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Article

Alteration of serpin specificity by a protein cofactor. Vitronectin endows plasminogen activator inhibitor 1 with thrombin inhibitory properties.

The Journal of biological chemistry - 5 Aug 1990

Ehrlich H J, Gebbink R K, Keijer J, Linders M, Preissner K T, Pannekoek H

Abstract excerpt

Serine protease inhibitors ("serpins") are highly homologous proteins which inhibit selected "target" serine proteases by acting as a pseudo-substrate. Their specificity is primarily determined by the amino acid sequence around the carboxyl-terminally located reactive center (P1-P1'). In addition, the association rate constant between a serpin and a serine protease can be dramatically increased by non-protein...

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Identifiers

PMID: 1695900

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

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Alteration of serpin specificity by a protein cofactor. Vitronectin endows plasminogen activator inhibitor 1 with thrombin inhibitory properties.PMID 1695900Read ↗

Vitronectin governs the interaction between plasminogen activator inhibitor 1 and tissue-type plasminogen activator.Semantic proximity Read ↗

The structural basis for the pathophysiological relevance of PAI-1 in cardiovascular diseases and the development of potential PAI-1 inhibitorsSemantic proximity Read ↗

The story of the serpin plasminogen activator inhibitor 1: is there any need for another mutant?Semantic proximity Read ↗

Evolution of serpin specificity: cooperative interactions in the reactive-site loop sequence of antithrombin specifically restrict the inhibition of activated protein C.Semantic proximity Read ↗

Thrombin-variable region 1 (VR1). Evidence for the dominant contribution of VR1 of serine proteases to their interaction with plasminogen activator inhibitor 1.Semantic proximity Read ↗

Identification of tissue-type plasminogen activator-specific plasminogen activator inhibitor-1 mutants. Evidence that second sites of interaction contribute to target specificity.Semantic proximity Read ↗

The M358R variant of α(1)-proteinase inhibitor inhibits coagulation factor VIIa.Semantic proximity Read ↗

Three Decades of Research on Plasminogen Activator Inhibitor-1: A Multifaceted SerpinSemantic proximity Read ↗

Structure-function relationships of plasminogen activator inhibitor-1 and its potential as a therapeutic agent.Semantic proximity Read ↗

Heparin-activated antithrombin interacts with the autolysis loop of target coagulation proteases.Semantic proximity Read ↗

Kinetic characterization of the proteinase binding defect in a reactive site variant of the serpin, antithrombin. Role of the P1' residue in transition-state stabilization of antithrombin-proteinase complex formation.Semantic proximity Read ↗

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

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