Crystal structure of the octameric pore of staphylococcal γ-hemolysin reveals the β-barrel pore formation mechanism by two components - Wikidata - wikimedia - TriplyDB

Crystal structure of the octameric pore of staphylococcal γ-hemolysin reveals the β-barrel pore formation mechanism by two components

Crystal structure of the octameric pore of staphylococcal γ-hemolysin reveals the β-barrel pore formation mechanism by two components

http://www.wikidata.org/entity/Q24634854

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Antimicrobial Mechanisms of Macrophages and the Immune Evasion Strategies of Staphylococcus aureus Obstructing toxin pathways by targeted pore blockage From evolution to pathogenesis: the link between β-barrel assembly machineries in the outer membrane of mitochondria and gram-negative bacteria Staphylococcal alpha-phenol soluble modulins contribute to neutrophil lysis after phagocytosis.Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein.Molecular Architecture and Functional Analysis of NetB, a Pore-forming Toxin from Clostridium perfringens Vibrio cholerae Cytolysin Recognizes the Heptasaccharide Core of Complex N-Glycans with Nanomolar Affinity Structural and Functional Analysis of the Pore-Forming Toxin NetB from Clostridium perfringens Structural Insights into Clostridium perfringens Delta Toxin Pore Formation Residues Essential for Panton-Valentine Leukocidin S Component Binding to Its Cell Receptor Suggest Both Plasticity and Adaptability in Its Interaction Surface Molecular basis of transmembrane beta-barrel formation of staphylococcal pore-forming toxins Structural basis for receptor recognition and pore formation of a zebrafish aerolysin-like protein De novo phasing with X-ray laser reveals mosquito larvicide BinAB structure Staphylococcus aureus Pore-Forming Toxins.X-ray and Cryo-electron Microscopy Structures of Monalysin Pore-forming Toxin Reveal Multimerization of the Pro-form.An intermolecular electrostatic interaction controls the prepore-to-pore transition in a cholesterol-dependent cytolysin.Hemolytic lectin CEL-III heptamerizes via a large structural transition from α-helices to a β-barrel during the transmembrane pore formation process.Identification of a crucial residue required for Staphylococcus aureus LukAB cytotoxicity and receptor recognition.New insight into the molecular control of bacterial functional amyloids The Relationship between Glycan Binding and Direct Membrane Interactions in Vibrio cholerae Cytolysin, a Channel-forming Toxin.Structural basis for self-assembly of a cytolytic pore lined by protein and lipid The bicomponent pore-forming leucocidins of Staphylococcus aureus Effects of MACPF/CDC proteins on lipid membranes.Role of pore-forming toxins in bacterial infectious diseases.Structurally designed attenuated subunit vaccines for S. aureus LukS-PV and LukF-PV confer protection in a mouse bacteremia model.Structure-function analysis of heterodimer formation, oligomerization, and receptor binding of the Staphylococcus aureus bi-component toxin LukGH.Separately or combined, LukG/LukH is functionally unique compared to other staphylococcal bicomponent leukotoxins Five birds, one stone: neutralization of α-hemolysin and 4 bi-component leukocidins of Staphylococcus aureus with a single human monoclonal antibody.Bovine Staphylococcus aureus Secretes the Leukocidin LukMF' To Kill Migrating Neutrophils through CCR1.Crystallization and preliminary crystallographic studies of both components of the staphylococcal LukE-LukD leukotoxin.Counter inhibition between leukotoxins attenuates Staphylococcus aureus virulence.Context matters: The importance of dimerization-induced conformation of the LukGH leukocidin of Staphylococcus aureus for the generation of neutralizing antibodies.Unzipping of A-Form DNA-RNA, A-Form DNA-PNA, and B-Form DNA-DNA in the α-Hemolysin Nanopore.Infectious keratitis: secreted bacterial proteins that mediate corneal damage.Crystal structures of the components of the Staphylococcus aureus leukotoxin ED.Exploiting dominant-negative toxins to combat Staphylococcus aureus pathogenesis Inhibiting bacterial toxins by channel blockage.Staphylococcus aureus elaborates leukocidin AB to mediate escape from within human neutrophils Role of pore-forming toxins in neonatal sepsis The effects of Staphylococcus aureus leukotoxins on the host: cell lysis and beyond.

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P2860

Crystal structure of the octameric pore of staphylococcal γ-hemolysin reveals the β-barrel pore formation mechanism by two components

http://www.wikidata.org/entity/Q24634854

description

2011 nî lūn-bûn

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2011 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2011 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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Crystal structure of the octam ...... on mechanism by two components

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Crystal structure of the octam ...... on mechanism by two components

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Crystal structure of the octam ...... on mechanism by two components

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Crystal structure of the octam ...... on mechanism by two components

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Crystal structure of the octam ...... on mechanism by two components

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Crystal structure of the octam ...... on mechanism by two components

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Crystal structure of the octam ...... on mechanism by two components

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Crystal structure of the octam ...... on mechanism by two components

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Crystal structure of the octam ...... on mechanism by two components

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Crystal structure of the octam ...... on mechanism by two components

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Crystal structure of the octam ...... on mechanism by two components

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PNAS.1110402108

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Proceedings of the National Academy of Sciences of the United States of America

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Crystal structure of the octam ...... on mechanism by two components

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Isao Tanaka

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Jun Kaneko

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Min Yao

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Nagisa Hirano

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Noriko Tomita

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Yoshikazu Tanaka

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Yoshiyuki Kamio

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Yuka Kawai

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P2860

Crystal structure of the Vibrio cholerae cytolysin heptamer reveals common features among disparate pore-forming toxins

The structure of a Staphylococcus aureus leucocidin component (LukF-PV) reveals the fold of the water-soluble species of a family of transmembrane pore-forming toxins

Crystal structure of staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel

A covalent S-F heterodimer of leucotoxin reveals molecular plasticity of beta-barrel pore-forming toxins

2-Methyl-2,4-pentanediol induces spontaneous assembly of staphylococcal α-hemolysin into heptameric pore structure

Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore

Bacterial two-component and hetero-heptameric pore-forming cytolytic toxins: structures, pore-forming mechanism, and organization of the genes

Crystal structure of leucotoxin S component: new insight into the Staphylococcal beta-barrel pore-forming toxins

Assembly of the Bi-component leukocidin pore examined by truncation mutagenesis.

The leukocidin pore: evidence for an octamer with four LukF subunits and four LukS subunits alternating around a central axis.

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42

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108

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Keitaro Yamashita

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