ArticleGlycoconjugate journal2020
Identification of novel glycosylation events on human serum-derived factor IX.
Article in Glycoconjugate journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Immunopeptidomics of blood coagulation factor IX: a core peptide derived from the protease domain is promiscuously presented on HLA-DR.Research and practice in thrombosis and haemostasis · 2026Article
- The role of N-glycosylation in spike antigenicity for the SARS-CoV-2 gamma variant.Glycobiology · 2024Article
- A Critical Analysis of the FDA's Omics-Driven Pharmacodynamic Biomarkers to Establish Biosimilarity.Pharmaceuticals (Basel, Switzerland) · 2023Review
- Structure and antigenicity of divergent Henipavirus fusion glycoproteins.Nature communications · 2023Article
- Coagulation abnormalities in a prospective cohort of 50 patients with PMM2-congenital disorder of glycosylation.Molecular genetics and metabolism · 2023Article
- Efficient TurboID-based proximity labelling method for identifying terminal sialic acid glycosylation in living cells.Acta biochimica et biophysica Sinica · 2022Article
- Recent Advances in Mass Spectrometry-Based Structural Elucidation Techniques.Molecules (Basel, Switzerland) · 2022Review
- Coagulation factor IX analysis in bioreactor cell culture supernatant predicts quality of the purified product.Communications biology · 2021Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human Factor IX is a highly post-translationally modified protein that is an important clotting factor in the blood coagulation cascade. Functional deficiencies in Factor IX result in the bleeding disorder haemophilia B, which is treated with plasma-derived or recombinant Factor IX concentrates. Here, we investigated the post-translational modifications of human serum-derived Factor IX and report previously undescribed O-linked monosaccharide compositions at serine 141 and a novel site of glycosylation. At serine 141 we observed two monosaccharide compositions, with HexNAc
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Registered trials
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