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Article

Construction of a plasminogen activator inhibitor-1 variant without measurable affinity to vitronectin but otherwise normal.

FEBS letters - 2 Jan 2004

Jensen Jan K, Durand Michelle K V, Skeldal Sune, Dupont Daniel M, Bødker Julie S, Wind Troels, Andreasen Peter A

Abstract excerpt

Vitronectin (VN) and plasminogen activator inhibitor-1 (PAI-1) have important functional interactions: VN stabilises the protease inhibitory activity of PAI-1 and PAI-1 inhibits binding of adhesion receptors to VN. Having previously mapped the PAI-1 binding area for VN, we have now constructed a PAI-1 variant, R103A-M112A-Q125A, without measurable affinity to VN, but with full protease inhibitory activity and...

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Identifiers

PMID: 14706846
DOI: 10.1016/s0014-5793(03)01405-4

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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.

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