Potential implications of the glycosylation patterns in collagen α1(I) and α2(I) chains for fibril assembly and growth

• Published in: Journal of structural biology Vol. 215; no. 1; p. 107938
• Main Authors: Visser, D.R., Loo, T.S., Norris, G.E, Parry, David A.D.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.03.2023
• Subjects: Animals; Collagen - metabolism; Collagen type I; Collagen Type I - metabolism; Fibrillogenesis; Glycosylation; Lysine - metabolism; Mass spectrometry; Periodicity; Proteomics; Fibrillogenesis; Glycosylation; Collagen type I; Mass spectrometry; Periodicity

[Display omitted] •Post-translational modifications of collagen from four animals are identified.•Nine new hydroxylysine glycosylation sites identified in collagen Type I.•Lysine oxidation patterns in collagen type I display species variation.•d-periodic axial distribution of glycosylated hydroxylys...