<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Kulkarni, Mahesh J.</style></author><author><style face="normal" font="default" size="100%">Korwar, Arvind M.</style></author><author><style face="normal" font="default" size="100%">Mary, Sheon</style></author><author><style face="normal" font="default" size="100%">Bhonsle, Hemangi S.</style></author><author><style face="normal" font="default" size="100%">Giri, Ashok P.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Glycated proteome: from reaction to intervention</style></title><secondary-title><style face="normal" font="default" size="100%">Proteomics Clinical Applications</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">aging</style></keyword><keyword><style  face="normal" font="default" size="100%">Diabetes</style></keyword><keyword><style  face="normal" font="default" size="100%">Glycation</style></keyword><keyword><style  face="normal" font="default" size="100%">RAGE</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2013</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JAN</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">1-2, SI</style></number><publisher><style face="normal" font="default" size="100%">WILEY-V C H VERLAG GMBH</style></publisher><pub-location><style face="normal" font="default" size="100%">POSTFACH 101161, 69451 WEINHEIM, GERMANY</style></pub-location><volume><style face="normal" font="default" size="100%">7</style></volume><pages><style face="normal" font="default" size="100%">155-170</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;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.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">1-2</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">2.683
</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Golegaonkar, Sandeep</style></author><author><style face="normal" font="default" size="100%">Tabrez, Syed S.</style></author><author><style face="normal" font="default" size="100%">Pandit, Awadhesh</style></author><author><style face="normal" font="default" size="100%">Sethurathinam, Shalini</style></author><author><style face="normal" font="default" size="100%">Jagadeeshaprasad, Mashanipalya G.</style></author><author><style face="normal" font="default" size="100%">Bansode, Sneha B.</style></author><author><style face="normal" font="default" size="100%">Sampathkumar, Srinivasa-Gopalan</style></author><author><style face="normal" font="default" size="100%">Kulkarni, Mahesh J.</style></author><author><style face="normal" font="default" size="100%">Mukhopadhyay, Arnab</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Rifampicin reduces advanced glycation end products and activates DAF-16 to increase lifespan in Caenorhabditis elegans</style></title><secondary-title><style face="normal" font="default" size="100%">Aging Cell</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">advanced glycation end products</style></keyword><keyword><style  face="normal" font="default" size="100%">aging</style></keyword><keyword><style  face="normal" font="default" size="100%">Caenorhabditis elegans</style></keyword><keyword><style  face="normal" font="default" size="100%">DAF-16</style></keyword><keyword><style  face="normal" font="default" size="100%">Glycation</style></keyword><keyword><style  face="normal" font="default" size="100%">lifespan</style></keyword><keyword><style  face="normal" font="default" size="100%">rifampicin</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2015</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JUN</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">3</style></number><publisher><style face="normal" font="default" size="100%">WILEY-BLACKWELL</style></publisher><pub-location><style face="normal" font="default" size="100%">111 RIVER ST, HOBOKEN 07030-5774, NJ USA</style></pub-location><volume><style face="normal" font="default" size="100%">14</style></volume><pages><style face="normal" font="default" size="100%">463-473</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Advanced glycation end products (AGEs) are formed when glucose reacts nonenzymatically with proteins; these modifications are implicated in aging and pathogenesis of many age-related diseases including type II diabetes, atherosclerosis, and neurodegenerative disorders. Thus, pharmaceutical interventions that can reduce AGEs may delay age-onset diseases and extend lifespan. Using LC-MSE, we show that rifampicin (RIF) reduces glycation of important cellular proteins in vivo and consequently increases lifespan in Caenorhabditis elegans by up to 60%. RIF analog rifamycin SV (RSV) possesses similar properties, while rifaximin (RMN) lacks antiglycation activity and therefore fails to affect lifespan positively. The efficacy of RIF and RSV as potent antiglycating agents may be attributed to the presence of a p-dihydroxyl moiety that can potentially undergo spontaneous oxidation to yield highly reactive p-quinone structures, a feature absent in RMN. We also show that supplementing rifampicin late in adulthood is sufficient to increase lifespan. For its effect on longevity, rifampicin requires DAF-18 (nematode PTEN) as well as JNK-1 and activates DAF-16, the FOXO homolog. Interestingly, the drug treatment modulates transcription of a different subset of DAF-16 target genes, those not controlled by the conserved Insulin-IGF-1-like signaling pathway. RIF failed to increase the lifespan of daf-16 null mutant despite reducing glycation, showing thereby that DAF-16 may not directly affect AGE formation. Together, our data suggest that the dual ability to reduce glycation in vivo and activate prolongevity processes through DAF-16 makes RIF and RSV effective lifespan-extending interventions.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">3</style></issue><custom3><style face="normal" font="default" size="100%">&lt;p&gt;Foreign&lt;/p&gt;</style></custom3><custom4><style face="normal" font="default" size="100%">5.76</style></custom4></record></records></xml>