The affinity of the FimH fimbrial adhesin is receptor-driven and quasi-independent of Escherichia coli pathotypes. - Wikidata - awgldk - TriplyDB

The affinity of the FimH fimbrial adhesin is receptor-driven and quasi-independent of Escherichia coli pathotypes.

The affinity of the FimH fimbrial adhesin is receptor-driven and quasi-independent of Escherichia coli pathotypes.

http://www.wikidata.org/entity/Q35103730

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Human neutrophils secrete bioactive paucimannosidic proteins from azurophilic granules into pathogen-infected sputum Intervening with urinary tract infections using anti-adhesives based on the crystal structure of the FimH-oligomannose-3 complex Genomic Microbial Epidemiology Is Needed to Comprehend the Global Problem of Antibiotic Resistance and to Improve Pathogen Diagnosis Glycosylation of uroplakins. Implications for bladder physiopathology Structural insight in histo-blood group binding by the F18 fimbrial adhesin FedF Structural Sampling of Glycan Interaction Profiles Reveals Mucosal Receptors for Fimbrial Adhesins of Enterotoxigenic Escherichia coli Uroplakins and their potential applications in urology Biofilm formation by multidrug resistant Escherichia coli ST131 is dependent on type 1 fimbriae and assay conditions.Differential stability and trade-off effects of pathoadaptive mutations in the Escherichia coli FimH adhesin Exploitation of the intestinal microflora by the parasitic nematode Trichuris muris.Evolutionary fine-tuning of conformational ensembles in FimH during host-pathogen interactions.Integrin-mediated host cell invasion by type 1-piliated uropathogenic Escherichia coli.FimH forms catch bonds that are enhanced by mechanical force due to allosteric regulation.Glyco-β-cyclodextrin capped quantum dots: synthesis, cytotoxicity and optical detection of carbohydrate-protein interactions.Nanobody mediated inhibition of attachment of F18 Fimbriae expressing Escherichia coli.Surfaces Presenting α-Phenyl Mannoside Derivatives Enable Formation of Stable, High Coverage, Non-pathogenic Escherichia coli Biofilms against Pathogen Colonization Surface Plasmon Resonance (SPR) for the Evaluation of Shear-Force-Dependent Bacterial Adhesion.Lead optimization studies on FimH antagonists: discovery of potent and orally bioavailable ortho-substituted biphenyl mannosides Desialylation of Spermatozoa and Epithelial Cell Glycocalyx Is a Consequence of Bacterial Infection of the Epididymis.Differentiation of Crohn's Disease-Associated Isolates from Other Pathogenic Escherichia coli by Fimbrial Adhesion under Shear Force.Bacteria-surface interactions Allosteric coupling in the bacterial adhesive protein FimH Lectin-Glycan Interaction Network-Based Identification of Host Receptors of Microbial Pathogenic Adhesins Positively selected FimH residues enhance virulence during urinary tract infection by altering FimH conformation Natural killer cell-mediated host defense against uropathogenic E. coli is counteracted by bacterial hemolysinA-dependent killing of NK cells.Adhesive organelles of Gram-negative pathogens assembled with the classical chaperone/usher machinery: structure and function from a clinical standpoint.The sweet connection: Solving the riddle of multiple sugar-binding fimbrial adhesins in Escherichia coli: Multiple E. coli fimbriae form a versatile arsenal of sugar-binding lectins potentially involved in surface-colonisation and tissue tropism.Glycomics for Microbes and Microbiologists.Structural and functional insight into the carbohydrate receptor binding of F4 fimbriae-producing enterotoxigenic Escherichia coli.Supported Lipid Bilayers for the Generation of Dynamic Cell-Material Interfaces.Repurposing Escherichia coli antiadhesives in Crohn's disease.Rational design strategies for FimH antagonists: new drugs on the horizon for urinary tract infection and Crohn's disease.FimH antagonists: structure-activity and structure-property relationships for biphenyl α-D-mannopyranosides.Sites for Dynamic Protein-Carbohydrate Interactions of O- and C-Linked Mannosides on the E. coli FimH Adhesin.Functional analysis of Escherichia coli Yad fimbriae reveals their potential role in environmental persistence.The Conformational Variability of FimH: Which Conformation Represents the Therapeutic Target?An evaluation of the virulence and adherence properties of avian pathogenic Escherichia coli.Synthesis of dodecavalent fullerene-based glycoclusters and evaluation of their binding properties towards a bacterial lectin.Role of type 1 fimbriae and mannose in the development of Escherichia coli K12 biofilm: from initial cell adhesion to biofilm formation.Glycosylation changes as important factors for the susceptibility to urinary tract infection.

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P2860

The affinity of the FimH fimbrial adhesin is receptor-driven and quasi-independent of Escherichia coli pathotypes.

http://www.wikidata.org/entity/Q35103730

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2006 nî lūn-bûn

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2006 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

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2006 թվականի օգոստոսին հրատարակված գիտական հոդված

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2006年の論文

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The affinity of the FimH fimbr ...... f Escherichia coli pathotypes.

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The affinity of the FimH fimbr ...... f Escherichia coli pathotypes.

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J.1365-2958.2006.05352.X

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Molecular Microbiology

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The affinity of the FimH fimbr ...... f Escherichia coli pathotypes.

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Beatrice Chipwaza

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Denis Piérard

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Devapriya Choudhury

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Henri De Greve

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Jennifer Anderson

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Jenny Mackenzie

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Julie Bouckaert

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Karin Mannerstedt

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Lode Wyns

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Peter H Seeberger

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P2860

Improved methods for building protein models in electron density maps and the location of errors in these models

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

Structure and biogenesis of the capsular F1 antigen from Yersinia pestis: preserved folding energy drives fiber formation

Bacterial adhesion to target cells enhanced by shear force

Prevention of mucosal Escherichia coli infection by FimH-adhesin-based systemic vaccination

Glycosylation sites and site-specific glycosylation in human Tamm-Horsfall glycoprotein

Uroplakin Ia is the urothelial receptor for uropathogenic Escherichia coli: evidence from in vitro FimH binding

Reduced surface: an efficient way to compute molecular surfaces

Molecular structure of adhesin domains in Escherichia coli fimbriae.

Differentiation and developmental pathways of uropathogenic Escherichia coli in urinary tract pathogenesis.

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Stefan D. Knight

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2006-08-23T00:00:00Z

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6858496

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