Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structural and functional study of the receptor binding site for FimH adhesin in uropathogenic strains of Escherichia coli.

Bulletin of experimental biology and medicine - 1 Oct 2003

Trinchina E V

Abstract excerpt

We evaluated binding capacity of FimH-FocH hybrid adhesins during their interaction with model 1M and 3M substrates and epithelial cells. Introduction of the Glu89Lys point mutation into the fimH gene induced a new 1M-specific phenotype of adhesin. The role of a new pathoadaptive sign in the population of E. coli is discussed.

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adhesins, Escherichia coli
Share to Bacterial Adhesion
Share to Epithelial Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Fimbriae, Bacterial

Share to Lysine

Share to Mouth Mucosa

Share to Operon

Share to Urinary Bladder

Source

Identifiers

PMID: 14714089
DOI: 10.1023/b:bebm.0000010958.02737.e7

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural and functional study of the receptor binding site for FimH adhesin in uropathogenic strains of Escherichia coli.PMID 14714089Read ↗

Structural and functional characterization of the FimH adhesin of uropathogenic Escherichia coli and its novel applicationsSemantic proximity Read ↗

Valency conversion in the type 1 fimbrial adhesin of Escherichia coli.Semantic proximity Read ↗

Probing the receptor recognition site of the FimH adhesin by fimbriae-displayed FimH-FocH hybrids.Semantic proximity Read ↗

Molecular Characterization of the<i>Escherichia coli</i>FimH AdhesinSemantic proximity Read ↗

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

Functional flexibility of the FimH adhesin: insights from a random mutant library.Semantic proximity Read ↗

Positively selected FimH residues enhance virulence during urinary tract infection by altering FimH conformation.Semantic proximity Read ↗

Selection for non-specific adhesion is a driver of FimH evolution increasing <i>Escherichia coli</i> biofilm capacitySemantic proximity Read ↗

Ultraslow conformational dynamics and catch bond formation of a bacterial adhesin revealed by a single-domain variant of FimH.Semantic proximity Read ↗

Comparative structure-function analysis of mannose-specific FimH adhesins from Klebsiella pneumoniae and Escherichia coli.Semantic proximity Read ↗

Pathogenic adaptation of Escherichia coli by natural variation of the FimH adhesin.Semantic proximity Read ↗

Asymptomatic bacteriuria Escherichia coli strain 83972 carries mutations in the foc locus and is unable to express F1C fimbriae.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.