Structure-Function Analysis of Inositol Hexakisphosphate-induced Autoprocessing in Clostridium difficile Toxin A - Test2 - elhamkhani - TriplyDB

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

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

http://www.wikidata.org/entity/Q27646280

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The repetitive oligopeptide sequences modulate cytopathic potency but are not crucial for cellular uptake of Clostridium difficile toxin A The acetyltransferase activity of the bacterial toxin YopJ of Yersinia is activated by eukaryotic host cell inositol hexakisphosphate Host S-nitrosylation inhibits clostridial small molecule-activated glucosylating toxins Clostridium difficile Toxins A and B: Insights into Pathogenic Properties and Extraintestinal Effects The Role of Rho GTPases in Toxicity of Clostridium difficile Toxins Cross Kingdom Activators of Five Classes of Bacterial Effectors Clostridium difficile infection: molecular pathogenesis and novel therapeutics Clostridial toxins: sensing a target in a hostile gut environment.Clostridium difficile Toxin B causes epithelial cell necrosis through an autoprocessing-independent mechanism Rational Design of Inhibitors and Activity-Based Probes Targeting Clostridium difficile Virulence Factor TcdB Defining an allosteric circuit in the cysteine protease domain of Clostridium difficile toxins The structure of Clostridium difficile toxin A glucosyltransferase domain bound to Mn2+ and UDP provides insights into glucosyltransferase activity and product release The structure of the cysteine protease and lectin-like domains of Cwp84, a surface layer-associated protein fromClostridium difficile Structure of a pathogen effector reveals the enzymatic mechanism of a novel acetyltransferase family Structural organization of the functional domains of Clostridium difficile toxins A and B Allosteric regulation of protease activity by small molecules.Inositol hexakisphosphate-induced autoprocessing of large bacterial protein toxins.Expression of inositol 1,3,4-trisphosphate 5/6-kinase (ITPK1) and its role in neural tube defects.Expression, purification, crystallization and preliminary crystallographic analysis of a putative Clostridium difficile surface protein Cwp19 The pathogenesis, detection, and prevention of Vibrio parahaemolyticus.Autoproteolytic activation of bacterial toxins.Vibrio type III effector VPA1380 is related to the cysteine protease domain of large bacterial toxins Crystal structure of a trapped catalytic intermediate suggests that forced atomic proximity drives the catalysis of mIPS Clostridium difficile toxins: mediators of inflammation.Toward a structural understanding of Clostridium difficile toxins A and B.Clostridium difficile virulence factors: Insights into an anaerobic spore-forming pathogen.Development of a Novel Vaccine Containing Binary Toxin for the Prevention of Clostridium difficile Disease with Enhanced Efficacy against NAP1 Strains MAPK-activated protein kinase 2 contributes to Clostridium difficile-associated inflammation Regulation of protein-ligand binding affinity by hydrogen bond pairing.Identification of an Essential Region for Translocation of Clostridium difficile Toxin B.Variations in virulence and molecular biology among emerging strains of Clostridium difficile.Super toxins from a super bug: structure and function of Clostridium difficile toxins.The enterotoxicity of Clostridium difficile toxins.Targeting bacterial toxins.Immunization strategies for Clostridium difficile infections.The host immune response to Clostridium difficile infection Regulation of Vibrio parahaemolyticus T3SS2 gene expression and function of T3SS2 effectors that modulate actin cytoskeleton.Comparative structural analysis of the caspase family with other clan CD cysteine peptidases.Two serine residues in Pseudomonas syringae effector HopZ1a are required for acetyltransferase activity and association with the host co-factor.Salubrinal protects against Clostridium difficile toxin B-induced CT26 cell death.

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P2860

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

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P2860

pH-induced conformational changes in Clostridium difficile toxin B

Clostridium difficile: its disease and toxins

Toxin B is essential for virulence of Clostridium difficile

Inositol hexakisphosphate is bound in the ADAR2 core and required for RNA editing

Processing of X-ray diffraction data collected in oscillation mode

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

Coot: model-building tools for molecular graphics

Automated structure solution with autoSHARP

Stereochemical quality of protein structure coordinates

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