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Article

Making tissue-type plasminogen activator more fibrin specific.

Protein engineering - 1 Jul 1993

Paoni N F, Chow A M, Peña L C, Keyt B A, Zoller M J, Bennett W F

Abstract excerpt

The fibrin specificity of tissue-type plasminogen activator can be increased by mutagenesis within at least four sites in the protease domain. These sites include residue I276, the new N-terminus formed by conversion to a two-chain structure, residues on either side of the active site cleft, KHRR 296-299 or DDD 364-366, a charged surface involved in fibrin interactions, which includes residues H432, R434, D460,...

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Identifiers

PMID: 8415579
DOI: 10.1093/protein/6.5.529

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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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Making tissue-type plasminogen activator more fibrin specific.PMID 8415579Read ↗

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