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Article

Amino acid residues that affect interaction of tissue-type plasminogen activator with plasminogen activator inhibitor 1.

Proceedings of the National Academy of Sciences of the United States of America - 1 May 1990

Madison E L, Goldsmith E J, Gerard R D, Gething M J, Sambrook J F, Bassel-Duby R S

Abstract excerpt

Fibrinolysis is regulated in part by the interaction between tissue-type plasminogen activator (t-PA) and plasminogen activator inhibitor 1 (PAI-1, a serine protease inhibitor of the serpin family). It is known from our earlier work that deletion of a loop of amino acids (residues 296-302) from the serine protease domain of t-PA suppresses the interaction between the two proteins without altering the reactivity...

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Identifiers

PMID: 2110366
DOI: 10.1073/pnas.87.9.3530
PMCID: PMC53935

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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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Amino acid residues that affect interaction of tissue-type plasminogen activator with plasminogen activator inhibitor 1.PMID 2110366Read ↗

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High resolution analysis of functional determinants on human tissue-type plasminogen activator.Semantic proximity Read ↗

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