Analysis of the in vivo activation of hemolysin (HlyA) from Escherichia coli.
about
RTX proteins: a highly diverse family secreted by a common mechanismIsolation and characterization of Escherichia coli tolC mutants defective in secreting enzymatically active alpha-hemolysin.Hemolytically active (acylated) alpha-hemolysin elicits interleukin-1beta (IL-1beta) but augments the lethality of Escherichia coli by an IL-1- and tumor necrosis factor-independent mechanism.Mass spectrometric analysis of recombinant adenylate cyclase toxin from Bordetella pertussis strain 18323/pHSP9.Role of Mannheimia haemolytica leukotoxin in the pathogenesis of bovine pneumonic pasteurellosis.The deletion of several amino acid stretches of Escherichia coli alpha-hemolysin (HlyA) suggests that the channel-forming domain contains beta-strands.Structure of a bacterial toxin-activating acyltransferase.Interaction between leukotoxin and Cu,Zn superoxide dismutase in Aggregatibacter actinomycetemcomitansAcyltransferases in bacteria.Highly divergent RfaH orthologs from pathogenic proteobacteria can substitute for Escherichia coli RfaH both in vivo and in vitro.Acylation of Escherichia coli hemolysin: a unique protein lipidation mechanism underlying toxin function.Prelytic and lytic conformations of erythrocyte-associated Escherichia coli hemolysin.Incomplete activation of Escherichia coli hemolysin (HlyA) due to mutations in the 3' region of hlyC.Aggregatibacter actinomycetemcomitans leukotoxin is post-translationally modified by addition of either saturated or hydroxylated fatty acyl chainsAcylation of lysine 983 is sufficient for toxin activity of Bordetella pertussis adenylate cyclase. Substitutions of alanine 140 modulate acylation site selectivity of the toxin acyltransferase CyaC.In vivo proteolytic degradation of the Escherichia coli acyltransferase HlyC.Cytotoxic activity of Kingella kingae RtxA toxin depends on post-translational acylation of lysine residues and cholesterol binding
P2860
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P2860
Analysis of the in vivo activation of hemolysin (HlyA) from Escherichia coli.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh
1996年學術文章
@zh-hant
name
Analysis of the in vivo activation of hemolysin (HlyA) from Escherichia coli.
@en
Analysis of the in vivo activation of hemolysin
@nl
type
label
Analysis of the in vivo activation of hemolysin (HlyA) from Escherichia coli.
@en
Analysis of the in vivo activation of hemolysin
@nl
prefLabel
Analysis of the in vivo activation of hemolysin (HlyA) from Escherichia coli.
@en
Analysis of the in vivo activation of hemolysin
@nl
P2093
P2860
P1476
Analysis of the in vivo activation of hemolysin (HlyA) from Escherichia coli.
@en
P2093
P2860
P304
P356
10.1128/JB.178.18.5422-5430.1996
P577
1996-09-01T00:00:00Z