ArticleJournal of proteome research2017
An Insight into Glyco-Microheterogeneity of Plasma von Willebrand Factor by Mass Spectrometry.
Article in Journal of proteome research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- Synthesis of Boronic Acid-Functionalized Core-Shell Mesoporous Silica-TiOSmall methods · 2026Article
- Quantification and Site-Specific Analysis of Co-occupied N- and O-Glycopeptides.Journal of proteome research · 2024Article
- Bleeding disorder of unknown cause: an illustrated review on current practice, knowledge gaps, and future perspectives.Research and practice in thrombosis and haemostasis · 2024Article
- Quantification and site-specific analysis of co-occupied N- and O-glycopeptides.bioRxiv : the preprint server for biology · 2024Article
- Sialylation on O-linked glycans protects von Willebrand factor from macrophage galactose lectin-mediated clearance.Haematologica · 2022Article
- Combination ofJournal of clinical medicine · 2022Article
- The relationship between ABO blood group, von Willebrand factor, and primary hemostasis.Blood · 2020Review
- Comprehensive N- and O-glycosylation mapping of human coagulation factor V.Journal of thrombosis and haemostasis : JTH · 2020Article
- Increased galactose expression and enhanced clearance in patients with low von Willebrand factor.Blood · 2019Article
- Article
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Authors and funding
12 authors at 4 institutions in 3 countries.
Funding
Abstract
Human plasma von Willebrand Factor (VWF) plays essential roles in primary hemostasis in cooperation with other coagulations factors. There is ample indication that glycosylation affects many biological phases during the protein life cycle. However, comprehensive characterization of all probable N-glycosites simultaneous with O-glycosites is still not fully revealed. Thus, the intention of this exploration was to estimate the occupancy of all canonical N-glycosites besides simultaneous characterization of N- and O-glycoforms. An RP-LC-MS/MS system functionalized with CID and HCD tandem mass was utilized to analyze VWF. N-Glycosite occupancy varied along the protein backbone chain. Out of 257 HCD spectra, 181 characterized glycoforms were specified as either N- or O-glycosites. Sequential cleavage of glycosidic bonds along with Human Database mass matching have confirmed the glycoform structures. A total of 173 glycoforms represented most commonly biantennary and infrequently tri- and tetra-antennary N-glycans beside high mannose, hybrid, ABH antigen-terminated, and sulfated N-glycans. Many glycoforms were common across all N-sites. Noteworthy, previously unreported N-glycosites within domain D'(TIL'-E') showed glycosylation. Moreover, sialylated core 1 and core 2 O-glycans were detected on 2298T. Given subtle characterization of site-specific glycoforms, we can attain a profound understanding of the biological roles of VWF as well as facilitate the production of VWF-based therapeutics.
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