Host S-nitrosylation inhibits clostridial small molecule-activated glucosylating toxins - Wikidata - wikimedia - TriplyDB

Host S-nitrosylation inhibits clostridial small molecule-activated glucosylating toxins

Host S-nitrosylation inhibits clostridial small molecule-activated glucosylating toxins

http://www.wikidata.org/entity/Q24633338

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Epigenetic Regulation of Enteric Neurotransmission by Gut Bacteria Clostridial toxins: sensing a target in a hostile gut environment.Clostridium difficile Toxin B causes epithelial cell necrosis through an autoprocessing-independent mechanism The CTSA as an exemplar framework for developing multidisciplinary translational teams Action of nitroheterocyclic drugs against Clostridium difficile.Using phenotype microarrays to determine culture conditions that induce or repress toxin production by Clostridium difficile and other microorganisms.Importance of NO and its related compounds in enteric nervous system regulation of gut homeostasis and disease susceptibility The roles of host and pathogen factors and the innate immune response in the pathogenesis of Clostridium difficile infection.Allele variants of enterotoxigenic Escherichia coli heat-labile toxin are globally transmitted and associated with colonization factors.Increased S-nitrosylation and proteasomal degradation of caspase-3 during infection contribute to the persistence of adherent invasive Escherichia coli (AIEC) in immune cells Critical roles of Clostridium difficile toxin B enzymatic activities in pathogenesis.Cysteine-mediated redox signaling: chemistry, biology, and tools for discovery Masking autoprocessing of Clostridium difficile toxin A by the C-terminus combined repetitive oligo peptides.Administration of probiotic kefir to mice with Clostridium difficile infection exacerbates disease.Clostridium difficile infection: toxins and non-toxin virulence factors, and their contributions to disease establishment and host response.Enzymatic mechanisms regulating protein S-nitrosylation: implications in health and disease.Clostridium difficile toxins: mediators of inflammation.Clostridium difficile colitis: pathogenesis and host defence Critical role for MyD88-mediated neutrophil recruitment during Clostridium difficile colitis.Regulation of protein-ligand binding affinity by hydrogen bond pairing.S-nitrosation of glutathione transferase p1-1 is controlled by the conformation of a dynamic active site helix.S-Nitrosylation Proteome Profile of Peripheral Blood Mononuclear Cells in Human Heart Failure Clostridium difficile toxin B-induced necrosis is mediated by the host epithelial cell NADPH oxidase complex.Gluten sensitivity: problems of an emerging condition separate from celiac disease.Targeting bacterial toxins.The host immune response to Clostridium difficile infection Cytotoxicity of Clostridium difficile toxin B does not require cysteine protease-mediated autocleavage and release of the glucosyltransferase domain into the host cell cytosol.Markers of nitric oxide are associated with sepsis severity: an observational study Biphasic modulation of NOS expression, protein and nitrite products by hydroxocobalamin underlies its protective effect in endotoxemic shock: downstream regulation of COX-2, IL-1β, TNF-α, IL-6, and HMGB1 expression.TcdB from hypervirulent Clostridium difficile exhibits increased efficiency of autoprocessing.Clostridium difficile antibodies: a patent evaluation (WO2013028810).Host-Mediated S-Nitrosylation Disarms the Bacterial Effector HopAI1 to Reestablish Immunity.S-Nitrosoglutathione formation at gastric pH is augmented by ascorbic acid and by the antioxidant vitamin complex, Resiston.The role of toxins in Clostridium difficile infection.Ceragenin CSA13 Reduces Clostridium difficile Infection in Mice by Modulating the Intestinal Microbiome and Metabolites.Discovery of Candidate Biomarkers.Treatment of Clostridium difficile infection with a small molecule inhibitor of toxin UDP-glucose hydrolysis activity.On and Off: A Dual Role for Cysteine Protease Autoprocessing of C difficile Toxin B on Cytotoxicity vs Proinflammatory Toxin Actions?Cysteine Protease-Mediated Autocleavage of Clostridium difficile Toxins Regulates Their Proinflammatory Activity.Symmetrical (SDMA) and asymmetrical dimethylarginine (ADMA) in sepsis: high plasma levels as combined risk markers for sepsis survival

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Host S-nitrosylation inhibits clostridial small molecule-activated glucosylating toxins

http://www.wikidata.org/entity/Q24633338

description

2011 nî lūn-bûn

@nan

2011 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

@zh-hant

2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Host S-nitrosylation inhibits clostridial small molecule-activated glucosylating toxins

@ast

Host S-nitrosylation inhibits clostridial small molecule-activated glucosylating toxins

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Host S-nitrosylation inhibits clostridial small molecule-activated glucosylating toxins

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type

label

Host S-nitrosylation inhibits clostridial small molecule-activated glucosylating toxins

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Host S-nitrosylation inhibits clostridial small molecule-activated glucosylating toxins

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Host S-nitrosylation inhibits clostridial small molecule-activated glucosylating toxins

@nl

prefLabel

Host S-nitrosylation inhibits clostridial small molecule-activated glucosylating toxins

@ast

Host S-nitrosylation inhibits clostridial small molecule-activated glucosylating toxins

@en

Host S-nitrosylation inhibits clostridial small molecule-activated glucosylating toxins

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Nature Medicine

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Host S-nitrosylation inhibits clostridial small molecule-activated glucosylating toxins

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Alfred Hausladen

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Aproteem Choudhury

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Bo Herman

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Charalabos Pothoulakis

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Hanping Feng

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Irina Pinchuk

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John E Wiktorowicz

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Jonathan S Stamler

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Kausar Ali

http://www.w3.org/2001/XMLSchema#string

Lianfa Shi

http://www.w3.org/2001/XMLSchema#string

P2860

Inducible nitric oxide synthase binds, S-nitrosylates, and activates cyclooxygenase-2

Toxin B is essential for virulence of Clostridium difficile

Protection from experimental asthma by an endogenous bronchodilator

Crystal structure of gingipain R: an Arg-specific bacterial cysteine proteinase with a caspase-like fold

Structure-Function Analysis of Inositol Hexakisphosphate-induced Autoprocessing in Clostridium difficile Toxin A

Structural and Molecular Mechanism for Autoprocessing of MARTX Toxin of Vibrio cholerae at Multiple Sites

Small Molecule-Induced Allosteric Activation of the Vibrio cholerae RTX Cysteine Protease Domain

Rational Design of Inhibitors and Activity-Based Probes Targeting Clostridium difficile Virulence Factor TcdB

Autoprocessing of the Vibrio cholerae RTX toxin by the cysteine protease domain

Structure-function analysis of inositol hexakisphosphate-induced autoprocessing of the Vibrio cholerae multifunctional autoprocessing RTX toxin

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1136-1141

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scholarly article

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4009919

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10.1038/NM.2405

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9

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17

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Alfredo G Torres

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2011-08-21T00:00:00Z

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51586472

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1035331422

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21857653

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3277400

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