Identification of Nε-(carboxyethyl)lysine, one of the methylglyoxal-derived AGE structures, in glucose-modified protein: mechanism for protein modification by reactive aldehydes
- 1 May 2003
- journal article
- Published by Elsevier in Journal of Chromatography B
- Vol. 788 (1) , 75-84
- https://doi.org/10.1016/s1570-0232(02)01019-x
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- Pyridoxamine, an Inhibitor of Advanced Glycation Reactions, Also Inhibits Advanced Lipoxidation ReactionsPublished by Elsevier ,2000
- Methylglyoxal Modification of ProteinJournal of Biological Chemistry, 1999
- Photo-Enhanced Modification of Human Skin Elastin in Actinic Elastosis by N∈-(Carboxymethyl)lysine, One of the Glycoxidation Products of the Maillard ReactionJournal of Investigative Dermatology, 1997
- Hydroxyl Radical Mediates Nϵ-(Carboxymethyl)lysine Formation from Amadori ProductBiochemical and Biophysical Research Communications, 1997
- Protein Cross-linking by the Maillard ReactionJournal of Biological Chemistry, 1996
- Nε-(Carboxymethyl)lysine Protein Adduct Is a Major Immunological Epitope in Proteins Modified with Advanced Glycation End Products of the Maillard ReactionBiochemistry, 1996
- Pathways of Formation of Glycoxidation Products during Glycation of CollagenBiochemistry, 1995
- Ultrastructure of nonenzymatically glycated mesangial matrix in diabetic nephropathyKidney International, 1995
- beta 2-Microglobulin modified with advanced glycation end products is a major component of hemodialysis-associated amyloidosis.Journal of Clinical Investigation, 1993
- The formation of methylglyoxal from triose phosphatesEuropean Journal of Biochemistry, 1993