Allosteric coupling in the bacterial adhesive protein FimH - Wikidata - awgldk - TriplyDB

Allosteric coupling in the bacterial adhesive protein FimH

Allosteric coupling in the bacterial adhesive protein FimH

http://www.wikidata.org/entity/Q37099778

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Adhesive Pili in UTI Pathogenesis and Drug Development The tyrosine gate of the bacterial lectin FimH: a conformational analysis by NMR spectroscopy and X-ray crystallography Mechanism of allosteric propagation across a β-sheet structure investigated by molecular dynamics simulations.Evolutionary fine-tuning of conformational ensembles in FimH during host-pathogen interactions.Inactive conformation enhances binding function in physiological conditions Positively selected FimH residues enhance virulence during urinary tract infection by altering FimH conformation Rational design strategies for FimH antagonists: new drugs on the horizon for urinary tract infection and Crohn's disease.Adhesion of Escherichia coli under flow conditions reveals potential novel effects of FimH mutations.Conformational Switch of the Bacterial Adhesin FimH in the Absence of the Regulatory Domain - Engineering a Minimalistic Allosteric System.Alternate thermoregulation and functional binding of Escherichia coli type 1 fimbriae in environmental and animal isolates.

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P2860

Allosteric coupling in the bacterial adhesive protein FimH

http://www.wikidata.org/entity/Q37099778

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

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scientific article published on 02 July 2013

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Allosteric coupling in the bacterial adhesive protein FimH

@en

Allosteric coupling in the bacterial adhesive protein FimH.

@nl

type

label

Allosteric coupling in the bacterial adhesive protein FimH

@en

Allosteric coupling in the bacterial adhesive protein FimH.

@nl

prefLabel

Allosteric coupling in the bacterial adhesive protein FimH

@en

Allosteric coupling in the bacterial adhesive protein FimH.

@nl

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JBC.M113.461376

P1433

Journal of Biological Chemistry

P1476

Allosteric coupling in the bacterial adhesive protein FimH

@en

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Evgeni V Sokurenko

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

Gianluca Interlandi

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

Veronika Tchesnokova

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

Victoria B Rodriguez

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

P2860

The Protein Data Bank

Type 1 fimbrial adhesin FimH elicits an immune response that enhances cell adhesion of Escherichia coli

Intervening with urinary tract infections using anti-adhesives based on the crystal structure of the FimH-oligomannose-3 complex

Native protein sequences are close to optimal for their structures

CHARMM: the biomolecular simulation program

X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli

Structural basis of tropism of Escherichia coli to the bladder during urinary tract infection

Structural Basis for Mechanical Force Regulation of the Adhesin FimH via Finger Trap-like β Sheet Twisting

All-atom empirical potential for molecular modeling and dynamics studies of proteins

Scalable molecular dynamics with NAMD

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24128-24139

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scholarly article

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10.1074/JBC.M113.461376

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33

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288

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2013-07-02T00:00:00Z

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23821547

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3745355

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