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The UV-vis absorption characteristics and nonlinear optical properties of a series of substituted dihydroazulene (DHA)/vinylheptafulvene (VHF) photoswitches are investigated by applying quantum calculations. Introduction of substituents at the seven-membered ring resulted in significant changes in their absorption properties depending on the nature and position of the substituent. Electron-donating groups at positions 5, 6, 7, and 8 generally exhibited red shifts with respect to the parent compound. However, the steric effect at positions 8a and 4 is responsible for the loss of planarity and conjugation, which generally leads to blue shifts. In contrast, any electron-withdrawing group, particularly at positions 8a and 4, would cause a blue shift. The presence of bulky groups at position 8a results in a loss of planarity and, as a result, a decrease in electronic conjugation within the molecule, resulting in a blue shift in the maximum absorption. When it comes to halogens, the red shift is directly correlated to the nucleophilicity; the higher the nucleophilicity, the larger the red shift. Regarding hyperpolarizability, the charge separation induces higher hyperpolarizabilities for all substituted VHFs compared to the corresponding DHAs, resulting in a much higher NLO response. In addition, for all DHA and VHF, the highest values of hyperpolarizabilities are calculated for 6-substituted systems. Finally, the objective of this detailed theoretical investigation is to continue exploring the photophysical properties of DHA-VHF through structural modifications.

Biochar was prepared by the hydrothermal carbonization (HTC) of palm leaves, characterized, and utilized as an adsorbent for Malachite Green dye (MG). The Higher Heating Value (HHV) of biochar depends on the carbonization temperature and has a maximum value of 24.81 MJ/kg. Activation using H2O2 oxidation of HTC biochar prepared at 208 °C produced AHTC with improved capacity. The optimum pH was found to be in the range 7–8. Freundlich, Langmuir, Temkin, and Dubinin–Radushkevich adsorption isotherms were used to study MG adsorption data. The Langmuir isotherm provided the best fit for experimental data. Experiments conducted using activated biochar AHTC at 25 °C resulted in an adsorption capacity of 62.80 mg/g, far greater than what was observed for HTC biochar (45.59 mg/g). The maximum adsorption capacity was 88% when the concentration of MG solution was 66 ppm. The free energy change in adsorption DG° indicated that the adsorption process was spontaneous. Adsorption followed pseudo-second-order kinetics. Fixed-column adsorptions models, namely, Thomas, Yan et al. and Yoon–Nelson models, were investigated for AHTC. The column adsorption capacity determined by the Thomas model was 33.57 mg/g. In addition, a computational investigation has been carried out to determine the structural and electronic features, as well as the quantum chemical parameters of HTC and MG. Moreover, the interaction between the HTC and MG is investigated, which is further elaborated by performing non-covalent interaction (NCI) through the reduced density gradient (RDG) analysis. Thus, the easily prepared hydrochar from abundant waste palm leaves can be used as a high-value biocoal and efficient adsorbent of the cationic dye malachite green.

Electronic and nonlinear optical properties of endohedral metallofullerenes are presented. The endohedral metallofullerenes contain transition metal encapsulated in inorganic fullerenes X12Y12 (X = B, Al & Y = N, P). The endohedral metallofullerenes (endo-TM@X12Y12) possess quite interesting geometric and electronic properties, which are the function of the nature of the atom and the size of fullerene. NBO charge and frontier molecular orbital analyses reveal that the transition metal encapsulated Al12N12 fullerenes (endo-TM@Al12N12) are true metalides when the transition metals are Ni, Cu and Zn. Endo-Cr@Al12N12 and endo-Co@Al12N12 are at the borderline between metalides and electrides with predominantly electride characteristics. The other members of the series are excess electron systems, which offer interesting electronic and nonlinear optical properties. The diversity of nature possessed by endo-TM@Al12N12 is not prevalent for other fullerenes. Endo-TM@Al12P12 are true metalides when the transition metals are (Cr-Zn). HOMO-LUMO gaps (EH-L) are reduced significantly for these endohedral metallofullerenes, with a maximum percent decrease in EH-L of up to 70%. Many complexes show odd–even oscillating behavior for EH-L and dipole moments. Odd electron species contain large dipole moments and small EH-L, whereas even electron systems have the opposite behavior. Despite the decrease in EH-L, these systems show high kinetic and thermodynamic stabilities. The encapsulation of transition metals is a highly exergonic process. These endo-TM@X12Y12 possess remarkable nonlinear optical response in which the first hyperpolarizability reaches up to 2.79 × 105 au for endo-V@Al12N12. This study helps in the comparative analysis of the potential nonlinear optical responses of electrides, metalides and other excess electron systems. In general, the potential nonlinear optical response of electrides is higher than metalides but lower than those of simple excess electron compounds. The higher non-linear optical response and interesting electronic characteristics of endo-TM@Al12N12 complexes may be promising contenders for potential NLO applications.

Knockdown of HOTAIR inhibits EMT

Figure S1 depicts the location of CpG islands in promoter region of miR-182-5p

Table S1 is for primer sequences

Patient characteristics

Attenuation of HOTAIR promotes upregulation of PTEN, p21 and p27

This study aims to investigate the role of miR-203–HOTAIR interaction in the suppression of renal cell carcinoma (RCC). We employed series of in vitro assays such as proliferation, invasion, migration, and colony formation along with in vivo tumor xenograft model. Profiling of miR-203 and HOTAIR expression revealed that miR-203 was significantly underexpressed, whereas HOTAIR was overexpressed in RCC cell lines and clinical specimens compared with normal cell line and tissue. Both miR-203 and HOTAIR expression significantly distinguished malignant from normal tissues and significantly correlated with clinicopathologic characteristics of patients. Overexpression of miR-203 significantly inhibited proliferation, migration, and invasion with an induction of apoptosis and cell-cycle arrest. However, HOTAIR suppression resulted in the similar functional effects in the same RCC cell lines. In silico, RNA-22 algorithm showed a binding site for miR-203 in HOTAIR. We observed a direct interaction between miR-203 and HOTAIR by RNA-immunoprecipitation (RIP) and luciferase reporter assays. We show that miR-203–HOTAIR interaction resulted in the inhibition of epithelial-to-mesenchymal transition (EMT) and metastatic genes as indicated by induction of key metastasis-suppressing proteins E-cadherin, claudin (epithelial markers), and PTEN along with induction of tumor suppressor genes p21 and p27. A significant decrease in vimentin (mesenchymal marker), KLF4, and Nanog (stemness markers) was also observed. This is the first report demonstrating miR-203–mediated regulation of HOTAIR induces tumor suppressor effects in RCC by regulating EMT and metastatic pathway genes. Thus, the study suggests that therapeutic regulation of HOTAIR by miR-203 overexpression may provide an opportunity to regulate RCC growth and metastasis. Mol Cancer Ther; 17(5); 1061–9. ©2018 AACR.

Table S2 is for Patient Characteristics

Figure S2 depicts the significantly de-regulated pathways based on KEGG and Reactome

Despite the adoption of Six-Sigma in different service sectors, its application in the Sales function of a Technology-based Start-up has not been explored. This paper deploys an action research-based study methodology and conducts a thorough analysis of a Technology Start-up company in Indonesia, using Six-Sigma principles and the Define-Measure-Analyse-Improve-Control (DMAIC) approach. Statistical validation of the causes of problems helped to formulate a strategy that may have otherwise not been possible. The results of the study and proposed solutions confirm the potential benefits of adopting Six-Sigma in the Sales function of technology start-ups to reduce, particularly, customer waiting time. The novelty of this research lies in the fact that it applies Six-Sigma in a transactional process such as sales, which earlier studies have not explored in depth. This paper can be employed as a reference for organisations to undertake and guide specific process improvement projects similar to the one presented.

Currently, hydrogen is recognized as the best alternative for fossil fuels because of its sustainable nature and environmentally friendly processing. In this study, hydrogen dissociation reaction is studied theoretically on the transition metal doped carbon nitride (C

The corrosion inhibition effect of the three extracts from Harmal roots (HRE), leaves (HLE), and flowers (HFE) were studied for carbon steel corrosion inhibition in 0.25 M H2SO4 solution. The electrochemical impedance study indicated that the three types of extracts decreased corrosion effectively through a charge transfer mechanism. Harmal roots and leaf extracts showed inhibition values of 94.1% and 94.2%, while it was 88.7% for Harmal flower extract at the inhibitor concentration of 82.6 ppm. Potentiodynamic polarization data revealed that Harmal extracts acted through predominant cathodic type inhibition. Both the corrosion current density and corrosion rate decreased significantly in the presence of Harmal extracts compared to blank solution. The corrosion rate (mpy) value was 63.3, 86.1, and 180.7 for HRE, HLE, and HFE, respectively. The adsorption-free energy change ΔGads (kJ·mol−1) values calculated from the Langmuir adsorption isotherm plots were for HRE (−35.08), HLE (−33.17), and HFE (−33.12). Thus, corrosion inhibition occurred due to the adsorption of Harmal extract on the carbon steel surface via the chemisorption mechanism. Moreover, a computational investigation using B3LYP/6-311G++(d,p) basis set in both gaseous and aqueous phases was performed for the major alkaloids (1–8) present in the Harmal extract.

Background H. pylori infection is the main risk factor for gastric cancer. In this study, we investigated H. pylori-mediated activation of STAT3 and NF-κB in gastric cancer, using in vitro and in vivo models. Methods To investigate the activation of NF-κB and STAT3 by H. pylori strains we used in vitro and in vivo mouse models, western blots, immunofluorescence, ChIP Assay, luciferase and quantitative real-time PCR assays. Results Following infection with H. pylori in vitro, we found an earlier phosphorylation of NF-kB-p65 (S536), followed by STAT3 (Y705). Immunofluorescence, using in vitro and in vivo models, demonstrated nuclear localization of NF-kB and STAT3, following H. pylori infection. NF-kB and STAT3 luciferase reporter assays confirmed earlier activation of NF-kB followed by STAT3. In vitro and in vivo models demonstrated induction of mRNA expression of IL-6 (p VEGF-α (p IL-17 (p IL-23 (p IL6 promoter. The reconstitution of Trefoil Factor 1 (TFF1) suppressed activation of NF-kB with reduction in IL6 levels and STAT3 activity, in response to H. pylori infection. Using pharmacologic (BAY11-7082) and genetic (IκB super repressor (IκBSR)) inhibitors of NF-kB-p65, we confirmed the requirement of NF-kB-p65 for activation of STAT3, as measured by phosphorylation, transcription activity, and nuclear localization of STAT3 in in vitro and in vivo models. Conclusion Our findings suggest the presence of an early autocrine NF-kB-dependent activation of STAT3 in response to H. pylori infection. TFF1 acts as an anti-inflammatory guard against H. pylori-mediated activation of pro-inflammatory networks.

Modern communication systems look for higher operating frequencies to find more bandwidth to enable higher data rates. At a same time, these systems use larger and larger antenna arrays to compensate for the increased propagation losses by using antenna directivity. Often these systems use phased array approach for realizing steerable beam patterns. In phased arrays, the signal is usually divided in analogue domain to multiple transmit paths and combined in analogue domain from multiple receive paths. In this thesis, the aim is to generate a wideband modelling approach for analog signal routing in phased array transceivers that use radio frequency (RF) beamforming. In particular, the aim is to model the transfer functions of different signal paths from the sum node of all paths to the individual antennas and finally to the free space, to form a three-dimensional beam pattern that has frequency selective beam squint. The modelling approach and their behaviour in different symmetric and asymmetric beamforming architectures are presented and the performance of the system is observed through simulations by using beam patterns and equivalent amplitude responses in different directions. The impacts of array size, steering angle, and relative bandwidth are studied for the observed beam squint with different signal routing architectures to find their bandwidth limitations in different scenarios. The routing model also includes the impact of the dielectric materials of the circuit implementations.

The toxicity of transition metals, including copper(II), manganese(II), iron(II), zinc(II), hexavalent chromium, and cobalt(II), at elevated concentrations presents a significant threat to living organisms. Thus, the development of efficient sensors capable of detecting these metals is of utmost importance. This study explores the utilization of two-dimensional nitrogenated holey graphene (C2N) nanosheet as a sensor for toxic transition metals. The C2N nanosheet’s periodic shape and standard pore size render it well suited for adsorbing transition metals. The interaction energies between transition metals and C2N nanosheets were calculated in both gas and solvent phases and were found to primarily result from physisorption, except for manganese and iron which exhibited chemisorption. To assess the interactions, we employed NCI, SAPT0, and QTAIM analyses, as well as FMO and NBO analysis, to examine the electronic properties of the TM@C2N system. Our results indicated that the adsorption of copper and chromium significantly reduced the HOMO–LUMO energy gap of C2N and significantly increased its electrical conductivity, confirming the high sensitivity of C2N towards copper and chromium. The sensitivity test further confirmed the superior sensitivity and selectivity of C2N towards copper. These findings offer valuable insight into the design and development of sensors for the detection of toxic transition metals.

Background: Fibroblast growth factor receptor 4 (FGFR4) is a member of the transmembrane tyrosine kinase receptor family and has been linked to a variety of malignancies. NRF2 (Nuclear factor-erythroid 2-related factor) is a cytoprotective factor and a critical regulator in the antioxidant response pathway. In this study, we sought to uncover novel functions of FGFR4 and its role in regulating the antioxidant response in gastric carcinogenesis. Methods and Results: Using western blot and immunofluorescence, H. pylori infection in gastric cancer cell lines demonstrated high levels of reactive oxygen species and induction of both FGFR4 and NRF2. Using Flow cytometry, FGFR4 silencing resulted in decrease of NRF2 with a significant spike in ROS levels and an increase in DNA damage and cell death. FGFR4 knockdown showed a significant decrease in NRF2 transcriptional activity as measured by NRF2 ARE luciferase reporter assay and resulted in reduced mRNA levels of HO-1 (Heme Oxygenase-1), which is a classical target of NRF2. These results were confirmed by immunofluorescence showing a significant increase of nuclear accumulation of NRF2 after H. pylori infection which was abolished after FGFR4 knockdown. Similar results were found using recombinant protein FGF19, a FGFR4 ligand. C57/B6 wild-type mice were infected with the pylori strain (PMSS1). An increase in FGFR4, NRF2, and HO-1 was seen by immunofluorescence, Western blot, and quantitative real-time PCR in H. pylori-infected mice vs control mice. We observed a reduction in NRF2 in our in vitro and in vivo models using H3B-6527, a specific FGFR4 inhibitor. We also discovered an association between an increase in FGFR4 and P62 protein expressions and NRF2 protein stability. We detected a significant increase in FGFR4, NRF2, and HO1 in dysplastic and neoplastic gastric lesions using the TFF1-KO mouse model which was further aggravated by H. pylori infection. In terms of the mechanism, utilizing proximity ligation and immunoprecipitation assays, we found that FGFR4 binds to P62 to inhibit the interaction between NRF2 and KEAP1, allowing NRF2 to avoid degradation facilitating its translocation and accumulation in the nucleus. Conclusion: These findings revealed that FGFR4 has a unique functional role in promoting gastric carcinogenesis by mediating accumulation and activation of the NRF2 antioxidant response. The use of FGFR4 inhibitors is a viable treatment option that warrants further research in patients with gastric cancer. Citation Format: Nadeem S. Bhat, Mohammed Soutto, Xing Zhang, Zheng Chen, Ahmed Gomaa, Marwah Al-Mathkour, Selma Maacha, Heng Lu, Dunfa Peng, Zekuan Xu, Wael El-Rifai. Helicobacter pylori-induced FGFR4 mediates nuclear accumulation of NRF2 in gastric tumorigenesis [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2023; Part 1 (Regular and Invited Abstracts); 2023 Apr 14-19; Orlando, FL. Philadelphia (PA): AACR; Cancer Res 2023;83(7_Suppl):Abstract nr 2592.

Zigzag molecular nanobelts have recently captured the interest of scientists because of their appealing aesthetic structures, intriguing chemical reactivities, and tantalizing features. In the current study, first-row transition metals supported on an H6-N3-belt[6]arene nanobelt are investigated for the electrocatalytic properties of these complexes for the hydrogen dissociation reaction (HDR). The interaction of the doped transition metal atom with the nanobelt is evaluated through interaction energy analysis, which reveals the significant thermodynamic stability of TM-doped nanobelt complexes. Electronic properties such as frontier molecular orbitals and natural bond orbitals analyses are also computed, to estimate the electronic perturbation upon doping. The highest reduction in the HOMO–LUMO energy gap compared to the bare nanobelt is seen in the case of the Zn@NB catalyst (4.76 eV). Furthermore, for the HDR reaction, the Sc@NB catalyst displays the best catalytic activity among the studied catalysts, with a hydrogen dissociation barrier of 0.13 eV, whereas the second-best catalytic activity is observed for the Zn@NB catalyst (0.36 eV). It is further found that multiple active sites, i.e., the presence of the metal atom and nitrogen atom moiety, help to facilitate the dissociation of the hydrogen molecule. These key findings of this study enhance the understanding of the relative stability, electronic features, and catalytic bindings of various TM@NB catalysts.

In this work it is demonstrated that enantiomerically enriched N-alkyl 2-oxazolinylazetidines undergo exclusive α-lithiation, and that the resulting lithiated intermediate is chemically stable but configurationally labile under the given experimental conditions that afford enantioenriched N-alkyl-2,2-disubstituted azetidines. Although this study reveals the configurational instability of the diastereomeric lithiated azetidines, it points out an interesting stereoconvergence of such lithiated intermediates towards the thermodynamically stable species, making the overall process highly stereoselective (er > 95:5, dr > 85:15) after trapping with electrophiles. This peculiar behavior has been rationalized by considering the dynamics at the azetidine nitrogen atom, the inversion at the C-Li center supported by in situ FT-IR experiments, and DFT calculations that suggested the presence of η3-coordinated species for diastereomeric lithiated azetidines. The described situation contrasted with the demonstrated stability of the smaller lithiated aziridine analogue. The capability of oxazolinylazetidines to undergo different reaction patterns with organolithium bases supports the model termed “dynamic control of reactivity” of relevance in organolithium chemistry. It has been demonstrated that only 2,2-substituted oxazolinylazetidines with suitable stereochemical requirements could undergo C=N addition of organolithiums in non-coordinating solvents, leading to useful precursors of chiral (er > 95:5) ketoazetidines.

Herein we report the development of a photocatalytic strategy for the divergent preparation of functionalized bicyclo[1.1.1]pentylamines. This approach exploits, for the first time, the ability of nitrogen‐radicals to undergo strain‐release reaction with [1.1.1]propellane. This reactivity is facilitated by the electrophilic nature of these open‐shell intermediates and the presence of strong polar effects in the transition‐state for C−N bond formation/ring‐opening. With the aid of a simple reductive quenching photoredox cycle, we have successfully harnessed this novel radical strain‐release amination as part of a multicomponent cascade compatible with several external trapping agents. Overall, this radical strategy enables the rapid construction of novel amino‐functionalized building blocks with potential application in medicinal chemistry programs as p‐substituted aniline bioisosteres., Electrophilic nitrogen‐radicals enable efficient strain‐release amino‐functionalization of [1.1.1]propellane. This radical reactivity can be used for the divergent assembly of 3‐substituted bicyclo[1.1.1]pentylamines, which are powerful aniline bioisosteres.

Carbon-based polynuclear clusters are designed and investigated for geometric, electronic, and nonlinear optical (NLO) properties at the CAM-B3LYP/6-311++G(d,p) level of theory. Significant binding energies per atom (ranging from −162.4 to −160.0 kcal mol−1) indicate excellent thermodynamic stabilities of these polynuclear clusters. The frontier molecular orbital (FMOs) analysis indicates excess electron nature of the clusters with low ionization potential, suggesting that they are alkali-like. The decreased energy gaps (EH-L) with increased alkali metals size revael the improved electrical conductivity (σ). The total density of state (TDOS) study reveals the alkali metals’ size-dependent electronic and conductive properties. The significant first and second hyperpolarizabilities are observed up to 5.78 × 103 and 5.55 × 106 au, respectively. The βo response shows dependence on the size of alkali metals. Furthermore, the absorption study shows transparency of these clusters in the deep-UV, and absorptions are observed at longer wavelengths (redshifted). The optical gaps from TD-DFT are considerably smaller than those of HOMO-LUMO gaps. The significant scattering hyperpolarizability (βHRS) value (1.62 × 104) is calculated for the C3 cluster, where octupolar contribution to βHRS is 92%. The dynamic first hyperpolarizability β(ω) is more pronounced for the EOPE effect at 532 nm, whereas SHG has notable values for second hyperpolarizability γ(ω).

V-series nerve agents are very lethal to health and cause the inactivation of acetylcholinesterase which leads to neuromuscular paralysis and, finally, death. Therefore, rapid detection and elimination of V-series nerve agents are very important. Herein, we have carried out a theoretical investigation of carbon nitride quantum dots (C2N) as an electrochemical sensor for the detection of V-series nerve agents, including VX, VS, VE, VG, and VM. Adsorption of V-series nerve agents on C2N quantum dots is explored at M05-2X/6-31++G(d,p) level of theory. The level of theory chosen is quite adequate in systems describing non-bonding interactions. The adsorption behavior of nerve agents is characterized by interaction energy, non-covalent interaction (NCI), Bader’s quantum theory of atoms in molecules (QTAIM), frontier molecular orbital (FMO), electron density difference (EDD), and charge transfer analysis. The computed adsorption energies of the studied complexes are in the range of −12.93 to −17.81 kcal/mol, which indicates the nerve agents are physiosorbed onto C2N surface through non-covalent interactions. The non-covalent interactions between V-series and C2N are confirmed through NCI and QTAIM analysis. EDD analysis is carried out to understand electron density shifting, which is further validated by natural bond orbital (NBO) analysis. FMO analysis is used to estimate the changes in energy gap of C2N on complexation through HOMO-LUMO energies. These findings suggest that C2N surface is highly selective toward VX, and it might be a promising candidate for the detection of V-series nerve agents.

Background The aim of this study was to describe the epidemiological and clinical presentation of Healthcare Workers (HCWs) affected by COVID-19. Methods A cross-sectional retrospective study was conducted at King Saud Medical City (KSMC), Saudi Arabia (KSA). All KSMC employees who acquired COVID-19 between March 22nd to July 15th, 2020 have been included. Their data has been anonymously analyzed. Findings 1170 HCWs were included in our study who represented 33% of all COVID-19 reported cases at KSMC during the study period. The source of HCWs infections was mainly community acquired (85%) which included incidences of transmission in hospital dormitories. Transmission among coworkers was the main source of hospital acquired incidences. Direct patient care was reported in 99.8% of study subjects among the high-risk areas, compared to 3.4% in low-risk areas (p-value

Continuous studies are being carried out to explore new methods and carrier surfaces for target drug delivery. Herein, we report the covalent triazine framework C6N6 as a drug delivery carrier for fluorouracil (FU) and nitrosourea (NU) anti-cancer drugs. FU and NU are physiosorbed on C6N6 with adsorption energies of −28.14 kcal/mol and −27.54 kcal/mol, respectively. The outcomes of the non-covalent index (NCI) and quantum theory of atoms in molecules (QTAIM) analyses reveal that the FU@C6N6 and NU@C6N6 complexes were stabilized through van der Waals interactions. Natural bond order (NBO) and electron density difference (EDD) analyses show an appreciable charge transfer from the drug and carrier. The FU@C6N6 complex had a higher charge transfer (−0.16 e−) compared to the NU@C6N6 complex (−0.02 e−). Frontier molecular orbital (FMO) analysis reveals that the adsorption of FU on C6N6 caused a more pronounced decrease in the HOMO-LUMO gap (EH-L) compared to that of NU. The results of the FMO analysis are consistent with the NBO and EDD analyses. The drug release mechanism was studied through dipole moments and pH effects. The highest decrease in adsorption energy was observed for the FU@C6N6 complex in an acidic medium, which indicates that FU can easily be off-loaded from the carrier (C6N6) to a target site because the cancerous cells have a low pH compared to a normal cell. Thus, it may be concluded that C6N6 possesses the therapeutic potential to act as a nanocarrier for FU to treat cancer. Furthermore, the current study will also provide motivation to the scientific community to explore new surfaces for drug delivery applications.

BackgroundUrine output is widely used as one of the criteria for the diagnosis and staging of acute renal failure, but few studies have specifically assessed the role of oliguria as a marker of acute renal failure or outcomes in general intensive care unit (ICU) patients. Using a large multinational database, we therefore evaluated the occurrence of oliguria (defined as a urine output 16 years) patients in the ICON audit who had a urine output measurement on the day of admission were included. To investigate the association between oliguria and mortality, we used a multilevel analysis.ResultsOf the 8292 patients included, 2050 (24.7%) were oliguric during the first 24 h of admission. Patients with oliguria on admission who had at least one additional 24-h urine output recorded during their ICU stay (n = 1349) were divided into three groups: transient—oliguria resolved within 48 h after the admission day (n = 390 [28.9%]), prolonged—oliguria resolved > 48 h after the admission day (n = 141 [10.5%]), and permanent—oliguria persisting for the whole ICU stay or again present at the end of the ICU stay (n = 818 [60.6%]). ICU and hospital mortality rates were higher in patients with oliguria than in those without, except for patients with transient oliguria who had significantly lower mortality rates than non-oliguric patients. In multilevel analysis, the need for RRT was associated with a significantly higher risk of death (OR = 1.51 [95% CI 1.19–1.91], p = 0.001), but the presence of oliguria on admission was not (OR = 1.14 [95% CI 0.97–1.34], p = 0.103).ConclusionsOliguria is common in ICU patients and may have a relatively benign nature if only transient. The duration of oliguria and need for RRT are associated with worse outcome., 0, info:eu-repo/semantics/published

Radical hydroxymethylation using formaldehyde as a C1 synthon is challenging due to the reversible and endothermic nature of the addition process. Here we report a strategy that couples alkyl iodide building blocks with formaldehyde through the use of photocatalysis and a phosphine additive. Halogen-atom transfer (XAT) from α-aminoalkyl radicals is leveraged to convert the iodide into the corresponding open-shell species, while its following addition to formaldehyde is rendered irreversible by trapping the transient O-radical with PPh3. This event delivers a phosphoranyl radical that re-generates the alkyl radical and provides the hydroxymethylated product., Halogen-atom transfer (XAT) based on phosphoranyl radical chemistry enables the hydroxymethylation of alkyl iodides with formaldehyde.

TFF1, a secreted protein, plays an essential role in keeping the integrity of gastric mucosa and its barrier function. Loss of TFF1 expression in the TFF1-knockout (KO) mouse leads to a pro-inflammatory phenotype with a cascade of gastric lesions that include low-grade dysplasia, high-grade dysplasia, and adenocarcinomas. In this study, we demonstrate nuclear localization of p-STATY705, with significant overexpression of several STAT3 target genes in gastric glands from the TFF1-KO mice. We also show frequent loss of TFF1 with nuclear localization of STAT3 in human gastric cancers. The reconstitution of TFF1 protein in human gastric cancer cells and 3D gastric glands organoids from TFF1-KO mice abrogates IL6-induced nuclear p-STAT3Y705 expression. Reconstitution of TFF1 inhibits IL6-induced STAT3 transcription activity, suppressing expression of its target genes. TFF1 blocks IL6Rα-GP130 complex formation through interfering with binding of IL6 to its receptor IL6Rα. These findings demonstrate a functional role of TFF1 in suppressing gastric tumorigenesis by impeding the IL6-STAT3 pro-inflammatory signaling axis., Trefoil factor 1 (TFF1) is a protein secreted by the gastric mucosa that protects against gastric tumourigenesis. Here, the authors show that TFF1 inhibits the oncogenic inflammatory response and IL-6-mediated STAT3 activation by interfering with the binding of IL6 to its receptor IL6Rα.

Purpose: To investigate age-related differences in outcomes of critically ill patients with sepsis around the world., Methods: We performed a secondary analysis of data from the prospective ICON audit, in which all adult ( >16 years ) patients admitted to participating ICUs between May 8 and 18, 2012, were included, except admissions for routine postoperative observation. For this sub-analysis, the 10,012 patients with completed age data were included. They were divided into five age groups - 80 years. Sepsis was defined as infection plus at least one organ failure., Results: A total of 2963 patients had sepsis, with similar proportions across the age groups (80 = 30.9%). Hospital mortality increased with age and in patients >80 years was almost twice that of patients 70 years was independently associated with increased risk of dying., Conclusions: The odds for death in ICU patients with sepsis increased with age with the maximal rate of increase occurring between the ages of 71 and 77 years. (C) 2019 Elsevier Inc. 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J.] Joondalup Hlth Campus, Joondalup, WA, Australia., [Kilminster, M.] Lismore Base Hosp, Lismore, NSW, Australia., [Sturgess, D.] Mater Adult Hosp, South Brisbane, Qld, Australia., [Ziegenfuss, M.] Prince Charles Hosp, Brisbane, Qld, Australia., [O'Connor, S.] Royal Adelaide Hosp, Adelaide, SA, Australia., [Lipman, J.] Royal Brisbane & Womens Hosp, Brisbane, Qld, Australia., [Campbell, L.] Royal Darwin Hosp, Tiwi, NT, Australia., [Mcallister, R.] Royal Hobart Hosp, Hobart, Tas, Australia., [Roberts, B.] Sir Charles Gairdner Hosp, Nedlands, WA, Australia., [Williams, P.] Queen Elizabeth Hosp, Woodville, SA, Australia., [Parke, R.] Auckland Dist Hlth Board, Auckland, New Zealand., [Seigne, P.] Christchurch Hosp, Christchurch, New Zealand., [Freebairn, R.] Hawkes Bay Hosp, Hastings, New Zealand., [Nistor, D.] Palmerston North Hosp, Midcent Hlth, Palmerston North, New Zealand., [Oxley, C.] Middlemore Hosp, Auckland, New Zealand., [Young, P.] Wellington Hosp, Wellington, New Zealand., [Valentini, R.] Cemic, Buenos Aires, DF, Argentina., [Wainsztein, N.] Fleni, Buenos Aires, DF, Argentina., [Comignani, P.] Hosp Aleman, Buenos Aires, DF, Argentina., [Casaretto, M.] Hosp Cent San Isidro, Buenos Aires, DF, Argentina., [Sutton, G.] Hosp Fernandez, Buenos Aires, DF, Argentina., [Villegas, P.] Hosp Francisco Lopez Lima Area Programa Gen Roca, Gen Roca, Argentina., [Galletti, C.] Sanatorio Allende, Cordoba, Argentina., [Neira, J.] Sanatorio Trinidad Palermo, Buenos Aires, DF, Argentina., [Rovira, D.] Sanatorio Julio Corzo Rosario, Rosario, Santa Fe, Argentina., [Hidalgo, J.] Karl Heusner Mem Hosp, Belize City, Belize., [Hidalgo, J.] Belize Healthcare Partner, Belize City, Belize., [Sandi, F.] Hosp Obrero 1, La Paz, Bolivia., [Caser, E.] Cias Unimed Vitoria, Vitoria, ES, Brazil., [Thompson, M.] Evangelical Hosp Cachoeiro De Itapemirim, Cachoeiro De Itapemirim, Brazil., [D'agostino Dias, M.] Hosp 9 Julho, Sao Paulo, Brazil., [Fontes, L.] Hosp Alcides Carneiro, Petropolis, Brazil., [Lunardi, M.] Hosp Clin Luzia De Pinho Melo, Mogi Das Cruzes, Brazil., [Youssef, N.] Hosp Nacoes Curitiba, Curitiba, Parana, Brazil., [Lobo, S.] Hosp Base Famerp, Sao Jose Do Rio Preto, Brazil., [Silva, R.] Hosp Clin Niteroi, Niteroi, RJ, Brazil., [Sales Jr, J.] Hosp Clin Padre Miguel, Rio De Janeiro, Brazil., [Madeira Campos Melo, L.] Hosp Terapia Intens, Sao Paulo, Brazil., [Oliveira, M.] Hosp Trabalhador, Curitiba, Parana, Brazil., [Fonte, M.] Hosp Esperanza, Olinda, PE, Brazil., [Grion, C.] Hosp Evangel Londrina, Londrina, Brazil., [Feijo, C.] Hosp Geral Fortaleza, Fortaleza, Ceara, Brazil., [Rezende, V] Hosp Geral Roraima, Boa Vista, Brazil., [Assuncao, M.] Hosp Israelita Albert Einstein, Sao Paulo, Brazil., [Neves, A.] Hosp Mater Dei, Belo Horizonte, MG, Brazil., [Gusman, P.; 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Juan Francisco, L.] Inst Mexicano Seguro Social, Mexico City, DF, Mexico., [Liamendys-Silva, S. 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Mareque] CAMS, Montevideo, Uruguay., [Deicas, A.] CASMU, Montevideo, Uruguay., [Hurtado, J.] Hosp Espanol Asse, Montevideo, Uruguay., [Burghi, G.] Hosp Maciel, Montevideo, Uruguay., [Martinelli, A.] Ctr Med Caracas, Caracas, Venezuela., [Von der Osten, I] Hosp Miguel Perez Carreno, Caracas, Venezuela., [Du Maine, C.] MSF Trauma Hosp Kunduz, Kunduz, Afghanistan., [Bhattacharyya, M.] Amri Hosp, Kolkata, India., [Bandyopadhyay, S.] Amri Hosp Salt Lake, Kolkata, W Bengal, India., [Yanamala, S.] Apollo Hosp, Hyderabad, India., [Gopal, P.] Apollo Hosp, Bangalore, Karnataka, India., [Sahu, S.] Apollo Hosp, Bhubaneswar, India., [Ibrahim, M.] Apollo Special Hosp, Chennai, Tamil Nadu, India., [Rathod, D.] Asian Heart Inst, Mumbai, Maharashtra, India., [Mukundan, N.] Baby Mem Hosp Ltd, Calicut, Kerala, India., [Dewan, A.] Batra Hosp & Mrc, New Delhi 110062, India., [Amin, P.] Bombay Hosp Inst Med Sci, Mumbai, Maharashtra, India., [Samavedam, S.] Care Hosp, Hyderabad, India., [Shah, B.] Cims Hosp, Ahmadabad, Gujarat, India., [Gurupal, D.] Columbiaasia Hosp, Mysore, Karnataka, India., [Lahkar, B.] Dispur Hosp, Gauhati, India., [Mandal, A.] Fortis Hosp, Bangalore, Karnataka, India., [Sircar, M.] Fortis Hosp, Noida, India., [Ghosh, S.] Fortis Escorts Hosp, Faridabad, India., [Balasubramani, V] Ganga Med Ctr & Hosp P Ltd, Coimbatore, Tamil Nadu, India., [Kapadia, F.] Hinduja Hosp, Mumbai, Maharashtra, India., [Vadi, S.] KDAH, Mumbai, Maharashtra, India., [Nair, K.] Kerala Inst Med Sci, RMCC, Thiruvananthapuram, Kerala, India., [Tripathy, S.] Kalinga Inst Med Sci, DTEM, Bhubaneswar, Odisha, India., [Nandakumar, S.] Kovai Med Ctr & Hosp, Coimbatore, Tamil Nadu, India., [Sharma, J.] Medanta Medic, Gurgaon, India., [Kar, A.] Med Superspecialty Hosp, Kolkata, W Bengal, India., [Jha, S.] Metro Heart Inst Multispecial, Faridabad, India., [Gurav, K. Zirpe] Ruby Hall Pune, Pune, Maharashtra, India., [Patel, M.] Saifee Hosp, Mumbai, Maharashtra, India., [Bhaysar, A.] Spandan Multispecial Hosp, Vadodara, India., [Samaddar, D.] Tata Main Hosp, Jamshedpur, Jharkhand, India., [Kulkarni, A.] Tata Mem Hosp, Mumbai, Maharashtra, India., [Hashmi, M.] Aga Khan Univ, Karachi, Pakistan., [Ali, W.] Hearts Int Hosp, Rawalpindi, Pakistan., [Nadeem, S.] Liaquat Natl Hosp, Karachi, Pakistan., [Indraratna, K.] Sri Jayewardenepura Gen Hosp, Sri Jayawardenepura Kott, Sri Lanka., [Margarit, A.] Hosp Nostra Senyora Meritxell, Les Escaldes, Andorra., [Urbanek, P.] Akh Wien, Vienna, Austria., [Schlieber, J.] Allgemeines & Orthopad Landeskrankenhaus Stolzalp, Stolzalpe, Austria., [Reisinger, J.] Barmherzige Schwestern Linz, Linz, Austria., [Auer, U.] Gen Hosp Braunau, Braunau, Austria., [Hartjes, A.] Krankenhaus D Barmherzigen Schwestern Ried II, Ried Im Innkreis, Austria., [Lerche, A.] Krankenhaus Floridsdorf, Vienna, Austria., [Janous, T.] LK Gmund Waidhofen Thaya Zwettl, Standort Zwettl, Austria., [Kink, E.] LKH Horgas Enzenbach, Gratwein, Austria., [Krahulec, W.] LKH West, Graz, Austria., [Smolle, K.] Univ Hosp, Graz, Austria., [Van der Schueren, M.] AZ Groeninge Kortrijk, Kortrijk, Belgium., [Thibo, P.] AZ Jan Palfijn Gent, Ghent, Belgium., [Vanhoof, M.] AZ Turnhout, Turnhout, Belgium., [Ahmet, I] Bracops Anderlecht, Anderlecht, Belgium., [Gadisseux, P.] Ctr Hosp Mouscron, Mouscron, Belgium., [Dufaye, P.] CH Peltzer La Tourelle, Verviers, Belgium., [Jacobs, O.] Chirec Edith Cavell, Auderghem, Belgium., [Fraipont, V] CHR Citadelle, Liege, Belgium., [Biston, P.] CHU Charleroi, Charleroi, Belgium., [Dive, A.] CHU Mt Godinne, Yvoir, Belgium., [Bouckaert, Y.] CHU Tivoli, La Louviere, Belgium., [Gilbert, E.] CHwapi, Tournai, Belgium., [Gressens, B.] Clin St Pierre Ottignies, Ottignies, Belgium., [Pinck, E.] Clin Maternite St Elisabeth, Namur, Belgium., [Collin, V] Clin Europe St Michel, Etterbeek, Belgium., [Vincent, J. L.] Erasme Univ Hosp, Anderlecht, Belgium., [De Waele, J.] Ghent Univ Hosp, Ghent, Belgium., [Rimachi, R.] Moliere Hosp, Forest, Belgium., [Gusu, D.] Notre Dame, Brussels, Belgium., [De Decker, K.] Onze Lieve Vrouw Hosp, Aalst, Belgium., [Mandianga, K.] Ixelles Hosp, Ixelles, Belgium., [Heytens, L.] Sint Augustinus, Antwerp, Belgium., [Wittebole, X.] St Luc Univ Hosp UCL, Brussels, Belgium., [Spapen, H.] UZ Brussel, Brussels, Belgium., [Olivier, V] Vivalia Site Libramt, Libramont, Belgium., [Vandenheede, W.] VZW Gezondheidszorg Oostkust Knokke Heist, Knokke Heist, Belgium., [Rogiers, P.] ZNA Middelheim, Antwerp, Belgium., [Kolodzeike, P.] Herning Hosp, Herning, Denmark., [Kruse, M.] Hjoerring Hosp, Hjorring, Denmark., [Andersen, T.] Vejle Hosp, Vejle, Denmark., [Harjola, V] Helsinki Univ Cent Hosp, Helsinki, Finland., [Saarinen, K.] Seinajoki Cent Hosp, Seinajoki, Finland., [Leone, M.] Aix Marseille Univ, Hop Nord, Marseille, France., [Durocher, A.] Calmette Hosp, Lille, France., [Moulront, S.] Ctr Hosp Dunkerque, Dunkerque, France., [Lepape, A.] Ctr Hosp Lyon Sud, Lyon, France., [Losser, M.] CHU Nancy Brabois, Nancy, France., [Cabaret, P.] CH St Philibert, GHICL, Lille, France., [Kalaitzis, E.] CHR Dax, Dax, France., [Zogheib, E.] CHU Amiens, Amiens, France., [Charve, P.] CHU Dijon, Dijon, France., [Francois, B.] CHU Dupuytren, Limoges, France., [Lefrant, J. Y.] CHU Nimes, Nimes, France., [Beilouny, B.] Ctr Hosp Troyes, Troyes, France., [Forceville, X.] Ctr Hosp Meaux, Grp Hosp Est Francilien, Meaux, France., [Misset, B.] Grp Hosp Paris St Joseph, Paris, France., [Jacobs, F.] Hop Antoine Beclere, Clamart, France., [Floccard, B.] Hop Edouard Herriot, Lyon, France., [Payen, D.] Hop Lariboisere, AP HP, Paris, France., [Wynckel, A.] Hop Maison Blanche, Reims, France., [Castelain, V] Hop Univ Strasbourg, Strasbourg, France., [Faure, A.] Hosp Civils Lyon, Lyon, France., [Lavagne, P.] CHU Grenoble, Grenoble, France., [Thierry, I] CHU Nantes, Nantes, France., [Moussa, M.] CHRU Lille, Reanimat Chirurg Cardiovasc, Lille, France., [Vieillard-Baron, A.] Univ Hosp Ambroise Pare, Boulogne, France., [Durand, M.] Univ Hosp Grenoble, La Tronche, France., [Gainnier, M.] Univ Hosp Marseille, Marseille, France., [Ichai, C.] Univ Nice, Nice, France., [Arens, S.] Alexianer Krefeld Gmbh, Krefeld, Germany., [Hoffmann, C.] Charite Hochschulmed Berlin, Berlin, Germany., [Kaffarnik, M.] Charite, Berlin, Germany., [Scharnofske, C.] Diakoniekrankenhaus Henriettenstiftung Gmbh, Hannover, Germany., [Voigt, I] Elisabeth Krankenhaus Essen, Essen, Germany., [Peckelsen, C.] Munich Municipal Hosp Grp, Harlaching Hosp, Munich, Germany., [Weber, M.] Helios St Johannes Klin, Duisburg, Germany., [Gille, J.] Hosp St Georg Leipzig, Leipzig, Germany., [Lange, A.] Klin Hennigsdorf Oberhavel Kliniken Gmbh, Hennigsdorf, Germany., [Schoser, G.] Klin Tettnang, Tettnang, Germany., [Sablotzki, A.] Klinikum St Georg Leipzig, Leipzig, Germany., [Jaschinski, U.; Bluethgen, A.] Klinikum Augsburg, Augsburg, Germany., [Vogel, F.] Klinikum Bremen Mitte, Bremen, Germany., [Tscheu, A.] Klinikum Bremen Ost, Bremen, Germany., [Fuchs, T.] Klinikum Heidenheim, Heidenheim, Germany., [Wattenberg, M.] Klinikum Links Weser Gmbh, Bremen, Germany., [Helmes, T.] Klinikum Luedenscheid, Luedenscheid, Germany., [Scieszka, S.] Krankenhaus Neuwerk, Monchengladbach, Germany., [Heintz, M.] Marienkrankenhaus Schwerte, Schwerte, Germany., [Sakka, S.] Med Ctr Cologne Merheim, Cologne, Germany., [Kohler, J.] Schwarzwald Baar Klinikum Villingen Schwenningen, Villingen Schwenningen, Germany., [Fiedler, F.] St Elisabeth Krankenhaus Koln Hohenlind, Cologne, Germany., [Danz, M.] St Martinus Hosp Olpe, Olpe, Germany., [Sakr, Y.] Uniklinikum Jena, Jena, Germany., [Riessen, R.] Univ Klinikum Tubingen, Tubingen, Germany., [Kerz, T.] Univ Med Mainz, Mainz, Germany., [Kersten, A.] Univ Hosp Aachen, CPACC, Aachen, Germany., [Tacke, F.] Univ Hosp Aachen, DMIII, Aachen, Germany., [Marx, G.] Univ Hosp Aachen, OIC, Aachen, Germany., [Volkert, T.] Univ Hosp Muenster, Munster, Germany., [Schmutz, A.] Univ Med Ctr Freiburg, Fr

Photoswitchable catalysis involves alteration in the intrinsic catalytic properties of an active species through a reversible photochemical transformation. Herein, we report dihydroazulene-vinylheptafulvene (DHA-VHF) based photoswitchable frustrated Lewis pairs (FLPs) for reversible hydrogen activation. The dihydroazulene-vinylheptafulvene moieties here do not act as template to control the catalytic activity, rather the core part of the catalyst. The rational design principle involves evaluation of proton and hydride affinities of Lewis acids (borane) and base (phosphine and amine) functionalities installed on dihydroazulene-vinylheptafulvene photoswitch pair. Significant differences are observed between open VHF and closed DHA for proton and hydride affinities, and these differences are explained by geometric and electronic factors. The individual proton and hydride affinities are utilized to logically formulate best relative positions of both Lewis acid and base on a single molecule in order to activate one H2 molecule per photochrome. For our judiciously designed FLPs, the behavior of phosphine based FLP resembles to that of amine based FLPs at position 2 and 3, however they differ at position 8a. For amine based FLP, the energy released for hydrogen splitting is higher than DHA for all positions (2, 3, 8a) whereas in VHF phosphine based FLP, the energy released on H2 splitting in VHF is lower than that of DHA at position 8a. Moreover, hydrogen splitting is studied on couple of cautiously selected molecules based on the proton and hydride affinities. The activation barriers for hydrogen splitting in VHFs are about 8–10 kcal mol−1 lower than the corresponding barriers in DHAs, chiefly due to the higher hydride and proton affinities.

Background: Gastric cancer is considered the 5th most common form of cancer and 4th leading cause of cancer-related deaths worldwide. Due to the late stage of diagnosis, gastric cancer carries poor prognosis and poor overall survival. Infection with H. pylori is the strongest known risk factor. Fibroblast Growth Factor Receptor 4 (FGFR4) belongs to a family of highly conserved tyrosine kinases. This study investigated the molecular mechanism of FGFR4 regulation in response to H. pylori infection. Methods and Results: Among all the FGFRs, FGFR4 mRNA expression level was the most significantly elevated in human gastric cancer samples as compared to normal samples, using Real-time qPCR. These results were confirmed using the TCGA and Geo database analysis, confirming that FGFR4 is highly expressed in gastric cancer. Using western blot, we found that FGFR4 is significantly expressed in dysplasia and adenocarcinoma lesions in the TFF1-KO gastric cancer mouse model. Following infection with H. pylori in in-vitro (J166, 7.13) and in-vivo (PMSS1) models, we detected a significant increase in the expression of FGFR4 at the protein and mRNA levels. We also detected activation of STAT3 in human gastric cell lines and mice gastric tissues. Furthermore, analysis of FGFR4 promoter revealed several putative binding sites for STAT3. To confirm that FGFR4 expression is dependent upon STAT3 activation, we performed ChIP assay and confirmed direct functional binding of STAT3 on FGFR4 promoter. Using the FGF19, the ligand for FGFR4, we found that FGF19-FGFR4 axis played a vital role in activating STAT3 through an SRC-dependent mechanism and discovered that there is a feedforward activation loop between FGFR4 and STAT3. Functionally, we found that FGFR4 protected against H. pylori-induced DNA damage and cell death. Conclusion: Our study established a feedforward activation loop between FGFR4 and STAT3 in response to H. pylori infection and FGFR4 could be a possible druggable moiety for future therapies in gastric cancer. Citation Format: Nadeem S. Bhat, Mohammed Soutto, Xing Zhang, Zheng Chen, Shoumin Zhu, Heng Lu, Dunfa Peng, Zekuan Xu, Wael El-Rifai. Activation of STAT3 is mediated by FGFR4 induction via SRC signaling after H. pylori infection [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2022; 2022 Apr 8-13. Philadelphia (PA): AACR; Cancer Res 2022;82(12_Suppl):Abstract nr 5849.

Boron functional groups are often introduced in place of aromatic carbon–hydrogen bonds to expedite small-molecule diversification through coupling of molecular fragments1–3. Current approaches based on transition-metal-catalysed activation of carbon–hydrogen bonds are effective for the borylation of many (hetero)aromatic derivatives4,5 but show narrow applicability to azines (nitrogen-containing aromatic heterocycles), which are key components of many pharmaceutical and agrochemical products6. Here we report an azine borylation strategy using stable and inexpensive amine-borane7 reagents. Photocatalysis converts these low-molecular-weight materials into highly reactive boryl radicals8 that undergo efficient addition to azine building blocks. This reactivity provides a mechanistically alternative tactic for sp2 carbon–boron bond assembly, where the elementary steps of transition-metal-mediated carbon–hydrogen bond activation and reductive elimination from azine-organometallic intermediates are replaced by a direct, Minisci9-style, radical addition. The strongly nucleophilic character of the amine-boryl radicals enables predictable and site-selective carbon–boron bond formation by targeting the azine’s most activated position, including the challenging sites adjacent to the basic nitrogen atom. This approach enables access to aromatic sites that elude current strategies based on carbon–hydrogen bond activation, and has led to borylated materials that would otherwise be difficult to prepare. We have applied this process to the introduction of amine-borane functionalities to complex and industrially relevant products. The diversification of the borylated azine products by mainstream cross-coupling technologies establishes aromatic amino-boranes as a powerful class of building blocks for chemical synthesis. Selective borylation of azines—nitrogen-containing aromatic heterocycles used in the synthesis of many pharmaceuticals—is made possible by forming a radical from an aminoborane using a photocatalyst.

The generation of aryl radicals from the corresponding halides by redox chemistry is generally considered a difficult task due to their highly negative reduction potentials. Here we demonstrate that α-aminoalkyl radicals can be used as both initiators and chain-carriers for the radical coupling of aryl halides with pyrrole derivatives, a transformation often employed to evaluate new highly reducing photocatalysts. This mode of reactivity obviates for the use of strong reducing species and was also competent in the formation of sp2 C–P bonds. Mechanistic studies have delineated some of the key features operating that trigger aryl radical generation and also propagate the chain process., Aminoalkyl radicals can be used as both initiators and chain-carriers for the conversion of aryl halides into the corresponding radicals. This approach by-passes the requirement for strongly reducing photocatalysts.

The molecular heterogeneity of renal cell carcinoma (RCC) complicates the therapeutic interventions for advanced metastatic disease and thus its management remains a significant challenge. This study investigates the role of the lncRNA CDKN2B-AS1 and miR-141-3p interactions in the progression and metastasis of kidney cancer. Human renal cancer cell lines (ACHN and Caki1), normal RPTEC cells, tissue cohorts, and a series of in vitro assays and in vivo mouse model were used for this study. An overexpression of CDKN2B-AS1 was observed in RCC compared to normal samples in TCGA and our in-house SFVAMC tissue cohorts. Reciprocally, we observed reduced expression of miR-141 in RCC compared to normal in the same cohorts. CDKN2B-AS1 shares regulatory miR-141 binding sites with CCND1 and CCND2 genes. Direct interactions of CDKN2B-AS1/miR-141/Cyclin D1–D2 were confirmed by RNA immunoprecipitation and luciferase reporter assays indicating that CDKN2B-AS1/miR-141/Cyclin D1–D2 acts as a ceRNA network in RCC. Functionally, attenuation of CDKN2B-AS1 and/or overexpression of miR-141 inhibited proliferation, clonogenicity, migration/invasion, induced apoptosis in vitro and suppressed tumor growth in xenograft mouse model. Further, overexpression of CDKN2B-AS1 is positively correlated with poor overall survival of RCC patients. Expression of miR-141 also robustly discriminated malignant from non-malignant tissues and its inhibition in normal RPTEC cells induced pro-cancerous characteristics. CDKN2B-AS1 attenuation or miR-141 overexpression decreased CCND1/CCND2 expression, resulting in reduced RAC1/pPXN that are involved in migration, invasion and epithelial–mesenchymal transition. This study, for the first time, deciphered the role of CDKN2B-AS1/miR-141/Cyclin D axis in RCC and highlights this network as a promising therapeutic target for the regulation of EMT driven metastasis in RCC.

This study aims to investigate the role of miR-203–HOTAIR interaction in the suppression of renal cell carcinoma (RCC). We employed series of in vitro assays such as proliferation, invasion, migration, and colony formation along with in vivo tumor xenograft model. Profiling of miR-203 and HOTAIR expression revealed that miR-203 was significantly underexpressed, whereas HOTAIR was overexpressed in RCC cell lines and clinical specimens compared with normal cell line and tissue. Both miR-203 and HOTAIR expression significantly distinguished malignant from normal tissues and significantly correlated with clinicopathologic characteristics of patients. Overexpression of miR-203 significantly inhibited proliferation, migration, and invasion with an induction of apoptosis and cell-cycle arrest. However, HOTAIR suppression resulted in the similar functional effects in the same RCC cell lines. In silico, RNA-22 algorithm showed a binding site for miR-203 in HOTAIR. We observed a direct interaction between miR-203 and HOTAIR by RNA-immunoprecipitation (RIP) and luciferase reporter assays. We show that miR-203–HOTAIR interaction resulted in the inhibition of epithelial-to-mesenchymal transition (EMT) and metastatic genes as indicated by induction of key metastasis-suppressing proteins E-cadherin, claudin (epithelial markers), and PTEN along with induction of tumor suppressor genes p21 and p27. A significant decrease in vimentin (mesenchymal marker), KLF4, and Nanog (stemness markers) was also observed. This is the first report demonstrating miR-203–mediated regulation of HOTAIR induces tumor suppressor effects in RCC by regulating EMT and metastatic pathway genes. Thus, the study suggests that therapeutic regulation of HOTAIR by miR-203 overexpression may provide an opportunity to regulate RCC growth and metastasis. Mol Cancer Ther; 17(5); 1061–9. ©2018 AACR.

Hydroxylamines are found in biologically active compounds and serve as building blocks for the preparation of nitrogen-containing molecules. Here the direct conversion of carboxylic acids into the corresponding alkylhydroxylamines using organo-photoredox catalysis is reported. The process relies in the generation of alkyl radicals via photoinduced oxidation-decarboxylation and their following reaction with nitrosoarenes. We have successfully applied this method to the late-stage modification of complex and biologically active acids and applied it in novel radical cascade processes.

A visible-light-mediated synthesis of 5-methylene-pyrrolidinones is reported. This constitutes to the first reported example of a 5-exo-dig hydroamination reaction involving a nitrogen-centered radical.

Amines as a gateway to alkyl radicals In recent years, photoredox catalysis driven by blue light has often been used to oxidize carbon centers adjacent to nitrogen. Constantin et al. now show that these aminoalkyl radicals can, in turn, conveniently strip iodine atoms from a variety of alkyl carbons. The new alkyl radicals that result readily undergo deuteration and couplings such as alkylation, allylation, and olefination. The upshot is that simple amines can replace more hazardous conventional reagents such as trialkyltin compounds in the homolytic activation and functionalization of halocarbons. Science , this issue p. 1021

An unprecedented direct fluorocyclopropanation of allylic alcohols is reported. This simple method involves the not so elusive fluoroiodomethyllithium, a carbenoidic intermediate that under the developed conditions discloses its electrophilic nature. Gratifyingly, the reaction turned out to be highly chemo- and stereoselective, and DFT calculations provided insights into the structure and nature of this new type of carbenoid.

Purpose: To investigate age-related differences in outcomes of critically ill patients with sepsis around the world. Methods: We performed a secondary analysis of data from the prospective ICON audit, in which all adult ( >16 years ) patients admitted to participating ICUs between May 8 and 18, 2012, were included, except admissions for routine postoperative observation. For this sub-analysis, the 10,012 patients with completed age data were included. They were divided into five age groups - 80 years. Sepsis was defined as infection plus at least one organ failure. Results: A total of 2963 patients had sepsis, with similar proportions across the age groups (80 = 30.9%). Hospital mortality increased with age and in patients >80 years was almost twice that of patients 70 years was independently associated with increased risk of dying. Conclusions: The odds for death in ICU patients with sepsis increased with age with the maximal rate of increase occurring between the ages of 71 and 77 years. (C) 2019 Elsevier Inc. All rights reserved.

Herein, we report a strategy for the generation of nitrogen‐radicals by ground‐state single electron transfer with organyl–NiI species. Depending on the philicity of the N‐radical, two types of processes have been developed. In the case of nucleophilic aminyl radicals direct N‐arylation with aryl organozinc, organoboron, and organosilicon reagents was achieved. In the case of electrophilic amidyl radicals, cascade processes involving intramolecular cyclization, followed by reaction with both aryl and alkyl organometallics have been developed. The N‐cyclization–alkylation cascade introduces a novel retrosynthetic disconnection for the assembly of substituted lactams and pyrrolidines with its potential demonstrated in the short total synthesis of four venom alkaloids.

Purpose: To investigate age-related differences in outcomes of critically ill patients with sepsis around the world. Methods: We performed a secondary analysis of data from the prospective ICON audit, in which all adult ( >16 years ) patients admitted to participating ICUs between May 8 and 18, 2012, were included, except admissions for routine postoperative observation. For this sub-analysis, the 10,012 patients with completed age data were included. They were divided into five age groups - 80 years. Sepsis was defined as infection plus at least one organ failure. Results: A total of 2963 patients had sepsis, with similar proportions across the age groups (80 = 30.9%). Hospital mortality increased with age and in patients >80 years was almost twice that of patients 70 years was independently associated with increased risk of dying. 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[Sutton, G.] Hosp Fernandez, Buenos Aires, DF, Argentina. [Villegas, P.] Hosp Francisco Lopez Lima Area Programa Gen Roca, Gen Roca, Argentina. [Galletti, C.] Sanatorio Allende, Cordoba, Argentina. [Neira, J.] Sanatorio Trinidad Palermo, Buenos Aires, DF, Argentina. [Rovira, D.] Sanatorio Julio Corzo Rosario, Rosario, Santa Fe, Argentina. [Hidalgo, J.] Karl Heusner Mem Hosp, Belize City, Belize. [Hidalgo, J.] Belize Healthcare Partner, Belize City, Belize. [Sandi, F.] Hosp Obrero 1, La Paz, Bolivia. [Caser, E.] Cias Unimed Vitoria, Vitoria, ES, Brazil. [Thompson, M.] Evangelical Hosp Cachoeiro De Itapemirim, Cachoeiro De Itapemirim, Brazil. [D'agostino Dias, M.] Hosp 9 Julho, Sao Paulo, Brazil. [Fontes, L.] Hosp Alcides Carneiro, Petropolis, Brazil. [Lunardi, M.] Hosp Clin Luzia De Pinho Melo, Mogi Das Cruzes, Brazil. [Youssef, N.] Hosp Nacoes Curitiba, Curitiba, Parana, Brazil. [Lobo, S.] Hosp Base Famerp, Sao Jose Do Rio Preto, Brazil. [Silva, R.] Hosp Clin Niteroi, Niteroi, RJ, Brazil. [Sales Jr, J.] Hosp Clin Padre Miguel, Rio De Janeiro, Brazil. [Madeira Campos Melo, L.] Hosp Terapia Intens, Sao Paulo, Brazil. [Oliveira, M.] Hosp Trabalhador, Curitiba, Parana, Brazil. [Fonte, M.] Hosp Esperanza, Olinda, PE, Brazil. [Grion, C.] Hosp Evangel Londrina, Londrina, Brazil. [Feijo, C.] Hosp Geral Fortaleza, Fortaleza, Ceara, Brazil. [Rezende, V] Hosp Geral Roraima, Boa Vista, Brazil. [Assuncao, M.] Hosp Israelita Albert Einstein, Sao Paulo, Brazil. [Neves, A.] Hosp Mater Dei, Belo Horizonte, MG, Brazil. [Gusman, P.; Dalcomune, D.] Hosp Meridional, Cariacica, ES, Brazil. [Teixeira, C.] Hosp Moinhos Vento, Porto Alegre, RS, Brazil. [Kaefer, K.] Hosp Municipal Ruth Cardoso, Balneario, Brazil. [Maia, I] Hosp Nereu Ramos, Florianopolis, SC, Brazil. [Souza Dantas, V] Hosp Pasteur, Rio De Janeiro, Brazil. [Costa Filho, R.] Hosp Pro Cardiaco, Rio De Janeiro, Brazil. [Amorim, F.] Hosp Reg Samambaia, Brasilia, DF, Brazil. [Assef, M.] Hosp Reg Hans Dieter Schmidt, Joinville, Brazil. [Schiavetto, P.] Hosp Santa Casa Campo Mourao, Campo Mourao, PR, Brazil. [Houly, J.] Hosp Santa Paula, Sao Paulo, SP, Brazil. [Houly, J.] Hosp Santapaula, Sao Paulo, Brazil. [Bianchi, F.] Hosp Sao Jose Avai, Itaperuna, RJ, Brazil. [Dias, F.] Hosp Sao Lucas Pucrs, Porto Alegre, RS, Brazil. [Avila, C.] Hosp Sao Vicente Paula, Rio De Janeiro, RJ, Brazil. [Gomez, J.] Hosp Sao Vicente Paulo, Rio De Janeiro, Brazil. [Rego, L.] Hosp Saude Mulher, Belem, Para, Brazil. [Castro, P.] Hosp Tacchini, Bento Goncalves, RS, Brazil. [Passos, J.] Hosp Unimed Costa Do Sol Macae Rj, Macae, RJ, Brazil. [Mendes, C.] Hosp Univ Ufpb Joao Pessoa, Joao Pessoa, Paraiba, Brazil. [Grion, C.] Hosp Univ Londrina, Londrina, Brazil. [Colozza Mecatti, G.] Hosp Univ Sao Francisco, Braganca Paulista, SP, Brazil. [Ferrreira, M.] Santa Casa Caridade Diamantina, Diamantina, MG, Brazil. [Irineu, V] Santa Casa Misericordia Tatui, Tatui, Brazil. [Guerreiro, M.] Sao Francisco de Paula Hosp, Sao Francisco De Paula, RS, Brazil. [Ugarte, S.] Clin Indisa, Providencia, Chile. [Tomicic, V] Clin Las Lilas, Providencia, Chile. [Godoy, C.] Hosp Carlos Van Buren, Valparaiso, Chile. [Samaniego, W.] Hosp Trabajador Santiago, Santiago, Chile. [Escamilla, I] Hosp El Pino, San Bernardo, Chile. [Escamilla, I] Hosp Mutual De Seguridad, Santiago, Chile. [Castro Castro, L.] Ctr Med Imbanaco, Valle Del Cauca, Colombia. [Libreros Duque, G.] Clin Colombia Cali, Cali, Colombia. [Diaz-Guio, D.] Clin Del Cafe, Armenia, Colombia. [Benitez, F.] Clin La Estancia SA, Popayan, Colombia. [Guerra Urrego, A.] Clin Medellin, Medellin, Colombia. [Buitrago, R.] Fdn Clin Shaio, Bogota, Colombia. [Ortiz, G.] Hosp Santa Clara, Bogota, Colombia. [Villalba Gaviria, M.] Hosp Univ Fdn Santa Fe De Bogota, Bogota, Colombia. [Salas, D.] Calderon Guardia Hosp, San Jose, Costa Rica. [Ramirez-Arce, J.] Hosp Dr Rafael Angel Varlderon Guardia Ccss, San Jose, Costa Rica. [Salgado, E.] Clin La Merced, Quito, Ecuador. [Morocho, D.] Hosp Eugenio Espejo, Quito, Ecuador. [Vergara, J.] Hosp Luis Vernaza, Quito, Ecuador. [Chung Sang, M.] Shdug Sistema Hosp Docente De La Univ Guayaquil, Quito, Ecuador. [Orellana-Jimenez, C.] Gen Hosp, San Salvador, El Salvador. [Garrido, L.] Hosp Ctr Med, Guatemala City, Guatemala. [Diaz, O.] Inst Hondureno Seguro Social, La Ceiba, Honduras. [Resiere, D.] Ctr Hosp Univ Ft De France, Fort De France, Martinique, France. [Osorio, C.] Ctr Estatal Cuidados Crit, Salamanca, Mexico. [De La Vega, A.] Ctr Med Nacl 20 Noviembre Issste, Mexico City, DF, Mexico. [Carrillo, R.] Fdn Clin Med Sur, Mexico City, DF, Mexico. [Sanchez, V] Hosp San Jose TEC Monterrey, Monterrey, Mexico. [Villagomez, A.] Hosp 1 Octubre, Issste, Mexico. [Martinez Zubieta, R.] Hosp Espanol Mexico, Mexico City, DF, Mexico. [Sandia, M.] Hosp Gen Ajusco Medio, Mexico City, DF, Mexico. [Zalatiel, M.] Hosp Gen Guadalupe Victoria, Texcoco, Mexico. [Poblano, M.] Hosp Juarez Mexico, Mexico City, DF, Mexico. [Rodriguez Gonzalez, D.] Hosp Civil Guadalajara, Hspitaljuan I Menchaca, Guadalajara, Jalisco, Mexico. [Arrazola, F.; Juan Francisco, L.] Inst Mexicano Seguro Social, Mexico City, DF, Mexico. [Liamendys-Silva, S. A.] Inst Nacl Cancerol, Mexico City, DF, Mexico. [Hernandez, M.] ISSSTE Guerra Moya, Mexico City, DF, Mexico. [Hernandez, M.] Med Ctr ISSEMYM Toluca, Mexico City, DF, Mexico. [Rodriguez Cadena, D.] Mixta, Mexico City, DF, Mexico. [Lopez Islas, I.] Secretaria Salud Dist Fed, Mexico City, DF, Mexico. [Ballesteros Zarzavilla, C.] Hosp Santo Comas, Panama City, Panama. [Matos, A.] Social Secur Hosp, La Chorrera, Panama. [Oyanguren, I] Clin Anglo Amer, Lima, Peru. [Cerna, J.] Essalud, Lima, Peru. [Quispe Sierra, R.] Hosp Nacl Dos De Mayo, Lima, Peru. [Jimenez, R.] Hosp Rebagliati, Lince Dist, Peru. [Castillo, L.] Inst Nacl Enfermedades Neoplas, Surquillo, Peru. [Ocal, R.] Gulhane Med Fac, Istanbul, Turkey. [Sencan, A.] Izmir Ataturk Educ & Res Hosp, Izmir, Turkey. [Gianoni, S. Mareque] CAMS, Montevideo, Uruguay. [Deicas, A.] CASMU, Montevideo, Uruguay. [Hurtado, J.] Hosp Espanol Asse, Montevideo, Uruguay. [Burghi, G.] Hosp Maciel, Montevideo, Uruguay. [Martinelli, A.] Ctr Med Caracas, Caracas, Venezuela. [Von der Osten, I] Hosp Miguel Perez Carreno, Caracas, Venezuela. [Du Maine, C.] MSF Trauma Hosp Kunduz, Kunduz, Afghanistan. [Bhattacharyya, M.] Amri Hosp, Kolkata, India. [Bandyopadhyay, S.] Amri Hosp Salt Lake, Kolkata, W Bengal, India. [Yanamala, S.] Apollo Hosp, Hyderabad, India. [Gopal, P.] Apollo Hosp, Bangalore, Karnataka, India. [Sahu, S.] Apollo Hosp, Bhubaneswar, India. [Ibrahim, M.] Apollo Special Hosp, Chennai, Tamil Nadu, India. [Rathod, D.] Asian Heart Inst, Mumbai, Maharashtra, India. [Mukundan, N.] Baby Mem Hosp Ltd, Calicut, Kerala, India. [Dewan, A.] Batra Hosp & Mrc, New Delhi 110062, India. [Amin, P.] Bombay Hosp Inst Med Sci, Mumbai, Maharashtra, India. [Samavedam, S.] Care Hosp, Hyderabad, India. [Shah, B.] Cims Hosp, Ahmadabad, Gujarat, India. [Gurupal, D.] Columbiaasia Hosp, Mysore, Karnataka, India. [Lahkar, B.] Dispur Hosp, Gauhati, India. [Mandal, A.] Fortis Hosp, Bangalore, Karnataka, India. [Sircar, M.] Fortis Hosp, Noida, India. [Ghosh, S.] Fortis Escorts Hosp, Faridabad, India. [Balasubramani, V] Ganga Med Ctr & Hosp P Ltd, Coimbatore, Tamil Nadu, India. [Kapadia, F.] Hinduja Hosp, Mumbai, Maharashtra, India. [Vadi, S.] KDAH, Mumbai, Maharashtra, India. [Nair, K.] Kerala Inst Med Sci, RMCC, Thiruvananthapuram, Kerala, India. [Tripathy, S.] Kalinga Inst Med Sci, DTEM, Bhubaneswar, Odisha, India. [Nandakumar, S.] Kovai Med Ctr & Hosp, Coimbatore, Tamil Nadu, India. [Sharma, J.] Medanta Medic, Gurgaon, India. [Kar, A.] Med Superspecialty Hosp, Kolkata, W Bengal, India. [Jha, S.] Metro Heart Inst Multispecial, Faridabad, India. [Gurav, K. Zirpe] Ruby Hall Pune, Pune, Maharashtra, India. [Patel, M.] Saifee Hosp, Mumbai, Maharashtra, India. [Bhaysar, A.] Spandan Multispecial Hosp, Vadodara, India. [Samaddar, D.] Tata Main Hosp, Jamshedpur, Jharkhand, India. [Kulkarni, A.] Tata Mem Hosp, Mumbai, Maharashtra, India. [Hashmi, M.] Aga Khan Univ, Karachi, Pakistan. [Ali, W.] Hearts Int Hosp, Rawalpindi, Pakistan. [Nadeem, S.] Liaquat Natl Hosp, Karachi, Pakistan. [Indraratna, K.] Sri Jayewardenepura Gen Hosp, Sri Jayawardenepura Kott, Sri Lanka. [Margarit, A.] Hosp Nostra Senyora Meritxell, Les Escaldes, Andorra. [Urbanek, P.] Akh Wien, Vienna, Austria. [Schlieber, J.] Allgemeines & Orthopad Landeskrankenhaus Stolzalp, Stolzalpe, Austria. [Reisinger, J.] Barmherzige Schwestern Linz, Linz, Austria. [Auer, U.] Gen Hosp Braunau, Braunau, Austria. [Hartjes, A.] Krankenhaus D Barmherzigen Schwestern Ried II, Ried Im Innkreis, Austria. [Lerche, A.] Krankenhaus Floridsdorf, Vienna, Austria. [Janous, T.] LK Gmund Waidhofen Thaya Zwettl, Standort Zwettl, Austria. [Kink, E.] LKH Horgas Enzenbach, Gratwein, Austria. [Krahulec, W.] LKH West, Graz, Austria. [Smolle, K.] Univ Hosp, Graz, Austria. [Van der Schueren, M.] AZ Groeninge Kortrijk, Kortrijk, Belgium. [Thibo, P.] AZ Jan Palfijn Gent, Ghent, Belgium. [Vanhoof, M.] AZ Turnhout, Turnhout, Belgium. [Ahmet, I] Bracops Anderlecht, Anderlecht, Belgium. [Gadisseux, P.] Ctr Hosp Mouscron, Mouscron, Belgium. [Dufaye, P.] CH Peltzer La Tourelle, Verviers, Belgium. [Jacobs, O.] Chirec Edith Cavell, Auderghem, Belgium. [Fraipont, V] CHR Citadelle, Liege, Belgium. [Biston, P.] CHU Charleroi, Charleroi, Belgium. [Dive, A.] CHU Mt Godinne, Yvoir, Belgium. [Bouckaert, Y.] CHU Tivoli, La Louviere, Belgium. [Gilbert, E.] CHwapi, Tournai, Belgium. [Gressens, B.] Clin St Pierre Ottignies, Ottignies, Belgium. [Pinck, E.] Clin Maternite St Elisabeth, Namur, Belgium. [Collin, V] Clin Europe St Michel, Etterbeek, Belgium. [Vincent, J. L.] Erasme Univ Hosp, Anderlecht, Belgium. [De Waele, J.] Ghent Univ Hosp, Ghent, Belgium. [Rimachi, R.] Moliere Hosp, Forest, Belgium. [Gusu, D.] Notre Dame, Brussels, Belgium. [De Decker, K.] Onze Lieve Vrouw Hosp, Aalst, Belgium. [Mandianga, K.] Ixelles Hosp, Ixelles, Belgium. [Heytens, L.] Sint Augustinus, Antwerp, Belgium. [Wittebole, X.] St Luc Univ Hosp UCL, Brussels, Belgium. [Spapen, H.] UZ Brussel, Brussels, Belgium. [Olivier, V] Vivalia Site Libramt, Libramont, Belgium. [Vandenheede, W.] VZW Gezondheidszorg Oostkust Knokke Heist, Knokke Heist, Belgium. [Rogiers, P.] ZNA Middelheim, Antwerp, Belgium. [Kolodzeike, P.] Herning Hosp, Herning, Denmark. [Kruse, M.] Hjoerring Hosp, Hjorring, Denmark. [Andersen, T.] Vejle Hosp, Vejle, Denmark. [Harjola, V] Helsinki Univ Cent Hosp, Helsinki, Finland. [Saarinen, K.] Seinajoki Cent Hosp, Seinajoki, Finland. [Leone, M.] Aix Marseille Univ, Hop Nord, Marseille, France. [Durocher, A.] Calmette Hosp, Lille, France. [Moulront, S.] Ctr Hosp Dunkerque, Dunkerque, France. [Lepape, A.] Ctr Hosp Lyon Sud, Lyon, France. [Losser, M.] CHU Nancy Brabois, Nancy, France. [Cabaret, P.] CH St Philibert, GHICL, Lille, France. [Kalaitzis, E.] CHR Dax, Dax, France. [Zogheib, E.] CHU Amiens, Amiens, France. [Charve, P.] CHU Dijon, Dijon, France. [Francois, B.] CHU Dupuytren, Limoges, France. [Lefrant, J. Y.] CHU Nimes, Nimes, France. [Beilouny, B.] Ctr Hosp Troyes, Troyes, France. [Forceville, X.] Ctr Hosp Meaux, Grp Hosp Est Francilien, Meaux, France. [Misset, B.] Grp Hosp Paris St Joseph, Paris, France. [Jacobs, F.] Hop Antoine Beclere, Clamart, France. [Floccard, B.] Hop Edouard Herriot, Lyon, France. [Payen, D.] Hop Lariboisere, AP HP, Paris, France. [Wynckel, A.] Hop Maison Blanche, Reims, France. [Castelain, V] Hop Univ Strasbourg, Strasbourg, France. [Faure, A.] Hosp Civils Lyon, Lyon, France. [Lavagne, P.] CHU Grenoble, Grenoble, France. [Thierry, I] CHU Nantes, Nantes, France. [Moussa, M.] CHRU Lille, Reanimat Chirurg Cardiovasc, Lille, France. [Vieillard-Baron, A.] Univ Hosp Ambroise Pare, Boulogne, France. [Durand, M.] Univ Hosp Grenoble, La Tronche, France. [Gainnier, M.] Univ Hosp Marseille, Marseille, France. [Ichai, C.] Univ Nice, Nice, France. [Arens, S.] Alexianer Krefeld Gmbh, Krefeld, Germany. [Hoffmann, C.] Charite Hochschulmed Berlin, Berlin, Germany. [Kaffarnik, M.] Charite, Berlin, Germany. [Scharnofske, C.] Diakoniekrankenhaus Henriettenstiftung Gmbh, Hannover, Germany. [Voigt, I] Elisabeth Krankenhaus Essen, Essen, Germany. [Peckelsen, C.] Munich Municipal Hosp Grp, Harlaching Hosp, Munich, Germany. [Weber, M.] Helios St Johannes Klin, Duisburg, Germany. [Gille, J.] Hosp St Georg Leipzig, Leipzig, Germany. [Lange, A.] Klin Hennigsdorf Oberhavel Kliniken Gmbh, Hennigsdorf, Germany. [Schoser, G.] Klin Tettnang, Tettnang, Germany. [Sablotzki, A.] Klinikum St Georg Leipzig, Leipzig, Germany. [Jaschinski, U.; Bluethgen, A.] Klinikum Augsburg, Augsburg, Germany. [Vogel, F.] Klinikum Bremen Mitte, Bremen, Germany. [Tscheu, A.] Klinikum Bremen Ost, Bremen, Germany. [Fuchs, T.] Klinikum Heidenheim, Heidenheim, Germany. [Wattenberg, M.] Klinikum Links Weser Gmbh, Bremen, Germany. [Helmes, T.] Klinikum Luedenscheid, Luedenscheid, Germany. [Scieszka, S.] Krankenhaus Neuwerk, Monchengladbach, Germany. [Heintz, M.] Marienkrankenhaus Schwerte, Schwerte, Germany. [Sakka, S.] Med Ctr Cologne Merheim, Cologne, Germany. [Kohler, J.] Schwarzwald Baar Klinikum Villingen Schwenningen, Villingen Schwenningen, Germany. [Fiedler, F.] St Elisabeth Krankenhaus Koln Hohenlind, Cologne, Germany. [Danz, M.] St Martinus Hosp Olpe, Olpe, Germany. [Sakr, Y.] Uniklinikum Jena, Jena, Germany. [Riessen, R.] Univ Klinikum Tubingen, Tubingen, Germany. [Kerz, T.] Univ Med Mainz, Mainz, Germany. [Kersten, A.] Univ Hosp Aachen, CPACC, Aachen, Germany. [Tacke, F.] Univ Hosp Aachen, DMIII, Aachen, Germany. [Marx, G.] Univ Hosp Aachen, OIC, Aachen, Germany. [Volkert, T.] Univ Hosp Muenster, Munster, Germany. [Schmutz, A.] Univ Med Ctr Freiburg, Freiburg, Germany. [Nierhaus, A.; Kluge, S.] Univ Med Ctr Hamburg Eppendorf, Hamburg, Germany. [Abel, P.] Univ Med Greifswald, Greifswald, Germany. [Janosi, R.] Univ Duisburg Essen, Essen, Germany. [Utzolino, S.] Univ Freiburg, Freiburg, Germany. [Bracht, H.] Univ Clin Ulm, Ulm, Germany. [Toussaint, S.] Vivantes Klinikum Neukoelln, Berlin, Germany. [Peftoulidou, M. Giannakou] Ahepa Univ Hosp, Thessaloniki, Greece. [Myrianthefs, P.] Univ Athens, Athens, Greece. [Armaganidis, A.] Univ Athens, Med Sch, Athens, Greece. [Routsi, C.] Evangelismos Med Ctr, Athens, Greece. [Xini, A.] Gen Hosp Chania, Iraklion, Greece. [Mouloudi, E.] Hippokrateion Hosp, Thessaloniki, Greece. [Kokoris, I] Gen Hosp Velos, Volos, Greece. [Kyriazopoulos, G.] Lamia Gen Hosp, Lamia, Greece. [Vlachos, S.] Naval & Vet Hosp, Athens, Greece. [Lavrentieva, A.] Apanikolaou Gen Hosp, Thessaloniki, Greece. [Partala, P.] Univ Hosp Alexandroupolis, Alexandroupolis, Greece. [Nakos, G.] Univ Ioannina, Ioannina, Greece. [Moller, A.] Landspitali Univ Hosp, Reykjavik, Iceland. [Stefansson, S.] Landspitali Univ Hosp Fossvogur, Reykjavik, Iceland. [Barry, J.] Cork Univ Hosp, Cork, Ireland. [O'Leary, R.] Mercy Univ Hosp, Cork, Ireland. [Motherway, C.] Mid Western Reg Hosp Complex, Limerick, Ireland. [Faheem, M.] Midland Reg Hosp Mullingar, Mullingar, Co Westmeath, Ireland. [Dunne, E.] St Vincents Univ Hosp, Dublin, Ireland. [Donnelly, M.] Tallaght Hosp, Dublin, Ireland. [Konrad, T.] Univ Hosp Galway, Galway, Ireland. [Bonora, E.] Anesthesiol & Intens Care, Milan, Italy. [Achilli, C.] AO Osped Niguarda Ca Granda, Milan, Italy. [Rossi, S.] Azienda Osped Padova, Padua, Italy. [Castiglione, G.] Azienda Ospedaliero Univ Policlin Vittorio Emanue, Catania, Italy. [Penis, A.] Careggi Teaching Hosp, Florence, Italy. [Albanese, D.] Clinicized Hosp Ss Annunziata Chieti, Chieti, Italy. [Stocchetti, N.] Fdn Irccs Ca Granda Osped Maggiore Policlin, Milan, Italy. [Stocchetti, N.] Univ Milan, Milan, Italy. [Citerio, G.] H San Gerardo Monza, Monza, Italy. [Mozzoni, L.] Icu Ceccarini Hosp Ricc, Rimini, Italy. [Sisillo, E.] Irccs Ctr Cardiol Monzino, Milan, Italy. [De Negri, P.] Irccs Ctr Riferimento Oncol Basilicata, Basilicata, Italy. [Savioli, M.] Irccs Fdn Ca Granda, Osped Maggiore Policlin, Milan, Italy. [Vecchiarelli, P.] Osped Belcolle Viterbo, Viterbo, Italy. [Puflea, F.; Stankovic, V] Osped Civile Maggiore AOUI Verona, Verona, Italy. [Minoja, G.] Osped Circolo E Fdn Macchi, Varese, Italy. [Montibeller, S.] Osped Trento, Azienda Prov I Servizi Sanitari Prov Autonoma Tre, Trento, Italy. [Calligaro, P.] Osped Orlandi, Bussolengo, Italy. [Sorrentino, R.] Osped Regionale U Parini Aosta, Aosta, Italy. [Feri, M.] Osped San Donato Arezzo, Arezzo, Italy. [Zambon, M.] Osped San Raffaele, Segrate, Italy. [Colombaroli, E.] Policlin GB Rossi AOUI Verona, Verona, Italy. [Giarratano, A.] Policlin Univ Palermo, Palermo, Italy. [Pellis, T.] Santa Maria Angeli Hosp, Rome, Italy. [Capra, C.] Saronno Hosp, Saronno, Italy. [Antonelli, M.] Univ Cattolica Sacro Cuore, Milan, Italy. [Gullo, A.] Univ Catania, Catania, Italy. [Chelazzi, C.] Univ Florence, Florence, Italy. [De Capraris, A.] Univ Foggia, Foggia, Italy. [Patroniti, N.] Univ Milano Bicocca, San Gerardo Hosp, Milan, Italy. [Girardis, M.] Univ Modena, Modena, Italy. [Franchi, F.] Univ Siena, Siena, Italy. [Berlot, G.] Univ Trieste, Trieste, Italy. [Buttigieg, M.] Mater Hosp, Msida, Malta. [Ponssen, H.] Albert Schweitzer Hosp, Dordrecht, Netherlands. [Cate, J. Ten] Antoni Van Leeuwenhoek Ziekenhuis, Amsterdam, Netherlands. [Bormans, L.] Atrium Med Ctr Parkstad, Heerlen, Netherlands. [Husada, S.] Bovenij Hosp, Amsterdam, Netherlands. [Buise, M.] Catharina Hosp, Eindhoven, Netherlands. [Van Der Hoven, B.] Erasmus MC, Rotterdam, Netherlands. [Reidinga, A.] Martiniziekenhuis Groningen, Groningen, Netherlands. [Kuiper, M.] Med Ctr Leeuwarden, Leeuwarden, Netherlands. [Pickkers, P.] Radboud Univ Nijmegen, Med Ctr, Nijmegen, Netherlands. [Kluge, G.] Slotervaart Ziekenhuis Amsterdam, Amsterdam, Netherlands. [Den Boer, S.] Spaarne Ziekenhuis, Hoofddrop, Netherlands. [Kesecioglu, J.] Univ Med Ctr Utrecht, Utrecht, Netherlands. [Van Leeuwen, H.] Ziekenhuis Rijnstate, Arnhem, Netherlands. [Flaatten, H.] Haukeland Hosp, Bergen, Norway. [Mo, S.] Trondheim Reg & Univ Hosp, St Olays Hosp, Trondheim, Norway. [Branco, V] Ctr Hosp Cova Da Beira, Covilha, Portugal. [Rua, F.] Ctr Hosp Porto, Porto, Portugal. [Lafuente, E.] Ctr Hosp Tamega E Sousa, Guilhufe, Portugal. [Sousa, M.] Ctr Hosp Gaia Espinho, Epe, Espinho, Portugal. [Catorze, N.] Ctr Hosp Medio Tejo, Lisbon, Portugal. [Barros, M.] Ctr Hosp Tondela Viseu, Viseu, Portugal. [Pereira, L.] Faro Hosp, Faro, Portugal. [De Oliveira, A. Vintern] Hosp Curry Cabral, Lisbon, Portugal. [Gomes, J.] Hosp Luz, Lisbon, Portugal. [Gaspar, I] Hosp Egas Moniz Chlo, Lisbon, Portugal. [Pereira, M.] Ctr Hosp Porto, Hosp Santo Antonio, Proto, Portugal. [Cymbron, M.] Hosp Divino Espirito Santo, Epe, Ponta Delgada, Portugal. [Dias, A.] Hosp Espirito Santo Evora Epe, Evora, Portugal. [Almeida, E.] Hosp Garcia Orta, Almada, Portugal. [Beirao, S.] Hosp Geral Ctr Hosp E Univ Coimbra, Coimbra, Portugal. [Serra, I] Hosp Prof Doutor Fernando Fonseca Epe, Amadora, Portugal. [Ribeiro, R.] Hosp Sao Bernardo, Setubal, Portugal. [Povoa, P.] Hosp Sao Francisco Xavier, Chlo, Lisbon, Portugal. [Faria, F.] Inst Portugues Oncol Francisco Gentil, Porto, Portugal. [Costa-E-Silva, Z.] Santa Maria Hosp, Lisbon, Portugal. [Nobrega, A.] Serv Saude Regiao Autonoma Madeira, Funchal, Portugal. [Fernandes, F.] UCIP, Lisbon, Portugal. [Gabriel, J.] ULS Castelo Branco, Castelo Branco, Portugal. [Voga, G.] Gen Hosp Celje, Celje, Slovenia. [Rupnik, E.] Gen Hosp Izola, Izola, Slovenia. [Kosec, L.] Gen Hosp Novo Mesto, Novo Mesto, Slovenia. [Povsic, M. Kerin] Oncol Inst, Ljubljana, Slovenia. [Osojnik, I] Ukc Maribor, Maribor, Slovenia. [Tomic, V] Univ Clin Resp & Allerg Dis, Golnik, Slovenia. [Sinkovic, A.] Univ Clin Ctr Maribor, Maribor, Slovenia. [Gonzalez, J.] CH Salamanca, Salamanca, Spain. [Zavala, E.] Clin Hosp, Barcelona, Spain. [Perez Valenzuela, A.] Complejo Hosp Jaen, Jaen, Spain. [Marina, L.] Complejo Hosp Toledo, Toledo, Spain. [Vidal-Cortes, P.] Complexo Hosp Univ Ourense, Orense, Spain. [Posada, I] Complexo Hosp Univ Vigo, Galicia, Spain. [Ignacio Martin-Loeches, A.] Corp Sanitaria Parc Tauli, Barcelona, Spain. [Munoz Guillen, N.] Cruz Roja Hosp, Seville, Spain. [Palomar, M.] H Vall Hebron, Barcelona, Spain. [Sole-Violan, U.] HGGC Dr Negrin, Madrid, Spain. [Torres, A.] Hosp Clin Barcelona, Barcelona, Spain. [Gonzalez Gallego, M.] Hosp Clin San Carlos, Madrid, Spain. [Aguilar, G.] Hosp Clin Univ Valencia, Valencia, Spain. [Montoiro Allue, R.] Hosp Clin Univ Lozano Blesa, Zaragoza, Spain. [Argueso, M.] Hosp Clin Valencia, Valencia, Spain. [Parejo, M.] Hosp La Ribera, Valencia, Spain. [Palomo Navarro, M.] Hosp Sagunto, Port De Sagunt, Spain. [Jose, A.] Hosp San Juan Alicante, Alicante, Spain. [Nin, N.] Hosp Torrejon de Ardoz, Madrid, Spain. [Alvarez Lerma, F.] Hosp Mar, Barcelona, Spain. [Martinez, O.] Hosp Tajo, Madrid, Spain. [Tenza Lozano, E.] Hosp Gen Univ Elche, Elche, Spain. [Arenal Lopez, S.; Perez Granda, M.] Hosp Gen Univ Gregorio Maranon, Madrid, Spain. [Moreno, S.] Hosp Gen Univ Santa Lucia, Murcia, Spain. [Llubia, C.] Hosp Badalona Germans Trias & Pujol, Barcelona, Spain. [De la Fuente Martos, C.] Hosp Infanta Margarita, Cabra, Spain. [Gonzalez-Arenas, P.] Hosp Infanta Sofia, Madrid, Spain. [Llamas Fernandez, N.; Gil Rueda, B.] Hosp JM Morales Meseguer, Murcia, Spain. [Estruch Pons, I] Hosp Marina Salu Denia Alicante, Alicante, Spain. [Cruza, N.] Hosp Nuestra Senora Prado, Toledo, Spain. [Maroto, F.] Hosp San Juan De Dios Aljarafe, Bormujos, Spain. [Estella, A.] Hosp Sas Jerez, Andalucia, Spain. [Ferrer, A.] Hosp Son Llatzer, Palma De Mallorca, Spain. [Iglesias Fraile, L.; Quindos, B.] Hosp Univ Cent Asturias, Oviedo, Spain. [Quintano, A.] Hosp Univ Alava, Santiago, Spain. [Tebar, M.] Hosp Univ Basurto, Bilbao, Spain. [Cardinal, I] Hosp Univ Getafe, Getafe, Spain. [Reyes, A.] Hosp Univ La Princesa, Madrid, Spain. [Rodriguez, A.] Hosp Univ Tarragona Joan Xxiii, Tarragona, Spain. [Abella, A.] Hosp Univ Henares, Coslada, Spain. [Garcia Del Valle, S.] Hosp Univ Fdn Alcorcon, Alcorcon, Spain. [Yus, S.; Maseda, E.] Hosp Univ La Paz, Madrid, Spain. [Berezo, U.] Hosp Univ Rio Hortega, Valladolid, Spain. [Tejero Pedregosa, A.] Hosp Univ San Cecilio, Granada, Spain. [Laplaza, C.] Hosp Virgen Del Camino, Pamplona, Spain. [Ferrer, R.] Mutua Terrassa Univ Hosp, Terrassa, Spain. [Rico-Feijoo, U.] Rao Hortega Univ Hosp, Valladolid, Spain. [Rodriguez, M.] Serv Andaluz Salud, Andalucia, Spain. [Monedero, P.] Univ Okalingaf Navarra, Navarra, Spain. [Eriksson, K.] Karolinska Univ Hosp, Solna, Sweden. [Eriksson, K.] Karolinska Inst, Solna, Sweden. [Lind, D.] Sunderby Hosp, Lulea, Sweden. [Chabanel, D.] Hop Intercantonal La Broye, Payerne, Switzerland. [Zender, H.] Hop Neuchatelois La Chaux De Fonds, La Chaux De Fonds, Switzerland. [Heer, K.] Lindenhofspital, Bern, Switzerland. [Frankenberger, B.] Regionalspital Surselva Ilanz, Ilanz, Switzerland. [Jakob, S.] Univ Hosp Bern, Bern, Switzerland. [Mathew, S.] Alexandra Hosp Redditch, Redditch, England. [Downes, R.] Blackpool Teaching Hosp, Blackpool, England. [Groba, C. Barrera] Brighton & Sussex Univ Hosp, Brighton, E Sussex, England. [Johnston, A.] Cambridge Univ Hosp NHS Fdn Trust, Cambridge, England. [Meacher, R.] Charing Cross Hosp, London, England. [Keays, R.] Chelsea & Westminster Hosp, London, England. [Haji-Michael, P.] Christie Fdn Trust, Manchester, Lancs, England. [Tyler, C.] Cty Hosp, Lincoln, England. [Ferguson, A.] Craigavon Area Hosp, Craigavon, North Ireland. [Jones, S.] Cumberland Infirm, Carlisle, England. [Tyl, D.] Darent Valley Hosp, Dartford, England. [Ball, A.] Dorset Cty Hosp, Dorchester, England. [Vogel, U.] Ealing Hosp NHS Trust, Southall, Middx, England. [Booth, M.] Glasgow Royal Infirm, Glasgow, Lanark, Scotland. [Downie, P.] Gloucester Royal Hosp, Gloucester, England. [Watters, M.] Great Western Hosp, Swindon, Wilts, England. [Brett, S.] Imperial Coll Healthcare NHS Trust, London, England. [Garfield, M.] Ipswich Hosp Nhs Trust, Ipswich, Suffolk, England. [Everett, L.] James Paget Univ Hosp NHS Fdn Trust, Great Yarmouth, Norfolk, England. [Heenen, S.] Kings Coll Hosp London, London, England. [Dhir, S.] Kings Mill Hosp, Sutton In Ashfield, England. [Beardow, Z.] Leeds Teaching Hosp NHS Trust, Leeds, W Yorkshire, England. [Mostert, M.] Lewisham Healthcare NHS Trust, London, England. [Brosnan, S.] Luton & Dunstable Hosp NHS Trust, Luton, Beds, England. [Pinto, N.] Medway Maritime Hosp, Gillingham, England. [Harris, S.] Musgrove Pk Hosp, Taunton, Somerset, England. [Summors, A.] Nevill Hall Hosp, Abergavenny, Wales. [Andrew, N.] Pilgrim Hosp, Boston, England. [Rose, A.] Mid Yorkshire NHS Trust, Pinderfields Hosp, Wakefield, England. [Appelboam, R.] Plymouth Hosp Nhs Trust, Plymouth, Devon, England. [Davies, O.] Princess Royal Hosp Telford, Telford, Shrops, England. [Vickers, E.] Royal Bournemouth Hosp, Bournemouth, Dorset, England. [Agarwal, B.] Royal Free Hampstead NHS Fdn Trust, London, England. [Szakmany, T.] Royal Glamorgan Hosp, Llantrisant, Wales. [Wimbush, S.] Royal Hampshire Cty Hosp, Winchester, Hants, England. [Welters, I] Royal Liverpool Univ Hosp, Liverpool, Merseyside, England. [Pearse, R.] Barts Hlth NHS Trust, Royal London Hosp, London, England. [Hollands, R.] Royal Shrewsbury Hosp, Shrewsbury, Salop, England. [Kirk-Bayley, U.] Royal Surrey Cty Hosp, Guildford, Surrey, England. [Fletcher, N.] St Georges Healthcare, London, England. [Bray, B.] Surrey & Sussex Healthcare Trust, Redhill, Surrey, England. [Brealey, D.] Univ Coll Hosp, London, England.