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Article

Tissue Factor residue Asp44 regulates catalytic function of the bound proteinase Factor VIIa.

The Biochemical journal - 1 Apr 1996

Kelly C R, Schullek J R, Ruf W, Edgington T S

Abstract excerpt

The coagulation pathways are initiated by the cell-surface receptor Tissue Factor (TF), which binds the serine proteinase coagulation Factor VIIa (VIIa), resulting in enhanced catalytic function, both amidolytic, towards small pseudo-substrates, and proteolytic, towards macromolecular substrates....

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Identifiers

PMID: 8670099
DOI: 10.1042/bj3150145
PMCID: PMC1217163

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-8670099-2026-09-02.1. Manifest publication-graph-cohort-2026-09-02.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Tissue Factor residue Asp44 regulates catalytic function of the bound proteinase Factor VIIa.PMID 8670099Read ↗

Identification of surface residues mediating tissue factor binding and catalytic function of the serine protease factor VIIa.Semantic proximity Read ↗

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

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 ↗

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

A frequent human coagulation Factor VII mutation (A294V, c152) in loop 140s affects the interaction with activators, tissue factor and substrates.Semantic proximity Read ↗

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

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

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

Characterisation of the molecular basis of protein S anticoagulant functionSemantic proximity Read ↗

Molecular Basis of Enhanced Activity in Factor VIIa-Trypsin Variants Conveys Insights into Tissue Factor-mediated Allosteric Regulation of Factor VIIa Activity.Semantic proximity Read ↗

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

Mutational analysis of the primary substrate specificity pocket of complement factor B. Asp(226) is a major structural determinant for p(1)-Arg binding.Semantic proximity Read ↗

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