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

C2362F mutation gives rise to an ADAMTS13-resistant von Willebrand factor.

Thrombosis and haemostasis - 1 Jun 2013

Casonato Alessandra, Pontara Elena, Battiston Monica, Morpurgo Margherita, Cattini Maria Grazia, Casarin Elisabetta, Saga Giorgia, Daidone Viviana, De Marco Luigi

Abstract excerpt

von Willebrand factor (VWF) multimers result from proteolysis by the metalloprotease ADAMTS13. Since C2362F-VWF features abnormally large multimers with their triplet oligomer structure replaced by a diffuse smear, we explored the susceptibility of C2362F-VWF to ADAMTS13. VWF-enriched blood samples, obtained by cryoethanol precipitation of plasma from a patient with von Willebrand disease (VWD) homozygous for the...

Read the complete abstract on PubMed

Topics

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

Share to Hemostasis
Share to von Willebrand Diseases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to ADAM Proteins

Share to ADAMTS13 Protein

Share to Biotinylation

Share to Cysteine

Share to Family Health

Share to von Willebrand Factor

Source

Identifiers

PMID: 23446343
DOI: 10.1160/TH12-11-0808

Genes

VWF
ADAMTS13

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

C2362F mutation gives rise to an ADAMTS13-resistant von Willebrand factor.PMID 23446343Read ↗

Altered von Willebrand factor subunit proteolysis and multimer processing associated with the Cys2362Phe mutation in the B2 domain.Semantic proximity Read ↗

Loss of cysteine 584 impairs the storage and release, but not the synthesis of von Willebrand factor.Semantic proximity Read ↗

A common mechanism by which type 2A von Willebrand disease mutations enhance ADAMTS13 proteolysis revealed with a von Willebrand factor A2 domain FRET construct.Semantic proximity Read ↗

Heightened proteolysis of the von Willebrand factor subunit in patients with von Willebrand disease hemizygous or homozygous for the C2362F mutation.Semantic proximity Read ↗

Autosomal recessive von Willebrand disease associated with compound heterozygosity for a novel nonsense mutation (2908 del C) and the missense mutation C2362F: definite evidence for the non-penetrance of the C2362F mutation.Semantic proximity Read ↗

An amino acid polymorphism in von Willebrand factor correlates with increased susceptibility to proteolysis by ADAMTS13.Semantic proximity Read ↗

Impact of mutations in the von Willebrand factor A2 domain on ADAMTS13-dependent proteolysis.Semantic proximity Read ↗

Effect of von Willebrand disease type 2B and type 2M mutations on the susceptibility of von Willebrand factor to ADAMTS-13.Semantic proximity Read ↗

[Increased susceptibility of recombinant type 2A von Willebrand factor mutant A1500E to proteolysis by ADAMTS13].Semantic proximity Read ↗

Mutation G1629E Increases von Willebrand Factor Cleavage via a Cooperative Destabilization Mechanism.Semantic proximity Read ↗

ADAMTS13 cleavage efficiency is altered by mutagenic and, to a lesser extent, polymorphic sequence changes in the A1 and A2 domains of von Willebrand factor.Semantic proximity Read ↗

Thermodynamic stabilization of the von Willebrand Factor A1 domain due to loss-of-function disease-related mutationsSemantic proximity Read ↗

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