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Article

Heparin cofactor II is regulated allosterically and not primarily by template effects. Studies with mutant thrombins and glycosaminoglycans.

The Journal of biological chemistry - 30 Dec 1994

Sheehan J P, Tollefsen D M, Sadler J E

Abstract excerpt

Besides its critical role in hemostasis, the serine protease thrombin also participates in wound healing, inflammation, and atherosclerosis. Thrombin is inhibited by the serpins antithrombin and heparin cofactor II (HCiI) in reactions that are accelerated markedly by specific glycosaminoglycans. Following vascular injury, thrombin must be inhibited at both intravascular and extravascular sites that impose...

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Identifiers

PMID: 7806495

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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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Heparin cofactor II is regulated allosterically and not primarily by template effects. Studies with mutant thrombins and glycosaminoglycans.PMID 7806495Read ↗

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The preferred pathway of glycosaminoglycan-accelerated inactivation of thrombin by heparin cofactor II.Semantic proximity Read ↗

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Comparison of heparin- and dermatan sulfate-mediated catalysis of thrombin inactivation by heparin cofactor II.Semantic proximity Read ↗

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The N-terminal acidic domain of heparin cofactor II mediates the inhibition of alpha-thrombin in the presence of glycosaminoglycans.Semantic proximity Read ↗

Amino acid residues of heparin cofactor II required for stimulation of thrombin inhibition by sulphated polyanions.Semantic proximity Read ↗

Conformational activation of antithrombin by heparin involves an altered exosite interaction with protease.Semantic proximity Read ↗

Selective disruption of heparin and antithrombin-mediated regulation of human factor IX.Semantic proximity Read ↗

Aspartic acid residues 72 and 75 and tyrosine-sulfate 73 of heparin cofactor II promote intramolecular interactions during glycosaminoglycan binding and thrombin inhibition.Semantic proximity Read ↗

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