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

Identification of ligand recognition sites in heat-stable enterotoxin receptor, membrane-associated guanylyl cyclase C by site-directed mutational analysis.

Infection and immunity - 1 Dec 1996

Wada A, Hirayama T, Kitaura H, Fujisawa J, Hasegawa M, Hidaka Y, Shimonishi Y

Abstract excerpt

Guanylyl cyclase C (STaR), a receptor protein for heat-stable enterotoxin (STa) elaborated by Escherichia coli, is associated with and spans the plasma membrane of mammalian intestinal cells. The extracellular domain functions in the binding of STa and the association of each domain to an oligomeric form. Two amino acid residues, Arg-136 and Asp-347, were identified as the residues binding to STa in the...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to Enterotoxins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Escherichia coli

Share to Hot Temperature

Share to Intestinal Mucosa

Share to Intestines

Share to Mutagenesis, Site-Directed

Share to Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 8945558
DOI: 10.1128/iai.64.12.5144-5150.1996
PMCID: PMC174500

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification of ligand recognition sites in heat-stable enterotoxin receptor, membrane-associated guanylyl cyclase C by site-directed mutational analysis.PMID 8945558Read ↗

Mutational landscape of receptor guanylyl cyclase C: Functional analysis and disease-related mutations.Semantic proximity Read ↗

Synergistic mutations in soluble guanylyl cyclase (sGC) reveal a key role for interfacial regions in the sGC activation mechanism.Semantic proximity Read ↗

Structural characterization of functionally important regions of the Escherichia coli heat-stable enterotoxin STIb.Semantic proximity Read ↗

Structure and function of cholera toxin and the related Escherichia coli heat-labile enterotoxinSemantic proximity Read ↗

A mutant Shiga-like toxin IIe bound to its receptor Gb(3): structure of a group II Shiga-like toxin with altered binding specificity.Semantic proximity Read ↗

Identification of residues in the heme domain of soluble guanylyl cyclase that are important for basal and stimulated catalytic activity.Semantic proximity Read ↗

Extracellular DsbA-insensitive folding of Escherichia coli heat-stable enterotoxin STa in vitro.Semantic proximity Read ↗

Neutralizing Anti-Heat-Stable Toxin (STa) Antibodies Derived from Enterotoxigenic Escherichia coli Toxoid Fusions with STa Proteins Containing N12S, L9A/N12S, or N12S/A14T Mutations Show Little Cross-Reactivity with Guanylin or Uroguanylin.Semantic proximity Read ↗

Identification of transmembrane domain 3, 4 & 5 residues that contribute to the formation of the ligand-binding pocket of the urotensin-II receptor.Semantic proximity Read ↗

Mutational analysis of the interaction between albumin-binding domain from streptococcal protein G and human serum albumin.Semantic proximity Read ↗

Residues stabilizing the heme moiety of the nitric oxide sensor soluble guanylate cyclase.Semantic proximity Read ↗

Role of tyrosine residues in modulation of claudin-4 by the C-terminal fragment of Clostridium perfringens enterotoxin.Semantic proximity Read ↗

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