01852nas a2200241   4500008004100000022001400041245012100055210006900176260016500245300001200410490000700422520084600429653001601275653003601291653002001327653001501347653001001362100002401372700002501396700003701421700002501458856012701483       2011                        eng d  a0388-135000aComparative and chemical proteomic approaches reveal gatifloxacin deregulates enzymes involved in glucose metabolism0 aComparative and chemical proteomic approaches reveal gatifloxaci  aINTERNATIONAL MEDICAL INFORMATION CENTER, SHINANOMACHI RENGAKAN, 35 SHINANO-MACHI, SHINJUKU-KU, TOKYO, 160-0016, JAPANbJAPANESE SOC TOXICOLOGICAL SCIENCEScDEC  a787-7960 v363 a<p>Gatifloxacin has been associated with increased risks of hypoglycemic and hyperglycemic side effects. In order to understand the molecular mechanism of gatifloxacin induced deregulation of glucose metabolism, a Combination of comparative and chemical proteomic approaches were employed using yeast as a model system. Differential protein expression studies using two dimensional electrophoresis and mass spectrometry reveal that gatifloxacin deregulates the expression of key enzymes involved in glucose metabolism. Furthermore, affinity chromatography and LC-MSE analysis led to identification of enolase, as one of the key gatifloxacin binding proteins. Fluorescence spectrometric studies confirmed that the gatifloxacin indeed binds to enolase. Role of enolase in regulation of gatifloxacin induced dysglycemic effect is discussed.</p>10aantibiotics10aDifferential protein expression10aFluoroquinolone10aGlycolysis10aYeast1 aSuresh, Kesavan, K.1 aBhosale, Santosh, D.1 aThulasiram, Hirekodathakallu, V.1 aKulkarni, Mahesh, J.  uhttps://library.ncl.res.in/content/comparative-and-chemical-proteomic-approaches-reveal-gatifloxacin-deregulates-enzymes-002064nas a2200253   4500008004100000022001400041245013500055210006900190260009300259300001200352490000700364520103800371653004301409653003301452653001301485653003701498100002501535700002301560700002401583700002501607700002301632700002501655856013001680       2012                        eng d  a1469-066700aZoom-in - a targeted database search for identification of glycation modifications analyzed by untargeted tandem mass spectrometry0 aZoomin a targeted database search for identification of glycatio  a6 CHARLTON MILL, CHARLTON, CHICHESTER,, W SUSSEX PO18 0HY, ENGLANDbIM PUBLICATIONScJAN  a475-4810 v183 a<p>Post-translational modifications (PTMs) are very important to biological function, however their identification and characterization is technically challenging. In this study, we have identified glycation modifications by nano LC-MSE, a data independent acquisition work flow, followed by database search using the Protein Lynx Global Server (PLGS). PLGS search with a complete human protein database hardly identified glycation modifications in a glycated human serum albumin (HSA), which was detected to be glycated by western blotting with advanced glycation end products (AGE) antibody and fluorescence spectroscopy. To overcome this difficulty, ``Zoom-In'' approach, a targeted database search was used to identify glycation modifications in a glycated HSA, which were further manually validated. This approach was useful for identification of glycation modifications from untargeted tandem mass spectrometry workflow such as MSE, but may require the development of a new algorithm or an upgrade of the existing software.</p>10aadvanced glycation end products (AGEs)10adata independent acquisition10aDiabetes10apost-translational modifications1 aBhonsle, Hemangi, S.1 aKorwar, Arvind, M.1 aKesavan, Suresh, K.1 aBhosale, Santosh, D.1 aBansode, Sneha, B.1 aKulkarni, Mahesh, J.  uhttps://library.ncl.res.in/content/zoom-targeted-database-search-identification-glycation-modifications-analyzed-untargeted-001910nas a2200265   4500008004100000022001400041245012700055210006900182260009000251300000900341490000600350520086400356100002401220700001701244700002901261700003901290700002401329700002301353700002501376700002401401700003701425700002601462700002501488856013101513       2013                        eng d  a2045-232200aProteome wide reduction in AGE modification in streptozotocin induced diabetic mice by hydralazine mediated transglycation0 aProteome wide reduction in AGE modification in streptozotocin in  aMACMILLAN BUILDING, 4 CRINAN ST, LONDON N1 9XW, ENGLANDbNATURE PUBLISHING GROUPcOCT  a29410 v33 a<p>The non-enzymatic reaction between glucose and protein can be chemically reversed by transglycation. Here we report the transglycation activity of hydralazine using a newly developed MALDI-TOF-MS based assay. Hydralazine mediated transglycation of HbA1c, plasma proteins and kidney proteins was demonstrated in streptozotocin (STZ) induced diabetic mice, as evidenced by decrease in protein glycation, as well as presence of hydralazine-glucose conjugate in urine of diabetic mice treated with hydralazine. Hydralazine down regulated the expression of Receptor for Advanced Glycation End products (RAGE), NADPH oxidase (NOX), and super oxide dismutase (SOD). These findings will provide a new dimension for developing intervention strategies for the treatment of glycation associated diseases such as diabetes complications, atherosclerosis, and aging.</p>1 aKesavan, Suresh, K.1 aBhat, Shweta1 aGolegaonkar, Sandeep, B.1 aJagadeeshaprasad, Mashanipalya, G.1 aDeshmukh, Arati, B.1 aPatil, Harshal, S.1 aBhosale, Santosh, D.1 aShaikh, Mahemud, L.1 aThulasiram, Hirekodathakallu, V.1 aBoppana, Ramanamurthy1 aKulkarni, Mahesh, J.  uhttps://library.ncl.res.in/content/proteome-wide-reduction-age-modification-streptozotocin-induced-diabetic-mice-hydralazine-0