Mechanistic and structural insights into the proteolytic activation of Vibrio cholerae MARTX toxin - sprookjes - yvandenbroek - TriplyDB

Mechanistic and structural insights into the proteolytic activation of Vibrio cholerae MARTX toxin

Mechanistic and structural insights into the proteolytic activation of Vibrio cholerae MARTX toxin

http://www.wikidata.org/entity/Q27655603

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RTX proteins: a highly diverse family secreted by a common mechanism Multifunctional-autoprocessing repeats-in-toxin (MARTX) Toxins of Vibrios 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 Crystal structure of a Trypanosoma brucei metacaspase MARTX toxins as effector delivery platforms Simplified, enhanced protein purification using an inducible, autoprocessing enzyme tag Cytotoxicity of the Vibrio vulnificus MARTX toxin effector DUF5 is linked to the C2A subdomain.Analysis of Vibrio cholerae genome sequences reveals unique rtxA variants in environmental strains and an rtxA-null mutation in recent altered El Tor isolates.Allosteric regulation of protease activity by small molecules.Inositol hexakisphosphate-induced autoprocessing of large bacterial protein toxins.Vibrio vulnificus rtxA1 gene recombination generates toxin variants with altered potency during intestinal infection Human defensins facilitate local unfolding of thermodynamically unstable regions of bacterial protein toxins.Autoproteolytic activation of bacterial toxins.Vibrio cholerae MARTX toxin heterologous translocation of beta-lactamase and roles of individual effector domains on cytoskeleton dynamics.Distinct roles of the repeat-containing regions and effector domains of the Vibrio vulnificus multifunctional-autoprocessing repeats-in-toxin (MARTX) toxin.Clostridium difficile toxins: mediators of inflammation.Induced autoprocessing of the cytopathic Makes caterpillars floppy-like effector domain of the Vibrio vulnificus MARTX toxin.New ligation independent cloning vectors for expression of recombinant proteins with a self-cleaving CPD/6xHis-tag.Autophagy and endosomal trafficking inhibition by Vibrio cholerae MARTX toxin phosphatidylinositol-3-phosphate-specific phospholipase A1 activity New approaches for dissecting protease functions to improve probe development and drug discovery Identification of a His-Asp-Cys catalytic triad essential for function of the Rho inactivation domain (RID) of Vibrio cholerae MARTX toxin.Reexamining the Germination Phenotypes of Several Clostridium difficile Strains Suggests Another Role for the CspC Germinant Receptor.Stereochemical features of glutathione-dependent enzymes in the Sphingobium sp. strain SYK-6 β-aryl etherase pathway.Recent insights into Pasteurella multocida toxin and other G-protein-modulating bacterial toxins.Activity-based probes: discovering new biology and new drug targets.Self-cleaving fusion tags for recombinant protein production.Targeting bacterial toxins.Comparative structural analysis of the caspase family with other clan CD cysteine peptidases.Targeting and inactivation of bacterial toxins by human defensins.Actin activates Pseudomonas aeruginosa ExoY nucleotidyl cyclase toxin and ExoY-like effector domains from MARTX toxins.Extracellular proteolytic enzymes produced by human pathogenic vibrio species.Simplified protein purification using an autoprocessing, inducible enzyme tag.A group of sequence-related sphingomonad enzymes catalyzes cleavage of β-aryl ether linkages in lignin β-guaiacyl and β-syringyl ether dimers.Substrate specificity and the effect of calcium on Trypanosoma brucei metacaspase 2.Architecture of the type IV coupling protein complex of Legionella pneumophila.CavityPlus: a web server for protein cavity detection with pharmacophore modelling, allosteric site identification and covalent ligand binding ability prediction.

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Mechanistic and structural insights into the proteolytic activation of Vibrio cholerae MARTX toxin

http://www.wikidata.org/entity/Q27655603

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2009 nî lūn-bûn

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2009 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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Mechanistic and structural ins ...... of Vibrio cholerae MARTX toxin

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Mechanistic and structural ins ...... of Vibrio cholerae MARTX toxin

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Mechanistic and structural ins ...... of Vibrio cholerae MARTX toxin

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Mechanistic and structural ins ...... of Vibrio cholerae MARTX toxin

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Mechanistic and structural ins ...... of Vibrio cholerae MARTX toxin

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Mechanistic and structural ins ...... of Vibrio cholerae MARTX toxin

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Mechanistic and structural ins ...... of Vibrio cholerae MARTX toxin

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Mechanistic and structural ins ...... of Vibrio cholerae MARTX toxin

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Mechanistic and structural ins ...... of Vibrio cholerae MARTX toxin

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Nature Chemical Biology

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Mechanistic and structural ins ...... of Vibrio cholerae MARTX toxin

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Andrew Guzzetta

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James C Powers

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K Christopher Garcia

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Patrick J Lupardus

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Victoria E Albrow

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Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8

MolProbity: all-atom contacts and structure validation for proteins and nucleic acids

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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

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

Coot: model-building tools for molecular graphics

A graphical user interface to the CCP4 program suite

Phasercrystallographic software

Refinement of macromolecular structures by the maximum-likelihood method

Irreversible inhibitors of serine, cysteine, and threonine proteases

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469-478

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10.1038/NCHEMBIO.178

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7

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2009-07-01T00:00:00Z

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19465933

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Vibrio cholerae

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2783333

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