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

Coagulation factor X Arg386 specifically affects activation by the intrinsic pathway: a novel patient mutation.

Journal of thrombosis and haemostasis : JTH - 1 Dec 2012

Vanden Hoek A L, Talbot K, Carter I S R, Vickars L, Carter C J, Jackson S C, MacGillivray R T A, Pryzdial E L G

Abstract excerpt

No abstract is available from the source.

Read the complete abstract on PubMed

Topics

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

Share to Aged
Share to Arginine
Share to Factor X
Share to Models, Molecular

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Source

Identifiers

PMID: 23039000
DOI: 10.1111/jth.12021

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 11 closest

Coagulation factor X Arg386 specifically affects activation by the intrinsic pathway: a novel patient mutation.PMID 23039000Read ↗

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

Factors X Nice I and II: two novel missense mutations (Met-40Val and Pro304Ser) in patient with coagulation factor X deficiency.Semantic proximity Read ↗

A new case of homozygous C1-inhibitor deficiency suggests a role for Arg378 in the control of kinin pathway activation.Semantic proximity Read ↗

Antithrombin III Sudbury: an Ala384----Pro mutation with abnormal thrombin-binding activity and thrombotic diathesis.Semantic proximity Read ↗

A new factor X defect (factor X Padua 3): a compound heterozygous between true deficiency (Gly(380)-->Arg) and an abnormality (Ser(334)-->Pro).Semantic proximity Read ↗

Novel missense mutation in the coagulation factor IX catalytic domain associated with moderate disease.Semantic proximity Read ↗

Cys482Trp missense mutation in the coagulation factor XI gene (F11) in a Korean patient with factor XI deficiency.Semantic proximity Read ↗

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

Deep venous thrombosis, protein S deficiency and homozygous Factor XII 46T mutation.Semantic proximity Read ↗

The impact of Glu102Lys on the factor X function in a patient with a doubly homozygous factor X deficiency (Gla14Lys and Glu102Lys).Semantic proximity Read ↗

Rapid factor XII (46C-->T) genotyping by fluorescence resonance energy transfer in patients with coronary artery disease or thrombophilia.Semantic proximity Read ↗

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