Search research articles
Contact Us
Filters
Showing results (91-100 of 192) with videos related to
Page
of 20
Sort By:
The Biochemical Journal
|
April 1, 1990
A fluorescent residualizing label for studies on protein uptake and catabolism in vivo and in vitro
J L Maxwell, L Terracio, T K Borg, et al.
Mass Spectrometry Reviews
|
October 12, 2013
The succinated proteome
Eric 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 proteins
S 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 disease
Qibin 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 cataracts
T 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 vitro
Ryoji 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 glucose
C 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 proteins
M 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 mellitus
C 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.
Page
of 20
Search research articles
Search
Showing results (91-100 of 192) with videos related to
Sort By:
Page
of 20
The Biochemical Journal
|
April 1, 1990
A fluorescent residualizing label for studies on protein uptake and catabolism in vivo and in vitro
J L Maxwell, L Terracio, T K Borg, et al.
Mass Spectrometry Reviews
|
October 12, 2013
The succinated proteome
Eric 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 proteins
S 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 disease
Qibin 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 cataracts
T 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 vitro
Ryoji 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 glucose
C 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 proteins
M 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 mellitus
C 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.
Page
of 20