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54. Surface modulatable nanocapsids for targeting and tracking toward nanotheranostic delivery

Author

Stark, Marie and Cheng, R Holland

Subjects
Medical Biotechnology, Biomedical and Clinical Sciences, Immunology, Nanotechnology, Bioengineering, Cancer, Digestive Diseases, Vaccine Related, Good Health and Well Being, Animals, Capsid Proteins, Gene Transfer Techniques, Genetic Therapy, Hepatitis E virus, Humans, Immunotherapy, Nanoparticles, Neoplasms, cancer targeting, nanotheranostics, viral capsid, Pharmacology and Pharmaceutical Sciences, Pharmacology and pharmaceutical sciences
Abstract

Nanoparticle diagnostics and therapeutics (nanotheranostics) have significantly advanced cancer detection and treatment. However, many nanotheranostics are ineffective due to defects in tumor localization and bioavailability. An engineered Hepatitis E Virus (HEV) nanocapsid is a proposed platform for targeted cancer-cell delivery. Self-assembling from HEV capsid subunits, nanocapsids retain the capacity to enter cells and resist proteolytic/acidic conditions, but lack infectious viral elements. The nanocapsid surface was modified for chemical activation to confer tumor-specific targeting and detection, immune-response manipulation and controlled theranostic delivery. Nanotheranostic molecules can be packaged in the hollow nanocapsid shell during in vitro assembly. Complementing the adapted stability and cell-entry characteristics of the HEV capsid, a modified nanocapsid serves as a tunable tumor-targeting platform for nanotheronostic delivery.

Published
2016

55. Chemically activatable viral capsid functionalized for cancer targeting

Author

Chen, Chun-Chieh, Xing, Li, Stark, Marie, Ou, Tingwei, Holla, Prasida, Xiao, Kai, Kamita, Shizuo G, Hammock, Bruce D, Lam, Kit, and Cheng, R Holland

Subjects
Medical Biotechnology, Biomedical and Clinical Sciences, Oncology and Carcinogenesis, Immunology, Prevention, Nanotechnology, Cancer, Digestive Diseases, Hepatitis, Biotechnology, Breast Cancer, Liver Disease, Bioengineering, Infectious Diseases, 2.2 Factors relating to the physical environment, Aetiology, Good Health and Well Being, Amino Acid Sequence, Animals, Breast Neoplasms, Capsid, Cell Line, Tumor, Cryoelectron Microscopy, Female, Fluorescent Dyes, Hepatitis E virus, Heterografts, Humans, Mice, Mice, Inbred BALB C, Molecular Sequence Data, cycloaddition of targeting ligand, cysteine replacement, hepatitis E, multivalent ligand display, virus-like particle, Physical Chemistry (incl. Structural), Nanoscience & Nanotechnology, Medical biotechnology, Biomedical engineering
Abstract

AimTo design a theranostic capsule using the virus-like nanoparticle of the hepatitis E virus modified to display breast cancer cell targeting functional group (LXY30).MethodsFive surface-exposed residues were mutated to cysteine to allow conjugation to maleimide-linked chemical groups via thiol-selective linkages. Engineered virus-like nanoparticles were then covalently conjugated to a breast cancer recognized ligand, LXY30 and an amine-coupled near-infrared fluorescence dye.ResultsLXY30-HEV VLP was checked for its binding and entry to a breast cancer cell line and for tumor targeting in vivo to breast cancer tissue in mice. The engineered virus-like nanoparticle not only targeted cancer cells, but also appeared immune silent to native hepatitis E virus antibodies due to epitope disruption at the antibody-binding site.ConclusionThese results demonstrate the production of a theranostic capsule suitable for cancer diagnostics and therapeutics based on surface modification of a highly stable virus-like nanoparticle.

Published
2016

56. Energy deposition by heavy ions: Additivity of kinetic and potential energy contributions in hillock formation on CaF2

Author

Wang, Y. Y., Grygiel, C., Dufour, C., Sun, J. R., Wang, Z. G., Zhao, Y. T., Xiao, G. Q., Cheng, R., Zhou, X. M., Ren, J. R., Liu, S. D., Lei, Y., Sun, Y. B., Ritter, R., Gruber, E., Cassimi, A., Monnet, I., Bouffard, S., Aumayr, F., and Toulemonde, M.

Subjects
Condensed Matter - Materials Science, Condensed Matter - Mesoscale and Nanoscale Physics
Abstract

The formation of nano-hillocks on CaF2 crystal surfaces by individual ion impact has been studied using medium energy (3 and 5 MeV) highly charged ions (Xe19+ to Xe30+) as well as swift (kinetic energies between 12 and 58 MeV) heavy ions. For very slow highly charged ions the appearance of hillocks is known to be linked to a threshold in potential energy while for swift heavy ions a minimum electronic energy loss is necessary. With our results we bridge the gap between these two extreme cases and demonstrate, that with increasing energy deposition via electronic energy loss the potential energy threshold for hillock production can be substantially lowered. Surprisingly, both mechanisms of energy deposition in the target surface seem to contribute in an additive way, as demonstrated when plotting the results in a phase diagram. We show that the inelastic thermal spike model, originally developed to describe such material modifications for swift heavy ions, can be extended to case where kinetic and potential energies are deposited into the surface., Comment: 12 pages, 4 figures

Published
2014
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57. Comparable Antigenicity and Immunogenicity of Oligomeric Forms of a Novel, Acute HIV-1 Subtype C gp145 Envelope for Use in Preclinical and Clinical Vaccine Research

Author

Wieczorek, Lindsay, Krebs, Shelly J, Kalyanaraman, Vaniambadi, Whitney, Stephen, Tovanabutra, Sodsai, Moscoso, Carlos G, Sanders-Buell, Eric, Williams, Constance, Slike, Bonnie, Molnar, Sebastian, Dussupt, Vincent, Alam, S Munir, Chenine, Agnes-Laurence, Tong, Tina, Hill, Edgar L, Liao, Hua-Xin, Hoelscher, Michael, Maboko, Leonard, Zolla-Pazner, Susan, Haynes, Barton F, Pensiero, Michael, McCutchan, Francine, Malek-Salehi, Shawyon, Cheng, R Holland, Robb, Merlin L, VanCott, Thomas, Michael, Nelson L, Marovich, Mary A, Alving, Carl R, Matyas, Gary R, Rao, Mangala, and Polonis, Victoria R

Subjects
Medical Microbiology, Biomedical and Clinical Sciences, Immunology, Vaccine Related, Infectious Diseases, Biotechnology, Prevention, Immunization, Vaccine Related (AIDS), HIV/AIDS, 3.4 Vaccines, Prevention of disease and conditions, and promotion of well-being, Development of treatments and therapeutic interventions, 5.1 Pharmaceuticals, Infection, Good Health and Well Being, AIDS Vaccines, Animals, Drug Evaluation, Preclinical, HIV Antibodies, HIV Infections, HIV-1, Humans, Leukocytes, Mononuclear, Molecular Sequence Data, Neutralization Tests, Rabbits, Vaccination, env Gene Products, Human Immunodeficiency Virus, Biological Sciences, Agricultural and Veterinary Sciences, Medical and Health Sciences, Virology, Agricultural, veterinary and food sciences, Biological sciences, Biomedical and clinical sciences
Abstract

UnlabelledEliciting broadly reactive functional antibodies remains a challenge in human immunodeficiency virus type 1 (HIV-1) vaccine development that is complicated by variations in envelope (Env) subtype and structure. The majority of new global HIV-1 infections are subtype C, and novel antigenic properties have been described for subtype C Env proteins. Thus, an HIV-1 subtype C Env protein (CO6980v0c22) from an infected person in the acute phase (Fiebig stage I/II) was developed as a research reagent and candidate immunogen. The gp145 envelope is a novel immunogen with a fully intact membrane-proximal external region (MPER), extended by a polylysine tail. Soluble gp145 was enriched for trimers that yielded the expected "fan blade" motifs when visualized by cryoelectron microscopy. CO6980v0c22 gp145 reacts with the 4E10, PG9, PG16, and VRC01 HIV-1 neutralizing monoclonal antibodies (MAbs), as well as the V1/V2-specific PGT121, 697, 2158, and 2297 MAbs. Different gp145 oligomers were tested for immunogenicity in rabbits, and purified dimers, trimers, and larger multimers elicited similar levels of cross-subtype binding and neutralizing antibodies to tier 1 and some tier 2 viruses. Immunized rabbit sera did not neutralize the highly resistant CO6980v0c22 pseudovirus but did inhibit the homologous infectious molecular clone in a peripheral blood mononuclear cell (PBMC) assay. This Env is currently in good manufacturing practice (GMP) production to be made available for use as a clinical research tool and further evaluation as a candidate vaccine.ImportanceAt present, the product pipeline for HIV vaccines is insufficient and is limited by inadequate capacity to produce large quantities of vaccine to standards required for human clinical trials. Such products are required to evaluate critical questions of vaccine formulation, route, dosing, and schedule, as well as to establish vaccine efficacy. The gp145 Env protein presented in this study forms physical trimers, binds to many of the well-characterized broad neutralizing MAbs that target conserved Env epitopes, and induce cross-subtype neutralizing antibodies as measured in both cell line and primary cell assays. This subtype C Env gp145 protein is currently undergoing good manufacturing practice production for use as a reagent for preclinical studies and for human clinical research. This product will serve as a reagent for comparative studies and may represent a next-generation candidate HIV immunogen.

Published
2015

58. EMX2 is a predictive marker for adjuvant chemotherapy in lung squamous cell carcinomas

Author

Jablons, David, Yue, D, Li, H, Che, J, Zhang, Y, Tolani, B, Mo, M, Zhang, H, Zheng, Q, Yang, Y, and Cheng, R

Abstract

© 2015 Yue et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.Bac

Published
2015

59. Developmentally Regulated Post-translational Modification of Nucleoplasmin Controls Histone Sequestration and Deposition

Author

Onikubo, Takashi, Nicklay, Joshua J, Xing, Li, Warren, Christopher, Anson, Brandon, Wang, Wei-Lin, Burgos, Emmanuel S, Ruff, Sophie E, Shabanowitz, Jeffrey, Cheng, R Holland, Hunt, Donald F, and Shechter, David

Subjects
Biological Sciences, Genetics, 1.1 Normal biological development and functioning, Underpinning research, Generic health relevance, Life on Land, Biochemistry and Cell Biology, Medical Physiology, Biological sciences
Abstract

Nucleoplasmin (Npm) is an abundant histone chaperone in vertebrate oocytes and embryos. During embryogenesis, regulation of Npm histone binding is critical for its function in storing and releasing maternal histones to establish and maintain the zygotic epigenome. Here, we demonstrate that Xenopus laevis Npm post-translational modifications (PTMs) specific to the oocyte and egg promote either histone deposition or sequestration, respectively. Mass spectrometry and Npm phosphomimetic mutations used in chromatin assembly assays identified hyperphosphorylation on the N-terminal tail as a critical regulator for sequestration. C-terminal tail phosphorylation and PRMT5-catalyzed arginine methylation enhance nucleosome assembly by promoting histone interaction with the second acidic tract of Npm. Electron microscopy reconstructions of Npm and TTLL4 activity toward the C-terminal tail demonstrate that oocyte- and egg-specific PTMs cause Npm conformational changes. Our results reveal that PTMs regulate Npm chaperoning activity by modulating Npm conformation and Npm-histone interaction, leading to histone sequestration in the egg.

Published
2015

60. Multiresolution MAPEM Method for 3D Reconstruction of Symmetrical Particles with Electron Microscopy

Author

Acar, Erman, Baikoghli, Mo A., Stark, Marie, Peltonen, Sari, Ruotsalainen, Ulla, Cheng, R. Holland, Magjarevic, Ratko, Editor-in-chief, Ładyżyński, Piotr, Series editor, Ibrahim, Fatimah, Series editor, Lacković, Igor, Series editor, Rock, Emilio Sacristan, Series editor, Eskola, Hannu, editor, Väisänen, Outi, editor, Viik, Jari, editor, and Hyttinen, Jari, editor

Published
2018
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63. Trimeric HIV Env provides epitope occlusion mediated by hypervariable loops.

Author

Moscoso, Carlos G, Xing, Li, Hui, Jinwen, Hu, Jeffrey, Kalkhoran, Mohammad Baikoghli, Yenigun, Onur M, Sun, Yide, Paavolainen, Lassi, Martin, Loïc, Vahlne, Anders, Zambonelli, Carlo, Barnett, Susan W, Srivastava, Indresh K, and Cheng, R Holland

Subjects
Humans, Peptide Fragments, Antigens, CD4, HIV Envelope Protein gp41, HIV Envelope Protein gp120, Epitopes, Sequence Deletion, Protein Conformation, Protein Binding, Models, Molecular, env Gene Products, Human Immunodeficiency Virus, Protein Interaction Domains and Motifs, Protein Multimerization, CD4 Antigens, Antigens, CD4, Models, Molecular, env Gene Products, Human Immunodeficiency Virus
Abstract

Hypervariable loops of HIV-1 Env protein gp120 are speculated to play roles in the conformational transition of Env to the receptor binding-induced metastable state. Structural analysis of full-length Env-based immunogens, containing the entire V2 loop, displayed tighter association between gp120 subunits, resulting in a smaller trimeric diameter than constructs lacking V2. A prominent basal quaternary location of V2 and V3' that challenges previous reports would facilitate gp41-independent gp120-gp120 interactions and suggests a quaternary mechanism of epitope occlusion facilitated by hypervariable loops. Deletion of V2 resulted in dramatic exposure of basal, membrane-proximal gp41 epitopes, consistent with its predicted basal location. The structural features of HIV-1 Env characterized here provide grounds for a paradigm shift in loop exposure and epitope occlusion, while providing substantive rationale for epitope display required for elicitation of broadly neutralizing antibodies, as well as substantiating previous pertinent literature disregarded in recent reports.

Published
2014

64. Arginine starvation-associated atypical cellular death involves mitochondrial dysfunction, nuclear DNA leakage, and chromatin autophagy

Author

Changou, Chun A, Chen, Yun-Ru, Xing, Li, Yen, Yun, Chuang, Frank YS, Cheng, R Holland, Bold, Richard J, Ann, David K, and Kung, Hsing-Jien

Subjects
Biochemistry and Cell Biology, Biomedical and Clinical Sciences, Biological Sciences, Prostate Cancer, Genetics, Urologic Diseases, Cancer, Underpinning research, 1.1 Normal biological development and functioning, 2.1 Biological and endogenous factors, Aetiology, Generic health relevance, Antineoplastic Agents, Arginine, Argininosuccinate Synthase, Autophagy, Cell Death, Cell Line, Tumor, Chromatin, DNA, Neoplasm, Humans, Hydrolases, Male, Membrane Potential, Mitochondrial, Microscopy, Electron, Transmission, Mitochondria, Nuclear Envelope, Polyethylene Glycols, Prostatic Neoplasms, Reactive Oxygen Species, arginine auxotrophy, ADI-PEG20, metabolic stress, cancer therapy, prostate cancer
Abstract

Autophagy is the principal catabolic prosurvival pathway during nutritional starvation. However, excessive autophagy could be cytotoxic, contributing to cell death, but its mechanism remains elusive. Arginine starvation has emerged as a potential therapy for several types of cancers, owing to their tumor-selective deficiency of the arginine metabolism. We demonstrated here that arginine depletion by arginine deiminase induces a cytotoxic autophagy in argininosuccinate synthetase (ASS1)-deficient prostate cancer cells. Advanced microscopic analyses of arginine-deprived dying cells revealed a novel phenotype with giant autophagosome formation, nucleus membrane rupture, and histone-associated DNA leakage encaptured by autophagosomes, which we shall refer to as chromatin autophagy, or chromatophagy. In addition, nuclear inner membrane (lamin A/C) underwent localized rearrangement and outer membrane (NUP98) partially fused with autophagosome membrane. Further analysis showed that prolonged arginine depletion impaired mitochondrial oxidative phosphorylation function and depolarized mitochondrial membrane potential. Thus, reactive oxygen species (ROS) production significantly increased in both cytosolic and mitochondrial fractions, presumably leading to DNA damage accumulation. Addition of ROS scavenger N-acetyl cysteine or knockdown of ATG5 or BECLIN1 attenuated the chromatophagy phenotype. Our data uncover an atypical autophagy-related death pathway and suggest that mitochondrial damage is central to linking arginine starvation and chromatophagy in two distinct cellular compartments.

Published
2014

65. Permeability changes of integrin-containing multivesicular structures triggered by picornavirus entry.

Author

Soonsawad, Pan, Paavolainen, Lassi, Upla, Paula, Weerachatyanukul, Wattana, Rintanen, Nina, Espinoza, Juan, McNerney, Gregory, Marjomäki, Varpu, and Cheng, R Holland

Subjects
Cell Line, Tumor, Cell Membrane, Cytoplasm, Endosomes, Humans, Picornaviridae, Picornaviridae Infections, Integrin alpha2beta1, Microscopy, Confocal, Permeability, Electron Microscope Tomography, Multivesicular Bodies, Cell Line, Tumor, Microscopy, Confocal, General Science & Technology
Abstract

Cellular uptake of clustered α2β1-integrin induces the formation of membrane compartments that subsequently mature into a multivesicular body (MVB). Enhanced internalization mediated by clustered integrins was observed upon infection by the picornavirus echovirus 1 (EVI). We elucidated the structural features of virus-induced MVBs (vMVBs) in comparison to antibody-induced control MVBs (mock infection) by means of high-pressure cryo fixation of cells followed by immuno electron tomography during early entry of the virus. Three-dimensional tomograms revealed a marked increase in the size and complexity of these vMVBs and the intraluminal vesicles (ILVs) at 2 and 3.5 hours post infection (p.i.), in contrast to the control MVBs without virus. Breakages in the membranes of vMVBs were detected from tomograms after 2 and especially after 3.5 h suggesting that these breakages could facilitate the genome release to the cytoplasm. The in situ neutral-red labeling of viral genome showed that virus uncoating starts as early as 30 min p.i., while an increase of permeability was detected in the vMVBs between 1 and 3 hours p.i., based on a confocal microscopy assay. Altogether, the data show marked morphological changes in size and permeability of the endosomes in the infectious entry pathway of this non-enveloped enterovirus and suggest that the formed breakages facilitate the transfer of the genome to the cytoplasm for replication.

Published
2014

66. Compensation of missing wedge effects with sequential statistical reconstruction in electron tomography.

Author

Paavolainen, Lassi, Acar, Erman, Tuna, Uygar, Peltonen, Sari, Moriya, Toshio, Soonsawad, Pan, Marjomäki, Varpu, Cheng, R Holland, and Ruotsalainen, Ulla

Subjects
Artifacts, Algorithms, Image Processing, Computer-Assisted, Electron Microscope Tomography, Image Processing, Computer-Assisted, General Science & Technology
Abstract

Electron tomography (ET) of biological samples is used to study the organization and the structure of the whole cell and subcellular complexes in great detail. However, projections cannot be acquired over full tilt angle range with biological samples in electron microscopy. ET image reconstruction can be considered an ill-posed problem because of this missing information. This results in artifacts, seen as the loss of three-dimensional (3D) resolution in the reconstructed images. The goal of this study was to achieve isotropic resolution with a statistical reconstruction method, sequential maximum a posteriori expectation maximization (sMAP-EM), using no prior morphological knowledge about the specimen. The missing wedge effects on sMAP-EM were examined with a synthetic cell phantom to assess the effects of noise. An experimental dataset of a multivesicular body was evaluated with a number of gold particles. An ellipsoid fitting based method was developed to realize the quantitative measures elongation and contrast in an automated, objective, and reliable way. The method statistically evaluates the sub-volumes containing gold particles randomly located in various parts of the whole volume, thus giving information about the robustness of the volume reconstruction. The quantitative results were also compared with reconstructions made with widely-used weighted backprojection and simultaneous iterative reconstruction technique methods. The results showed that the proposed sMAP-EM method significantly suppresses the effects of the missing information producing isotropic resolution. Furthermore, this method improves the contrast ratio, enhancing the applicability of further automatic and semi-automatic analysis. These improvements in ET reconstruction by sMAP-EM enable analysis of subcellular structures with higher three-dimensional resolution and contrast than conventional methods.

Published
2014

72. Enhancement of stimulated Brillouin scattering in multiple resonance regions by two-color light in inhomogeneous flowing plasmas

Author

Huang, Z. M., primary, Wang, Qing, additional, Cheng, R. J., additional, Li, X. X., additional, Lv, S. Y., additional, Liu, D. J., additional, Li, X. M., additional, Zhang, S. T., additional, Chen, Z. J., additional, Wang, Qiang, additional, Liu, Z. J., additional, Cao, L. H., additional, and Zheng, C. Y., additional

Published
2023
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73. Is ramucirumab and paclitaxel therapy beneficial for second-line treatment of metastatic gastric or junctional adenocarcinoma for patients with ascites? Analysis of RAINBOW phase 3 trial data

Author

Muro K, Jen MH, and Cheng R

Subjects
gastric cancer, GEJ, peritoneal metastases, efficacy, safety, Neoplasms. Tumors. Oncology. Including cancer and carcinogens, RC254-282
Abstract

Kei Muro,1 Min-Hua Jen,2 Rebecca Cheng3 1Department of Clinical Oncology, Outpatient Treatment Center, Aichi Cancer Center Hospital, Nagoya, Japan; 2Eli Lilly and Company Ltd, Windlesham, Surrey, UK; 3Eli Lilly and Company, Taipei, Taiwan Purpose: Second-line treatment with ramucirumab-paclitaxel has demonstrated statistically significant and clinically meaningful survival outcomes compared to paclitaxel-alone in patients with advanced gastric cancer (HR=0.807, 95% CI 0.678–0.962; P=0.017). Post hoc, exploratory analyses of RAINBOW patient data were performed to examine whether ascites impacted the efficacy and safety of ramucirumab-paclitaxel.Patients and methods: Patients were placed in with- or without-ascites subgroups based on baseline information collected on case report forms. The Kaplan–Meier method was used to estimate median progression-free survival (PFS) and overall survival (OS) of the ascites subgroups. HR and 95% CI were calculated using the Cox proportional hazards model. Survival distributions within the two arms in each ascites subgroup were compared using the log-rank test.Results: There were 36% of RAINBOW trial patients (237/665) that had ascites at baseline (with-ascites subgroup); 64% of patients (428/665) had no baseline ascites (without-ascites subgroup). Most baseline characteristics were balanced. The with-ascites subgroup had a higher percentage of patients with peritoneal metastases (91% vs 23%) as expected. Overall survival for the with-ascites subgroup was worse than for the without-ascites subgroup (median OS for placebo-treated patients: 5.2 vs 8.5 months, respectively). However, OS treatment effects did not seem to differ significantly among patients with ascites (OS stratified HR=0.864, 95% CI=0.644–1.161; P=0.3362) vs those without ascites (OS stratified HR=0.745, 95% CI=0.593–0.936; P=0.0115). Similar results were observed for PFS. Ramucirumab treatment was associated with a greater incidence of all-grade vomiting for the with-ascites subgroup vs the without-ascites subgroup (ramucirumab arm: 39.2% vs 18.8%; placebo arm: 23.3% vs 19.5%, respectively). The incidence of adverse events of special interest was not elevated among the ramucirumab-treated ascites subgroup over the without-ascites subgroup.Conclusion: The benefit/risk profile of ramucirumab-paclitaxel remains favorable in patients with ascites and is consistent with the findings of the RAINBOW trial. Keywords: gastric cancer, GEJ, peritoneal metastases, efficacy, safety

Published
2019

76. Structure of the arginine methyltransferase PRMT5-MEP50 reveals a mechanism for substrate specificity.

Author

Ho, Meng-Chiao, Wilczek, Carola, Bonanno, Jeffrey B, Xing, Li, Seznec, Janina, Matsui, Tsutomu, Carter, Lester G, Onikubo, Takashi, Kumar, P Rajesh, Chan, Man K, Brenowitz, Michael, Cheng, R Holland, Reimer, Ulf, Almo, Steven C, and Shechter, David

Subjects
Animals, Xenopus laevis, Xenopus Proteins, Chromosomal Proteins, Non-Histone, Catalytic Domain, Protein Conformation, Substrate Specificity, Dimerization, Models, Molecular, Protein-Arginine N-Methyltransferases, Chromosomal Proteins, Non-Histone, Models, Molecular, General Science & Technology
Abstract

The arginine methyltransferase PRMT5-MEP50 is required for embryogenesis and is misregulated in many cancers. PRMT5 targets a wide variety of substrates, including histone proteins involved in specifying an epigenetic code. However, the mechanism by which PRMT5 utilizes MEP50 to discriminate substrates and to specifically methylate target arginines is unclear. To test a model in which MEP50 is critical for substrate recognition and orientation, we determined the crystal structure of Xenopus laevis PRMT5-MEP50 complexed with S-adenosylhomocysteine (SAH). PRMT5-MEP50 forms an unusual tetramer of heterodimers with substantial surface negative charge. MEP50 is required for PRMT5-catalyzed histone H2A and H4 methyltransferase activity and binds substrates independently. The PRMT5 catalytic site is oriented towards the cross-dimer paired MEP50. Histone peptide arrays and solution assays demonstrate that PRMT5-MEP50 activity is inhibited by substrate phosphorylation and enhanced by substrate acetylation. Electron microscopy and reconstruction showed substrate centered on MEP50. These data support a mechanism in which MEP50 binds substrate and stimulates PRMT5 activity modulated by substrate post-translational modifications.

Published
2013

77. Calpains promote α2β1 integrin turnover in nonrecycling integrin pathway

Author

Rintanen, Nina, Karjalainen, Mikko, Alanko, Jonna, Paavolainen, Lassi, Mäki, Anita, Nissinen, Liisa, Lehkonen, Moona, Kallio, Katri, Cheng, R Holland, Upla, Paula, Ivaska, Johanna, and Marjomäki, Varpu

Subjects
Biochemistry and Cell Biology, Biological Sciences, Calpain, Cell Line, Tumor, Cell Membrane, Enterovirus B, Human, Focal Adhesions, Humans, Integrin alpha2beta1, Protein Transport, Signal Transduction, Medical and Health Sciences, Developmental Biology, Biochemistry and cell biology
Abstract

Collagen receptor integrins recycle between the plasma membrane and endosomes and facilitate formation and turnover of focal adhesions. In contrast, clustering of α2β1 integrin with antibodies or the human pathogen echovirus 1 (EV1) causes redistribution of α2 integrin to perinuclear multivesicular bodies, α2-MVBs. We show here that the internalized clustered α2 integrin remains in α2-MVBs and is not recycled back to the plasma membrane. Instead, receptor clustering and internalization lead to an accelerated down-regulation of α2β1 integrin compared to the slow turnover of unclustered α2 integrin. EV1 infection or integrin degradation is not associated with proteasomal or autophagosomal processes and shows no significant association with lysosomal pathway. In contrast, degradation is dependent on calpains, such that it is blocked by calpain inhibitors. We show that active calpain is present in α2-MVBs, internalized clustered α2β1 integrin coprecipitates with calpain-1, and calpain enzymes can degrade α2β1 integrin. In conclusion, we identified a novel virus- and clustering-specific pathway that diverts α2β1 integrin from its normal endo/exocytic traffic to a nonrecycling, calpain-dependent degradative endosomal route.

Published
2012

79. Roles of cysteines Cys115 and Cys201 in the assembly and thermostability of grouper betanodavirus particles

Author

Wang, Chun-Hsiung, Hsu, Chi-Hsin, Wu, Yi-Min, Luo, Yu-Chun, Tu, Mei-Hui, Chang, Wei-hau, Cheng, R. Holland, and Lin, Chan-Shing

Subjects
Biomedicine, Plant Sciences, Virology, Medical Microbiology, Nervous necrosis virus, Virus-like particle, Disulfide linkages, Reassembly
Abstract

The virus-like particle (VLP) assembled from capsid subunits of the dragon grouper nervous necrosis virus (DGNNV) is very similar to its native T = 3 virion. In order to investigate the effects of four cysteine residues in the capsid polypeptide on the assembly/dissociation pathways of DGNNV virions, we recombinantly cloned mutant VLPs by mutating each cysteine to destroy the specific disulfide linkage as compared with thiol reduction to destroy all S–S bonds. The mutant VLPs of C187A and C331A mutations were similar to wild-type VLPs (WT-VLPs); hence, the effects of Cys187 and Cys331 on the particle formation and thermostability were presumably negligible. Electron microscopy showed that either C115A or C201A mutation disrupted de novo VLP formation significantly. As shown in micrographs and thermal decay curves, β-mercaptoethanol-treated WT-VLPs remained intact, merely resulting in lower tolerance to thermal disruption than native WT-VLPs. This thiol reduction broke disulfide linkages inside the pre-fabricated VLPs, but it did not disrupt the appearance of icosahedrons. Small dissociated capsomers from EGTA-treated VLPs were able to reassemble back to icosahedrons in the presence of calcium ions, but additional treatment with β-mercaptoethanol during EGTA dissociation resulted in inability of the capsomers to reassemble into the icosahedral form. These results indicated that Cys115 and Cys201 were essential for capsid formation of DGNNV icosahedron structure in de novo assembly and reassembly pathways, as well as for the thermal stability of pre-fabricated particles.

Published
2010

82. Three-dimensional structure of the enveloped bacteriophage phi12: an incomplete T = 13 lattice is superposed on an enclosed T = 1 shell.

Author

Wei, Hui, Cheng, R Holland, Berriman, John, Rice, William J, Stokes, David L, Katz, A, Morgan, David Gene, and Gottlieb, Paul

Subjects
Pseudomonas syringae, Bacteriophages, Cystoviridae, Virion, Nucleocapsid, Capsid, Viral Envelope Proteins, RNA, Double-Stranded, RNA, Viral, Cryoelectron Microscopy, Molecular Conformation, Protein Conformation, Genome, Viral, RNA, Double-Stranded, Viral, Genome, General Science & Technology
Abstract

BackgroundBacteriophage phi12 is a member of the Cystoviridae, a unique group of lipid containing membrane enveloped bacteriophages that infect the bacterial plant pathogen Pseudomonas syringae pv. phaseolicola. The genomes of the virus species contain three double-stranded (dsRNA) segments, and the virus capsid itself is organized in multiple protein shells. The segmented dsRNA genome, the multi-layered arrangement of the capsid and the overall viral replication scheme make the Cystoviridae similar to the Reoviridae.Methodology/principal findingsWe present structural studies of cystovirus phi12 obtained using cryo-electron microscopy and image processing techniques. We have collected images of isolated phi12 virions and generated reconstructions of both the entire particles and the polymerase complex (PC). We find that in the nucleocapsid (NC), the phi12 P8 protein is organized on an incomplete T = 13 icosahedral lattice where the symmetry axes of the T = 13 layer and the enclosed T = 1 layer of the PC superpose. This is the same general protein-component organization found in phi6 NC's but the detailed structure of the entire phi12 P8 layer is distinct from that found in the best classified cystovirus species phi6. In the reconstruction of the NC, the P8 layer includes protein density surrounding the hexamers of P4 that sit at the 5-fold vertices of the icosahedral lattice. We believe these novel features correspond to dimers of protein P7.Conclusions/significanceIn conclusion, we have determined that the phi12 NC surface is composed of an incomplete T = 13 P8 layer forming a net-like configuration. The significance of this finding in regard to cystovirus assembly is that vacancies in the lattice could have the potential to accommodate additional viral proteins that are required for RNA packaging and synthesis.

Published
2009

83. Adjustable Ellipsoid Nanoparticles Assembled from Re-engineered Connectors of the Bacteriophage Phi29 DNA Packaging Motor

Author

Xiao, Feng, Cai, Ying, Wang, Joseph Che-Yen, Green, Dominik, Cheng, R Holland, Demeler, Borries, and Guo, Peixuan

Subjects
Medical Biotechnology, Biological Sciences, Biomedical and Clinical Sciences, Chemical Sciences, Nanotechnology, Bioengineering, Algorithms, Bacteriophages, DNA Packaging, DNA, Viral, Microscopy, Electron, Transmission, Models, Molecular, Monte Carlo Method, Nanoparticles, Nucleic Acid Conformation, Peptide Hydrolases, Peptides, nanobiotechnology, bionanotechnology, viral DNA packaging, phi29 DNA packaging motor, protein nanoparticles, virus assemble, bacteriophage phi29 connector, Nanoscience & Nanotechnology
Abstract

A 24 x 30 nm ellipsoid nanoparticle containing 84 subunits or 7 dodecamers of the re-engineered core protein of the bacteriophage phi29 DNA packaging motor was constructed. Homogeneous nanoparticles were obtained with simple one-step purification. Electron microscopy and analytical ultracentrifugation were employed to elucidate the structure, shape, size, and mechanism of assembly. The formation of this structure was mediated and stabilized by N-terminal peptide extensions. Reversal of the 84-subunit ellipsoid nanoparticle to its dodecamer subunit was controlled by the cleavage of the extended N-terminal peptide with a protease. The 84 outward-oriented C-termini were conjugated with a streptavidin binding peptide which can be used for the incorporation of markers. This further extends the application of this nanoparticle to pathogen detection and disease diagnosis by signal enhancement.

Published
2009

86. Fabrication of Massive Sheets of Single Layer Patterned Arrays Using Lipid Directed Reengineered Phi29 Motor Dodecamer

Author

Xiao, Feng, Sun, Jinchuan, Coban, Oana, Schoen, Peter, Wang, Joseph Che-Yen, Cheng, R Holland, and Guo, Peixuan

Subjects
Engineering, Nanotechnology, Bioengineering, Bacteriophages, Biotechnology, Escherichia coli, Fourier Analysis, Lipids, Microscopy, Atomic Force, Microscopy, Electron, Transmission, Protein Array Analysis, Protein Engineering, Protein Structure, Tertiary, Viral Proteins, bacteriophage phi29, portal vertex, dodecamer, single layer patterned arrays, Nanoscience & Nanotechnology
Abstract

The bottom-up assembly of patterned arrays is an exciting and important area in current nanotechnology. Arrays can be engineered to serve as components in chips for a virtually inexhaustible list of applications ranging from disease diagnosis to ultra-high-density data storage. Phi29 motor dodecamer has been reported to form elegant multilayer tetragonal arrays. However, multilayer protein arrays are of limited use for nanotechnological applications which demand nanoreplica or coating technologies. The ability to produce a single layer array of biological structures with high replication fidelity represents a significant advance in the area of nanomimetics. In this paper, we report on the assembly of single layer sheets of reengineered phi29 motor dodecamer. A thin lipid monolayer was used to direct the assembly of massive sheets of single layer patterned arrays of the reengineered motor dodecamer. Uniform, clean and highly ordered arrays were constructed as shown by both transmission electron microscopy and atomic force microscopy imaging.

Published
2009

87. Three-Dimensional Structure of the Enveloped Bacteriophage Φ12: An Incomplete T = 13 Lattice Is Superposed on an Enclosed T = 1 Shell

Author

Wei, Hui, Cheng, R Holland, Berriman, John, Rice, William J, Stokes, David L, Katz, A, Morgan, David Gene, and Gottlieb, Paul

Subjects
Plant Biology, Biological Sciences, Infectious Diseases, 2.2 Factors relating to the physical environment, Aetiology, Infection, Bacteriophages, Capsid, Cryoelectron Microscopy, Cystoviridae, Genome, Viral, Molecular Conformation, Nucleocapsid, Protein Conformation, Pseudomonas syringae, RNA, Double-Stranded, RNA, Viral, Viral Envelope Proteins, Virion, General Science & Technology
Abstract

BackgroundBacteriophage phi12 is a member of the Cystoviridae, a unique group of lipid containing membrane enveloped bacteriophages that infect the bacterial plant pathogen Pseudomonas syringae pv. phaseolicola. The genomes of the virus species contain three double-stranded (dsRNA) segments, and the virus capsid itself is organized in multiple protein shells. The segmented dsRNA genome, the multi-layered arrangement of the capsid and the overall viral replication scheme make the Cystoviridae similar to the Reoviridae.Methodology/principal findingsWe present structural studies of cystovirus phi12 obtained using cryo-electron microscopy and image processing techniques. We have collected images of isolated phi12 virions and generated reconstructions of both the entire particles and the polymerase complex (PC). We find that in the nucleocapsid (NC), the phi12 P8 protein is organized on an incomplete T = 13 icosahedral lattice where the symmetry axes of the T = 13 layer and the enclosed T = 1 layer of the PC superpose. This is the same general protein-component organization found in phi6 NC's but the detailed structure of the entire phi12 P8 layer is distinct from that found in the best classified cystovirus species phi6. In the reconstruction of the NC, the P8 layer includes protein density surrounding the hexamers of P4 that sit at the 5-fold vertices of the icosahedral lattice. We believe these novel features correspond to dimers of protein P7.Conclusions/significanceIn conclusion, we have determined that the phi12 NC surface is composed of an incomplete T = 13 P8 layer forming a net-like configuration. The significance of this finding in regard to cystovirus assembly is that vacancies in the lattice could have the potential to accommodate additional viral proteins that are required for RNA packaging and synthesis.

Published
2009

90. Variance in multiplex suspension array assays: microsphere size variation impact

Author

Hanley, Brian P, Xing, Li, and Cheng, R Holland

Subjects
Biological Sciences, Ecology, Fluorescence, Microarray Analysis, Microscopy, Electron, Transmission, Microspheres, Reproducibility of Results, Bioinformatics, Biological sciences
Abstract

BackgroundLuminex suspension microarray assays are in widespread use. There are issues of variability of assay readings using this technology.Methods and resultsSize variation is demonstrated by transmission electron microscopy. Size variations of microspheres are shown to occur in stepwise increments. A strong correspondence between microsphere size distribution and distribution of fluorescent events from assays is shown. An estimate is made of contribution of microsphere size variation to assay variance.ConclusionA probable significant cause of variance in suspended microsphere assay results is variation in microsphere diameter. This can potentially be addressed by changes in the manufacturing process. Provision to users of mean size, median size, skew, the number of standard deviations that half the size range represents (sigma multiple), and standard deviation is recommended. Establishing a higher sigma multiple for microsphere production is likely to deliver a significant improvement in precision of raw instrument readings. Further research is recommended on the molecular architecture of microsphere coatings.

Published
2007

93. Tilt-angle stimulated Raman projection tomography

Author

Lin, P., LI, C., Flores Valle, A., https://orcid.org/0000-0003-0830-1126, Wang, Z., Zhang, M., Cheng, R., and Cheng, J.

Subjects
Imaging, Three-Dimensional, Image Processing, Computer-Assisted, Animals, Polystyrenes, Caenorhabditis elegans, Tomography, X-Ray Computed, Tomography, Atomic and Molecular Physics, and Optics
Abstract

Stimulated Raman projection tomography is a label-free volumetric chemical imaging technology allowing three-dimensional (3D) reconstruction of chemical distribution in a biological sample from the angle-dependent stimulated Raman scattering projection images. However, the projection image acquisition process requires rotating the sample contained in a capillary glass held by a complicated sample rotation stage, limiting the volumetric imaging speed, and inhibiting the study of living samples. Here, we report a tilt-angle stimulated Raman projection tomography (TSPRT) system which acquires angle-dependent projection images by utilizing tilt-angle beams to image the sample from different azimuth angles sequentially. The TSRPT system, which is free of sample rotation, enables rapid scanning of different views by a tailor-designed four-galvo-mirror scanning system. We present the design of the optical system, the theory, and calibration procedure for chemical tomographic reconstruction. 3D vibrational images of polystyrene beads and C. elegans are demonstrated in the C-H vibrational region.(c) 2022 Optica Publishing Group under the terms of the Optica Open Access Publishing Agreement

Published
2023

94. Global multi-stakeholder endorsement of the MAFLD definition

Author

Mendez-Sanchez, N, Bugianesi, E, Gish, R, Lammert, F, Tilg, H, Nguyen, M, Sarin, S, Fabrellas, N, Zelber-Sagi, S, Fan, J, Shiha, G, Targher, G, Zheng, M, Chan, W, Vinker, S, Kawaguchi, T, Castera, L, Yilmaz, Y, Korenjak, M, Spearman, C, Ungan, M, Palmer, M, El-Shabrawi, M, Gruss, H, Dufour, J, Dhawan, A, Wedemeyer, H, George, J, Valenti, L, Fouad, Y, Romero-Gomez, M, Eslam, M, Abate, M, Abbas, B, Abbassy, A, Abd El Ghany, W, Abd Elkhalek, A, Abd ElMajeed, E, Abdalgaber, M, Abdallah, M, Abdallah, N, Abdelaleem, S, Abdelghani, Y, Abdelghany, W, Abdelhalim, S, Abdelhamid, W, Abdelhamid, N, Abdelkader, N, Abdelkreem, E, Abdelmohsen, A, Abdelrahman, A, Abd-elsalam, S, Abdeltawab, D, Abduh, A, Abdulhakam, N, Abdulla, M, Abedpoor, N, Abenavoli, L, Aberg, F, Ablack, O, Abo elftouh, M, Abo-Amer, Y, Aboubkr, A, Aboud, A, Abouelnaga, A, Aboufarrag, G, Aboutaleb, A, Abundis, L, Adali, G, Adames, E, Adams, L, Adda, D, Adel, N, Adel Sayed, M, Afaa, T, Afredj, N, Aghayeva, G, Aghemo, A, Aguilar-Salinas, C, Ahlenstiel, G, Ahmady, W, Ahmed, W, Ahmed, A, Ahmed, S, Ahmed, H, Ahmed, R, Aigner, E, Akarsu, M, Akroush, M, Akyuz, U, Al Mahtab, M, Al Qadiri, T, Al Rawahi, Y, AL rubaee, R, Al Saffar, M, Alam, S, Al-Ani, Z, Albillos, A, Alboraie, M, Al-Busafi, S, Al-Emam, M, Alharthi, J, Ali, K, Ali, B, Ali, M, Ali, R, Alisi, A, AL-Khafaji, A, Alkhatry, M, Aller, R, Almansoury, Y, Al-Naamani, K, Alnakeeb, A, Alonso, A, Alqahtani, S, Alrabadi, L, Alswat, K, Altaher, M, Altamimi, T, Altamirano, J, Alvares-da-Silva, M, Aly, E, Alzahaby, A, Alzamzamy, A, Amano, K, Amer, M, Amin, M, Amin, S, Amir, A, Ampuero, J, Anas, N, Andreone, P, Andriamandimby, S, Anees, M, Angela, P, Antonios, M, Arafat, W, Araya, J, Armendariz-Borunda, J, Armstrong, M, Ashktorab, H, Aspichueta, P, Assal, F, Atef, M, Attia, D, Atwa, H, Awad, R, Awad, M, Awny, S, Awolowo, O, Awuku, Y, Ayada, I, Aye, T, Ayman, S, Ayman, H, Ayoub, H, Azmy, H, Babaran, R, Badreldin, O, Badry, A, Bahcecioglu, I, Bahour, A, Bai, J, Balaban, Y, Balasubramanyam, M, Bamakhrama, K, Banales, J, Bangaru, B, Bao, J, Barahona, J, Barakat, S, Barbalho, S, Barbra, B, Barranco, B, Barrera, F, Baumann, U, Bazeed, S, Bech, E, Benayad, A, Benesic, A, Bernstein, D, Bessone, F, Birney, S, Bisseye, C, Blake, M, Bobat, B, Bonfrate, L, Bordin, D, Bosques-Padilla, F, Boursier, J, Boushab, B, Bowen, D, Bravo, P, Brennan, P, Bright, B, Broekaert, I, Buque, X, Burgos-Santamaria, D, Burman, J, Busetto, L, Byrne, C, Cabral-Prodigalidad, P, Cabrera-Alvarez, G, Cai, W, Cainelli, F, Caliskan, A, Canbay, A, Cano-Contreras, A, Cao, H, Cao, Z, Carrion, A, Carubbi, F, Casanovas, T, Castellanos Fernandez, M, Chai, J, Chan, S, Charatcharoenwitthaya, P, Chavez-Tapia, N, Chayama, K, Chen, J, Chen, L, Chen, Z, Chen, H, Chen, S, Chen, Q, Chen, Y, Chen, G, Chen, E, Chen, F, Chen, P, Cheng, R, Cheng, W, Chieh, J, Chokr, I, Cholongitas, E, Choudhury, A, Chowdhury, A, Chukwudike, E, Ciardullo, S, Clayton, M, Clement, K, Cloa, M, Coccia, C, Collazos, C, Colombo, M, Cosar, A, Cotrim, H, Couillerot, J, Coulibaly, A, Crespo, G, Crespo, J, Cruells, M, Cua, I, Dabbous, H, Dalekos, G, D'Alia, P, Dan, L, Dao, V, Darwish, M, Datz, C, Davalos-Moscol, M, Dawoud, H, de Careaga, B, de Knegt, R, de Ledinghen, V, de Silva, J, Debzi, N, Decraecker, M, Del Pozo, E, Delgado, T, Delgado-Blanco, M, Dembinski, L, Depina, A, Derbala, M, Desalegn, H, Desbois-Mouthon, C, Desoky, M, Dev, A, Di Ciaula, A, Diago, M, Diallo, I, Diaz, L, Dirchwolf, M, Dongiovanni, P, Dorofeyev, A, Dou, X, Douglas, M, Doulberis, M, Dovia, C, Doyle, A, Dragojevic, I, Drenth, J, Duan, X, Dulskas, A, Dumitrascu, D, Duncan, O, Dusabejambo, V, Dwawhi, R, Eiketsu, S, El Amrousy, D, El Deeb, A, El Deriny, G, El Din, H, El Kamshishy, S, El Kassas, M, El Raziky, M, Elagamy, O, Elakel, W, Elalfy, D, Elaraby, H, Elawady, H, Elbadawy, R, Eldash, H, Eldefrawy, M, Elecharri, C, Elfaramawy, A, Elfatih, M, Elfiky, M, Elgamsy, M, Elgendy, M, El-Guindi, M, Elhussieny, N, Eliwa, A, Elkabbany, Z, El-Khayat, H, El-Koofy, N, Elmetwalli, A, Elrabat, A, El-Raey, F, Elrashdy, F, Elsahhar, M, Elsaid, E, Elsayed, S, Elsayed, H, Elsayed, A, El-Serafy, M, Elsharkawy, A, Elsheemy, R, Elshemy, E, Elsherbini, S, Eltoukhy, N, Elwakil, R, Emad, O, Emad, S, Embabi, M, Ergenc, I, Ermolova, T, Esmat, G, Esmat, D, Estupinan, E, Ettair, S, Eugen, T, Ezz-Eldin, M, Falcon, L, Fan, Y, Fandari, S, Farag, M, Farahat, T, Fares, E, Fares, M, Fassio, E, Fathy, H, Fathy, D, Fathy, W, Fayed, S, Feng, D, Feng, G, Fernandez-Bermejo, M, Ferreira, C, Ferrer, J, Forbes, A, Fouad, R, Fouad, H, Frisch, T, Fujii, H, Fukunaga, S, Fukunishi, S, Fulya, H, Furuhashi, M, Gaber, Y, Galang, A, Gallardo, J, Galloso, R, Gamal, M, Gamal, R, Gamal, H, Gan, J, Ganbold, A, Gao, X, Garas, G, Garba, T, Garcia-Cortes, M, Garcia-Monzon, C, Garcia-Samaniego, J, Gastaldelli, A, Gatica, M, Gatley, E, Gegeshidze, T, Geng, B, Ghazinyan, H, Ghoneem, S, Giacomelli, L, Giannelli, G, Giannini, E, Giefer, M, Gines, P, Girala, M, Giraudi, P, Goh, G, Gomaa, A, Gong, B, Gonzales, D, Gonzalez, H, Gonzalez-Huezo, M, Graupera, I, Grgurevic, I, Gronbaek, H, Gu, X, Guan, L, Gueye, I, Guingane, A, Gul, O, Gul, C, Guo, Q, Gupta, P, Gurakar, A, Gutierrez, J, Habib, G, Hafez, A, Hagman, E, Halawa, E, Hamdy, O, Hamed, A, Hamed, D, Hamid, S, Hamoudi, W, Han, Y, Haridy, J, Haridy, H, Harris, D, Hart, M, Hasan, F, Hashim, A, Hassan, I, Hassan, A, Hassan, E, Hassan, M, Hassanin, F, Hassnine, A, Haukeland, J, Hawal, A, He, J, He, Q, He, Y, He, F, Hegazy, M, Hegazy, A, Henegil, O, Hernandez, N, Hernandez-Guerra, M, Higuera-de-la-Tijera, F, Hindy, I, Hirota, K, Ho, L, Hodge, A, Hosny, M, Hou, X, Huang, J, Huang, Y, Huang, Z, Huang, A, Huang, X, Hui-ping, S, Hunyady, B, Hussein, M, Hussein, O, Hussien, S, Ibanez-Samaniego, L, Ibdah, J, Ibrahim, L, Ibrahim, M, Ibrahim, I, Icaza-Chavez, M, Idelbi, S, Idilman, R, Ikeda, M, Indolfi, G, Invernizzi, F, Irshad, I, Isa, H, Iskandar, N, Ismaiel, A, Ismail, M, Ismail, Z, Ismail, F, Iwamoto, H, Jack, K, Jacob, R, Jafarov, F, Jafri, W, Jahshan, H, Jalal, P, Jancoriene, L, Janicko, M, Jayasena, H, Jefferies, M, Jha, V, Ji, F, Ji, Y, Jia, J, Jiang, C, Jiang, N, Jiang, Z, Jin, X, Jin, Y, Jing, X, Jingyu, Q, Jinjolava, M, Jong, F, Jucov, A, Julius, I, Kaddah, M, Kamada, Y, Kamal, A, Kamal, E, Kamel, A, Kao, J, Karin, M, Karlas, T, Kashwaa, M, Katsidzira, L, Kaya, E, Kayasseh, M, Keenan, B, Keklikkiran, C, Keml, W, Khalaf, D, Khalefa, R, Khamis, S, Khater, D, Khattab, H, Khavkin, A, Khlynova, O, Khmis, N, Kobyliak, N, Koffas, A, Koike, K, Kok, K, Koller, T, Komas, N, Korochanskaya, N, Koulla, Y, Koya, S, Kraft, C, Kraja, B, Krawczyk, M, Kuchay, M, Kulkarni, A, Kumar, A, Kumar, M, Lakoh, S, Lam, P, Lan, L, Lange, N, Lankarani, K, Lanthier, N, Lapshyna, K, Lashen, S, Laure, K, Lazebnik, L, Lebrec, D, Lee, S, Lee, W, Lee, Y, Leeming, D, Leite, N, Leon, R, Lesmana, C, Li, J, Li, Q, Li, Y, Li, L, Li, M, Liang, H, Lijuan, T, Lim, S, Lim, L, Lin, S, Lin, H, Lin, R, Lithy, R, Liu, Y, Liu, X, Liu, W, Liu, S, Liu, K, Liu, T, Lonardo, A, Lopez, M, Lopez-Benages, E, Lopez-Jaramillo, P, Lu, H, Lu, L, Lu, Y, Lubel, J, Lui, R, Lupasco, I, Luzina, E, Lv, X, Lynch, K, Ma, H, Machado, M, Maduka, N, Madzharova, K, Magdaong, R, Mahadeva, S, Mahfouz, A, Mahmood, N, Mahmoud, E, Mahrous, M, Maiwall, R, Majeed, A, Majumdar, A, Mak, L, Maklouf, M, Malekzadeh, R, Mandato, C, Mangia, A, Mann, J, Mansour, H, Mansouri, A, Mantovani, A, Mao, J, Maramag, F, Marchesini, G, Marcus, C, Marinho, R, Martinez-Chantar, M, Martins, A, Marwan, R, Mason, K, Masoud, G, Massoud, M, Matamoros, M, Mateos, R, Mawed, A, Mbanya, J, Mbendi, C, Mccolaugh, L, Mcleod, D, Medina, J, Megahed, A, Mehrez, M, Memon, I, Merat, S, Mercado, R, Mesbah, A, Meskini, T, Metwally, M, Metwaly, R, Miao, L, Micah, E, Miele, L, Milivojevic, V, Milovanovic, T, Mina, Y, Mishkovik, M, Mishriki, A, Mitchell, T, Mohamed, A, Mohamed, M, Mohamed, S, Mohammed, S, Mohammed, A, Mohan, V, Mohie, S, Mokhtar, A, Moniem, R, Montilla, M, Morales, J, Morata, M, Moreno-Planas, J, Morise, S, Mosaad, S, Moselhy, M, Mostafa, A, Mostafa, E, Mouane, N, Mousa, N, Moustafa, H, Msherif, A, Muller, K, Munoz, C, Munoz-Urribarri, A, Murillo, O, Mustapha, F, Muzurovic, E, Nabil, Y, Nafady, S, Nagamatsu, A, Nakajima, A, Nakano, D, Nan, Y, Nascimbeni, F, Naseef, M, Nashat, N, Natalia, T, Negro, F, Nersesov, A, Neuman, M, Ng'Wanasayi, M, Ni, Y, Nicoll, A, Niizeki, T, Nikolova, D, Ningning, W, Niriella, M, Nogoibaeva, K, Nordien, R, O Sullivan, C, O'Beirne, J, Obekpa, S, Ocama, P, Ochwoto, M, Ogolodom, M, Ojo, O, Okrostsvaridze, N, Oliveira, C, Omana, R, Omar, O, Omar, H, Omar, M, Omran, S, Omran, R, Osman, M, Owise, N, Owusu-Ansah, T, Padilla- Machaca, P, Palle, S, Pan, Z, Pan, X, Pan, Q, Papaefthymiou, A, Paquissi, F, Par, G, Parkash, A, Payawal, D, Peltekian, K, Peng, X, Peng, L, Peng, Y, Pengoria, R, Perez, M, Perez, J, Perez, N, Persico, M, Pessoa, M, Petta, S, Philip, M, Plaz Torres, M, Polavarapu, N, Poniachik, J, Portincasa, P, Pu, C, Purnak, T, Purwanto, E, Qi, X, Qian, Z, Qiang, Z, Qiao, Z, Qiao, L, Queiroz, A, Rabiee, A, Radwan, M, Rahetilahy, A, Ramadan, Y, Ramadan, D, Ramli, A, Ramm, G, Ran, A, Rankovic, I, Rao, H, Raouf, S, Ray, S, Reau, N, Refaat, A, Reiberger, T, Remes-Troche, J, Reyes, E, Richardson, B, Ridruejo, E, Riestra Jimenez, S, Rizk, I, Roberts, S, Roblero, J, Robles, J, Rockey, D, Rodriguez, M, Rodriguez Hernandez, H, Roman, E, Romeiro, F, Romeo, S, Rosales-Zabal, J, Roshdi, G, Rosso, N, Ruf, A, Ruiz, P, Runes, N, Ruzzenente, A, Ryan, M, Saad, A, Sabbagh, E, Sabbah, M, Saber, S, Sabrey, R, Sabry, R, Saeed, M, Said, D, Said, E, Sakr, M, Salah, Y, Salama, R, Salama, A, Saleh, H, Saleh, A, Salem, A, Salifou, A, Salih, A, Salman, A, Samouda, H, Sanai, F, Sanchez-Avila, J, Sanker, L, Sano, T, Sanz, M, Saparbu, T, Sawhney, R, Sayed, F, Sayed, S, Sayed, A, Sayed, M, Sebastiani, G, Secadas, L, Sediqi, K, Seif, S, Semida, N, Senates, E, Serban, E, Serfaty, L, Seto, W, Sghaier, I, Sha, M, Shabaan, H, Shalaby, L, Shaltout, I, Sharara, A, Sharma, V, Shawa, I, Shawkat, A, Shawky, N, Shehata, O, Sheils, S, Shewaye, A, Shi, G, Shi, J, Shimose, S, Shirono, T, Shou, L, Shrestha, A, Shui, G, Sievert, W, Sigurdardottir, S, Sira, M, Siradj, R, Sison, C, Smyth, L, Soliman, R, Sollano, J, Sombie, R, Sonderup, M, Sood, S, Soriano, G, Stedman, C, Stefanyuk, O, Stimac, D, Strasser, S, Strnad, P, Stuart, K, Su, W, Su, M, Sumida, Y, Sumie, S, Sun, D, Sun, J, Suzuki, H, Svegliati-Baroni, G, Swar, M, Taharboucht, S, Taher, Z, Takamura, S, Tan, L, Tan, S, Tanwandee, T, Tarek, S, Tatiana, G, Tavaglione, F, Tecson, G, Tee, H, Teschke, R, Tharwat, M, Thong, V, Thursz, M, Tine, T, Tiribelli, C, Tolmane, I, Tong, J, Tongo, M, Torkie, M, Torre, A, Torres, E, Trajkovska, M, Treeprasertsuk, S, Tsutsumi, T, Tu, T, Tur, J, Turan, D, Turcan, S, Turkina, S, Tutar, E, Tzeuton, C, Ugiagbe, R, Uygun, A, Vacca, M, Vajro, P, Van der Poorten, D, Van Kleef, L, Vashakidze, E, Velazquez, C, Velazquez, M, Vento, S, 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G., Lammert F., Tilg H., Nguyen M. H., Sarin S. K., Fabrellas N., Zelber-Sagi S., Fan J. -G., Shiha G., Targher G., Zheng M. -H., Chan W. -K., Vinker S., Kawaguchi T., Castera L., Yilmaz Y., Korenjak M., Spearman C. W., Ungan M., Palmer M., El-Shabrawi M., Gruss H. -J., Dufour J. -F., Dhawan A., Wedemeyer H., George J., Valenti L., Fouad Y., Romero-Gomez M., Eslam M., Abate M. L., Abbas B., Abbassy A. A., Abd El Ghany W., Abd Elkhalek A., Abd ElMajeed E., Abdalgaber M., AbdAllah M., Abdallah M., Abdallah N., Abdelaleem S., Abdelghani Y., Abdelghany W., Abdelhalim S. M., Abdelhamid W., Abdelhamid N., Abdelkader N. A., Abdelkreem E., Abdelmohsen A. M., Abdelrahman A. A., Abd-elsalam S. M., Abdeltawab D., Abduh A., Abdulhakam N., Abdulla M., Abedpoor N., Abenavoli L., Aberg F., Ablack O., Abo elftouh M., Abo-Amer Y. E. -E., Aboubkr A., Aboud A., Abouelnaga A. M., Aboufarrag G. A., Aboutaleb A., Abundis L., Adali G., Adames E., Adams L., Adda D., Adel N., Adel Sayed M., Afaa T. 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H., Hamid S., Hamoudi W., Han Y., Haridy J., Haridy H., Harris D. C. H. H., Hart M., Hasan F., Hashim A., Hassan I., Hassan A., Hassan E. A., Hassan A. A., Hassan M. S., Hassanin F., Hassnine A., Haukeland J. W., Hawal A. I. M., He J., He Q., He Y., He F. -P., Hegazy M., Hegazy A., Henegil O., Hernandez N., Hernandez-Guerra M., Higuera-de-la-Tijera F., Hindy I., Hirota K., Ho L. C., Hodge A., Hosny M., Hou X., Huang J. -F., Huang Y., Huang Z., Huang A., Huang X. -P., Hui-ping S., Hunyady B., Hussein M. A., Hussein O., Hussien S. M., Ibanez-Samaniego L., Ibdah J., Ibrahim L., Ibrahim M., Ibrahim I., Icaza-Chavez M. E., Idelbi S., Idilman R. I., Ikeda M., Indolfi G., Invernizzi F., Irshad I., Isa H. M. A., Iskandar N. J., Ismaiel A., Ismail M., Ismail Z., Ismail F., Iwamoto H., Jack K., Jacob R., Jafarov F., Jafri W., Jahshan H., Jalal P. K., Jancoriene L., Janicko M., Jayasena H., Jefferies M., Jha V., Ji F., Ji Y., Jia J., Jiang C., Jiang N., Jiang Z. -Z., Jin X., Jin Y., Jing X., Jingyu Q., Jinjolava M., Jong F. H. H., Jucov A., Julius I., Kaddah M., Kamada Y., kamal A., Kamal E. M., Kamel A. S., Kao J. -H., Karin M., Karlas T., Kashwaa M., Katsidzira L., Kaya E., Kayasseh M. A., Keenan B., Keklikkiran C., Keml W., Khalaf D. K., Khalefa R., Khamis S., Khater D., khattab H., Khavkin A., Khlynova O., Khmis N., Kobyliak N., Koffas A., Koike K., Kok K. Y. Y., Koller T., Komas N. P., Korochanskaya N. V., Koulla Y., Koya S., Kraft C., Kraja B., Krawczyk M., Kuchay M. S., Kulkarni A. V., Kumar A., Kumar M., Lakoh S., Lam P., Lan L., Lange N. F., Lankarani K. B., Lanthier N., Lapshyna K., Lashen S. A., Laure K. N. J., Lazebnik L., Lebrec D., Lee S. S., Lee W. S., Lee Y. Y., Leeming D. J., Leite N. C., Leon R., Lesmana C. R. A., Li J., Li Q., Li Y. -Y., Li Y., Li L., Li M., li Y., Liang H., Lijuan T., Lim S. G., Lim L. -L., Lin S., Lin H. -C., Lin R., Lithy R., Liu Y., Liu X., Liu W. -Y., Liu S., Liu K., Liu T., Lonardo A., Lopez M. B., Lopez-Benages E., Lopez-Jaramillo P., Lu H., Lu L. G., Lu Y., Lubel J., Lui R., Lupasco I., Luzina E., Lv X. -H., Lynch K., Ma H. -L., Machado M. V., Maduka N., Madzharova K., Magdaong R., Mahadeva S., Mahfouz A., Mahmood N. R. K. N., Mahmoud E., Mahrous M., Maiwall R., Majeed A., Majumdar A., Mak L., Maklouf M. M., Malekzadeh R., Mandato C., Mangia A., Mann J., Mansour H. H., Mansouri A., Mantovani A., Mao J. Q., Maramag F., Marchesini G., Marcus C., Marinho R. A. R. T., Martinez-Chantar M. L., Martins A. A. S., Marwan R., Mason K. F., Masoud G., Massoud M. N., Matamoros M. A., Mateos R. M., Mawed A., Mbanya J. C., Mbendi C., McColaugh L., McLeod D., Medina J. F. R., Megahed A., Mehrez M., Memon I., Merat S., Mercado R., Mesbah A., Meskini T., Metwally M., Metwaly R., Miao L., Micah E., Miele L., Milivojevic V., Milovanovic T., Mina Y. L., Mishkovik M., Mishriki A., Mitchell T., Mohamed A., Mohamed M., Mohamed S., Mohammed S., Mohammed A., Mohan V., Mohie S., Mokhtar A., Moniem R., Montilla M. S., Morales J. A. O., Morata M. M. S., Moreno-Planas J. M., Morise S., Mosaad S., Moselhy M., Mostafa A. M., Mostafa E., Mouane N., Mousa N., Moustafa H. M., Msherif A., Muller K., Munoz C., Munoz-Urribarri A. B., Murillo O. A., Mustapha F. I., Muzurovic E., Nabil Y., Nafady S., Nagamatsu A., Nakajima A., Nakano D., Nan Y., Nascimbeni F., Naseef M. S., Nashat N., Natalia T., Negro F., Nersesov A. V., Neuman M., Ng'wanasayi M., Ni Y., Nicoll A., Niizeki T., Nikolova D., Ningning W., Niriella M., Nogoibaeva K. A., Nordien R., O Sullivan C., O'Beirne J., Obekpa S., Ocama P., Ochwoto M., Ogolodom M. P., Ojo O., Okrostsvaridze N., Oliveira C. P., Omana R. C., Omar O. M., Omar H., Omar M., Omran S., Omran R., Osman M. M., Owise N., Owusu-Ansah T., Padilla- Machaca P. M., Palle S., Pan Z., Pan X. -Y., Pan Q., Papaefthymiou A., Paquissi F. C., Par G., Parkash A., Payawal D., Peltekian K. M., Peng X., Peng L., Peng Y., Pengoria R., Perez M., Perez J. L., Perez N. M., Persico M., Pessoa M. G., Petta S., Philip M., Plaz Torres M. C., Polavarapu N., Poniachik J., Portincasa P., Pu C., Purnak T., Purwanto E., Qi X., Qian Z., Qiang Z., Qiao Z., Qiao L., Queiroz A., Rabiee A., Radwan M., Rahetilahy A. M., Ramadan Y., Ramadan D., Ramli A. S., Ramm G. A., Ran A., Rankovic I., RAO H., Raouf S., Ray S., Reau N., Refaat A., Reiberger T., Remes-Troche J. M., Reyes E. C., Richardson B., Ridruejo E., Riestra Jimenez S., Rizk I., Roberts S., Roblero J. P., Robles J. A. P., Rockey D., Rodriguez M., Rodriguez Hernandez H., Roman E., Romeiro F. G., Romeo S., Rosales-Zabal J. M., Roshdi G. R., Rosso N., Ruf A., Ruiz P. C., Runes N. R., Ruzzenente A., Ryan M., Saad A., Sabbagh E. B., Sabbah M., Saber S., Sabrey R., Sabry R., Saeed M. A., Said D., Said E. M., Sakr M. A., Salah Y., Salama R. M., Salama A., Saleh H., Saleh A., Salem A., Salem A. T., Salifou A., Salih A. F., Salman A., Samouda H., Sanai F., Sanchez-Avila J. F., Sanker L., Sano T., Sanz M., Saparbu T., Sawhney R., Sayed F., Sayed S. A., Sayed A. O., Sayed M., Sebastiani G., Secadas L., Sediqi K. Q., Seif S., Semida N., Senates E., Serban E. D., Serfaty L., Seto W. -K., Sghaier I., Sha M., Shabaan H. M., Shalaby L., Shaltout I., Sharara A. I., Sharma V., Shawa I. T., Shawkat A., Shawky N., Shehata O., Sheils S., Shewaye A. B., Shi G., Shi J., Shimose S., Shirono T., Shou L., Shrestha A., Shui G., Sievert W., Sigurdardottir S., Sira M. M., Siradj R., Sison C., Smyth L., Soliman R., Sollano J. D., Sombie R., Sonderup M., Sood S., Soriano G., Stedman C. A. M., Stefanyuk O., Stimac D., Strasser S., Strnad P., Stuart K., Su W., Su M., Sumida Y., Sumie S., Sun D. -Q., Sun J., Suzuki H., Svegliati-Baroni G., Swar M. O., TAHARBOUCHT S., Taher Z., Takamura S., Tan L., Tan S. -S., Tanwandee T., Tarek S., Tatiana G., Tavaglione F., Tecson G. Y., Tee H. -P., Teschke R., Tharwat M., Thong V. D., Thursz M., Tine T., Tiribelli C., Tolmane I., Tong J., Tongo M., Torkie M., Torre A., Torres E. A., Trajkovska M., Treeprasertsuk S., Tsutsumi T., Tu T., Tur J. A., Turan D., Turcan S., Turkina S., Tutar E., Tzeuton C., Ugiagbe R., Uygun A., Vacca M., Vajro P., Van der Poorten D., Van Kleef L. A., Vashakidze E., Velazquez C. M., Velazquez M. I., Vento S., Verhoeven V., Vespasiani-Gentilucci U., Vethakkan S. R., Vilaseca J., Vitek L., Volkanovska A., Wallace M., Wan W., Wang Y., Wang X., Wang C., Wang M., Wangchuk P., Weltman M., White M., Wiegand J., Wifi M. -N., Wigg A., Wilhelmi M., William R., Wittenburg H., Wu S., Wubeneh A. M., Xia H., Xiao J., Xiao X., Xiaofeng W., Xiong W., Xu L., Xu J., Xu W., Xu J. -H., Xu K., Xu Y., Xu S. -H., Xu M., Xu A., Xu C., Yan H., Yang J., Yang R. -X., Yang Y., Yang Q., Yang N., Yao J., Yara J., Yaras S., Yilmaz N., Younes R., younes H., Young S., Youssef F., Yu Y., Yu M. -L., Yuan J., Yue Z., Yuen M. -F., Yun W., Yurukova N., Zakaria S., Zaky S., Zaldastanishvili M., Zapata R., Zare N., Zerem E., Zeriban N., Zeshuai X., Zhang H., Zhang X., Zhang Y., Zhang W. -H., Zhang Y. -P., Zhang Z. -Q., Zhao J., Zhao R. -R., Zhao H., Zheng C., Zheng Y., Zheng R., Zheng T. -L., Zheng K., Zhou X. Q., Zhou Y., Zhou Y. -J., Zhou H., Zhou L., Zhu L. D., Zhu Y. F., Zhu Y., Zhu P. -W., Ziada E., Ziring D., Ziyi L., Zou S., Zou Z., Zou H., and Zuart Ruiz R.

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2022

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