Glycation of type I collagen selectively targets the same helical domain lysine sites as lysyl oxidase–mediated cross-linking-Reference-Cited by-同舟云学术

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Glycation of type I collagen selectively targets the same helical domain lysine sites as lysyl oxidase–mediated cross-linking

Published:2018-10 Issue:40 Volume:293 Page:15620-15627
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Hudson David M.,Archer Marilyn,King Karen B.,Eyre David R.

Funder

HHS | NIH | National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIAMS)

National Institute of Child Health and Human Development (NICHD)

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference48 articles.

1. The effects of the Maillard reaction on the physical properties and cell interactions of collagen;Avery;Pathol. Biol,2006

2. Effect of collagen turnover on the accumulation of advanced glycation end products;Verzijl;J. Biol. Chem,2000

3. Aspartic acid racemization and collagen degradation markers reveal an accumulation of damage in tendon collagen that is enhanced with aging;Thorpe;J. Biol. Chem,2010

4. Lack of tissue renewal in human adult Achilles tendon is revealed by nuclear bomb 14C;Heinemeier;FASEB J,2013

5. Ageing and zonal variation in post-translational modification of collagen in normal human articular cartilage. The age-related increase in non-enzymatic glycation affects biomechanical properties of cartilage;Bank;Biochem. J,1998

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