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

Plasminogen mutants activated by thrombin. Potential thrombus-selective thrombolytic agents.

The Journal of biological chemistry - 10 Jun 1994

Dawson K M, Cook A, Devine J M, Edwards R M, Hunter M G, Raper R H, Roberts G

Abstract excerpt

Plasmin, the enzyme responsible for degradation of fibrin in blood clots and thus thrombolysis, is normally formed when its zymogen plasminogen is activated by cleavage of the Arg561-Val562 bond by specific plasminogen activators. We have altered the activation characteristics of plasminogen by substituting the P3, P2, and P1' cleavage site residues with sequences from thrombin-cleavable proteins to produce a...

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
Share to Enzyme Activation

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

Share to Fibrinogen

Share to Molecular Sequence Data

Share to Mutation

Share to Protein Processing, Post-Translational

Share to Recombinant Proteins

Source

Identifiers

PMID: 8206894

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

Plasminogen mutants activated by thrombin. Potential thrombus-selective thrombolytic agents.PMID 8206894Read ↗

Effective lysis of model thrombi by a t-PA mutant (A473S) that is resistant to alpha2-antiplasmin.Semantic proximity Read ↗

Identification of the factor XII contact activation site enables sensitive coagulation diagnostics.Semantic proximity Read ↗

P1 and P2' site mutations convert protease nexin-2 from a factor XIa inhibitor to a plasmin inhibitor.Semantic proximity Read ↗

Identification of the mechanism responsible for the increased fibrin specificity of TNK-tissue plasminogen activator relative to tissue plasminogen activator.Semantic proximity Read ↗

Pharmacological and clinical impact of the unique molecular structure of a new plasminogen activator.Semantic proximity Read ↗

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 ↗

Recombinant variants of tissue-type plasminogen activator containing amino acid substitutions in the fibronectin finger-like domain and the kringle 1 domain.Semantic proximity Read ↗

Structure-function relationships in thrombin-activatable fibrinolysis inhibitor.Semantic proximity Read ↗

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

Site-directed mutagenesis in human tissue-plasminogen activator. Distinguishing sites in the amino-terminal region required for full fibrinolytic activity and rapid clearance from the circulation.Semantic proximity Read ↗

Variants of tissue-type plasminogen activator which display substantially enhanced stimulation by fibrin.Semantic proximity Read ↗

Simplified recombinant plasmin: production and functional comparison of a novel thrombolytic molecule with plasma-derived plasmin.Semantic proximity Read ↗

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