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

Cofactor-induced and mutational activity enhancement of coagulation factor VIIa.

Cellular and molecular life sciences : CMLS - 1 Mar 2008

Olsen O H, Persson E

Abstract excerpt

Coagulation factor VIIa (FVIIa) is an atypical member of the trypsin family of serine proteases. It fails to attain spontaneously its catalytically competent conformation and requires its protein cofactor tissue factor (TF) to accomplish this. Over a number of years, this unique behaviour of FVIIa has prompted investigations of the TF-induced activation mechanism and the zymogenicity determinants in factor VIIa....

Read the complete abstract on PubMed

Topics

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

Share to Allosteric Regulation
Share to Cell Membrane
Share to Enzyme Activation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Factor VIIa

Share to Mutation

Share to Thromboplastin

Source

Open in PubMed Open full text

Identifiers

PMID: 18066494
DOI: 10.1007/s00018-007-7480-5
PMCID: PMC11131838

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Cofactor-induced and mutational activity enhancement of coagulation factor VIIa.PMID 18066494Read ↗

Rational design of coagulation factor VIIa variants with substantially increased intrinsic activity.Semantic 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 ↗

Variants of recombinant factor VIIa with increased intrinsic activity.Semantic proximity Read ↗

Molecular interaction between factor VII and tissue factor.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 ↗

Mutating factor VIII: lessons from structure to function.Semantic proximity Read ↗

Activation mechanisms of coagulation factor IX.Semantic proximity Read ↗

Crystal structures of uninhibited factor VIIa link its cofactor and substrate-assisted activation to specific interactions.Semantic proximity Read ↗

Identification of a thrombomodulin interaction site on thrombin-activatable fibrinolysis inhibitor that mediates accelerated activation by thrombin.Semantic proximity Read ↗

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

The protein structure and effect of factor VIII.Semantic proximity Read ↗

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