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Article

N-linked glycosylation of VWF modulates its interaction with ADAMTS13.

Blood - 15 Mar 2008

McKinnon Thomas A J, Chion Alain C K, Millington Alexander J, Lane David A, Laffan Mike A

Abstract excerpt

We examined the role of N-linked glycan structures of VWF on its interaction with ADAMTS13. PNGase F digestion followed by lectin analysis demonstrated that more than 90% of VWF N-linked glycan chains could be removed from the molecule (PNG-VWF) without disruption of its multimeric structure or its ability to bind to collagen. PNG-VWF had an approximately 4-fold increased affinity for ADAMTS13 compared with...

Read the complete abstract on PubMed

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Share to Glycosylation
Share to ADAM Proteins
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Molecular

Share to Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase

Share to Protein Structure, Tertiary

Share to Recombinant Proteins

Share to von Willebrand Factor

Source

Identifiers

PMID: 17975018
DOI: 10.1182/blood-2007-06-095042

Genes

VWF
ADAMTS13
ABO

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.

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