Putative identification of an amphipathic alpha-helical sequence in hemolysin of Escherichia coli (HlyA) involved in transmembrane pore formation.
about
Reverse micelles as a tool for probing solvent modulation of protein dynamics: Reverse micelle encapsulated hemoglobin.The deletion of several amino acid stretches of Escherichia coli alpha-hemolysin (HlyA) suggests that the channel-forming domain contains beta-strands.The RTX pore-forming toxin α-hemolysin of uropathogenic Escherichia coli: progress and perspectives.
P2860
Putative identification of an amphipathic alpha-helical sequence in hemolysin of Escherichia coli (HlyA) involved in transmembrane pore formation.
description
2008 nî lūn-bûn
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2008年の論文
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2008年学术文章
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name
Putative identification of an ...... transmembrane pore formation.
@en
Putative identification of an ...... hemolysin of Escherichia coli
@nl
type
label
Putative identification of an ...... transmembrane pore formation.
@en
Putative identification of an ...... hemolysin of Escherichia coli
@nl
prefLabel
Putative identification of an ...... transmembrane pore formation.
@en
Putative identification of an ...... hemolysin of Escherichia coli
@nl
P2093
P2860
P356
P1433
P1476
Putative identification of an ...... transmembrane pore formation.
@en
P2093
Angela Valeva
Christina Fischer
Isabel Siegel
Iwan Walev
Mark Wylenzek
Natalia Heinz
Ricarda Reinartz
Robert Schmitt
Silvia Weis
Sucharit Bhakdi
P2860
P304
P356
10.1515/BC.2008.136
P577
2008-09-01T00:00:00Z