Site-specific analysis of advanced glycation end products in plasma proteins of type 2 diabetes mellitus patients-Reference-Cited by-同舟云学术

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Site-specific analysis of advanced glycation end products in plasma proteins of type 2 diabetes mellitus patients

Published:2016-05-28 Issue:20 Volume:408 Page:5557-5566
ISSN:1618-2642
Container-title:Analytical and Bioanalytical Chemistry
language:en
Short-container-title:Anal Bioanal Chem

Author:

Greifenhagen Uta,Frolov Andrej,Blüher Matthias,Hoffmann Ralf

Funder

Deutsche Forschungsgemeinschaft

Ernst Schering Foundation

Publisher

Springer Science and Business Media LLC

Subject

Biochemistry,Analytical Chemistry

Link

http://link.springer.com/content/pdf/10.1007/s00216-016-9651-4.pdf

Reference50 articles.

1. Ulrich P, Cerami A. Protein glycation, diabetes, and aging. Recent Prog Horm Res. 2001;56:1. Vol 56.

2. Schalkwijk CG, Stehouwer CDA, van Hinsbergh VWM. Fructose-mediated non-enzymatic glycation: sweet coupling or bad modification. Diabetes Metab Res Rev. 2004;20:369–82.

3. Wolff SP, Dean RT. Glucose autoxidation and protein modification—the potential role of autoxidative glycosylation in diabetes. Biochem J. 1987;245:243.

4. Niyatishrikhodaee F, Shibamoto T. Gas-chromatographic analysis of glyoxal and methylglyoxal formed from lipids and related-compounds upon ultraviolet-irradiation. J Agric Food Chem. 1993;41:227–30.

5. Ray M, Ray S. Aminoacetone oxidase from goat liver—formation of methylglyoxal from aminoacetone. J Biol Chem. 1987;262:5974.

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