Auto-catalytic cleavage of Clostridium difficile toxins A and B depends on cysteine protease activity.
about
Clostridial glucosylating toxins enter cells via clathrin-mediated endocytosisCharacterization of the membrane-targeting C1 domain in Pasteurella multocida toxinHost S-nitrosylation inhibits clostridial small molecule-activated glucosylating toxinsClostridium difficile Toxins A and B: Insights into Pathogenic Properties and Extraintestinal EffectsReactive Oxygen Species as Additional Determinants for Cytotoxicity of Clostridium difficile Toxins A and BThe Role of Rho GTPases in Toxicity of Clostridium difficile ToxinsClostridium difficile infection: molecular pathogenesis and novel therapeuticsClostridial toxins: sensing a target in a hostile gut environment.Conformational analysis of Clostridium difficile toxin B and its implications for substrate recognitionClostridium difficile Toxin B causes epithelial cell necrosis through an autoprocessing-independent mechanismStructure-Function Analysis of Inositol Hexakisphosphate-induced Autoprocessing in Clostridium difficile Toxin ASmall Molecule-Induced Allosteric Activation of the Vibrio cholerae RTX Cysteine Protease DomainMechanistic and structural insights into the proteolytic activation of Vibrio cholerae MARTX toxinRational Design of Inhibitors and Activity-Based Probes Targeting Clostridium difficile Virulence Factor TcdBDefining an allosteric circuit in the cysteine protease domain of Clostridium difficile toxinsStructural Determinants of Clostridium difficile Toxin A Glucosyltransferase ActivityThe structure of Clostridium difficile toxin A glucosyltransferase domain bound to Mn2+ and UDP provides insights into glucosyltransferase activity and product releaseThe CD27L and CTP1L Endolysins Targeting Clostridia Contain a Built-in Trigger and Release FactorVariations in TcdB activity and the hypervirulence of emerging strains of Clostridium difficileStructure-function analysis of inositol hexakisphosphate-induced autoprocessing of the Vibrio cholerae multifunctional autoprocessing RTX toxin[Clostridium difficile infections in geriatric patients].Systems analysis of the transcriptional response of human ileocecal epithelial cells to Clostridium difficile toxins and effects on cell cycle control.Structural organization of the functional domains of Clostridium difficile toxins A and BExpression of recombinant Clostridium difficile toxin A and B in Bacillus megateriumAllosteric regulation of protease activity by small molecules.Inositol hexakisphosphate-induced autoprocessing of large bacterial protein toxins.LRP1 is a receptor for Clostridium perfringens TpeL toxin indicating a two-receptor model of clostridial glycosylating toxinsThe role of toxin A and toxin B in Clostridium difficile-associated disease: Past and present perspectives.Bacterial factors exploit eukaryotic Rho GTPase signaling cascades to promote invasion and proliferation within their host.Using phenotype microarrays to determine culture conditions that induce or repress toxin production by Clostridium difficile and other microorganisms.The roles of host and pathogen factors and the innate immune response in the pathogenesis of Clostridium difficile infection.Clostridium difficile 027/BI/NAP1 encodes a hypertoxic and antigenically variable form of TcdB.Critical roles of Clostridium difficile toxin B enzymatic activities in pathogenesis.Toxin-specific antibodies for the treatment of Clostridium difficile: current status and future perspectives.Autoproteolytic activation of bacterial toxins.Retargeting Clostridium difficile Toxin B to Neuronal Cells as a Potential Vehicle for Cytosolic Delivery of Therapeutic Biomolecules to Treat Botulism.Masking autoprocessing of Clostridium difficile toxin A by the C-terminus combined repetitive oligo peptides.The impact of phosphorus on the immune system and the intestinal microbiota with special focus on the pig.Increased toxin expression in a Clostridium difficile mfd mutant.Clostridium difficile toxins: mediators of inflammation.
P2860
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P2860
Auto-catalytic cleavage of Clostridium difficile toxins A and B depends on cysteine protease activity.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
2007年學術文章
@zh
2007年學術文章
@zh-hant
name
Auto-catalytic cleavage of Clo ...... on cysteine protease activity.
@en
Auto-catalytic cleavage of Clo ...... on cysteine protease activity.
@nl
type
label
Auto-catalytic cleavage of Clo ...... on cysteine protease activity.
@en
Auto-catalytic cleavage of Clo ...... on cysteine protease activity.
@nl
prefLabel
Auto-catalytic cleavage of Clo ...... on cysteine protease activity.
@en
Auto-catalytic cleavage of Clo ...... on cysteine protease activity.
@nl
P2093
P356
P1476
Auto-catalytic cleavage of Clo ...... on cysteine protease activity.
@en
P2093
Karla J Fullner Satchell
Klaus Aktories
Martina Egerer
Thomas Jank
Torsten Giesemann
P304
25314-25321
P356
10.1074/JBC.M703062200
P407
P577
2007-06-25T00:00:00Z