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

In vivo detection of hetero-association of glycophorin-A and its mutants within the membrane.

The Journal of biological chemistry - 17 Aug 2001

Gerber D, Shai Y

Abstract excerpt

Protein recognition within the membrane is a crucial process for numerous biological activities. Detection of such interaction is limited because of difficulties that arise from the hydrophobic environment of the membrane. We detected direct hetero-oligomerization of the glycophorin-A (GPA) transmembrane segments in vivo through inhibition of ToxR transcription activator dimer formation. We investigated the amino...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Bacterial Proteins
Share to Cell Membrane

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dimerization

Share to DNA-Binding Proteins

Share to Glycophorins

Share to Molecular Sequence Data

Share to Transcription Factors

Source

Identifiers

PMID: 11402026
DOI: 10.1074/jbc.M101889200

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

In vivo detection of hetero-association of glycophorin-A and its mutants within the membrane.PMID 11402026Read ↗

Dimerisation of the glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator.Semantic proximity Read ↗

Influence of hydrophobic matching on association of model transmembrane fragments containing a minimised glycophorin A dimerisation motif.Semantic proximity Read ↗

Lipid-mediated interactions tune the association of glycophorin A helix and its disruptive mutants in membranes.Semantic proximity Read ↗

Dimerization of the transmembrane domain of Integrin alphaIIb subunit in cell membranes.Semantic proximity Read ↗

Lipid solvation effects contribute to the affinity of Gly-xxx-Gly motif-mediated helix-helix interactions.Semantic proximity Read ↗

Approaches to Characterize and Quantify Oligomerization of GPCRs.Semantic proximity Read ↗

A ToxR-based dominant-negative system to investigate heterotypic transmembrane domain interactions.Semantic proximity Read ↗

A modified, dual reporter TOXCAT system for monitoring homodimerization of transmembrane segments of proteins.Semantic proximity Read ↗

Oligomerization of G protein-coupled receptors: biochemical and biophysical methods.Semantic proximity Read ↗

Membrane insertion and dimerization of glycophorin-A mutations studied by free energy simulations.Semantic proximity Read ↗

Oligomerization of the {gamma}-aminobutyric acid transporter-1 is driven by an interplay of polar and hydrophobic interactions in transmembrane helix II.Semantic proximity Read ↗

Molecular dissection of the membrane aggregation mechanisms induced by monomeric annexin A2.Semantic proximity Read ↗

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