Interdomain interaction in the FimH adhesin of Escherichia coli regulates the affinity to mannose. - Wikidata - wikimedia - TriplyDB

Interdomain interaction in the FimH adhesin of Escherichia coli regulates the affinity to mannose.

Interdomain interaction in the FimH adhesin of Escherichia coli regulates the affinity to mannose.

http://www.wikidata.org/entity/Q52579774

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Subcutaneous immunization with inactivated bacterial components and purified protein of Escherichia coli, Fusobacterium necrophorum and Trueperella pyogenes prevents puerperal metritis in Holstein dairy cows Evolution of Salmonella enterica virulence via point mutations in the fimbrial adhesin.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 Adhesive Pili in UTI Pathogenesis and Drug Development Catch-bond mechanism of the bacterial adhesin FimH.Structural Basis for Mechanical Force Regulation of the Adhesin FimH via Finger Trap-like β Sheet Twisting Tight Conformational Coupling between the Domains of the Enterotoxigenic Escherichia coli Fimbrial Adhesin CfaE Regulates Binding State Transition Mechanism of allosteric propagation across a β-sheet structure investigated by molecular dynamics simulations.Mutation of Tyr137 of the universal Escherichia coli fimbrial adhesin FimH relaxes the tyrosine gate prior to mannose binding.Force spectroscopy reveals multiple "closed states" of the muscle thin filament.Shear-enhanced binding of intestinal colonization factor antigen I of enterotoxigenic Escherichia coli.Adaptive evolution of class 5 fimbrial genes in enterotoxigenic Escherichia coli and its functional consequences.The bacterial fimbrial tip acts as a mechanical force sensor FimH forms catch bonds that are enhanced by mechanical force due to allosteric regulation.Complete genome sequence of Crohn's disease-associated adherent-invasive E. coli strain LF82.Shear-stabilized rolling behavior of E. coli examined with simulations.Force is a signal that cells cannot ignore.Point mutations in FimH adhesin of Crohn's disease-associated adherent-invasive Escherichia coli enhance intestinal inflammatory response.Allosteric catch bond properties of the FimH adhesin from Salmonella enterica serovar Typhimurium.Inhibition and Reversal of Microbial Attachment by an Antibody with Parasteric Activity against the FimH Adhesin of Uropathogenic E. coli Microevolution in fimH gene of mucosa-associated Escherichia coli strains isolated from pediatric patients with inflammatory bowel disease Inactive conformation enhances binding function in physiological conditions Allelic variation contributes to bacterial host specificity.Evolutionary analysis points to divergent physiological roles of type 1 fimbriae in Salmonella and Escherichia coli Adaptive mutations in the signal peptide of the type 1 fimbrial adhesin of uropathogenic Escherichia coli Differentiation of Crohn's Disease-Associated Isolates from Other Pathogenic Escherichia coli by Fimbrial Adhesion under Shear Force.Allosteric coupling in the bacterial adhesive protein FimH Catch-bond mechanism of force-enhanced adhesion: counterintuitive, elusive, but ... widespread?Conformational inactivation induces immunogenicity of the receptor-binding pocket of a bacterial adhesin.Uropathogenic E. coli adhesin-induced host cell receptor conformational changes: implications in transmembrane signaling transduction.Positive selection identifies an in vivo role for FimH during urinary tract infection in addition to mannose binding.Comparative structure-function analysis of mannose-specific FimH adhesins from Klebsiella pneumoniae and Escherichia coli.Adhesive organelles of Gram-negative pathogens assembled with the classical chaperone/usher machinery: structure and function from a clinical standpoint.Glycoconjugates play a key role in Campylobacter jejuni Infection: interactions between host and pathogen.Application of nanotechnology to control bacterial adhesion and patterning on material surfaces.Biomechanics of cell adhesion: how force regulates the lifetime of adhesive bonds at the single molecule level.FimH antagonists: structure-activity and structure-property relationships for biphenyl α-D-mannopyranosides.Enterotoxigenic Escherichia coli CS1 pilus: not one structure but several.The Conformational Variability of FimH: Which Conformation Represents the Therapeutic Target?

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P2860

Interdomain interaction in the FimH adhesin of Escherichia coli regulates the affinity to mannose.

http://www.wikidata.org/entity/Q52579774

description

2007 nî lūn-bûn

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2007年の論文

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2007年学术文章

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Interdomain interaction in the ...... lates the affinity to mannose.

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Interdomain interaction in the ...... lates the affinity to mannose.

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Interdomain interaction in the ...... lates the affinity to mannose.

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Interdomain interaction in the ...... lates the affinity to mannose.

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Journal of Biological Chemistry

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Interdomain interaction in the ...... ulates the affinity to mannose

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P2093

Elena Trinchina

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Evgeni Sokurenko

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Olga Yakovenko

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Pavel Aprikian

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Veronika Tchesnokova

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P2860

Mechanics of actomyosin bonds in different nucleotide states are tuned to muscle contraction

Mechanical switching and coupling between two dissociation pathways in a P-selectin adhesion bond

Remodeling of the lectin-EGF-like domain interface in P- and L-selectin increases adhesiveness and shear resistance under hydrodynamic force

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

A structural basis for integrin activation by the cytoplasmic tail of the alpha IIb-subunit

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

Insight into E-selectin/ligand interaction from the crystal structure and mutagenesis of the lec/EGF domains

Mammalian Ras interacts directly with the serine/threonine kinase Raf

Protein-protein docking with simultaneous optimization of rigid-body displacement and side-chain conformations

Bacterial adhesion to target cells enhanced by shear force

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23437-23446

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10.1074/JBC.M702037200

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32

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282

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Vladimir Yarov-Yarovoy

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2007-06-13T00:00:00Z

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17567583

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Escherichia coli