ArticleJournal of translational medicine2024
Defining albumin as a glycoprotein with multiple N-linked glycosylation sites.
Article in Journal of translational medicine, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The trial behind it
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Who cites it
7 citing papers in PubMed.
- Mapping ophthalmic research on glycosylation and glycation: a PRISMA-compliant bibliometric and co‑citation analysis.Future science OA · 2026Article
- Optimized Simultaneous N/O-Glycopeptide Enrichment Strategy Identifies Lung Cancer Diagnostic Biomarkers in Serum.Journal of proteome research · 2026Article
- Albumin as a glycoprotein biomarker in congenital disorders of glycosylation.Molecular genetics and metabolism · 2026Article
- Extensive Hypoglycosylation of Serum N-Glycoproteins in SRD5A3 Deficiency.Journal of inherited metabolic disease · 2026Article
- Therapeutic Targeting of Viral N-Glycosylation Modification: From Molecular Mechanisms to Clinical Application Prospects.Infectious diseases and therapy · 2025Review
- Harnessing Ultrasonic Technologies to TreatMolecules (Basel, Switzerland) · 2025Review
- A complement C4-derived glycopeptide is a biomarker for PMM2-CDG.JCI insight · 2024Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
backgroundGlycosylation is an enzyme-catalyzed post-translational modification that is distinct from glycation and is present on a majority of plasma proteins. N-glycosylation occurs on asparagine residues predominantly within canonical N-glycosylation motifs (Asn-X-Ser/Thr) although non-canonical N-glycosylation motifs Asn-X-Cys/Val have also been reported. Albumin is the most abundant protein in plasma whose glycation is well-studied in diabetes mellitus. However, albumin has long been considered a non-glycosylated protein due to absence of canonical motifs. Albumin contains two non-canonical N-glycosylation motifs, of which one was recently reported to be glycosylated.
methodsWe enriched abundant serum proteins to investigate their N-linked glycosylation followed by trypsin digestion and glycopeptide enrichment by size-exclusion or mixed-mode anion-exchange chromatography. Glycosylation at canonical as well as non-canonical sites was evaluated by liquid chromatography-tandem mass spectrometry (LC-MS/MS) of enriched glycopeptides. Deglycosylation analysis was performed to confirm N-linked glycosylation at non-canonical sites. Albumin-derived glycopeptides were fragmented by MS3 to confirm attached glycans. Parallel reaction monitoring was carried out on twenty additional samples to validate these findings. Bovine and rabbit albumin-derived glycopeptides were similarly analyzed by LC-MS/MS.
resultsHuman albumin is N-glycosylated at two non-canonical sites, Asn
conclusionsAlbumin is a glycoprotein with conserved N-linked glycosylation sites that could have potential clinical applications.
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