Related Experiment Video
Updated: Jan 22, 2026

A Facile and Efficient Approach for the Production of Reversible Disulfide Cross-linked Micelles
Published on: December 23, 2016
Lysine Hydroxylation and Cross-Linking of Collagen
Mitsuo Yamauchi1, Masahiko Terajima2, Masashi Shiiba3
1Department of Oral and Craniofacial Health Sciences, School of Dentistry, University of North Carolina, Chapel Hill, NC, USA. mitsuo_yamauchi@unc.edu.
Abstract:
Collagens represent a large family of structurally related proteins containing a unique triple-helical structure. Among them, the fibril-forming collagens are the most abundant in vertebrates providing tissues with form and stability. One of the characteristics of the fibrillar collagens is its sequential posttranslational modifications of specific lysine residues that have major effects on molecular assembly and stability of the fibrils in the extracellular space. Hydroxylation of lysine residues is the first modification catalyzed by lysyl hydroxylases, and is critical for the following glycosylation and in determining the fate of covalent cross-linking. This chapter presents an overview of lysine hydroxylation and cross-linking of collagen, and the analytical methods we have developed.
More Related Videos
Related Concept Videos
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein....
Crossing Over
The homologous pairs of sister chromosomes—one from the maternal and one from the paternal genome—then begin to align alongside each other lengthwise, matching corresponding DNA positions in a process...
Crossing Over
Monohybrid Crosses
Cross-Sectional Research
Dihybrid Crosses

