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Biochemistry|November 28, 1989
Oxidation of glycated proteins: age-dependent accumulation of N epsilon-(carboxymethyl)lysine in lens proteinsJ A Dunn, J S Patrick, S R Thorpe, et al.
Diabetes|October 1, 1992
Role of oxygen in cross-linking and chemical modification of collagen by glucoseM X Fu, K J Knecht, S R Thorpe, et al.
The Journal of Biological Chemistry|July 21, 1998
Role of the Maillard reaction in aging of tissue proteins. Advanced glycation end product-dependent increase in imidazolium cross-links in human lens proteinsE B Frye, T P Degenhardt, S R Thorpe, et al.
The Journal of Biological Chemistry|July 25, 1980
Carbohydrate-mediated clearance of immune complexes from the circulation. A role for galactose residues in the hepatic uptake of IgG-antigen complexesR W Thornburg, J F Day, J W Baynes, et al.
Clinical Chemistry|December 1, 1993
Mechanism of fructosamine assay: evidence against role of superoxide as intermediate in nitroblue tetrazolium reductionJ R Baker, D V Zyzak, S R Thorpe, et al.
Clinical Chemistry|October 1, 1994
Chemistry of the fructosamine assay: D-glucosone is the product of oxidation of Amadori compoundsJ R Baker, D V Zyzak, S R Thorpe, et al.
The Biochemical Journal|April 16, 1998
Presence of dopa and amino acid hydroperoxides in proteins modified with advanced glycation end products (AGEs): amino acid oxidation products as a possible source of oxidative stress induced by AGE proteinsS Fu, M X Fu, J W Baynes, et al.
The Biochemical Journal|April 1, 1990
A fluorescent residualizing label for studies on protein uptake and catabolism in vivo and in vitroJ L Maxwell, L Terracio, T K Borg, et al.
Biochemistry|August 29, 1995
N epsilon-(carboxymethyl)lysine is a dominant advanced glycation end product (AGE) antigen in tissue proteinsS Reddy, J Bichler, K J Wells-Knecht, et al.
Diabetes|August 1, 1991
Role of glycation in modification of lens crystallins in diabetic and nondiabetic senile cataractsT J Lyons, G Silvestri, J A Dunn, et al.
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