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

Crucial role for the VWF A1 domain in binding to type IV collagen.

Blood - 2 Apr 2015

Flood Veronica H, Schlauderaff Abraham C, Haberichter Sandra L, Slobodianuk Tricia L, Jacobi Paula M, Bellissimo Daniel B, Christopherson Pamela A, Friedman Kenneth D, Gill Joan Cox, Hoffmann Raymond G, Montgomery Robert R

Abstract excerpt

Von Willebrand factor (VWF) contains binding sites for platelets and for vascular collagens to facilitate clot formation at sites of injury. Although previous work has shown that VWF can bind type IV collagen (collagen 4), little characterization of this interaction has been performed. We examined the binding of VWF to collagen 4 in vitro and extended this characterization to a murine model of defective...

Read the complete abstract on PubMed

Topics

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

Share to Collagen Type IV
Share to Flow Cytometry

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutagenesis, Site-Directed

Share to Protein Conformation

Share to Protein Structure, Tertiary

Share to Structure-Activity Relationship

Share to von Willebrand Diseases

Share to von Willebrand Factor

Source

Open in PubMed Open full text

Identifiers

PMID: 25662333
DOI: 10.1182/blood-2014-11-610824
PMCID: PMC4383803

Genes

VWF

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Crucial role for the VWF A1 domain in binding to type IV collagen.PMID 25662333Read ↗

Critical von Willebrand factor A1 domain residues influence type VI collagen binding.Semantic proximity Read ↗

Variability in platelet- and collagen-binding defects in type 2M von Willebrand disease.Semantic proximity Read ↗

M1761K mutation in the von Willebrand factor A3 domain associated with impaired collagen binding and without platelet dysfunction.Semantic proximity Read ↗

Abnormal hemostasis in a knock-in mouse carrying a variant of factor IX with impaired binding to collagen type IV.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 ↗

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

A3 domain is essential for interaction of von Willebrand factor with collagen type III.Semantic proximity Read ↗

Molecular modeling of the seven tandem leucine-rich repeats within the ligand-binding region of platelet glycoprotein Ib alpha.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 ↗

Characterisation of von Willebrand factor A1 domain mutants I1416N and I1416T: correlation of clinical phenotype with flow-based platelet adhesion.Semantic proximity Read ↗

Exploiting the kinetic interplay between GPIbα-VWF binding interfaces to regulate hemostasis and thrombosis.Semantic proximity Read ↗

Recombinant von Willebrand factor Arg578-->Gln. A type IIB von Willebrand disease mutation affects binding to glycoprotein Ib but not to collagen or heparin.Semantic proximity Read ↗

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