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

Murine thrombin lacks Na+ activation but retains high catalytic activity.

The Journal of biological chemistry - 17 Mar 2006

Bush Leslie A, Nelson Ryan W, Di Cera Enrico

Abstract excerpt

Human thrombin utilizes Na+ as a driving force for the cleavage of substrates mediating its procoagulant, prothrombotic, and signaling functions. Murine thrombin has Asp-222 in the Na+ binding site of the human enzyme replaced by Lys. The charge reversal substitution abrogates Na+ activation, which is partially restored with the K222D mutation, and ensures high activity even in the absence of Na+. This property...

Read the complete abstract on PubMed

Topics

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

Share to Fibrinogen
Share to Coagulants
Share to Extracellular Matrix

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

Share to Hydrolysis

Share to Platelet Activation

Share to Protein C

Share to Sodium

Share to Thrombin

Source

Identifiers

PMID: 16428384
DOI: 10.1074/jbc.M512082200

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

Murine thrombin lacks Na+ activation but retains high catalytic activity.PMID 16428384Read ↗

Mutation of W215 compromises thrombin cleavage of fibrinogen, but not of PAR1 or protein C.Semantic proximity Read ↗

The Na+ binding channel of human coagulation proteases: novel insights on the structure and allosteric modulation revealed by molecular surface analysis.Semantic proximity Read ↗

Residue Asp-189 controls both substrate binding and the monovalent cation specificity of thrombin.Semantic proximity Read ↗

Mutations in autolytic loop-2 and at Asp554 of human prothrombin that enhance protein C activation by meizothrombin.Semantic proximity Read ↗

Mutagenesis studies toward understanding allostery in thrombin.Semantic proximity Read ↗

Engineering thrombin for selective specificity toward protein C and PAR1.Semantic proximity Read ↗

The anticoagulant thrombin mutant W215A/E217A has a collapsed primary specificity pocket.Semantic proximity Read ↗

Lack of canonical PAR4 activation is associated with reduced arterial and venous thrombosis in miceSemantic proximity Read ↗

The thrombin high-affinity binding site on platelets is a negative regulator of thrombin-induced platelet activation. Structure-function studies using two mutant thrombins, Quick I and Quick II.Semantic proximity Read ↗

Heparin Binds Lamprey Angiotensinogen and Promotes Thrombin Inhibition through a Template Mechanism.Semantic proximity Read ↗

Thrombin activation of factor XI on activated platelets requires the interaction of factor XI and platelet glycoprotein Ib alpha with thrombin anion-binding exosites I and II, respectively.Semantic proximity Read ↗

The molecular environment of the Na+ binding site of thrombin.Semantic proximity Read ↗

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