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Article

Activation of individual alphaIIbbeta3 integrin molecules by disruption of transmembrane domain interactions in the absence of clustering.

Biochemistry - 18 Apr 2006

Litvinov Rustem I, Vilaire Gaston, Li Wei, DeGrado William F, Weisel John W, Bennett Joel S

Abstract excerpt

We used laser tweezers-based force spectroscopy to measure the binding strength between fibrinogen molecules covalently bound to latex beads and either wild-type alphaIIbbeta3 molecules or alphaIIbbeta3 molecules containing the transmembrane domain mutations beta3 G708N or alphaIIb G972N expresse...

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Identifiers

PMID: 16605263
DOI: 10.1021/bi0526581

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-16605263-2026-09-04.1. Manifest publication-graph-cohort-2026-09-04.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

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