@article { ISI:000302437100008,
	title = {Analysis of AGE modified proteins and RAGE expression in HER2/neu negative invasive ductal carcinoma},
	journal = {Biochemical and Biophysical Research Communications},
	volume = {419},
	number = {3},
	year = {2012},
	month = {MAR},
	pages = {490-494},
	publisher = {ACADEMIC PRESS INC ELSEVIER SCIENCE},
	address = {525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA},
	abstract = {<p>Cancer is associated with increased glycolysis and carbonyl stress. In view of this, AGE modified proteins were identified from clinical breast cancer tissue using 2DE-immunoblot and mass-spectrometry. These proteins were identified to be serotransferrin, fibrinogen gamma chain, glycerol-3-phosphate dehydrogenase, lactate dehydrogenase, annexin II, prohibitin and peroxiredoxin 6, which have established role in cancer. Further, RAGE expression and its downstream signaling proteins NADPH oxidase and NF-kB were studied. Role of these AGE modified proteins and RAGE signaling in breast cancer is discussed. (C) 2012 Elsevier Inc. All rights reserved.</p>},
	keywords = {advanced glycation end products, Breast cancer, RAGE},
	issn = {0006-291X},
	doi = {10.1016/j.bbrc.2012.02.039},
	author = {Korwar, Arvind M. and Bhonsle, Hemangi S. and Chougale, Ashok D. and Kote, Sachin S. and Gawai, Kachru R. and Ghole, Vikram S. and Koppikar, Chaitanyananda B. and Kulkarni, Mahesh J.}
}
@article { ISI:000313903700015,
	title = {Glycated proteome: from reaction to intervention},
	journal = {Proteomics Clinical Applications},
	volume = {7},
	number = {1-2, SI},
	year = {2013},
	month = {JAN},
	pages = {155-170},
	publisher = {WILEY-V C H VERLAG GMBH},
	address = {POSTFACH 101161, 69451 WEINHEIM, GERMANY},
	abstract = {<p>Glycation, a nonenzymatic reaction between reducing sugars and proteins, is a proteome wide phenomenon, predominantly observed in diabetes due to hyperglycemia. Glycated proteome of plasma, kidney, lens, and brain are implicated in the pathogenesis of various diseases, including diabetic complications, neurodegenerative diseases, cancer, and aging. This review discusses the strategies to characterize protein glycation, its functional implications in different diseases, and intervention strategies to protect the deleterious effects of protein glycation.</p>},
	keywords = {aging, Diabetes, Glycation, RAGE},
	issn = {1862-8346},
	doi = {10.1002/prca.201200101},
	author = {Kulkarni, Mahesh J. and Korwar, Arvind M. and Mary, Sheon and Bhonsle, Hemangi S. and Giri, Ashok P.}
}
