Effects of temperature, time, and toxin concentration on lesion formation by the Escherichia coli hemolysin.
about
RTX proteins: a highly diverse family secreted by a common mechanismEscherichia coli strains colonising the gastrointestinal tract protect germfree mice against Salmonella typhimurium infectionDifferences in purinergic amplification of osmotic cell lysis by the pore-forming RTX toxins Bordetella pertussis CyaA and Actinobacillus pleuropneumoniae ApxIA: the role of pore size.Alpha hemolysin induces an increase of erythrocytes calcium: a FLIM 2-photon phasor analysis approachMacrophage damage by Leishmania amazonensis cytolysin: evidence of pore formation on cell membraneParadoxical lipid dependence of pores formed by the Escherichia coli alpha-hemolysin in planar phospholipid bilayer membranes.Hemolytic activity of the Pasteurella haemolytica leukotoxin.The 46-kilodalton-hemolysin gene from Treponema denticola encodes a novel hemolysin homologous to aminotransferases.The deletion of several amino acid stretches of Escherichia coli alpha-hemolysin (HlyA) suggests that the channel-forming domain contains beta-strands.Escherichia coli hemolysin mutants with altered target cell specificity.Channel-forming activity and channel size of the RTX toxins ApxI, ApxII, and ApxIII of Actinobacillus pleuropneumoniae.Binding of Pasteurella haemolytica leukotoxin to bovine leukocytesInactivation of host Akt/protein kinase B signaling by bacterial pore-forming toxins.Uropathogenic Escherichia coli-Associated ExotoxinsThe RTX pore-forming toxin α-hemolysin of uropathogenic Escherichia coli: progress and perspectives.Helicobacter pylori pore-forming cytolysin orthologue TlyA possesses in vitro hemolytic activity and has a role in colonization of the gastric mucosa.Acylation of Escherichia coli hemolysin: a unique protein lipidation mechanism underlying toxin function.Association of RTX toxins with erythrocytes.Prelytic and lytic conformations of erythrocyte-associated Escherichia coli hemolysin.Relevance of fatty acid covalently bound to Escherichia coli alpha-hemolysin and membrane microdomains in the oligomerization process.Membrane Repair Mechanisms against Permeabilization by Pore-Forming Toxins.
P2860
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P2860
Effects of temperature, time, and toxin concentration on lesion formation by the Escherichia coli hemolysin.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
Effects of temperature, time, ...... he Escherichia coli hemolysin.
@en
type
label
Effects of temperature, time, ...... he Escherichia coli hemolysin.
@en
prefLabel
Effects of temperature, time, ...... he Escherichia coli hemolysin.
@en
P2860
P1476
Effects of temperature, time, ...... the Escherichia coli hemolysin
@en
P2093
P2860
P304
P407
P577
1994-10-01T00:00:00Z