woo Jin Park, Annika, Passfeld, Blahoslav, Pastircak, Dmitri Ivanovich Patalakha, Vincenzo, Paticchio, Biswarup, Paul, Alexei, Pavlinov, Tomasz Jan Pawlak, Thomas, Peitzmann, Hugo Denis Antonio Pereira Da Costa, Elienos Pereira De Oliveira Filho, Dmitri, Peresunko, Carlos Eugenio Perez Lara, Diego, Perini, Davide, Perrino, Wiktor Stanislaw Peryt, Alessandro, Pesci, Vladimir, Peskov, Yury, Pestov, Vojtech, Petracek, Michal, Petran, Mariana, Petri, Plamen Rumenov Petrov, Mihai, Petrovici, Catia, Petta, Piano, Stefano, Miroslav, Pikna, Philippe, Pillot, Ombretta, Pinazza, Lawrence, Pinsky, Nora, Pitz, Danthasinghe, Piyarathna, Mirko, Planinic, Mateusz Andrzej Ploskon, Jan Marian Pluta, Timur, Pocheptsov, Sona, Pochybova, Pedro Luis Manuel Podesta Lerma, Martin, Poghosyan, Karel, Polak, Boris, Polichtchouk, Amalia, Pop, Sarah Porteboeuf Houssais, Vladimir, Pospisil, Baba, Potukuchi, Sidharth Kumar Prasad, Roberto, Preghenella, Francesco, Prino, Claude Andre Pruneau, Igor, Pshenichnov, Giovanna, Puddu, Valery, Punin, Marian, Puti, Jorn Henning Putschke, Emanuele, Quercigh, Henrik, Qvigstad, Alexandre, Rachevski, Alphonse, Rademaker, Tomi Samuli Raiha, Jan, Rak, Andry Malala Rakotozafindrabe, Luciano, Ramello, Abdiel Ramirez Reyes, Rashmi, Raniwala, Sudhir, Raniwala, Sami Sakari Rasanen, Bogdan Theodor Rascanu, Deepika, Rathee, Kenneth Francis Read, Jean Sebastien Real, Krzysztof, Redlich, Rosi Jan Reed, Attiq Ur Rehman, Patrick, Reichelt, Martijn, Reicher, Rainer Arno Ernst Renfordt, Anna Rita Reolon, Andrey, Reshetin, Felix Vincenz Rettig, Jean Pierre Revol, Klaus Johannes Reygers, Lodovico, Riccati, Renato Angelo Ricci, Tuva, Richert, Matthias Rudolph Richter, Petra, Riedler, Werner, Riegler, Francesco, Riggi, Mario Rodriguez Cahuantzi, Alis Rodriguez Manso, Ketil, Roed, David, Rohr, Dieter, Rohrich, Rosa, Romita, Federico, Ronchetti, Philippe, Rosnet, Stefan, Rossegger, Andrea, Rossi, Christelle Sophie Roy, Pradip Kumar Roy, Antonio Juan Rubio Montero, Rui, Rinaldo, Riccardo, Russo, Evgeny, Ryabinkin, Andrzej, Rybicki, Sergey, Sadovsky, Karel, Safarik, Raghunath, Sahoo, Pradip Kumar Sahu, Jogender, Saini, Hiroaki, Sakaguchi, Shingo, Sakai, Dosatsu, Sakata, Carlos Albert Salgado, Jai, Salzwedel, Sanjeev Singh Sambyal, Vladimir, Samsonov, Xitzel Sanchez Castro, Ladislav, Sandor, Andres, Sandoval, Masato, Sano, Gianluca, Santagati, Romualdo, Santoro, Juho Jaako Sarkamo, Eugenio, Scapparone, Fernando, Scarlassara, Rolf Paul Scharenberg, Claudiu Cornel Schiaua, Rainer Martin Schicker, Christian Joachim Schmidt, Hans Rudolf Schmidt, Simone, Schuchmann, Jurgen, Schukraft, Tim, Schuster, Yves Roland Schutz, Kilian Eberhard Schwarz, Kai Oliver Schweda, Gilda, Scioli, Enrico, Scomparin, Patrick Aaron Scott, Rebecca, Scott, Gianfranco, Segato, Ilya, Selyuzhenkov, Serhiy, Senyukov, Jeewon, Seo, Sergio, Serci, Eulogio, Serradilla, Adrian, Sevcenco, Alexandre, Shabetai, Galina, Shabratova, Ruben, Shahoyan, Natasha, Sharma, Satish, Sharma, Rohini, Sharma, Kenta, Shigaki, Katherin, Shtejer, Yury, Sibiriak, Eva, Sicking, Sabyasachi, Siddhanta, Teodor, Siemiarczuk, David Olle Rickard Silvermyr, Catherine, Silvestre, Goran, Simatovic, Giuseppe, Simonetti, Rama Narayana Singaraju, Ranbir, Singh, Subhash, Singha, Vikas, Singhal, Bikash, Sinha, Tinku, Sinha, Branislav, Sitar, Mario, Sitta, Bernhard, Skaali, Kyrre, Skjerdal, Radek, Smakal, Nikolai, Smirnov, Raimond, Snelling, Carsten, Sogaard, Ron Ariel Soltz, Hyungsuk, Son, Jihye, Song, Myunggeun, Song, Csaba, Soo, Francesca, Soramel, Iwona, Sputowska, Martha Spyropoulou Stassinaki, Brijesh Kumar Srivastava, Johanna, Stachel, Ionel, Stan, Grzegorz, Stefanek, Matthew, Steinprei, Evert Anders Stenlund, Gideon Francois Steyn, Johannes Hendrik Stiller, Diego, Stocco, Mikhail, Stolpovskiy, Peter, Strmen, Alexandre Alarcon do Passo Suaide, Martin Alfonso Subieta Vasquez, Toru, Sugitate, Christophe Pierre Suire, Rishat, Sultanov, Michal, Sumbera, Tatjana, Susa, Timothy, Symon, Alejandro Szanto de Toledo, Imrich, Szarka, Adam, Szczepankiewicz, Artur Krzysztof Szostak, Maciej, Szymanski, Jun, Takahashi, Daniel Jesus Tapia Takaki, Attilio Tarantola Peloni, Alfonso Tarazona Martinez, Arturo, Tauro, Guillermo Tejeda Munoz, Adriana, Telesca, Cristina, Terrevoli, Jochen Mathias Thader, Deepa, Thoma, Raphael Noel Tieulent, Anthony, Timmin, David, Tlusty, Alberica, Toia, Hisayuki, Torii, Luca, Toscano, Victor, Trubnikov, David Christopher Truesdale, Wladyslaw Henryk Trzaska, Tomoya, Tsuji, Alexandr, Tumkin, Rosario, Turrisi, Trine Spedstad Tveter, Jason Glyndwr Ulery, Kjetil, Ullaland, Jochen, Ulrich, Antonio, Ura, Jozef, Urban, Guido Marie Urciuoli, Gianluca, Usai, Michal, Vajzer, Martin, Vala, Lizardo Valencia Palomo, Sara, Vallero, Pierre Vande Vyvre, Marco van Leeuwen, Luigi, Vannucci, Aurora Diozcora Vargas, Raghava, Varma, Maria, Vasileiou, Andrey, Vasiliev, Vladimir, Vechernin, Misha, Veldhoen, Venaruzzo, Massimo, Ermanno, Vercellin, Sergio, Vergara, Renaud, Vernet, Marta, Verweij, Linda, Vickovic, Giuseppe, Viesti, Jussi, Viinikainen, Zabulon, Vilakazi, Orlando Villalobos Baillie, Yury, Vinogradov, Alexander, Vinogradov, Leonid, Vinogradov, Tiziano, Virgili, Yogendra, Viyogi, Alexander, Vodopianov, Sergey, Voloshin, Kirill, Voloshin, Giacomo, Volpe, Barthelemy von Haller, Ivan, Vorobyev, Danilo, Vranic, Janka, Vrlakova, Bogdan, Vulpescu, Alexey, Vyushin, Boris, Wagner, Vladimir, Wagner, Renzhuo, Wan, Yaping, Wang, Yifei, Wang, Mengliang, Wang, Dong, Wang, Kengo, Watanabe, Michael, Weber, Johannes, Wessel, Uwe, Westerhoff, Jens, Wiechula, Jon, Wikne, Martin Rudolf Wilde, Grzegorz Andrzej Wilk, Alexander, Wilk, Crispin, William, Bernd Stefan Windelband, Leonidas Xaplanteris Karampatsos, Yaldo, Chris G., Yorito, Yamaguchi, Hongyan, Yang, Shiming, Yang, Stanislav, Yasnopolsky, Jungyu, Yi, Zhongbao, Yin, In Kwon Yoo, Jongik, Yoon, Weilin, Yu, Xianbao, Yuan, Igor, Yushmanov, Zaccolo, Valentina, Cenek, Zach, Chiara, Zampolli, Sergey, Zaporozhet, Andrey, Zarochentsev, Petr, Zavada, Nikolai, Zaviyalov, Hanna Paulina Zbroszczyk, Pierre, Zelnicek, Sorin Ion Zgura, Mikhail, Zhalov, Haitao, Zhang, Xiaoming, Zhang, Fengchu, Zhou, You, Zhou, Daicui, Zhou, Hongsheng, Zhu, Jianhui, Zhu, Jianlin, Zhu, Xiangrong, Zhu, Antonino, Zichichi, Alice, Zimmermann, Gennady, Zinovjev, Yannick Denis Zoccarato, Mykhaylo, Zynovyev, and Maksym, Zyzak
Subjects: p-Pb collisions
Abstract: Angular correlations between charged trigger and associated particles are measured by the ALICE detector in p–Pb collisions at a nucleon–nucleon centre-of-mass energy of 5.02 TeV for transverse momentum ranges within 0.5 < pT,assoc < pT,trig < 4 GeV/c. The correlations are measured over two units of pseudorapidity and full azimuthal angle in different intervals of event multiplicity, and expressed as associated yield per trigger particle. Two long-range ridge-like structures, one on the near side and one on the away side, are observed when the per-trigger yield obtained in low-multiplicity events is subtracted from the one in high-multiplicity events. The excess on the near-side is qualitatively similar to that recently reported by the CMS Collaboration, while the excess on the away-side is reported for the first time. The two-ridge structure projected onto azimuthal angle is quantified with the second and third Fourier coefficients as well as by near-side and away-side yields and widths. The yields on the near side and on the away side are equal within the uncertainties for all studied event multiplicity and pT bins, and the widths show no significant evolution with event multiplicity or pT. These findings suggest that the near-side ridge is accompanied by an essentially identical away-side ridge.
Published: 2013

46. Pik3ip1 Modulates Cardiac Hypertrophy by Inhibiting PI3K Pathway

Author: Jiyeon Kim, Hae Chang Jeong, Jihwa Kim, Jong Sub Lee, Hong Ki Song, Do Han Kim, Kyoung Jin Nho, Youngkeun Ahn, and Woo Jin Park
Subjects: Male, medicine.medical_specialty, Class I Phosphatidylinositol 3-Kinases, Protein subunit, lcsh:Medicine, Cardiomegaly, Biology, Rats, Sprague-Dawley, Mice, Downregulation and upregulation, Physical Conditioning, Animal, Internal medicine, medicine, Animals, Myocyte, Myocytes, Cardiac, Gene Silencing, RNA, Small Interfering, lcsh:Science, Protein kinase B, Cells, Cultured, PI3K/AKT/mTOR pathway, Phosphoinositide-3 Kinase Inhibitors, Multidisciplinary, Kinase, Akt/PKB signaling pathway, lcsh:R, Intracellular Signaling Peptides and Proteins, Membrane Proteins, Rats, Cell biology, Mice, Inbred C57BL, Endocrinology, Animals, Newborn, lcsh:Q, Signal transduction, Carrier Proteins, Proto-Oncogene Proteins c-akt, Protein Binding, Research Article
Abstract: Cardiac hypertrophy is an adaptive response to various physiological and pathological stimuli. Phosphoinositide-3 kinase (PI3K) is a highly conserved lipid kinase involved in physiological cardiac hypertrophy (PHH). PI3K interacting protein1 (Pik3ip1) shares homology with the p85 regulatory subunit of PI3K and is known to interact with the p110 catalytic subunit of PI3K, leading to attenuation of PI3K activity in liver and immune cells. However, the role of Pik3ip1 in the heart remains unknown. In the present study, the effects of Pik3ip1 on cardiac hypertrophy were examined. We found that the expression level of Pik3ip1 was markedly higher in cardiomyocytes than in fibroblasts. The interaction of Pik3ip1 with the p110a subunit of PI3K in the heart was identified by immunoprecipitation using neonatal rat cardiomyocytes (NRCM). Approximately 35% knockdown of Pik3ip1 was sufficient to induce myocardial hypertrophy. Pik3ip1 deficiency was shown to lead to activation of PI3K/protein kinase B (AKT)/ mammalian target of rapamycin (mTOR) signaling pathway, increasing protein synthesis and cell size. However, adenovirus-mediated overexpression of Pik3ip1 attenuated PI3K-mediated cardiac hypertrophy. Pik3ip1 was upregulated by PHH due to swimming training, but not by pathological cardiac hypertrophy (PAH) due to pressure-overload, suggesting that Pik3ip1 plays a compensatory negative role for PHH. Collectively, our results elucidate the mechanisms for the roles of Pik3ip1 in PI3K/AKT signaling pathway.
Published: 2015

47. Beta-lapachone inhibits pathological retinal neovascularization inoxygen-induced retinopathy via regulation of HIF-1a

Author: Ko Eun Kim, Moon Hee Jeong, Jin Hyoung Kim, Bongju Park, Woo Jin Park, Hyunsung Park, Young-Ger Suh, Jeong Hun Kim, and Sung Wook Park
Subjects: Vascular Endothelial Growth Factor A, medicine.medical_specialty, Transcription, Genetic, genetic structures, Angiogenesis, oxygen-induced retinopathy, Apoptosis, Biology, Retinal Neovascularization, Retina, chemistry.chemical_compound, medicine, Animals, Humans, retinopathy of prematurity, vascular endothelial growth factor, β-lapachone, Endothelial Cells, Retinopathy of prematurity, Retinal, Cell Biology, Original Articles, medicine.disease, Hypoxia-Inducible Factor 1, alpha Subunit, lapachone, hypoxia-induced factor 1, retinal neovascularization, vascularendothelial growth factor, Cell Hypoxia, eye diseases, Surgery, hypoxia-induced factor 1-α, Vascular endothelial growth factor, Mice, Inbred C57BL, Oxygen, Vascular endothelial growth factor A, medicine.anatomical_structure, chemistry, Hypoxia-inducible factors, Astrocytes, Proteolysis, Cancer research, Molecular Medicine, sense organs, Injections, Intraocular, Retinopathy, Naphthoquinones
Abstract: Retinal neovascularization in retinopathy of prematurity (ROP) is the most common cause of blindness for children. Despite evidence that hypoxia inducible factor (HIF)-1α -VEGF axis is associated with the pathogenesis of ROP, the inhibitors of HIF-1α have not been established as a therapeutic target in the control of ROP pathophysiology. We investigated the hypothesis that degradation of HIF-1α as a master regulator of angiogenesis in hypoxic condition, using β-lapachone, would confer protection against hypoxia-induced retinopathy without affecting physiological vascular development in mice with oxygen-induced retinopathy (OIR), an animal model of ROP. The effects of β-lapachone were examined after intraocular injection in mice with OIR. Intraocular administration of β-lapachone resulted in significant reduction in hypoxia-induced retinal neovascularization without retinal toxicity or perturbation of developmental retinal angiogenesis. Our results demonstrate that HIF-1α–mediated VEGF expression in OIR is associated with pathological neovascularization, not physiological angiogenesis. Thus, strategies blocking HIF-1α in the developing eye in the pathological hypoxia could serve as a novel therapeutic target for ROP.
Published: 2014

48. Intracellular Cleavage of Amyloid beta by a Viral Protease NIa PreventsAmyloid beta-Mediated Cytotoxicity

Author: Michael Ye, Woo Jin Park, Woo Keun Song, Hye-Eun Han, Sang Min Park, Hye Jin Oh, and Baehyun Shin
Subjects: Proteases, Programmed cell death, medicine.medical_treatment, Proteolysis, Intracellular Space, lcsh:Medicine, Bioenergetics, Mitochondrion, Bioinformatics, Biochemistry, Cell Line, Viral Proteins, Alzheimer Disease, Endopeptidases, Molecular Cell Biology, Mental Health and Psychiatry, Medicine and Health Sciences, medicine, Humans, lcsh:Science, Neprilysin, Energy-Producing Organelles, Amyloid beta-Peptides, Multidisciplinary, Protease, Cell Death, medicine.diagnostic_test, Chemistry, lcsh:R, fungi, Biology and Life Sciences, Neurodegenerative Diseases, DNA-Directed RNA Polymerases, Cell Biology, Molecular biology, Mitochondria, Cytosol, Neurology, Cell Processes, Dementia, lcsh:Q, Protein Multimerization, Molecular Neuroscience, Intracellular, Research Article, Neuroscience
Abstract: Nuclear inclusion a (NIa) of turnip mosaic virus is a cytosolic protease that cleaves amyloid beta (A beta) when heterologously overexpressed. Lentivirus-mediated expression of NIa in the brains of APP(sw)/PS1 mice significantly reduces cerebral A beta levels and plaque depositions, and improves behavioral deficits. Here, the effects of NIa and neprilysin (NEP), a well-known A beta-cleaving protease, on oligomeric A beta-induced cell death were evaluated. NIa cleaved monomeric and oligomeric A beta at a similar rate, whereas NEP only cleaved monomeric A beta. Oligomeric A beta-induced cytotoxicity and mitochondrial dysfunction were significantly ameliorated by NIa, but not by NEP. Endocytosed fluorescently-labeled A beta localized to mitochondria, and this was significantly reduced by NIa, but not by NEP. These data suggest that NIa may exerts its protective roles by degrading Ab and thus preventing mitochondrial deposition of A beta.
Published: 2014

49. Long-range angular correlations on the near and away side in p–Pb collisions at

Author: Betty, Abelev, Jaroslav, Adam, Dagmar, Adamova, Andrew Marshall Adare, Madan, Aggarwal, Gianluca Aglieri Rinella, Michelangelo, Agnello, Andras Gabor Agocs, Andrea, Agostinelli, Zubayer, Ahammed, Nazeer, Ahmad, Arshad, Ahmad, Sul Ah Ahn, Sang Un Ahn, Muhammad, Ajaz, Alexander, Akindinov, Dmitry, Aleksandrov, Bruno, Alessandro, Andrea, Alici, Anton, Alkin, Erick Jonathan Almaraz Avina, Johan, Alme, Torsten, Alt, Valerio, Altini, Sedat, Altinpinar, Igor, Altsybeev, Cristian, Andrei, Anton, Andronic, Venelin, Anguelov, Jonas, Anielski, Christopher Daniel Anson, Tome, Anticic, Federico, Antinori, Pietro, Antonioli, Laurent Bernard Aphecetche, Harald, Appelshauser, Nicolas, Arbor, Silvia, Arcelli, Andreas, Arend, Nestor, Armesto, Arnaldi, Roberta, Tomas Robert Aronsson, Ionut Cristian Arsene, Mesut, Arslandok, Andzhey, Asryan, Andre, Augustinus, Ralf Peter Averbeck, Terry, Awes, Juha Heikki Aysto, Mohd Danish Azmi, Matthias Jakob Bach, Angela, Badala, Yong Wook Baek, Raphaelle Marie Bailhache, Renu, Bala, Rinaldo Baldini Ferroli, Alberto, Baldisseri, Fernando Baltasar Dos Santos Pedrosa, Jaroslav, Ban, Rama Chandra Baral, Roberto, Barbera, Francesco, Barile, Gergely Gabor Barnafoldi, Lee Stuart Barnby, Valerie, Barret, Jerzy Gustaw Bartke, Maurizio, Basile, Nicole, Bastid, Sumit, Basu, Bastian, Bathen, Guillaume, Batigne, Boris, Batyunya, Christoph Heinrich Baumann, Ian Gardner Bearden, Hans, Beck, Nirbhay Kumar Behera, Iouri, Belikov, Francesca, Bellini, Rene, Bellwied, Ernesto Belmont Moreno, Gyula, Bencedi, Beole', Stefania, Ionela, Berceanu, Alexandru, Bercuci, Yaroslav, Berdnikov, Daniel, Berenyi, Anais Annick Erica Bergognon, Berzano, DARIO CARLO DOMENICO, Latchezar, Betev, Anju, Bhasin, Ashok Kumar Bhati, Jihyun, Bhom, Bianchi, Livio, Nicola, Bianchi, Jaroslav, Bielcik, Jana, Bielcikova, Ante, Bilandzic, Sandro, Bjelogrlic, Francesco, Blanco, Blanco, F., Dmitry, Blau, Christoph, Blume, Marco, Boccioli, Stefan, Boettger, Alexey, Bogdanov, Hans, Boggild, Mikhail, Bogolyubsky, Laszlo, Boldizsar, Marek, Bombara, Julian, Book, Herve, Borel, Alexander, Borissov, Bossu', Francesco, Michiel, Botje, Botta, Elena, Ermes, Braidot, Peter Braun Munzinger, Marco, Bregant, Timo Gunther Breitner, Theo Alexander Broker, Tyler Allen Browning, Michal, Broz, Rene, Brun, Elena, Bruna, Giuseppe Eugenio Bruno, Dmitry, Budnikov, Henner, Buesching, Bufalino, Stefania, Predrag, Buncic, Oliver, Busch, Edith Zinhle Buthelezi, Diego Caballero Orduna, Davide, Caffarri, Cai, Xu, Helen Louise Caines, Ernesto Calvo Villar, Paolo, Camerini, Veronica Canoa Roman, Giovanni Cara Romeo, Wisla, Carena, Francesco, Carena, Nelson Carlin Filho, Federico, Carminati, Amaya Ofelia Casanova Diaz, Javier Ernesto Castillo Castellanos, Juan Francisco Castillo Hernandez, Ester Anna Rita Casula, Vasile, Catanescu, Costanza, Cavicchioli, Cesar Ceballos Sanchez, Jan, Cepila, Piergiaio, Cerello, Beomsu, Chang, Sylvain, Chapeland, Jean Luc Fernand Charvet, Sukalyan, Chattopadhyay, Subhasis, Chattopadhyay, Isha, Chawla, Michael Gerard Cherney, Cvetan, Cheshkov, Brigitte, Cheynis, Vasco Miguel Chibante Barroso, David, Chinellato, Peter, Chochula, Marek, Chojnacki, Subikash, Choudhury, Panagiotis, Christakoglou, Christian Holm Christensen, Peter, Christiansen, Tatsuya, Chujo, Suh Urk Chung, Corrado, Cicalo, Luisa, Cifarelli, Federico, Cindolo, Jean Willy Andre Cleymans, Fabrizio, Coccetti, Fabio, Colamaria, Domenico, Colella, Alberto, Collu, Gustavo Conesa Balbastre, Zaida Conesa del Valle, Megan Elizabeth Connors, Giacomo, Contin, Jesus Guillermo Contreras, Thomas Michael Cormier, CORRALES MORALES, Yasser, Pietro, Cortese, Ismael Cortes Maldonado, Mauro Rogerio Cosentino, Filippo, Costa, Manuel Enrique Cotallo, Elisabetta, Crescio, Philippe, Crochet, Emilia Cruz Alaniz, Rigoberto Cruz Albino, Eleazar, Cuautle, Leticia, Cunqueiro, Andrea, Dainese, Hans Hjersing Dalsgaard, Andrea, Danu, Indranil, Das, Debasish, Das, Supriya, Das, Kushal, Das, Ajay Kumar Dash, Sadhana, Dash, Sudipan, De, Gabriel de Barros, Annalisa De Caro, Giacinto de Cataldo, Jan de Cuveland, Alessandro De Falco, Daniele De Gruttola, Hugues, Delagrange, Andrzej, Deloff, Nora De Marco, Ervin, Denes, Salvatore De Pasquale, Airton, Deppman, Ginevra, Dʼerasmo, Raoul Stefan de Rooij, Miguel Angel Diaz Corchero, Domenico Di Bari, Thomas, Dietel, Carmelo Di Giglio, Sergio Di Liberto, Antonio Di Mauro, Pasquale Di Nezza, Roberto, Divia, Oeystein, Djuvsland, Alexandru Florin Dobrin, Tadeusz Antoni Dobrowolski, Benjamin, Donigus, Olja, Dordic, Olga, Driga, Anand Kumar Dubey, Andrea, Dubla, Laurent, Ducroux, Pascal, Dupieux, Dutta Majumdar, A. K., Domenico, Elia, David Philip Emschermann, Heiko, Engel, Barbara, Erazmus, Hege Austrheim Erdal, Bruno, Espagnon, Magali Danielle Estienne, Shinichi, Esumi, David, Evans, Gyulnara, Eyyubova, Daniela, Fabris, Julien, Faivre, Davide, Falchieri, Alessandra, Fantoni, Markus, Fasel, Roger Worsley Fearick, Dominik, Fehlker, Linus, Feldkamp, Daniel, Felea, Alessandro, Feliciello, Bo Fenton Olsen, Grigory, Feofilov, Arturo Fernandez Tellez, Ferretti, Alessandro, Andrea, Festanti, Jan, Figiel, Marcel, Figueredo, Sergey, Filchagin, Dmitry, Finogeev, Fiorella, Fionda, Enrichetta Maria Fiore, Emmanuel, Floratos, Michele, Floris, Siegfried Valentin Foertsch, Panagiota, Foka, Sergey, Fokin, Enrico, Fragiacomo, Andrea, Francescon, Ulrich Michael Frankenfeld, Ulrich, Fuchs, Christophe, Furget, Mario Fusco Girard, Jens Joergen Gaardhoje, Gagliardi, Martino, Alberto, Gago, Gallio, Mauro, Dhevan Raja Gangadharan, Paraskevi, Ganoti, Jose, Garabatos, Edmundo Garcia Solis, Irakli, Garishvili, Jochen, Gerhard, Marie, Germain, Claudio, Geuna, Mihaela, Gheata, Andrei Geae Gheata, Bruno, Ghidini, Premomoy, Ghosh, Paola, Gianotti, Martin Robert Girard, Paolo, Giubellino, Ewa Gladysz Dziadus, Peter, Glassel, Ramon, Gomez, Elena Gonzalez Ferreiro, Laura Helena Gonzalez Trueba, Pedro Gonzalez Zamora, Sergey, Gorbunov, Ankita, Goswami, Sven, Gotovac, Lukasz Kamil Graczykowski, Robert, Grajcarek, Alessandro, Grelli, Costin, Grigoras, Alina Gabriela Grigoras, Vladislav, Grigoriev, Ara, Grigoryan, Smbat, Grigoryan, Boris, Grinyov, Nevio, Grion, Philippe, Gros, Jan Fiete Grosse Oetringhaus, Jean Yves Grossiord, Raffaele, Grosso, Fedor, Guber, Rachid, Guernane, Barbara, Guerzoni, Maxime Rene Joseph Guilbaud, Kristjan Herlache Gulbrandsen, Hrant, Gulkanyan, Taku, Gunji, Anik, Gupta, Ramni, Gupta, Rudiger, Haake, Oystein Senneset Haaland, Cynthia Marie Hadjidakis, Maria, Haiduc, Hideki, Hamagaki, Gergoe, Hamar, Byounghee, Han, Luke David Hanratty, Alexander, Hansen, Zuzana, Harmanova, John William Harris, Matthias, Hartig, Austin, Harton, Despoina, Hatzifotiadou, Shinichi, Hayashi, Arsen, Hayrapetyan, Stefan Thomas Heckel, Markus Ansgar Heide, Haavard, Helstrup, Andrei Ionut Herghelegiu, Gerardo Antonio Herrera Corral, Norbert, Herrmann, Benjamin Andreas Hess, Kristin Fanebust Hetland, Bernard, Hicks, Boris, Hippolyte, Yasuto, Hori, Peter Zahariev Hristov, Ivana, Hrivnacova, Meidana, Huang, Thomas, Humanic, Dae Sung Hwang, Raphaelle, Ichou, Radiy, Ilkaev, Iryna, Ilkiv, Motoi, Inaba, Elisa, Incani, Pier Giaio Innocenti, Innocenti, GIAN MICHELE, Mikhail, Ippolitov, Muhammad, Irfan, Cristian Geae Ivan, Vladimir, Ivanov, Andrey, Ivanov, Marian, Ivanov, Oleksii, Ivanytskyi, Adam Wlodzimierz Jacholkowski, Peter, Jacobs, Haeng Jin Jang, Malgorzata Anna Janik, Rudolf, Janik, Sandun, Jayarathna, Satyajit, Jena, Deeptanshu Manu Jha, Raul Tonatiuh Jimenez Bustamante, Peter Graham Jones, Hyung Taik Jung, Anton, Jusko, Alexei, Kaidalov, Sebastian, Kalcher, Peter, Kalinak, Tuomo Esa Aukusti Kalliokoski, Alexander Philipp Kalweit, Ju Hwan Kang, Vladimir, Kaplin, Ayben Karasu Uysal, Oleg, Karavichev, Tatiana, Karavicheva, Evgeny, Karpechev, Andrey, Kazantsev, Udo Wolfgang Kebschull, Ralf, Keidel, Palash, Khan, Shuaib Ahmad Khan, Mohisin Mohammed Khan, Kamal Hussain Khan, Alexei, Khanzadeev, Yury, Kharlov, Bjarte, Kileng, Beomkyu, Kim, Jin Sook Kim, Jonghyun, Kim, Dong Jo Kim, Do Won Kim, Taesoo, Kim, Se Yong Kim, Mimae, Kim, Minwoo, Kim, Stefan, Kirsch, Ivan, Kisel, Sergey, Kiselev, Adam Ryszard Kisiel, Jennifer Lynn Klay, Jochen, Klein, Christian Klein Bosing, Michael, Kliemant, Alexander, Kluge, Michael Linus Knichel, Anders Garritt Knospe, Markus, Kohler, Thorsten, Kollegger, Anatoly, Kolojvari, Mikhail, Kompaniets, Valery, Kondratiev, Natalia, Kondratyeva, Artem, Konevskih, Vladimir, Kovalenko, Marek, Kowalski, Serge, Kox, Greeshma Koyithatta Meethaleveedu, Jiri, Kral, Ivan, Kralik, Frederick, Kramer, Adela, Kravcakova, Tobias, Krawutschke, Michal, Krelina, Matthias, Kretz, Marian, Krivda, Filip, Krizek, Miroslav, Krus, Evgeny, Kryshen, Mikolaj, Krzewicki, Yury, Kucheriaev, Thanushan, Kugathasan, Christian Claude Kuhn, Paul, Kuijer, Igor, Kulakov, Jitendra, Kumar, Podist, Kurashvili, Kurepin, A., Kurepin, A. B., Alexey, Kuryakin, Svetlana, Kushpil, Vasily, Kushpil, Henning, Kvaerno, Min Jung Kweon, Youngil, Kwon, Pedro Ladron de Guevara, Igor, Lakomov, Rune, Langoy, Sarah Louise La Pointe, Camilo Ernesto Lara, Antoine Xavier Lardeux, Paola La Rocca, Ramona, Lea, Mateusz, Lechman, Ki Sang Lee, Sung Chul Lee, Graham Richard Lee, Iosif, Legrand, Joerg Walter Lehnert, Matthieu Laurent Lenhardt, Vito, Lenti, Hermes, Leon, Ildefonso Leon Monzon, Hermes Leon Vargas, Peter, Levai, Shuang, Li, Jaen, Lien, Roman, Lietava, Svein, Lindal, Volker, Lindenstruth, Christian, Lippmann, Michael Annan Lisa, Hans Martin Ljunggren, Per Ivar Loenne, Vera, Loggins, Vitaly, Loginov, Daniel, Lohner, Constantinos, Loizides, Kai Krister Loo, Xavier Bernard Lopez, Ernesto Lopez Torres, Gunnar, Lovhoiden, Xianguo, Lu, Philipp, Luettig, Marcello, Lunardon, Jiebin, Luo, Grazia, Luparello, Cinzia, Luzzi, Rongrong, Ma, Ke, Ma, Dilan Minthaka Madagodahettige Don, Alla, Maevskaya, Magnus, Mager, Durga Prasad Mahapatra, Antonin, Maire, Mikhail, Malaev, Ivonne Alicia Maldonado Cervantes, Ludmila, Malinina, Dmitry, Malʼkevich, Peter, Malzacher, Alexander, Mamonov, Loic Henri Antoine Manceau, Lalit Kumar Mangotra, Vladislav, Manko, Franck, Manso, Vito, Manzari, Yaxian, Mao, Marchisone, Massimiliano, Jiri, Mares, Giacomo Vito Margagliotti, Anselmo, Margotti, Ana Maria Marin, Christina, Markert, Marco, Marquard, Irakli, Martashvili, Nicole Alice Martin, Paolo, Martinengo, Mario Ivan Martinez, Arnulfo Martinez Davalos, Gines Martinez Garcia, Yevgen, Martynov, Alexis Jean Michel Mas, Silvia, Masciocchi, Masera, Massimo, Alberto, Masoni, Laure Marie Massacrier, Annalisa, Mastroserio, Adam Tomasz Matyja, Christoph, Mayer, Joel, Mazer, Alessandra Maria Mazzoni, Franco, Meddi, Arturo Alejandro Menchaca Rocha, Jae Mercado Perez, Michal, Meres, Yasuo, Miake, Milano, Leonardo, Jovan, Milosevic, Andre, Mischke, Aditya Nath Mishra, Dariusz, Miskowiec, Ciprian Mihai Mitu, Sanshiro, Mizuno, Jocelyn, Mlynarz, Bedangadas, Mohanty, Levente, Molnar, Luis Manuel Montano Zetina, Marco, Monteno, Esther, Montes, Taebong, Moon, Maurizio, Morando, Denise Aparecida Moreira De Godoy, Sandra, Moretto, Astrid, Morreale, Andreas, Morsch, Valeria, Muccifora, Eugen, Mudnic, Sanjib, Muhuri, Maitreyee, Mukherjee, Hans, Muller, Marcelo, Munhoz, Sean, Murray, Luciano, Musa, Jan, Musinsky, Alfredo, Musso, Basanta Kumar Nandi, Rosario, Nania, Eugenio, Nappi, Christine, Nattrass, Tapan Kumar Nayak, Sergey, Nazarenko, Alexander, Nedosekin, Maria, Nicassio, Mihai, Niculescu, Bae Svane Nielsen, Takafumi, Niida, Sergey, Nikolaev, Vedran, Nikolic, Sergey, Nikulin, Vladimir, Nikulin, Bjorn Steven Nilsen, Mads Stormo Nilsson, Francesco, Noferini, Petr, Nomokonov, Gerardus, Nooren, Norbert, Novitzky, Alexandre, Nyanin, Anitha, Nyatha, Casper, Nygaard, Joakim Ingemar Nystrand, Alexander, Ochirov, Helmut Oskar Oeschler, Saehanseul, Oh, Sun Kun Oh, Janusz, Oleniacz, Antonio Carlos Oliveira Da Silva, Oppedisano, Chiara, Antonio Ortiz Velasquez, Anders Nils Erik Oskarsson, Piotr Krystian Ostrowski, Jacek Tomasz Otwinowski, Ken, Oyama, Kyoichiro, Ozawa, Yvonne Chiara Pachmayer, Milos, Pachr, Fatima, Padilla, Paola, Pagano, Guy, Paic, Florian, Painke, Carlos, Pajares, Susanta Kumar Pal, Arvinder Singh Palaha, Armando, Palmeri, Vardanush, Papikyan, Giuseppe, Pappalardo, Woo Jin Park, Annika, Passfeld, Blahoslav, Pastircak, Dmitri Ivanovich Patalakha, Vincenzo, Paticchio, Biswarup, Paul, Alexei, Pavlinov, Tomasz Jan Pawlak, Thomas, Peitzmann, Hugo Denis Antonio Pereira Da Costa, Elienos Pereira De Oliveira Filho, Dmitri, Peresunko, Carlos Eugenio Perez Lara, Diego, Perini, Davide, Perrino, Wiktor Stanislaw Peryt, Alessandro, Pesci, Vladimir, Peskov, Yury, Pestov, Vojtech, Petracek, Michal, Petran, Mariana, Petris, Plamen Rumenov Petrov, Mihai, Petrovici, Catia, Petta, Stefano, Piano, Miroslav, Pikna, Philippe, Pillot, Ombretta, Pinazza, Lawrence, Pinsky, Nora, Pitz, Danthasinghe, Piyarathna, Mirko, Planinic, Mateusz Andrzej Ploskon, Jan Marian Pluta, Timur, Pocheptsov, Sona, Pochybova, Pedro Luis Manuel Podesta Lerma, Martin, Poghosyan, Karel, Polak, Boris, Polichtchouk, Amalia, Pop, Sarah Porteboeuf Houssais, Vladimir, Pospisil, Baba, Potukuchi, Sidharth Kumar Prasad, Roberto, Preghenella, Francesco, Prino, Claude Andre Pruneau, Igor, Pshenichnov, Giovanna, Puddu, Valery, Punin, Marian, Putis, Jorn Henning Putschke, Emanuele, Quercigh, Henrik, Qvigstad, Alexandre, Rachevski, Alphonse, Rademakers, Tomi Samuli Raiha, Jan, Rak, Andry Malala Rakotozafindrabe, Ramello, Luciano, Abdiel Ramirez Reyes, Rashmi, Raniwala, Sudhir, Raniwala, Sami Sakari Rasanen, Bogdan Theodor Rascanu, Deepika, Rathee, Kenneth Francis Read, Jean Sebastien Real, Krzysztof, Redlich, Rosi Jan Reed, Attiq Ur Rehman, Patrick, Reichelt, Martijn, Reicher, Rainer Arno Ernst Renfordt, Anna Rita Reolon, Andrey, Reshetin, Felix Vincenz Rettig, Jean Pierre Revol, Klaus Johannes Reygers, Lodovico, Riccati, Renato Angelo Ricci, Tuva, Richert, Matthias Rudolph Richter, Petra, Riedler, Werner, Riegler, Francesco, Riggi, Mario Rodriguez Cahuantzi, Alis Rodriguez Manso, Ketil, Roed, David, Rohr, Dieter, Rohrich, Rosa, Romita, Federico, Ronchetti, Philippe, Rosnet, Stefan, Rossegger, Andrea, Rossi, Christelle Sophie Roy, Pradip Kumar Roy, Antonio Juan Rubio Montero, Rinaldo, Rui, Russo, Riccardo, Evgeny, Ryabinkin, Andrzej, Rybicki, Sergey, Sadovsky, Karel, Safarik, Raghunath, Sahoo, Pradip Kumar Sahu, Jogender, Saini, Hiroaki, Sakaguchi, Shingo, Sakai, Dosatsu, Sakata, Carlos Albert Salgado, Jai, Salzwedel, Sanjeev Singh Sambyal, Vladimir, Samsonov, Xitzel Sanchez Castro, Ladislav, Sandor, Andres, Sandoval, Masato, Sano, Gianluca, Santagati, Romualdo, Santoro, Juho Jaako Sarkamo, Eugenio, Scapparone, Fernando, Scarlassara, Rolf Paul Scharenberg, Claudiu Cornel Schiaua, Rainer Martin Schicker, Christian Joachim Schmidt, Hans Rudolf Schmidt, Simone, Schuchmann, Jurgen, Schukraft, Tim, Schuster, Yves Roland Schutz, Kilian Eberhard Schwarz, Kai Oliver Schweda, Gilda, Scioli, Scomparin, Enrico, Patrick Aaron Scott, Rebecca, Scott, Gianfranco, Segato, Ilya, Selyuzhenkov, Serhiy, Senyukov, Jeewon, Seo, Sergio, Serci, Eulogio, Serradilla, Adrian, Sevcenco, Alexandre, Shabetai, Galina, Shabratova, Ruben, Shahoyan, Natasha, Sharma, Satish, Sharma, Rohini, Sharma, Kenta, Shigaki, SHTEJER DIAZ, Katherin, Yury, Sibiriak, Eva, Sicking, Sabyasachi, Siddhanta, Teodor, Siemiarczuk, David Olle Rickard Silvermyr, Catherine, Silvestre, Goran, Simatovic, Giuseppe, Simonetti, Rama Narayana Singaraju, Ranbir, Singh, Subhash, Singha, Vikas, Singhal, Bikash, Sinha, Tinku, Sinha, Branislav, Sitar, Sitta, Mario, Bernhard, Skaali, Kyrre, Skjerdal, Radek, Smakal, Nikolai, Smirnov, Raimond, Snellings, Carsten, Sogaard, Ron Ariel Soltz, Hyungsuk, Son, Jihye, Song, Myunggeun, Song, Csaba, Soos, Francesca, Soramel, Iwona, Sputowska, Martha Spyropoulou Stassinaki, Brijesh Kumar Srivastava, Johanna, Stachel, Ionel, Stan, Grzegorz, Stefanek, Matthew, Steinpreis, Evert Anders Stenlund, Gideon Francois Steyn, Johannes Hendrik Stiller, Diego, Stocco, Mikhail, Stolpovskiy, Peter, Strmen, Alexandre Alarcon do Passo Suaide, Martin Alfonso Subieta Vasquez, Toru, Sugitate, Christophe Pierre Suire, Rishat, Sultanov, Michal, Sumbera, Tatjana, Susa, Timothy, Symons, Alejandro Szanto de Toledo, Imrich, Szarka, Adam, Szczepankiewicz, Artur Krzysztof Szostak, Maciej, Szymanski, Jun, Takahashi, Daniel Jesus Tapia Takaki, Attilio Tarantola Peloni, Alfonso Tarazona Martinez, Arturo, Tauro, Guillermo Tejeda Munoz, Adriana, Telesca, Cristina, Terrevoli, Jochen Mathias Thader, Deepa, Thomas, Raphael Noel Tieulent, Anthony, Timmins, David, Tlusty, Alberica, Toia, Hisayuki, Torii, Luca, Toscano, Victor, Trubnikov, David Christopher Truesdale, Wladyslaw Henryk Trzaska, Tomoya, Tsuji, Alexandr, Tumkin, Rosario, Turrisi, Trine Spedstad Tveter, Jason Glyndwr Ulery, Kjetil, Ullaland, Jochen, Ulrich, Antonio, Uras, Jozef, Urban, Guido Marie Urciuoli, Gianluca, Usai, Michal, Vajzer, Martin, Vala, Lizardo Valencia Palomo, Sara, Vallero, Pierre Vande Vyvre, Marco van Leeuwen, Luigi, Vannucci, Aurora Diozcora Vargas, Raghava, Varma, Maria, Vasileiou, Andrey, Vasiliev, Vladimir, Vechernin, Misha, Veldhoen, Massimo, Venaruzzo, Vercellin, Ermanno, Sergio, Vergara, Renaud, Vernet, Marta, Verweij, Linda, Vickovic, Giuseppe, Viesti, Jussi, Viinikainen, Zabulon, Vilakazi, Orlando Villalobos Baillie, Yury, Vinogradov, Alexander, Vinogradov, Leonid, Vinogradov, Tiziano, Virgili, Yogendra, Viyogi, Alexander, Vodopianov, Sergey, Voloshin, Kirill, Voloshin, Giacomo, Volpe, Barthelemy von Haller, Ivan, Vorobyev, Danilo, Vranic, Janka, Vrlakova, Bogdan, Vulpescu, Alexey, Vyushin, Boris, Wagner, Vladimir, Wagner, Renzhuo, Wan, Yaping, Wang, Yifei, Wang, Mengliang, Wang, Dong, Wang, Kengo, Watanabe, Michael, Weber, Johannes, Wessels, Uwe, Westerhoff, Jens, Wiechula, Jon, Wikne, Martin Rudolf Wilde, Grzegorz Andrzej Wilk, Alexander, Wilk, Crispin, Williams, Bernd Stefan Windelband, Leonidas Xaplanteris Karampatsos, Yaldo, Chris G., Yorito, Yamaguchi, Hongyan, Yang, Shiming, Yang, Stanislav, Yasnopolsky, Jungyu, Yi, Zhongbao, Yin, In Kwon Yoo, Jongik, Yoon, Weilin, Yu, Xianbao, Yuan, Igor, Yushmanov, Valentina, Zaccolo, Cenek, Zach, Chiara, Zampolli, Sergey, Zaporozhets, Andrey, Zarochentsev, Petr, Zavada, Nikolai, Zaviyalov, Hanna Paulina Zbroszczyk, Pierre, Zelnicek, Sorin Ion Zgura, Mikhail, Zhalov, Haitao, Zhang, Xiaoming, Zhang, Fengchu, Zhou, You, Zhou, Daicui, Zhou, Hongsheng, Zhu, Jianhui, Zhu, Jianlin, Zhu, Xiangrong, Zhu, Antonino, Zichichi, Alice, Zimmermann, Gennady, Zinovjev, Yannick Denis Zoccarato, Mykhaylo, Zynovyev, and Maksym, Zyzak
Subjects: emitted particles in p-Pb collisions, angular correlations, emitted particles in p-Pb collisions, angular correlations
Published: 2013

50. Pharmacological activation of Sirt1 ameliorates polyglutamine-induced toxicity through the regulation of autophagy

Author: Hye Jin Oh, Joohong Ahnn, Tae Hwan Kwak, Sunkyung Lee, Do Han Kim, Sang Min Park, Baehyun Shin, Woo Keun Song, Yunki Lim, and Woo Jin Park
Subjects: Huntingtin, lcsh:Medicine, Apoptosis, Toxicology, Small hairpin RNA, Animals, Genetically Modified, Immunoenzyme Techniques, Neuroblastoma, Sirtuin 1, Cell Movement, Molecular Cell Biology, RNA, Small Interfering, lcsh:Science, Huntingtin Protein, Multidisciplinary, biology, Cell Death, Reverse Transcriptase Polymerase Chain Reaction, digestive, oral, and skin physiology, Neurodegenerative Diseases, Animal Models, Cell biology, Huntington Disease, Neurology, Sirtuin, Reverse Transcriptase Inhibitors, Medicine, Intracellular, Research Article, Neurotoxicology, Drugs and Devices, ATG5, Blotting, Western, Green Fluorescent Proteins, Nerve Tissue Proteins, Real-Time Polymerase Chain Reaction, Model Organisms, Neuropharmacology, Autophagy, Animals, Humans, Immunoprecipitation, RNA, Messenger, Caenorhabditis elegans, Biology, Cell Proliferation, Adenine, lcsh:R, Molecular biology, Microscopy, Fluorescence, Cellular Neuroscience, biology.protein, lcsh:Q, Molecular Neuroscience, Peptides, Naphthoquinones, Neuroscience
Abstract: Intracellular accumulation of polyglutamine (polyQ)-expanded Huntingtin (Htt) protein is a hallmark of Huntington's disease (HD). This study evaluated whether activation of Sirt1 by the anti-cancer agent, beta-lapachone (beta-lap), induces autophagy in human neuroblastoma SH-SY5Y cells, thereby reducing intracellular levels of polyQ aggregates and their concomitant cytotoxicity. Treatment of cells with beta-lap markedly diminished the cytotoxicity induced by forced expression of Htt exon 1 containing a pathogenic polyQ stretch fused to green fluorescent protein (HttEx1(97Q)-GFP). beta-lap increased autophagy in SH-SY5Y cells, as evidenced by the increased formation of LC3-II and autolysosomes. Furthermore, beta-lap reduced HttEx1(97Q)-GFP aggregation, which was significantly prevented by co-incubation with 3-methyladenine, an inhibitor of autophagy. beta-lap increased Sirt1 activity, as shown by the increased deacetylation of the Sirt1 substrates, PARP-1 and Atg5, and the nuclear translocation of FOXO1. Both the induction of autophagy and attenuation of HttEx1(97Q)-GFP aggregation by beta-lap were significantly prevented by co-incubation with sirtinol, a general sirtuin inhibitor or by co-transfection with shRNA against Sirt1. The pro-autophagic actions of beta-lap were further investigated in a transgenic Caenorhabditis elegans (C. elegans) line that expressed Q67 fused to cyanine fluorescent protein (Q67). Notably, beta-lap reduced the number of Q67 puncta and restored Q67-induced defects in motility, which were largely prevented by pre-treatment with RNAi against sir-2.1, the C. elegans orthologue of Sirt1. Collectively, these data suggest that beta-lap induces autophagy through activation of Sirt1, which in turn leads to a reduction in polyQ aggregation and cellular toxicity. Thus, beta-lap provides a novel therapeutic opportunity for the treatment of HD.
Published: 2013

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