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W Baynes

Showing results (91-100 of 192) with videos related to

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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.
Mass Spectrometry Reviews|October 12, 2013
The succinated proteomeEric D Merkley, Thomas O Metz, Richard D Smith, 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.
Journal of Proteome Research|December 20, 2008
A perspective on the Maillard reaction and the analysis of protein glycation by mass spectrometry: probing the pathogenesis of chronic diseaseQibin Zhang, Jennifer M Ames, Richard D Smith, 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.
Annals of the New York Academy of Sciences|July 23, 2005
Effect of glucose concentration on formation of AGEs in erythrocytes in vitroRyoji Nagai, Elizabeth K Deemer, Jonathan W Brock, 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.
The Biochemical Journal|June 1, 1997
N-epsilon-(carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in human lens proteinsM U Ahmed, E Brinkmann Frye, T P Degenhardt, et al.
Proceedings of the National Academy of Sciences of the United States of America|September 1, 1979
Enhanced nonenzymatic glucosylation of human serum albumin in diabetes mellitusC E Guthrow, M A Morris, J F Day, et al.
The Diabetes Educator|March 24, 2006
What is the future of diabetic wound care?Sarah M Sweitzer, Stephen A Fann, Thomas K Borg, et al.
Pageof 20

Showing results (91-100 of 192) with videos related to

Sort By:
Pageof 20
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.
Mass Spectrometry Reviews|October 12, 2013
The succinated proteomeEric D Merkley, Thomas O Metz, Richard D Smith, 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.
Journal of Proteome Research|December 20, 2008
A perspective on the Maillard reaction and the analysis of protein glycation by mass spectrometry: probing the pathogenesis of chronic diseaseQibin Zhang, Jennifer M Ames, Richard D Smith, 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.
Annals of the New York Academy of Sciences|July 23, 2005
Effect of glucose concentration on formation of AGEs in erythrocytes in vitroRyoji Nagai, Elizabeth K Deemer, Jonathan W Brock, 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.
The Biochemical Journal|June 1, 1997
N-epsilon-(carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in human lens proteinsM U Ahmed, E Brinkmann Frye, T P Degenhardt, et al.
Proceedings of the National Academy of Sciences of the United States of America|September 1, 1979
Enhanced nonenzymatic glucosylation of human serum albumin in diabetes mellitusC E Guthrow, M A Morris, J F Day, et al.
The Diabetes Educator|March 24, 2006
What is the future of diabetic wound care?Sarah M Sweitzer, Stephen A Fann, Thomas K Borg, et al.
Pageof 20