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

Thrombin-variable region 1 (VR1). Evidence for the dominant contribution of VR1 of serine proteases to their interaction with plasminogen activator inhibitor 1.

The Journal of biological chemistry - 15 Jan 1993

Horrevoets A J, Tans G, Smilde A E, van Zonneveld A J, Pannekoek H

Abstract excerpt

The importance of a specific variable region in different serine proteases for the interaction with plasminogen activator inhibitor 1 (PAI-1) is studied. To that end, we have constructed a thrombin substitution variant, thrombin-VR1, in which the entire variable region 1 (VR1) of the protease domain (Phe-34 to Leu-40) has been replaced by the corresponding sequence (Phe-294 to Phe-305) of tissue-type plasminogen...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Base Sequence

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cell Line

Share to Genetic Variation

Share to Kinetics

Share to Molecular Sequence Data

Share to Mutagenesis, Site-Directed

Share to Recombinant Proteins

Source

Identifiers

PMID: 8419354

Genes

SDS

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Thrombin-variable region 1 (VR1). Evidence for the dominant contribution of VR1 of serine proteases to their interaction with plasminogen activator inhibitor 1.PMID 8419354Read ↗

Identification of tissue-type plasminogen activator-specific plasminogen activator inhibitor-1 mutants. Evidence that second sites of interaction contribute to target specificity.Semantic proximity Read ↗

Alteration of serpin specificity by a protein cofactor. Vitronectin endows plasminogen activator inhibitor 1 with thrombin inhibitory properties.Semantic proximity Read ↗

The M358R variant of α(1)-proteinase inhibitor inhibits coagulation factor VIIa.Semantic proximity Read ↗

Human thrombin variable region 1, including E39, is involved in interactions with alpha 1-antitrypsin M358R and protein C.Semantic proximity Read ↗

Kinetic characterization of the proteinase binding defect in a reactive site variant of the serpin, antithrombin. Role of the P1' residue in transition-state stabilization of antithrombin-proteinase complex formation.Semantic proximity Read ↗

The story of the serpin plasminogen activator inhibitor 1: is there any need for another mutant?Semantic proximity Read ↗

Structure-function analysis of the reactive site in the first Kunitz-type domain of human tissue factor pathway inhibitor-2.Semantic proximity Read ↗

Cooperative regulation of the activity of factor Xa within prothrombinase by discrete amino acid regions from factor Va heavy chain.Semantic proximity Read ↗

Evolution of serpin specificity: cooperative interactions in the reactive-site loop sequence of antithrombin specifically restrict the inhibition of activated protein C.Semantic proximity Read ↗

Distal hinge of plasminogen activator inhibitor-1 involves its latency transition and specificities toward serine proteases.Semantic proximity Read ↗

Vitronectin governs the interaction between plasminogen activator inhibitor 1 and tissue-type plasminogen activator.Semantic proximity Read ↗

Substitution of arginine for Leu444 in the reactive site of heparin cofactor II enhances the rate of thrombin inhibition.Semantic proximity Read ↗

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