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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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| Опубликовано в: : | J Thromb Haemost |
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| Главные авторы: | , , , , |
| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
2019
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| Предметы: | |
| Online-ссылка: | 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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