Cellular Functions and X-ray Structure of Anthrolysin O, a Cholesterol-dependent Cytolysin Secreted by Bacillus anthracis - Test2 - elhamkhani - TriplyDB

Cellular Functions and X-ray Structure of Anthrolysin O, a Cholesterol-dependent Cytolysin Secreted by Bacillus anthracis

Cellular Functions and X-ray Structure of Anthrolysin O, a Cholesterol-dependent Cytolysin Secreted by Bacillus anthracis

http://www.wikidata.org/entity/Q27654239

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The cholesterol-dependent cytolysin signature motif: a critical element in the allosteric pathway that couples membrane binding to pore assembly Bacillus anthracis factors for phagosomal escape More than a pore: the cellular response to cholesterol-dependent cytolysins The pore-forming haemolysins of bacillus cereus: a review A new model for pore formation by cholesterol-dependent cytolysins Structure of the Lectin Regulatory Domain of the Cholesterol-Dependent Cytolysin Lectinolysin Reveals the Basis for Its Lewis Antigen Specificity Structural Basis for Recognition of the Pore-Forming Toxin Intermedilysin by Human Complement Receptor CD59 Crystal structure of listeriolysin O reveals molecular details of oligomerization and pore formation pH dependence of listeriolysin O aggregation and pore-forming ability Disentangling the roles of cholesterol and CD59 in intermedilysin pore formation.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 cytolysins Membrane assembly of the cholesterol-dependent cytolysin pore complex.Only two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface.Development of a single-gene, signature-tag-based approach in combination with alanine mutagenesis to identify listeriolysin O residues critical for the in vivo survival of Listeria monocytogenes.A novel cholesterol-insensitive mode of membrane binding promotes cytolysin-mediated translocation by Streptolysin O Anthrolysin O and fermentation products mediate the toxicity of Bacillus anthracis to lung epithelial cells under microaerobic conditions.Structural studies of Streptococcus pyogenes streptolysin O provide insights into the early steps of membrane penetration.New insights into gastrointestinal anthrax infection.Stepwise visualization of membrane pore formation by suilysin, a bacterial cholesterol-dependent cytolysin.Listeriolysin O Affects the Permeability of Caco-2 Monolayer in a Pore-Dependent and Ca2+-Independent Manner.The role of anthrolysin O in gut epithelial barrier disruption during Bacillus anthracis infection.Packing a punch: the mechanism of pore formation by cholesterol dependent cytolysins and membrane attack complex/perforin-like proteins.Crystal structure of Streptococcus pneumoniae pneumolysin provides key insights into early steps of pore formation.Crystal structure of cytotoxin protein suilysin from Streptococcus suis.The adenylyl cyclase activity of anthrax edema factor.Variability of cholesterol accessibility in human red blood cells measured using a bacterial cholesterol-binding toxin Anthrax vaccines: present status and future prospects.Bacterial Virulence Factors: Secreted for Survival.Listeriolysin O: from bazooka to Swiss army knife.Switch-like responses of two cholesterol sensors do not require protein oligomerization in membranes.Continuous transport of a small fraction of plasma membrane cholesterol to endoplasmic reticulum regulates total cellular cholesterol.Targeted amino acid substitutions impair streptolysin O toxicity and group A Streptococcus virulence.Calcium-induced folding of intrinsically disordered repeat-in-toxin (RTX) motifs via changes of protein charges and oligomerization states.Crystallization and X-ray crystallographic analysis of the cholesterol-dependent cytolysin listeriolysin O from Listeria monocytogenes.Mechanistic Insights into the Cholesterol-dependent Binding of Perfringolysin O-based Probes and Cell Membranes.

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Cellular Functions and X-ray Structure of Anthrolysin O, a Cholesterol-dependent Cytolysin Secreted by Bacillus anthracis

http://www.wikidata.org/entity/Q27654239

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2009 nî lūn-bûn

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2009年の論文

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Cellular Functions and X-ray S ...... Secreted by Bacillus anthracis

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Cellular Functions and X-ray S ...... Secreted by Bacillus anthracis

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Cellular Functions and X-ray S ...... Secreted by Bacillus anthracis

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Cellular Functions and X-ray S ...... Secreted by Bacillus anthracis

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Cellular Functions and X-ray S ...... Secreted by Bacillus anthracis

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Cellular Functions and X-ray S ...... Secreted by Bacillus anthracis

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Cellular Functions and X-ray S ...... Secreted by Bacillus anthracis

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Elise M Mosser

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Enrico Malito

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Richard F Rest

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P2860

Cholesterol-dependent cytolysins, a family of versatile pore-forming toxins

Bacillus cereus and related species

High-resolution structure prediction and the crystallographic phase problem

Redefining cholesterol's role in the mechanism of the cholesterol-dependent cytolysins

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

PROCHECK: a program to check the stereochemical quality of protein structures

Processing of X-ray diffraction data collected in oscillation mode

A common fold mediates vertebrate defense and bacterial attack

Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form

Coot: model-building tools for molecular graphics

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21

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284

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Alexandre Chenal

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