Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form
about
The cholesterol-dependent cytolysin signature motif: a critical element in the allosteric pathway that couples membrane binding to pore assemblyCholesterol-dependent cytolysins, a family of versatile pore-forming toxinsCholesterol exposure at the membrane surface is necessary and sufficient to trigger perfringolysin O bindingListeriolysin O: a genuine cytolysin optimized for an intracellular parasitePerfringolysin O Theta Toxin as a Tool to Monitor the Distribution and Inhomogeneity of Cholesterol in Cellular MembranesObstructing toxin pathways by targeted pore blockagePutting the structure into complementMultifaceted activity of listeriolysin O, the cholesterol-dependent cytolysin of Listeria monocytogenesMore than a pore: the cellular response to cholesterol-dependent cytolysinsThe pore-forming haemolysins of bacillus cereus: a reviewConformational changes during pore formation by the perforin-related protein pleurotolysinA new model for pore formation by cholesterol-dependent cytolysinsStructural basis of complement membrane attack complex formation.Structure of a membrane-attack complex/perforin (MACPF) family protein from the human gut symbiont Bacteroides thetaiotaomicronStructural Basis of Sterol Binding by NPC2, a Lysosomal Protein Deficient in Niemann-Pick Type C2 DiseaseA common fold mediates vertebrate defense and bacterial attackStructure of C8alpha-MACPF reveals mechanism of membrane attack in complement immune defenseX-ray crystal structure of the B component of Hemolysin BL fromBacillus cereusCellular Functions and X-ray Structure of Anthrolysin O, a Cholesterol-dependent Cytolysin Secreted by Bacillus anthracisAssembly and regulation of the membrane attack complex based on structures of C5b6 and sC5b9.Anthrax toxin protective antigen integrates poly- -D-glutamate and pH signals to sense the optimal environment for channel formationManipulating the Lewis antigen specificity of the cholesterol-dependent cytolysin lectinolysinStructure of Complement C6 Suggests a Mechanism for Initiation and Unidirectional, Sequential Assembly of Membrane Attack Complex (MAC)Structure of the Lectin Regulatory Domain of the Cholesterol-Dependent Cytolysin Lectinolysin Reveals the Basis for Its Lewis Antigen SpecificityStructural Basis for Recognition of the Pore-Forming Toxin Intermedilysin by Human Complement Receptor CD59Phosphoinositide-mediated oligomerization of a defensin induces cell lysisCrystal structure of listeriolysin O reveals molecular details of oligomerization and pore formationStructural Basis for Receptor Recognition by the Human CD59-Responsive Cholesterol-Dependent CytolysinsCholesterol-dependent interaction of syncollin with the membrane of the pancreatic zymogen granulepH dependence of listeriolysin O aggregation and pore-forming abilityDisentangling the roles of cholesterol and CD59 in intermedilysin pore formation.Revisiting the membrane interaction mechanism of a membrane-damaging β-barrel pore-forming toxin Vibrio cholerae cytolysin.The Cholesterol-dependent Cytolysin Membrane-binding Interface Discriminates Lipid Environments of Cholesterol to Support β-Barrel Pore Insertion.The Apicomplexan CDC/MACPF-like pore-forming proteins.Decreasing Transmembrane Segment Length Greatly Decreases Perfringolysin O Pore Size.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.Monomer-monomer interactions propagate structural transitions necessary for pore formation by the cholesterol-dependent cytolysins.
P2860
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P2860
Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form
description
1997 nî lūn-bûn
@nan
1997 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
Structure of a cholesterol-bin ...... d a model of its membrane form
@ast
Structure of a cholesterol-bin ...... d a model of its membrane form
@en
Structure of a cholesterol-bin ...... d a model of its membrane form
@nl
type
label
Structure of a cholesterol-bin ...... d a model of its membrane form
@ast
Structure of a cholesterol-bin ...... d a model of its membrane form
@en
Structure of a cholesterol-bin ...... d a model of its membrane form
@nl
prefLabel
Structure of a cholesterol-bin ...... d a model of its membrane form
@ast
Structure of a cholesterol-bin ...... d a model of its membrane form
@en
Structure of a cholesterol-bin ...... d a model of its membrane form
@nl
P2093
P3181
P1433
P1476
Structure of a cholesterol-bin ...... d a model of its membrane form
@en
P2093
M W Parker
R K Tweten
W J McKinstry
P304
P3181
P356
10.1016/S0092-8674(00)80251-2
P407
P577
1997-05-30T00:00:00Z