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

Breaking the Integrin Hinge

1 Mar 1996

Abstract excerpt

Integrins are heterodimeric (alpha, beta) cell adhesion receptors. We demonstrate that point mutations in the cytoplasmic domains of both the alpha and beta subunits promote constitutive signaling by the integrin alphaIIbbeta3. By generating charge reversal mutations, we show these "activating" mutations may act by disrupting a potential salt bridge between the membrane-proximal portions of the alpha and beta...

Read the complete abstract on PubMed

Topics

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

Share to Cell Adhesion Molecules Research
Share to Monoclonal and Polyclonal Antibodies Research
Share to Platelet Disorders and Treatments

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

Source

Identifiers

PMID: 8636068
DOI: 10.1074/jbc.271.12.6571

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

Breaking the Integrin HingePMID 8636068Read ↗

Membrane-proximal {alpha}/{beta} stalk interactions differentially regulate integrin activation.Semantic proximity Read ↗

Flipping the Switch: Integrin Switching Provides Metastatic CompetenceSemantic proximity Read ↗

A beta 3 integrin mutation abolishes ligand binding and alters divalent cation-dependent conformation.Semantic proximity Read ↗

Activation of integrin alphaIIbbeta3 by modulation of transmembrane helix associations.Semantic proximity Read ↗

Targeted mutations in integrins and their ligands: their implications for vascular biology.Semantic proximity Read ↗

Structure of collagen receptor integrin α(1)I domain carrying the activating mutation E317A.Semantic proximity Read ↗

The novel S527F mutation in the integrin beta3 chain induces a high affinity alphaIIbbeta3 receptor by hindering adoption of the bent conformation.Semantic proximity Read ↗

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

Novel activating and inactivating mutations in the integrin beta1 subunit A domain.Semantic proximity Read ↗

A novel form of integrin dysfunction involving β1, β2, and β3 integrinsSemantic proximity Read ↗

Negative regulators of integrin activitySemantic proximity Read ↗

A tumor-associated β1 integrin mutation that abrogates epithelial differentiation controlSemantic proximity Read ↗

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