Propagation of protein glycation damage involves modification of tryptophan residues via reactive oxygen species: inhibition by pyridoxamine

Free Radical Biology and Medicine

Volumn 44, Issue 7, 2008, Pages 1276-1285

  Chetyrkin, Sergei V ^a   Mathis, Missy E ^a   Ham, Amy Joan L ^b   Hachey, David L ^b   Hudson, Billy G ^a,b   Voziyan, Paul A ^a,b  

^a VANDERBILT UNIVERSITY MEDICAL CENTER   (United States)

^b VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Advanced glycation end products; Amadori intermediate; Free radicals; Lysozyme; Protein glycation; Pyridoxamine; Reactive oxygen species; Tryptophan oxidation

Indexed keywords

ALBUMIN; AMINOGUANIDINE; ARGININE; GLUCOSE; HYDROXYL RADICAL; LYSINE; LYSOZYME; METAL ION; PROTEIN; PYRIDOXAMINE; REACTIVE OXYGEN METABOLITE; RIBOSE; TRYPTOPHAN;

ANIMAL MODEL; ARTICLE; CATALYSIS; DIABETES MELLITUS; DRUG INHIBITION; ENZYME ACTIVITY; GLUCOSE OXIDATION; NONHUMAN; OXIDATIVE STRESS; PHYSIOLOGY; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN GLYCOSYLATION; PROTEIN MODIFICATION; PROTEIN STRUCTURE; RAT; THERAPY EFFECT;

ANIMALS; CHICKENS; GLYCOSYLATION END PRODUCTS, ADVANCED; HYDROXYL RADICAL; HYPERGLYCEMIA; MODELS, BIOLOGICAL; MODELS, CHEMICAL; MURAMIDASE; OXIDATIVE STRESS; PROTEINS; PYRIDOXAMINE; REACTIVE OXYGEN SPECIES; SPECTROPHOTOMETRY, ULTRAVIOLET; SUPEROXIDES; TRYPTOPHAN;

EID: 40949155274     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2007.09.016     Document Type: Article

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