MARTX, multifunctional autoprocessing repeats-in-toxin toxins.
about
RTX proteins: a highly diverse family secreted by a common mechanismHost S-nitrosylation inhibits clostridial small molecule-activated glucosylating toxinsConnecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxinMultifunctional-autoprocessing repeats-in-toxin (MARTX) Toxins of VibriosClostridial toxins: sensing a target in a hostile gut environment.Structural and Molecular Mechanism for Autoprocessing of MARTX Toxin of Vibrio cholerae at Multiple SitesSmall 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 TcdBMARTX toxins as effector delivery platformsIdentification of a conserved membrane localization domain within numerous large bacterial protein toxinsStructure-function analysis of inositol hexakisphosphate-induced autoprocessing of the Vibrio cholerae multifunctional autoprocessing RTX toxinDiversity and impact of prokaryotic toxins on aquatic environments: a reviewGenetic and phenotypic analysis of Vibrio cholerae non-O1, non-O139 isolated from German and Austrian patientsCytotoxicity of the Vibrio vulnificus MARTX toxin effector DUF5 is linked to the C2A subdomain.Type III secretion is essential for the rapidly fatal diarrheal disease caused by non-O1, non-O139 Vibrio cholerae.The burden of cholera.Analysis of Vibrio cholerae genome sequences reveals unique rtxA variants in environmental strains and an rtxA-null mutation in recent altered El Tor isolates.Using small molecules to dissect mechanisms of microbial pathogenesis.Allosteric regulation of protease activity by small molecules.Inositol hexakisphosphate-induced autoprocessing of large bacterial protein toxins.The Haemophilus ducreyi LspA1 protein inhibits phagocytosis by using a new mechanism involving activation of C-terminal Src kinase.Actin Crosslinking Toxins of Gram-Negative BacteriaThe repeat-in-toxin family member TosA mediates adherence of uropathogenic Escherichia coli and survival during bacteremiaVirulence of an emerging pathogenic lineage of Vibrio nigripulchritudo is dependent on two plasmids.Comparison of Xenorhabdus bovienii bacterial strain genomes reveals diversity in symbiotic functions.Vibrio vulnificus rtxA1 gene recombination generates toxin variants with altered potency during intestinal infectionMonoclonal antibodies against Vibrio vulnificus RtxA1 elicit protective immunity through distinct mechanisms.Using phenotype microarrays to determine culture conditions that induce or repress toxin production by Clostridium difficile and other microorganisms.Autoproteolytic activation of bacterial toxins.Homodimerization and binding of specific domains to the target DNA are essential requirements for HlyU to regulate expression of the virulence gene rtxA1, encoding the repeat-in-toxin protein in the human pathogen Vibrio vulnificusVibrio cholerae MARTX toxin heterologous translocation of beta-lactamase and roles of individual effector domains on cytoskeleton dynamics.An Enriched European Eel Transcriptome Sheds Light upon Host-Pathogen Interactions with Vibrio vulnificus.Actin cross-linking domain of Aeromonas hydrophila repeat in toxin A (RtxA) induces host cell rounding and apoptosis.Abundant toxin-related genes in the genomes of beneficial symbionts from deep-sea hydrothermal vent mussels.Draft Genome Sequence of the Marine Pathogen Vibrio coralliilyticus RE22The regulator HlyU, the repeat-in-toxin gene rtxA1, and their roles in the pathogenesis of Vibrio vulnificus infectionsIdentification of a His-Asp-Cys catalytic triad essential for function of the Rho inactivation domain (RID) of Vibrio cholerae MARTX toxin.Characterization of the enzymatic activity of the actin cross-linking domain from the Vibrio cholerae MARTX Vc toxin.Identification and characterization of a repeat-in-toxin gene cluster in Vibrio anguillarum
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MARTX, multifunctional autoprocessing repeats-in-toxin toxins.
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
MARTX, multifunctional autoprocessing repeats-in-toxin toxins.
@ast
MARTX, multifunctional autoprocessing repeats-in-toxin toxins.
@en
type
label
MARTX, multifunctional autoprocessing repeats-in-toxin toxins.
@ast
MARTX, multifunctional autoprocessing repeats-in-toxin toxins.
@en
prefLabel
MARTX, multifunctional autoprocessing repeats-in-toxin toxins.
@ast
MARTX, multifunctional autoprocessing repeats-in-toxin toxins.
@en
P2860
P356
P1476
MARTX, multifunctional autoprocessing repeats-in-toxin toxins.
@en
P2093
Karla J Fullner Satchell
P2860
P304
P356
10.1128/IAI.00525-07
P407
P577
2007-07-23T00:00:00Z