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

Analysis of the Drosophila betaPS subunit indicates that regulation of integrin activity is a primal function of the C8-C9 loop.

Experimental cell research - 10 Mar 2004

Bunch Thomas A, Miller Steven W, Brower Danny L

Abstract excerpt

Integrin-ligand interactions can be influenced by the sequence in a disulfide-bridged loop between the 8th and 9th beta subunit cysteines. Previous experiments are consistent with C8-C9 loop residues being involved in direct ligand-integrin interactions and/or being important in heterodimer regulation. In betaPS from Drosophila melanogaster and three other dipterans, the C8-C9 loop consists of only two amino...

Read the complete abstract on PubMed

Topics

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

Share to Cell Adhesion
Share to Drosophila
Share to Drosophila Proteins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Integrin alpha Chains

Share to Integrins

Share to Manduca

Share to Protein Subunits

Share to Sequence Homology, Amino Acid

Source

Identifiers

PMID: 14980507
DOI: 10.1016/j.yexcr.2003.11.002

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Analysis of the Drosophila betaPS subunit indicates that regulation of integrin activity is a primal function of the C8-C9 loop.PMID 14980507Read ↗

Requirements for the cytoplasmic domain of the alphaPS1, alphaPS2 and betaPS integrin subunits during Drosophila development.Semantic proximity Read ↗

Disruption of C-terminal cytoplasmic domain of betaPS integrin subunit has dominant negative properties in developing Drosophila.Semantic proximity Read ↗

Identification of integrin beta subunit mutations that alter heterodimer function in situ.Semantic proximity Read ↗

Identification of integrin beta subunit mutations that alter affinity for extracellular matrix ligand.Semantic proximity Read ↗

Genetic analysis of the Drosophila alphaPS2 integrin subunit reveals discrete adhesive, morphogenetic and sarcomeric functions.Semantic proximity Read ↗

Cell-cell adhesion via the ECM: integrin genetics in fly and worm.Semantic proximity Read ↗

Genetic analysis of the Drosophila PS integrins.Semantic proximity Read ↗

Functions of the cytoplasmic domain of the beta PS integrin subunit during Drosophila development.Semantic proximity Read ↗

Tiggrin, a novel Drosophila extracellular matrix protein that functions as a ligand for Drosophila αPS2βPS integrinsSemantic proximity Read ↗

Mutations in the Drosophila alphaPS2 integrin subunit uncover new features of adhesion site assembly.Semantic proximity Read ↗

Amino acid changes in Drosophila alphaPS2betaPS integrins that affect ligand affinity.Semantic proximity Read ↗

Specificity of PS integrin function during embryogenesis resides in the alpha subunit extracellular domain.Semantic proximity Read ↗

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