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

Impaired prothrombinase activity of factor X Gly381Asp results in severe familial CRM+ FX deficiency.

Thrombosis and haemostasis - 1 Feb 2003

Pinotti Mirko, Camire Rodney M, Baroni Marcello, Rajab Anna, Marchetti Giovanna, Bernardi Francesco

Abstract excerpt

We investigated three members of a large Omani family affected by severe factor X (FX) deficiency (coagulant activity <1%) and showing marked differences in the onset of severe hemorrhagic symptoms. All patients were homozygous for a novel FX mutation (Gly381Asp) in the structurally conserved region of the serine protease active site. Expression levels of recombinant 381D-FX were similar to those of wt-FX,...

Read the complete abstract on PubMed

Topics

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

Share to Codon
Share to Consanguinity
Share to Factor X

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

Share to Genetic Heterogeneity

Share to Hemorrhagic Disorders

Share to Prothrombin Time

Share to Recombinant Fusion Proteins

Source

Identifiers

PMID: 12574802

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

Impaired prothrombinase activity of factor X Gly381Asp results in severe familial CRM+ FX deficiency.PMID 12574802Read ↗

Molecular and functional characterization of a natural homozygous Arg67His mutation in the prothrombin gene of a patient with a severe procoagulant defect contrasting with a mild hemorrhagic phenotype.Semantic proximity Read ↗

Characterization of the intracellular signalling capacity of natural FXa mutants with reduced pro-coagulant activity.Semantic proximity Read ↗

Asymmetric processing of mutant factor X Arg386Cys reveals differences between intrinsic and extrinsic pathway activation.Semantic proximity Read ↗

Residual factor VII activity and different hemorrhagic phenotypes in CRM(+) factor VII deficiencies (Gly331Ser and Gly283Ser).Semantic proximity Read ↗

Reduced activation of the Gla19Ala FX variant via the extrinsic coagulation pathway results in symptomatic CRMred FX deficiency.Semantic proximity Read ↗

The mild phenotype in severe hemophilia A with Arg1781His mutation is associated with enhanced binding affinity of factor VIII for factor X.Semantic proximity Read ↗

Molecular characterization of two novel mutations causing factor XI deficiency: A splicing defect and a missense mutation responsible for a CRM+ defect.Semantic proximity Read ↗

Gene mutations and three-dimensional structural analysis in 13 families with severe factor X deficiency.Semantic proximity Read ↗

Molecular and clinical aspects of factor VII deficiency.Semantic proximity Read ↗

Molecular bases of CRM+ factor X deficiency: a frequent mutation (Ser334Pro) in the catalytic domain and a substitution (Glu102Lys) in the second EGF-like domain.Semantic proximity Read ↗

A recurrent Gly43Asp substitution in coagulation Factor X rigidifies its catalytic pocket and impairs catalytic activity and intracellular trafficking.Semantic proximity Read ↗

Biological activity of recombinant factor VIII variants lacking the central B-domain and the heavy-chain sequence Lys713-Arg740: discordant in vitro and in vivo activity.Semantic proximity Read ↗

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