02064nas 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-001301nas a2200241   4500008004100000022001400041245005300055210005200108260007500160300001200235490000600247520057000253653001000823653001300833653001400846653000900860100002500869700002300894700001600917700002500933700002000958856008100978       2013                        eng d  a1862-834600aGlycated proteome: from reaction to intervention0 aGlycated proteome from reaction to intervention  aPOSTFACH 101161, 69451 WEINHEIM, GERMANYbWILEY-V C H VERLAG GMBHcJAN  a155-1700 v73 a<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>10aaging10aDiabetes10aGlycation10aRAGE1 aKulkarni, Mahesh, J.1 aKorwar, Arvind, M.1 aMary, Sheon1 aBhonsle, Hemangi, S.1 aGiri, Ashok, P.  uhttps://library.ncl.res.in/content/glycated-proteome-reaction-intervention-002720nas a2200289   4500008004100000022001400041245015100055210006900206260008100275300002200356490000700378520163500385653001302020653001402033653001402047653002102061653001002082653002202092100003902114700002502153700002502178700002002203700002302223700002902246700002502275856013002300       2016                        eng d  a1542-641600aTargeted quantification of N-1-(carboxymethyl) valine and N-1-(carboxyethyl) valine peptides of beta-hemoglobin for better diagnostics in diabetes0 aTargeted quantification of N1carboxymethyl valine and N1carboxye  a236 GRAYS INN RD, FLOOR 6, LONDON WC1X 8HL, ENGLANDbBIOMED CENTRAL LTDcMAR  aArticle Number: 70 v133 a<p>Background: N-1-(Deoxyfructosyl) valine (DFV) beta-hemoglobin (beta-Hb), commonly referred as HbA1c, is widely used diagnostic marker in diabetes, believed to provide glycemic status of preceding 90-120 days. However, the turnover of hemoglobin is about 120 days, the DFV-beta-Hb, an early and reversible glycation product eventually may undergo irreversible advanced glycation modifications such as carboxymethylation or carboxyethylation. Hence quantification of N-1-(carboxymethyl) valine (CMV) and N-1-(carboxyethyl) valine (CEV) peptides of beta-Hb would be useful in assessing actual glycemic status. Results: Fragment ion library for synthetically glycated peptides of hemoglobin was generated by using high resolution-accurate mass spectrometry (HR/AM). Using parallel reaction monitoring, deoxyfructosylated, carboxymethylated and carboxyethylated peptides of hemoglobin were quantified in clinical samples from healthy control, pre-diabetes, diabetes and poorly controlled diabetes. For the first time, we report N-1-beta-valine undergoes carboxyethylation and mass spectrometric quantification of CMV and CEV peptides of beta-hemoglobin. Carboxymethylation was found to be the most abundant modification of N-1-beta-valine. Both CMV-beta-Hb and CEV-beta-Hb peptides showed better correlation with severity of diabetes in terms of fasting glucose, postprandial glucose and microalbuminuria. Conclusions: This study reports carboxymethylation as a predominant modification of N-1-beta-valine of Hb, and quantification of CMV-beta-Hb and CEV-beta-Hb could be useful parameter for assessing the severity of diabetes.</p>10aDiabetes10aDiagnosis10aGlycation10aGlycemic control10aHbA1c10aMass spectrometry1 aJagadeeshaprasad, Mashanipalya, G.1 aBatkulwar, Kedar, B.1 aMeshram, Nishita, N.1 aTiwari, Shalbha1 aKorwar, Arvind, M.1 aUnnikrishnan, Ambika, G.1 aKulkarni, Mahesh, J.  uhttps://library.ncl.res.in/content/targeted-quantification-n-1-carboxymethyl-valine-and-n-1-carboxyethyl-valine-peptides-beta