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

Structures of VWF tubules before and after concatemerization reveal a mechanism of disulfide bond exchange.

Blood - 22 Sept 2022

Anderson Jacob R, Li Jing, Springer Timothy A, Brown Alan

Abstract excerpt

von Willebrand factor (VWF) is an adhesive glycoprotein that circulates in the blood as disulfide-linked concatemers and functions in primary hemostasis. The loss of long VWF concatemers is associated with the excessive bleeding of type 2A von Willebrand disease (VWD). Formation of the disulfide bonds that concatemerize VWF requires VWF to self-associate into helical tubules, yet how the helical tubules template...

Read the complete abstract on PubMed

Topics

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

Share to Disulfides
Share to Mutation
Share to Protein Domains

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to von Willebrand Disease, Type 2

Share to von Willebrand Diseases

Share to von Willebrand Factor

Source

Open in PubMed Open full text

Identifiers

PMID: 35776905
DOI: 10.1182/blood.2022016467
PMCID: PMC9507011

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structures of VWF tubules before and after concatemerization reveal a mechanism of disulfide bond exchange.PMID 35776905Read ↗

Highly reinforced structure of a C-terminal dimerization domain in von Willebrand factor.Semantic proximity Read ↗

von Willebrand factor is dimerized by protein disulfide isomerase.Semantic proximity Read ↗

Dynamic Disulfide Bond Topologies in von-Willebrand-Factor’s C4-Domain Undermine Platelet BindingSemantic proximity Read ↗

Biogenesis of Weibel-Palade bodies in von Willebrand's disease variants with impaired von Willebrand factor intrachain or interchain disulfide bond formation.Semantic proximity Read ↗

What We Know About Kininogen Structure – Importance for Function and Perspectives from Cryo-EMSemantic proximity Read ↗

Nonnative interactions between cysteines direct productive assembly of P22 tailspike protein.Semantic proximity Read ↗

The disulfide bonding pattern in ficolin multimers.Semantic proximity Read ↗

One-Way Allosteric Communication between the Two Disulfide Bonds in Tissue Factor.Semantic proximity Read ↗

A 3.3-Å cryo-EM structure of an engineered high-affinity human prothrombinase complex.Semantic proximity Read ↗

Family-wide Structural and Biophysical Analysis of Binding Interactions among Non-clustered δ-Protocadherins.Semantic proximity Read ↗

The von Willebrand factor predicted unpaired cysteines are essential for secretion.Semantic proximity Read ↗

Electrostatic Interactions between Elongated Monomers Drive Filamentation of Drosophila Shrub, a Metazoan ESCRT-III ProteinSemantic proximity Read ↗

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