Membrane interaction of Escherichia coli hemolysin: flotation and insertion-dependent labeling by phospholipid vesicles.
about
RTX proteins: a highly diverse family secreted by a common mechanismAn insight into the sialome of the blood-sucking bug Triatoma infestans, a vector of Chagas’ diseaseTP0453, a concealed outer membrane protein of Treponema pallidum, enhances membrane permeability.Insight into the salivary transcriptome and proteome of Dipetalogaster maximaPython erythrocytes are resistant to α-hemolysin from Escherichia coli.The deletion of several amino acid stretches of Escherichia coli alpha-hemolysin (HlyA) suggests that the channel-forming domain contains beta-strands.P2X receptor-dependent erythrocyte damage by α-hemolysin from Escherichia coli triggers phagocytosis by THP-1 cells.The RTX pore-forming toxin α-hemolysin of uropathogenic Escherichia coli: progress and perspectives.Inhibition of P2X Receptors Protects Human Monocytes against Damage by Leukotoxin from Aggregatibacter actinomycetemcomitans and α-Hemolysin from Escherichia coliLoop Diuretics Diminish Hemolysis Induced by α-Hemolysin from Escherichia coli.Sialic acid residues are essential for cell lysis mediated by leukotoxin from Aggregatibacter actinomycetemcomitans.Brief heat treatment causes a structural change and enhances cytotoxicity of the Escherichia coli α-hemolysin.Putative identification of an amphipathic alpha-helical sequence in hemolysin of Escherichia coli (HlyA) involved in transmembrane pore formation.Oligomeric states of the Shigella translocator protein IpaB provide structural insights into formation of the type III secretion translocon.Relevance of fatty acid covalently bound to Escherichia coli alpha-hemolysin and membrane microdomains in the oligomerization process.Identification and characterization of an amphipathic leucine zipper-like motif in Escherichia coli toxin hemolysin E. Plausible role in the assembly and membrane destabilization.Haemolysis induced by α-toxin from Staphylococcus aureus requires P2X receptor activation.Binding of Escherichia coli hemolysin and activation of the target cells is not receptor-dependent.The calcium-binding C-terminal domain of Escherichia coli alpha-hemolysin is a major determinant in the surface-active properties of the protein.Membrane insertion of Escherichia coli alpha-hemolysin is independent from membrane lysis.Novel evidence for the specific interaction between cholesterol and α-haemolysin ofEscherichia coli
P2860
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P2860
Membrane interaction of Escherichia coli hemolysin: flotation and insertion-dependent labeling by phospholipid vesicles.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
@zh
2001年學術文章
@zh-hant
name
Membrane interaction of Escher ...... ling by phospholipid vesicles.
@en
Membrane interaction of Escher ...... ling by phospholipid vesicles.
@nl
type
label
Membrane interaction of Escher ...... ling by phospholipid vesicles.
@en
Membrane interaction of Escher ...... ling by phospholipid vesicles.
@nl
prefLabel
Membrane interaction of Escher ...... ling by phospholipid vesicles.
@en
Membrane interaction of Escher ...... ling by phospholipid vesicles.
@nl
P2093
P2860
P1476
Membrane interaction of Escher ...... ling by phospholipid vesicles.
@en
P2093
P2860
P304
P356
10.1128/JB.183.18.5364-5370.2001
P407
P577
2001-09-01T00:00:00Z