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Glycosylation Sterically Inhibits Platelet Adhesion to von Willebrand Factor without Altering Intrinsic Conformational Dynamics

BACKGROUND: A molecular basis for VWF self-inhibition has been proposed by which the N- and C-terminal flanking sequences of the globular A1 domain disulfide loop bind to and suppress the conformational dynamics of A1. These flanking sequences are rich in O-linked glycosylation (OLG) which is known...

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Detalhes bibliográficos
Publicado no:J Thromb Haemost
Main Authors: Tischer, Alexander, Machha, Venkata R., Moon-Tasson, Laurie, Benson, Linda M., Auton, Matthew
Formato: Artigo
Idioma:Inglês
Publicado em: 2019
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Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC6940534/
https://ncbi.nlm.nih.gov/pubmed/31479573
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1111/jth.14628
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