Interactions between residues in staphylococcal alpha-hemolysin revealed by reversion mutagenesis.
about
Cholesterol-dependent cytolysins, a family of versatile pore-forming toxinsCrystal structure of the Vibrio cholerae cytolysin heptamer reveals common features among disparate pore-forming toxinsCrystal structure of the octameric pore of staphylococcal γ-hemolysin reveals the β-barrel pore formation mechanism by two componentsNovel structurally designed vaccine for S. aureus α-hemolysin: protection against bacteremia and pneumoniaAn intermolecular electrostatic interaction controls the prepore-to-pore transition in a cholesterol-dependent cytolysin.Role of the amino latch of staphylococcal alpha-hemolysin in pore formation: a co-operative interaction between the N terminus and position 217.Membrane insertion of the heptameric staphylococcal alpha-toxin pore. A domino-like structural transition that is allosterically modulated by the target cell membrane.alpha-Hemolysin, gamma-hemolysin, and leukocidin from Staphylococcus aureus: distant in sequence but similar in structure.Membrane insertion: The strategies of toxins (review).Partial C-terminal unfolding is required for channel formation by staphylococcal alpha-toxin.Tumor protease-activated, pore-forming toxins from a combinatorial library.Protective efficacy of a novel alpha hemolysin subunit vaccine (AT62) against Staphylococcus aureus skin and soft tissue infections.When coupled to natural transformation in Acinetobacter sp. strain ADP1, PCR mutagenesis is made less random by mismatch repair.The H35A mutated alpha-toxin interferes with cytotoxicity of staphylococcal alpha-toxin.Localization and environment of tryptophans in soluble and membrane-bound states of a pore-forming toxin from Staphylococcus aureus.Molecular architecture of a toxin pore: a 15-residue sequence lines the transmembrane channel of staphylococcal alpha-toxin.Structure-function relationships of a membrane pore forming toxin revealed by reversion mutagenesis.Key residues for membrane binding, oligomerization, and pore forming activity of staphylococcal alpha-hemolysin identified by cysteine scanning mutagenesis and targeted chemical modification.
P2860
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P2860
Interactions between residues in staphylococcal alpha-hemolysin revealed by reversion mutagenesis.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
1995年學術文章
@zh
1995年學術文章
@zh-hant
name
Interactions between residues ...... aled by reversion mutagenesis.
@en
type
label
Interactions between residues ...... aled by reversion mutagenesis.
@en
prefLabel
Interactions between residues ...... aled by reversion mutagenesis.
@en
P2860
P356
P1476
Interactions between residues ...... aled by reversion mutagenesis.
@en
P2093
P2860
P304
23072-23076
P356
10.1074/JBC.270.39.23072
P407
P577
1995-09-01T00:00:00Z