Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

Journal of molecular biology - 13 Apr 2001

Jin J, Perera L, Stafford D, Pedersen L

Abstract excerpt

The presence of tissue factor is essential for factor VIIa (FVIIa) to reach its full catalytic potential. The previous work in this laboratory demonstrated that substitution of the EGF1 domain of factor VIIa with that of factor IX (FVII((IXegf1))a) results in a substantial decrease in TF-binding affinity and catalytic activity. Supporting simulations of the solution structures of Ca(2+)-bound factor VIIa and...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Apoproteins
Share to Chymotrypsin
Share to Epidermal Growth Factor

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Factor VII

Share to Factor VIIa

Share to Motion

Share to Solutions

Share to Thromboplastin

Source

Identifiers

PMID: 11292356
DOI: 10.1006/jmbi.2001.4556

Genes

EGF

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Four loops of the catalytic domain of factor viia mediate the effect of the first EGF-like domain substitution on factor viia catalytic activity.PMID 11292356Read ↗

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 ↗

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 ↗

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

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

Structural and functional characterization of novel F7 mutations identified in Chinese factor VII-deficient patients.Semantic proximity Read ↗

The origins of enhanced activity in factor VIIa analogs and the interplay between key allosteric sites revealed by hydrogen exchange mass spectrometry.Semantic proximity Read ↗

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

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

Hydrophobic contact between the two epidermal growth factor-like domains of blood coagulation factor IX contributes to enzymatic activity.Semantic proximity Read ↗

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

Cofactor-induced and mutational activity enhancement of coagulation factor VIIa.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.