<?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%">Bansode, Sneha B.</style></author><author><style face="normal" font="default" size="100%">Jana, Asis K.</style></author><author><style face="normal" font="default" size="100%">Batkulwar, Kedar B.</style></author><author><style face="normal" font="default" size="100%">Warkad, Shrikant D.</style></author><author><style face="normal" font="default" size="100%">Joshi, Rakesh S.</style></author><author><style face="normal" font="default" size="100%">Sengupta, Neelanjana</style></author><author><style face="normal" font="default" size="100%">Kulkarni, Mahesh J.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Molecular investigations of protriptyline as a multi-target directed ligand in alzheimer's disease</style></title><secondary-title><style face="normal" font="default" size="100%">Plos One</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2014</style></year><pub-dates><date><style  face="normal" font="default" size="100%">AUG</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">8</style></number><publisher><style face="normal" font="default" size="100%">PUBLIC LIBRARY SCIENCE</style></publisher><pub-location><style face="normal" font="default" size="100%">1160 BATTERY STREET, STE 100, SAN FRANCISCO, CA 94111 USA</style></pub-location><volume><style face="normal" font="default" size="100%">9</style></volume><pages><style face="normal" font="default" size="100%">e105196</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Alzheimer's disease (AD) is a complex neurodegenerative disorder involving multiple cellular and molecular processes. The discovery of drug molecules capable of targeting multiple factors involved in AD pathogenesis would greatly facilitate in improving therapeutic strategies. The repositioning of existing non-toxic drugs could dramatically reduce the time and costs involved in developmental and clinical trial stages. In this study, preliminary screening of 140 FDA approved nervous system drugs by docking suggested the viability of the tricyclic group of antidepressants against three major AD targets, viz. Acetylcholinesterase (AChE), beta-secretase (BACE-1), and amyloid beta (A beta) aggregation, with one member, protriptyline, showing highest inhibitory activity. Detailed biophysical assays, together with isothermal calorimetry, fluorescence quenching experiments, kinetic studies and atomic force microscopy established the strong inhibitory activity of protriptyline against all three major targets. The molecular basis of inhibition was supported with comprehensive molecular dynamics simulations. Further, the drug inhibited glycation induced amyloid aggregation, another important causal factor in AD progression. This study has led to the discovery of protriptyline as a potent multi target directed ligand and established its viability as a promising candidate for AD treatment.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">8</style></issue><custom3><style face="normal" font="default" size="100%">Foreign
</style></custom3><custom4><style face="normal" font="default" size="100%">4.17
</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%">Batkulwar, Kedar B.</style></author><author><style face="normal" font="default" size="100%">Bansode, Sneha B.</style></author><author><style face="normal" font="default" size="100%">Patil, Gouri V.</style></author><author><style face="normal" font="default" size="100%">Godbole, Rashmi K.</style></author><author><style face="normal" font="default" size="100%">Kazi, Rubina S.</style></author><author><style face="normal" font="default" size="100%">Chinnathambi, Subashchandrabose</style></author><author><style face="normal" font="default" size="100%">Shanmugam, Dhanasekaran</style></author><author><style face="normal" font="default" size="100%">Kulkarni, Mahesh J.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Investigation of phosphoproteome in RAGE signaling</style></title><secondary-title><style face="normal" font="default" size="100%">Proteomics</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Cell biology</style></keyword><keyword><style  face="normal" font="default" size="100%">Disease</style></keyword><keyword><style  face="normal" font="default" size="100%">Glycation</style></keyword><keyword><style  face="normal" font="default" size="100%">Kinase</style></keyword><keyword><style  face="normal" font="default" size="100%">Phosphoproteome</style></keyword><keyword><style  face="normal" font="default" size="100%">RAGE</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%">JAN</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">2-3, SI</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%">15</style></volume><pages><style face="normal" font="default" size="100%">245-259</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The receptor for advanced glycation end products (RAGE) is one of the most important proteins implicated in diabetes, cardiovascular diseases, neurodegenerative diseases, and cancer. It is a pattern recognition receptor by virtue of its ability to interact with multiple ligands, RAGE activates several signal transduction pathways through involvement of various kinases that phosphorylate their respective substrates. Only few substrates have been known to be phosphorylated in response to activation by RAGE (e.g., nuclear factor kappa B); however, it is possible that these kinases can phosphorylate multiple substrates depending upon their expression and localization, leading to altered cellular responses in different cell types and conditions. One such example is, glycogen synthase kinase 3 beta which is known to phosphorylate glycogen synthase, acts downstream to RAGE, and hyperphosphorylates microtubule-associated protein tau causing neuronal damage. Thus, it is important to understand the role of various RAGE-activated kinases and their substrates. Therefore, we have reviewed here the details of RAGE-activated kinases in response to different ligands and their respective phosphoproteome. Furthermore, we discuss the analysis of the data mined for known substrates of these kinases from the PhosphoSitePlus (http://www.phosphosite.org) database, and the role of some of the important substrates involved in cancer, diabetes, cardiovascular diseases, and neurodegenerative diseases. In summary, this review provides information on RAGE-activated kinases and their phosphoproteome, which will be helpful in understanding the possible role of RAGE and its ligands in progression of diseases.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">2-3</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%">4.079</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%">Bansode, Sneha B.</style></author><author><style face="normal" font="default" size="100%">Batkulwar, Kedar B.</style></author><author><style face="normal" font="default" size="100%">Warkad, Shrikant D.</style></author><author><style face="normal" font="default" size="100%">Jana, Asis K.</style></author><author><style face="normal" font="default" size="100%">Sengupta, Neelanjana</style></author><author><style face="normal" font="default" size="100%">Kulkarni, Mahesh J.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Tolbutamide induces conformational change and promotes albumin glycation</style></title><secondary-title><style face="normal" font="default" size="100%">RSC Advances</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2015</style></year><pub-dates><date><style  face="normal" font="default" size="100%">APR</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">50</style></number><publisher><style face="normal" font="default" size="100%">ROYAL SOC CHEMISTRY</style></publisher><pub-location><style face="normal" font="default" size="100%">THOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLAND</style></pub-location><volume><style face="normal" font="default" size="100%">5</style></volume><pages><style face="normal" font="default" size="100%">40070-40075</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Tolbutamide is a first generation sulfonylurea drug used for the treatment of type II diabetes. In the present study, the effect of tolbutamide on albumin conformation was investigated using BSA as a model protein. The binding of tolbutamide induced a conformational change in albumin, which was confirmed by thioflavin T assay, ANS assay, and CD spectroscopy. Computer simulations suggested that the binding of tolbutamide increases the solvent accessibility of lysine residues, the hotspots of glycation. Furthermore, the change in conformation of albumin facilitates increased glycation, which was observed by AGE specific fluorescence and the results were corroborated by mass spectrometric analysis. This study suggested that tolbutamide enhances albumin glycation by inducing conformational change in BSA and hence could be a potential risk factor if used for a prolonged period.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">50</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%">3.289</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%">Jana, Asis K.</style></author><author><style face="normal" font="default" size="100%">Batkulwar, Kedar B.</style></author><author><style face="normal" font="default" size="100%">Kulkarni, Mahesh J.</style></author><author><style face="normal" font="default" size="100%">Sengupta, Neelanjana</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Glycation induces conformational changes in Amyloid-? peptide and enhances its aggregation propensity: molecular insights</style></title><secondary-title><style face="normal" font="default" size="100%">Physical Chemistry Chemical Physics</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2016</style></year><pub-dates><date><style  face="normal" font="default" size="100%">OCT</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">18</style></volume><pages><style face="normal" font="default" size="100%">31446-31458</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><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%">4.449</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%">Batkulwar, Kedar B.</style></author><author><style face="normal" font="default" size="100%">Jana, Asis K.</style></author><author><style face="normal" font="default" size="100%">Godbole, Rashmi K.</style></author><author><style face="normal" font="default" size="100%">Khandelwal, Puneet</style></author><author><style face="normal" font="default" size="100%">Sengupta, Neelanjana</style></author><author><style face="normal" font="default" size="100%">Kulkarni, Mahesh J.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Hydralazine inhibits amyloid beta (Aβ) aggregation and glycation and ameliorates Aβ1–42 induced neurotoxicity</style></title><secondary-title><style face="normal" font="default" size="100%">RSC Advances</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2016</style></year><pub-dates><date><style  face="normal" font="default" size="100%">NOV</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">6</style></volume><pages><style face="normal" font="default" size="100%">108768-108776</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><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%">3.289</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%">Jagadeeshaprasad, Mashanipalya G.</style></author><author><style face="normal" font="default" size="100%">Batkulwar, Kedar B.</style></author><author><style face="normal" font="default" size="100%">Meshram, Nishita N.</style></author><author><style face="normal" font="default" size="100%">Tiwari, Shalbha</style></author><author><style face="normal" font="default" size="100%">Korwar, Arvind M.</style></author><author><style face="normal" font="default" size="100%">Unnikrishnan, Ambika G.</style></author><author><style face="normal" font="default" size="100%">Kulkarni, Mahesh J.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Targeted quantification of N-1-(carboxymethyl) valine and N-1-(carboxyethyl) valine peptides of beta-hemoglobin for better diagnostics in diabetes</style></title><secondary-title><style face="normal" font="default" size="100%">Clinical Proteomics</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Diabetes</style></keyword><keyword><style  face="normal" font="default" size="100%">Diagnosis</style></keyword><keyword><style  face="normal" font="default" size="100%">Glycation</style></keyword><keyword><style  face="normal" font="default" size="100%">Glycemic control</style></keyword><keyword><style  face="normal" font="default" size="100%">HbA1c</style></keyword><keyword><style  face="normal" font="default" size="100%">Mass spectrometry</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2016</style></year><pub-dates><date><style  face="normal" font="default" size="100%">MAR</style></date></pub-dates></dates><publisher><style face="normal" font="default" size="100%">BIOMED CENTRAL LTD</style></publisher><pub-location><style face="normal" font="default" size="100%">236 GRAYS INN RD, FLOOR 6, LONDON WC1X 8HL, ENGLAND</style></pub-location><volume><style face="normal" font="default" size="100%">13</style></volume><pages><style face="normal" font="default" size="100%">Article Number: 7</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;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.&lt;/p&gt;</style></abstract><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%">3.476</style></custom4></record></records></xml>