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

Shielding of the A1 domain by the D'D3 domains of von Willebrand factor modulates its interaction with platelet glycoprotein Ib-IX-V.

The Journal of biological chemistry - 24 Feb 2006

Ulrichts Hans, Udvardy Miklós, Lenting Peter J, Pareyn Inge, Vandeputte Nele, Vanhoorelbeke Karen, Deckmyn Hans

Abstract excerpt

Soluble von Willebrand factor (VWF) has a low affinity for platelet glycoprotein (GP) Ibalpha and needs immobilization and/or high shear stress to enable binding of its A1 domain to the receptor. The previously described anti-VWF monoclonal antibody 1C1E7 enhances VWF/GPIbalpha binding and recogn...

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 Collagen Type III
Share to Crotalid Venoms

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Epitope Mapping

Share to Epitopes

Share to Hybridomas

Share to Platelet Glycoprotein GPIb-IX Complex

Share to von Willebrand Factor

Source

Identifiers

PMID: 16373331
DOI: 10.1074/jbc.M513314200

Genes

VWF

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-16373331-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Shielding of the A1 domain by the D'D3 domains of von Willebrand factor modulates its interaction with platelet glycoprotein Ib-IX-V.PMID 16373331Read ↗

Crystal structure of the wild-type von Willebrand factor A1-glycoprotein Ibalpha complex reveals conformation differences with a complex bearing von Willebrand disease mutations.Semantic proximity Read ↗

Shielding the front-strand beta 3 of the von Willebrand factor A1 domain inhibits its binding to platelet glycoprotein Ibalpha.Semantic proximity Read ↗

O-linked glycosylation of von Willebrand factor modulates the interaction with platelet receptor glycoprotein Ib under static and shear stress conditions.Semantic proximity Read ↗

Structural basis of regulation of von Willebrand factor binding to glycoprotein Ib.Semantic proximity Read ↗

The physical spacing between the von Willebrand factor D'D3 and A1 domains regulates platelet adhesion in vitro and in vivo.Semantic proximity Read ↗

Structures of glycoprotein Ibalpha and its complex with von Willebrand factor A1 domain.Semantic proximity Read ↗

Identification of a novel 14-3-3zeta binding site within the cytoplasmic domain of platelet glycoprotein Ibalpha that plays a key role in regulating the von Willebrand factor binding function of glycoprotein Ib-IX.Semantic proximity Read ↗

Destabilization of the A1 domain in von Willebrand factor dissociates the A1A2A3 tri-domain and provokes spontaneous binding to glycoprotein Ibalpha and platelet activation under shear stress.Semantic proximity Read ↗

Crystal structure of the von Willebrand Factor A1 domain and implications for the binding of platelet glycoprotein Ib.Semantic proximity Read ↗

Platelet glycoprotein Ibalpha forms catch bonds with human WT vWF but not with type 2B von Willebrand disease vWF.Semantic proximity Read ↗

Structure and function of the von Willebrand factor A1 domain.Semantic proximity Read ↗

Platelet adhesion: a game of catch and release.Semantic proximity Read ↗

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