[HTML][HTML] Glycosylation Modulates the Structure and Functions of Collagen: A Review

I Tvaroška - Molecules, 2024 - mdpi.com
Collagens are fundamental constituents of the extracellular matrix and are the most
abundant proteins in mammals. Collagens belong to the family of fibrous or fiber-forming …

[HTML][HTML] Exploring domain architectures of human glycosyltransferases: Highlighting the functional diversity of non-catalytic add-on domains

H Yagi, K Takagi, K Kato - Biochimica et Biophysica Acta (BBA)-General …, 2024 - Elsevier
Human glycosyltransferases (GTs) play crucial roles in glycan biosynthesis, exhibiting
diverse domain architectures. This study explores the functional diversity of “add-on” …

Molecular Structure and Enzymatic Mechanism of the Human Collagen Hydroxylysine Galactosyltransferase GLT25D1/COLGALT1

M De Marco, SR Rai, L Scietti, D Mattoteia, S Liberi… - bioRxiv, 2024 - biorxiv.org
During biosynthesis, collagen lysine residues undergo extensive post-translational
modifications essential for the stability and functions of collagen supramolecular assemblies …

Facts About: Collagen and its Glycosylation–one of the Most Common Glycoproteins in all Animals

RD Cummings - research.bidmc.org
Collagen is the most common and abundant glycoprotein in animals (1). Even sponges
have collagen (termed spongin) and it is glycosylated much like mammalian collagen. Its …