Membrane insertion of Escherichia coli alpha-hemolysin is independent from membrane lysis.
about
Binding of β-amyloid (1-42) peptide to negatively charged phospholipid membranes in the liquid-ordered state: modeling and experimental studiesMembranes: a meeting point for lipids, proteins and therapiesCommon and pathogen-specific virulence factors are different in function and structure.Mechanisms of cytolysin-induced cell damage -- a role for auto- and paracrine signalling.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.Relevance of fatty acid covalently bound to Escherichia coli alpha-hemolysin and membrane microdomains in the oligomerization process.Lysenin-His, a sphingomyelin-recognizing toxin, requires tryptophan 20 for cation-selective channel assembly but not for membrane binding.The calcium-binding C-terminal domain of Escherichia coli alpha-hemolysin is a major determinant in the surface-active properties of the protein.Novel evidence for the specific interaction between cholesterol and α-haemolysin ofEscherichia coli
P2860
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P2860
Membrane insertion of Escherichia coli alpha-hemolysin is independent from membrane lysis.
description
2005 nî lūn-bûn
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2005年の論文
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2005年学术文章
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2005年学术文章
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2005年学术文章
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2005年学术文章
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name
Membrane insertion of Escheric ...... dependent from membrane lysis.
@en
Membrane insertion of Escheric ...... dependent from membrane lysis.
@nl
type
label
Membrane insertion of Escheric ...... dependent from membrane lysis.
@en
Membrane insertion of Escheric ...... dependent from membrane lysis.
@nl
prefLabel
Membrane insertion of Escheric ...... dependent from membrane lysis.
@en
Membrane insertion of Escheric ...... dependent from membrane lysis.
@nl
P2093
P2860
P356
P1476
Membrane insertion of Escheric ...... dependent from membrane lysis.
@en
P2093
Félix M Goñi
Helena Ostolaza
Lissete Sánchez-Magraner
P2860
P304
P356
10.1074/JBC.M512897200
P407
P577
2005-12-22T00:00:00Z