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Article

Influence of mutations in tissue factor on the fine specificity of macromolecular substrate activation.

The Biochemical journal - 1 Feb 1997

Dittmar S, Ruf W, Edgington T S

Abstract excerpt

The C-terminal fibronectin-type-III-like module of the tissue factor (TF) extracellular domain plays a requisite role in the activation of macromolecular substrates by factor VIIa (VIIa) in complex with TF. Unlike the mutations Lys165-->Ala, Lys166-->Ala in TF, which prevent efficient proteolysis of factor X, we found that the coagulant defect of a site-specific Trp158-->Arg, Ser160-->Gly replacement mutant of TF...

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Share to Electrophoresis, Polyacrylamide Gel
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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 9032467
DOI: 10.1042/bj3210787
PMCID: PMC1218136

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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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Influence of mutations in tissue factor on the fine specificity of macromolecular substrate activation.PMID 9032467Read ↗

Tissue factor residues Lys165 and Lys166 are essential for rapid formation of the quaternary complex of tissue factor.VIIa with Xa.tissue factor pathway inhibitor.Semantic proximity Read ↗

Molecular interaction between factor VII and tissue factor.Semantic proximity Read ↗

Tissue factor residues that putatively interact with membrane phospholipids.Semantic proximity Read ↗

Severe factor VII deficiency caused by mutations abolishing the cleavage site for activation and altering binding to tissue factor.Semantic proximity Read ↗

Tissue Factor residue Asp44 regulates catalytic function of the bound proteinase Factor VIIa.Semantic proximity Read ↗

The first epidermal growth factor-like domains of factor Xa and factor IXa are important for the activation of the factor VII--tissue factor complex.Semantic proximity Read ↗

Structure of extracellular tissue factor complexed with factor VIIa inhibited with a BPTI mutant.Semantic proximity Read ↗

Engineering of substrate selectivity for tissue factor.factor VIIa complex signaling through protease-activated receptor 2.Semantic proximity Read ↗

Impaired human tissue factor-mediated activity in blood clotting factor VIINagoya (Arg304-->Trp). Evidence that a region in the catalytic domain of factor VII is important for the association with tissue factor.Semantic proximity Read ↗

Four loops of the catalytic domain of factor viia mediate the effect of the first EGF-like domain substitution on factor viia catalytic activity.Semantic proximity Read ↗

Surface loop 199-204 in blood coagulation factor IX is a cofactor-dependent site involved in macromolecular substrate interaction.Semantic proximity Read ↗

Residue Met(156) contributes to the labile enzyme conformation of coagulation factor VIIa.Semantic proximity Read ↗

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