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

The mutation N528S in the von Willebrand factor (VWF) propeptide causes defective multimerization and storage of VWF.

Blood - 3 Jun 2010

Haberichter Sandra L, Budde Ulrich, Obser Tobias, Schneppenheim Sonja, Wermes Cornelia, Schneppenheim Reinhard

Abstract excerpt

We characterized a consanguineous Turkish family suffering from von Willebrand disease (VWD) with significant mucocutaneous and joint bleeding. The relative reduction of large plasma von Willebrand factor (VWF) multimers and the absent VWF triplet structure was consistent with type 2A (phenotype IIC) VWD. Surprisingly, platelet VWF was completely deficient of multimers beyond the VWF protomer, suggesting...

Read the complete abstract on PubMed

Topics

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

Share to Blood Platelets
Share to Consanguinity

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

Share to Glycosylation

Share to In Vitro Techniques

Share to Protein Multimerization

Share to Protein Precursors

Share to von Willebrand Disease, Type 2

Share to von Willebrand Factor

Source

Open in PubMed Open full text

Identifiers

PMID: 20335223
DOI: 10.1182/blood-2009-09-244327
PMCID: PMC2881501

Genes

VWF

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

The mutation N528S in the von Willebrand factor (VWF) propeptide causes defective multimerization and storage of VWF.PMID 20335223Read ↗

von Willebrand factor propeptide missense variants affect anterograde transport to Golgi resulting in ER retention.Semantic proximity Read ↗

von Willebrand factor-T441N, a novel missense variant in the von Willebrand factor D2 domain, exhibits impaired multimerization and deformed Weibel-Palade bodies.Semantic proximity Read ↗

Identification and functional analysis of a novel von Willebrand factor mutation in a family with type 2A von Willebrand disease.Semantic proximity Read ↗

von Willebrand factor propeptide: biology and clinical utilitySemantic proximity Read ↗

Von Willebrand disease mutation spectrum and associated mutation mechanisms.Semantic proximity Read ↗

The dominant p.Thr274Pro mutation in the von Willebrand factor propeptide causes the von Willebrand disease type 1 phenotype in two unrelated patients.Semantic proximity Read ↗

Genetic alteration of the D2 domain abolishes von Willebrand factor multimerization and trafficking into storage.Semantic proximity Read ↗

Multifaceted pathomolecular mechanism of a VWF large deletion involved in the pathogenesis of severe VWD.Semantic proximity Read ↗

Combined deficiency of coagulation factors V and VIII: an update.Semantic proximity Read ↗

Type 2A and 2M von Willebrand Disease: Differences in Phenotypic Parameters According to the Affected Domain by Disease-Causing Variants and Assessment of Pathophysiological Mechanisms.Semantic proximity Read ↗

Landscape and Spectrum of VWF Variants in Type 2 Von Willebrand Disease: Insights from a German Patient Cohort.Semantic proximity Read ↗

Homozygous type 2N R854W von Willebrand factor is poorly secreted and causes a severe von Willebrand disease phenotype.Semantic proximity Read ↗

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