Article

Engineering a membrane-independent human prothrombinase through parsimonious mutation of factor Xa

2025-04-16

Abstract excerpt

<h4>ABSTRACT</h4> <h4>Background</h4> Thrombin is generated from its precursor prothrombin by sequential cleavage at Arg320 and Arg271 by the prothrombinase complex, composed of factor (f) Xa and fVa on phospholipid (PL) membrane surfaces. The affinity of human fXa for fVa is low in the absence of PL. However, fXa orthologues from the venom of group D snakes bind to fVa with high affinity, forming an active comp...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 0684085b-0eb3-5aa5-9d3c-c8203b7588fa
DOI: 10.1101/2025.04.16.649061

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Engineering a membrane-independent human prothrombinase through parsimonious mutation of factor XaDOI 10.1101/2025.04.16.649061Read

Engineering a membrane-independent human prothrombinase through parsimonious mutation of factor Xa.Semantic proximity Read

A 3.3-Å cryo-EM structure of an engineered high-affinity human prothrombinase complex.Semantic proximity Read

Crystal structure of the prothrombinase complex from the venom of Pseudonaja textilis.Semantic proximity Read

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

A critical role for Gly25 in the B chain of human thrombin.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

Evolutionary insights into coagulation factor IX Padua and other high-specific-activity variantsSemantic proximity Read

Structural analysis of eight novel and 112 previously reported missense mutations in the interactive FXI mutation database reveals new insight on FXI deficiency.Semantic proximity Read

Contribution of amino acid region 334-335 from factor Va heavy chain to the catalytic efficiency of prothrombinase.Semantic proximity Read

In vitro secretion deficits are common among human coagulation factor XIII subunit B missense mutants: correlations with patient phenotypes and molecular models.Semantic proximity Read

An integrated multitool analysis contributes elements to interpreting unclassified factor IX missense variants associated with hemophilia B.Semantic proximity Read

Identification of residues Asn89, Ile90, and Val107 of the factor IXa second epidermal growth factor domain that are essential for the assembly of the factor X-activating complex on activated platelets.Semantic proximity Read