Force-dependent polymorphism in type IV pili reveals hidden epitopes. - sprookjes - yvandenbroek - TriplyDB

Force-dependent polymorphism in type IV pili reveals hidden epitopes.

Force-dependent polymorphism in type IV pili reveals hidden epitopes.

http://www.wikidata.org/entity/Q30495238

about

Exceptionally widespread nanomachines composed of type IV pilins: the prokaryotic Swiss Army knives Type IV pilin proteins: versatile molecular modules Steered molecular dynamics simulations of a type IV pilus probe initial stages of a force-induced conformational transition Rapid cytoskeletal response of epithelial cells to force generation by type IV pili Structure and Assembly of a Trans-Periplasmic Channel for Type IV Pili in Neisseria meningitidis The structure of the CS1 pilus of enterotoxigenic Escherichia coli reveals structural polymorphism.Structure of the Type IVa Major Pilin from the Electrically Conductive Bacterial Nanowires of Geobacter sulfurreducens Architecture of the type IVa pilus machine Type-IV Pilus deformation can explain retraction behavior Structure of the Neisseria meningitidis Type IV pilus.Distinct docking and stabilization steps of the Pseudopilus conformational transition path suggest rotational assembly of type IV pilus-like fibers.Bundle-forming pilus retraction enhances enteropathogenic Escherichia coli infectivity Strength of Neisseria meningitidis binding to endothelial cells requires highly-ordered CD147/β2-adrenoceptor clusters assembled by alpha-actinin-4.Formation of bacterial pilus-like nanofibres by designed minimalistic self-assembling peptides.Asymmetric distribution of type IV pili triggered by directional light in unicellular cyanobacteria.N. elongata produces type IV pili that mediate interspecies gene transfer with N. gonorrhoeae.Uncovering the mechanism of trapping and cell orientation during Neisseria gonorrhoeae twitching motility Nanoscale adhesion forces of Pseudomonas aeruginosa type IV Pili.Speed switching of gonococcal surface motility correlates with proton motive force.Mechanotransduction: use the force(s).Type IV pili mechanochemically regulate virulence factors in Pseudomonas aeruginosa.Retraction of enteropathogenic E. coli type IV pili promotes efficient host cell colonization, effector translocation and tight junction disruption The Vibrio cholerae Minor Pilin TcpB Initiates Assembly and Retraction of the Toxin-Coregulated Pilus.Low Energy Atomic Models Suggesting a Pilus Structure that could Account for Electrical Conductivity of Geobacter sulfurreducens Pili.Domain-domain interactions in filamin A (16-23) impose a hierarchy of unfolding forces The type II secretion system: biogenesis, molecular architecture and mechanism.Mutation of the conserved calcium-binding motif in Neisseria gonorrhoeae PilC1 impacts adhesion but not piliation.The hypervariable region of meningococcal major pilin PilE controls the host cell response via antigenic variation.Neisseria meningitidis colonization of the brain endothelium and cerebrospinal fluid invasion.Cyclic diguanylate signaling in Gram-positive bacteria Cryo-EM of bacterial pili and archaeal flagellar filaments.Enterotoxigenic Escherichia coli CS1 pilus: not one structure but several.Nanoscale Pulling of Type IV Pili Reveals Their Flexibility and Adhesion to Surfaces over Extended Lengths of the Pili The Screw-Like Movement of a Gliding Bacterium Is Powered by Spiral Motion of Cell-Surface Adhesins.Phenotypic Heterogeneity in Attachment of Marine Bacteria toward Antifouling Copolymers Unraveled by AFM The meningococcal minor pilin PilX is responsible for type IV pilus conformational changes associated with signaling to endothelial cells.Type IV pili-a numbers game.Mass spectrometry unmasks mystery Methanococcus pilin.Functional role of the type 1 pilus rod structure in mediating host-pathogen interactions.Twitching motility of bacteria with type-IV pili: Fractal walks, first passage time, and their consequences on microcolonies.

P2860

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P2860

Force-dependent polymorphism in type IV pili reveals hidden epitopes.

http://www.wikidata.org/entity/Q30495238

description

2010 nî lūn-bûn

@nan

2010 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Force-dependent polymorphism in type IV pili reveals hidden epitopes.

@ast

Force-dependent polymorphism in type IV pili reveals hidden epitopes.

@en

type

label

Force-dependent polymorphism in type IV pili reveals hidden epitopes.

@ast

Force-dependent polymorphism in type IV pili reveals hidden epitopes.

@en

prefLabel

Force-dependent polymorphism in type IV pili reveals hidden epitopes.

@ast

Force-dependent polymorphism in type IV pili reveals hidden epitopes.

@en

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PNAS.0911328107

P1433

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

P1476

Force-dependent polymorphism in type IV pili reveals hidden epitopes

@en

P2093

Dustin L Higashi

http://www.w3.org/2001/XMLSchema#string

Jasna Brujic

http://www.w3.org/2001/XMLSchema#string

Michael P Sheetz

http://www.w3.org/2001/XMLSchema#string

Nicolas Biais

http://www.w3.org/2001/XMLSchema#string

P2860

Structural plasticity in actin and tubulin polymer dynamics.

The N. gonorrhoeae type IV pilus stimulates mechanosensitive pathways and cytoprotection through a pilT-dependent mechanism.

Cooperative retraction of bundled type IV pili enables nanonewton force generation

Uncoiling mechanics of Escherichia coli type I fimbriae are optimized for catch bonds

3D structure/function analysis of PilX reveals how minor pilins can modulate the virulence properties of type IV pili

The nature of the globular- to fibrous-actin transition

Pilus retraction powers bacterial twitching motility

Dynamic instability of microtubule growth

Type IV pili and twitching motility

Stretching single talin rod molecules activates vinculin binding

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11358-11363

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scholarly article

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10.1073/PNAS.0911328107

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25

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107

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2010-06-03T00:00:00Z

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44660043

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20534431

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2895099

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