Monomer-monomer interactions propagate structural transitions necessary for pore formation by the cholesterol-dependent cytolysins.
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A new model for pore formation by cholesterol-dependent cytolysinsStructural Basis for Recognition of the Pore-Forming Toxin Intermedilysin by Human Complement Receptor CD59Disentangling the roles of cholesterol and CD59 in intermedilysin pore formation.The Cholesterol-dependent Cytolysin Membrane-binding Interface Discriminates Lipid Environments of Cholesterol to Support β-Barrel Pore Insertion.An intermolecular electrostatic interaction controls the prepore-to-pore transition in a cholesterol-dependent cytolysin.Crucial role of perfringolysin O D1 domain in orchestrating structural transitions leading to membrane-perforating pores: a hydrogen-deuterium exchange study.Perfringolysin O structure and mechanism of pore formation as a paradigm for cholesterol-dependent cytolysinsDisulfide-bond scanning reveals assembly state and β-strand tilt angle of the PFO β-barrel.Mouse, but not human, ApoB-100 lipoprotein cholesterol is a potent innate inhibitor of Streptococcus pneumoniae pneumolysin.Streptolysin O and its co-toxin NAD-glycohydrolase protect group A Streptococcus from Xenophagic killing.The cytolytic activity of vaginolysin strictly depends on cholesterol and is potentiated by human CD59.Stepwise visualization of membrane pore formation by suilysin, a bacterial cholesterol-dependent cytolysin.Perfringolysin O: The Underrated Clostridium perfringens Toxin?Crystal structure of Streptococcus pneumoniae pneumolysin provides key insights into early steps of pore formation.Stonefish toxin defines an ancient branch of the perforin-like superfamily.Real-time visualization of perforin nanopore assembly.Mechanistic Insights into the Cholesterol-dependent Binding of Perfringolysin O-based Probes and Cell Membranes.Environmental pH modulates inerolysin activity via post-binding blockade.
P2860
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P2860
Monomer-monomer interactions propagate structural transitions necessary for pore formation by the cholesterol-dependent cytolysins.
description
2012 nî lūn-bûn
@nan
2012 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Monomer-monomer interactions p ...... lesterol-dependent cytolysins.
@ast
Monomer-monomer interactions p ...... lesterol-dependent cytolysins.
@en
type
label
Monomer-monomer interactions p ...... lesterol-dependent cytolysins.
@ast
Monomer-monomer interactions p ...... lesterol-dependent cytolysins.
@en
prefLabel
Monomer-monomer interactions p ...... lesterol-dependent cytolysins.
@ast
Monomer-monomer interactions p ...... lesterol-dependent cytolysins.
@en
P2093
P2860
P356
P1476
Monomer-monomer interactions p ...... lesterol-dependent cytolysins.
@en
P2093
Allison J Farrand
Arthur E Johnson
Eileen M Hotze
Elizabeth Wilson-Kubalek
Lori Bentsen
Rodney K Tweten
P2860
P304
24534-24543
P356
10.1074/JBC.M112.380139
P407
P577
2012-05-29T00:00:00Z