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Biochemical and Biophysical Research Communications

Volumn 260, Issue 2, 1999, Pages 332-338

Protein aging by carboxymethylation of lysines generates sites for divalent metal and redox active copper binding: Relevance to diseases of glycoxidative stress

(6) Saxena, Amit K a Saxena, Poonam a Wu, Xinle a Obrenovich, Mark a Weiss, Miriam F a Monnier, Vincent M a

a CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASCORBIC ACID; BOVINE SERUM ALBUMIN; CHELATING AGENT; COPPER; HYDROGEN PEROXIDE; LIPID; LYSINE DERIVATIVE; N (CARBOXYMETHYL)LYSINE; PENTETIC ACID; POLYLYSINE; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG;

AGING; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; DEPOLYMERIZATION; DIABETES MELLITUS; DNA MODIFICATION; DRUG OXIDATION; IMMUNOPRECIPITATION; LIPID OXIDATION; METAL BINDING; NONHUMAN; OXIDATION REDUCTION REACTION; OXIDATIVE STRESS; PERITONEAL CAVITY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN METHYLATION; PROTEIN MODIFICATION; RAT; TENDON; UREMIA;

EID: 0033526832 PISSN: 0006291X EISSN: None Source Type: Journal
DOI: 10.1006/bbrc.1999.0898 Document Type: Article

Times cited : (92)

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