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

Functional characterization of factor V-Ile359Thr: a novel mutation associated with thrombosis.

Blood - 1 May 2004

Steen Mårten, Norstrøm Eva A, Tholander Ann-Louise, Bolton-Maggs Paula H B, Mumford Andrew, McVey John H, Tuddenham Edward G D, Dahlbäck Björn

Abstract excerpt

A missense mutation, FV-Ile359Thr (FV Liverpool), associated with thrombosis has recently been described. This mutation creates an additional potential N-linked glycosylation site (Asn-X-Ser/Thr) in factor V (FV) at Asn357 that could interfere with secretion and/or protein interactions. To investigate the molecular pathology of FV-Ile359Thr, the mutation was created by site-directed mutagenesis and expressed...

Read the complete abstract on PubMed

Topics

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

Share to Blood Coagulation
Share to Factor V

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

Share to Glycosylation

Share to Mutagenesis, Site-Directed

Share to Protein C

Share to Protein Processing, Post-Translational

Share to Protein S

Share to Thrombosis

Source

Identifiers

PMID: 14695241
DOI: 10.1182/blood-2003-06-2092

Genes

APC

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

Functional characterization of factor V-Ile359Thr: a novel mutation associated with thrombosis.PMID 14695241Read ↗

Antithrombin Debrecen (p.Leu205Pro) - Clinical and molecular characterization of a novel mutation associated with severe thrombotic tendency.Semantic proximity Read ↗

Met343Val mutation disrupts the shuttling of Trp380 leading to a low-activity conformer of activated protein C and causes thrombosis.Semantic proximity Read ↗

Pro- and anticoagulant properties of factor V in pathogenesis of thrombosis and bleeding disorders.Semantic proximity Read ↗

Two SERPINC1 variants affecting N-glycosylation of Asn224 cause severe thrombophilia not detected by functional assays.Semantic proximity Read ↗

Asn384Ser Mutation in Protein C is Associated with Multiple-Site Thrombosis in a Young Heterozygous Male.Semantic proximity Read ↗

Impaired factor V-related anticoagulant mechanisms and deep vein thrombosis associated with A2086D and W1920R mutations.Semantic proximity Read ↗

Protein C deficiency caused by homozygosity for a novel PROC D180G mutation--in vitro expression and structural analysis of the mutation.Semantic proximity Read ↗

A novel factor V compound heterozygous mutation associated with thrombosis (Y1961C; FV-Kanazawa, together with 1982_1983del).Semantic proximity Read ↗

Fibrinogen bellingham: a gamma-chain R275C substitution and a beta-promoter polymorphism in a thrombotic member of an asymptomatic family.Semantic proximity Read ↗

A novel frameshift mutation in FGA (c.1846 del A) leading to congenital afibrinogenemia in a consanguineous Syrian family.Semantic proximity Read ↗

Antithrombin III Budapest: a single amino acid substitution (429Pro to Leu) in a region highly conserved in the serpin family.Semantic proximity Read ↗

Novel Mutation p.Asp374Val of SERPINC1 in a Turkish Family with Inherited Antithrombin DeficiencySemantic proximity Read ↗

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