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• W3167457246 startingPage "855" @default.
• W3167457246 abstract "Glycosylation is a key posttranslational modification, known to occur on more than half of all secreted proteins in man. As such, the role of N- and O-linked glycan structures in modulating various aspects of protein biology is an area of much research. Given their prevalence, it is perhaps unsurprising that variations in glycan structures have been demonstrated to play critical roles in modulating protein function and have been implicated in the pathophysiology of human diseases. von Willebrand factor (VWF), a plasma glycoprotein that is essential for normal hemostasis, is heavily glycosylated, containing 13 N-linked and 10 O-linked glycans. Together, these carbohydrate chains account for 20% of VWF monomeric mass, and have been shown to modulate VWF structure, function, and half-life. In this review, we focus on the specific role played by O-linked glycans in modulating VWF biology. Specifically, VWF O-linked glycans have been shown to modulate tertiary protein structure, susceptibility to ADAMTS13 proteolysis, platelet tethering, and VWF circulatory half-life." @default.
• W3167457246 created "2021-06-22" @default.
• W3167457246 creator A5007517961 @default.
• W3167457246 creator A5084545467 @default.
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• W3167457246 date "2021-06-15" @default.
• W3167457246 modified "2023-09-26" @default.
• W3167457246 title "The Biological Significance of von Willebrand Factor O-Linked Glycosylation" @default.
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• W3167457246 doi "https://doi.org/10.1055/s-0041-1726373" @default.
• W3167457246 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/34130346" @default.
• W3167457246 hasPublicationYear "2021" @default.
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