J W Baynes|S R Thorpe - JoVE Visualize

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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.

The Journal of Biological Chemistry|May 10, 1985

Characterization of glycated proteins by 13C NMR spectroscopy. Identification of specific sites of protein modification by glucoseC I Neglia, H J Cohen, A R Garber, et al.

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Showing results (31-40 of 129) with videos related to

Sort By:

Pageof 13

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.

The Journal of Biological Chemistry|May 10, 1985

Characterization of glycated proteins by 13C NMR spectroscopy. Identification of specific sites of protein modification by glucoseC I Neglia, H J Cohen, A R Garber, et al.

Pageof 13