<?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%">Prabhu, R. R.</style></author><author><style face="normal" font="default" size="100%">Kulkarni, Mahesh J.</style></author><author><style face="normal" font="default" size="100%">Parasharami, V. A.</style></author><author><style face="normal" font="default" size="100%">Santhakumari, B.</style></author><author><style face="normal" font="default" size="100%">Paranjape, S.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Attempt at taxonomical characterization of some Rhizobial species by intact cell MALDI mass spectrometry</style></title><secondary-title><style face="normal" font="default" size="100%">World Journal of Microbiology &amp; Biotechnology</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">ICM-MS</style></keyword><keyword><style  face="normal" font="default" size="100%">legume</style></keyword><keyword><style  face="normal" font="default" size="100%">molecular taxonomy</style></keyword><keyword><style  face="normal" font="default" size="100%">Rhizobium</style></keyword><keyword><style  face="normal" font="default" size="100%">symbiotic</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2007</style></year><pub-dates><date><style  face="normal" font="default" size="100%">FEB</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">2</style></number><publisher><style face="normal" font="default" size="100%">SPRINGER</style></publisher><pub-location><style face="normal" font="default" size="100%">233 SPRING STREET, NEW YORK, NY 10013 USA</style></pub-location><volume><style face="normal" font="default" size="100%">23</style></volume><pages><style face="normal" font="default" size="100%">177-185</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;In the present study an attempt was made to exploit the benefit of intact cell MALDI mass spectrometry (ICM-MS) in bringing out similarities and differences among some Rhizobium species and a species of Agrobacterium based on specific mass:charge (m/z) values. Rhizobium species isolated from the root nodules of selected leguminous plants were analysed by ICM-MS. The spectra were acquired in the range of 500-10,000 Da yielding several peaks specific to each species. The peaks obtained corresponded to the respective bacterial cell surface molecules which were desorbed during matrix-assisted laser desorption ionization. The number of peaks were more in the range of 500-1200 Da. Dice similarity coefficient analysis of m/z values indicated that Rhizobium species isolated from Trigonella foenum-graecum and Pisum arvense showed more similarity than any other species. Agrobacterium species did show a few common m/z values in comparison with other Rhizobium species. This clearly shows that Agrobacterium is closely related to Rhizobium. Eventually, ICM-MS technique offers clear, distinct, and consistent results for replicates, in less than an hour's time, therefore this technique has high potential in molecular taxonomy.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">2</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><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%">&lt;p&gt;1.532&lt;/p&gt;
</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%">Bhonsle, Hemangi S.</style></author><author><style face="normal" font="default" size="100%">Singh, Sameer Kumar</style></author><author><style face="normal" font="default" size="100%">Srivastava, Ghanshyam</style></author><author><style face="normal" font="default" size="100%">Boppana, Ramanamurthy</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%">Albumin competitively inhibits glycation of less abundant proteins</style></title><secondary-title><style face="normal" font="default" size="100%">Protein and Peptide Letters</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Diabetes</style></keyword><keyword><style  face="normal" font="default" size="100%">glucose</style></keyword><keyword><style  face="normal" font="default" size="100%">insulin</style></keyword><keyword><style  face="normal" font="default" size="100%">MALDI-TOF-MS</style></keyword><keyword><style  face="normal" font="default" size="100%">vascular complication</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2008</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JUL</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">7</style></number><publisher><style face="normal" font="default" size="100%">BENTHAM SCIENCE PUBL LTD</style></publisher><pub-location><style face="normal" font="default" size="100%">EXECUTIVE STE Y26, PO BOX 7917, SAIF ZONE, 1200 BR SHARJAH, U ARAB EMIRATES</style></pub-location><volume><style face="normal" font="default" size="100%">15</style></volume><pages><style face="normal" font="default" size="100%">663-667</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 non-enzymatic reaction between glucose and protein is the primary cause of diabetic complications. Albumin, the most abundant plasma protein undergoes glycation both in vivo and in vitro. The influence of albumin on glycation of less abundant proteins has not been addressed. For the first time, we show that albumin competitively inhibits the glycation of less abundant proteins. This study suggests that at least in the initial stages of diabetes, albumin may protect other proteins from glycation.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">7</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">1.069</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%">Korwar, Arvind M.</style></author><author><style face="normal" font="default" size="100%">Bhonsle, Hemangi S.</style></author><author><style face="normal" font="default" size="100%">Chougale, Ashok D.</style></author><author><style face="normal" font="default" size="100%">Kote, Sachin S.</style></author><author><style face="normal" font="default" size="100%">Gawai, Kachru R.</style></author><author><style face="normal" font="default" size="100%">Ghole, Vikram S.</style></author><author><style face="normal" font="default" size="100%">Koppikar, Chaitanyananda B.</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%">Analysis of AGE modified proteins and RAGE expression in HER2/neu negative invasive ductal carcinoma</style></title><secondary-title><style face="normal" font="default" size="100%">Biochemical and Biophysical Research Communications</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%">Breast cancer</style></keyword><keyword><style  face="normal" font="default" size="100%">RAGE</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2012</style></year><pub-dates><date><style  face="normal" font="default" size="100%">MAR</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">3</style></number><publisher><style face="normal" font="default" size="100%">ACADEMIC PRESS INC ELSEVIER SCIENCE</style></publisher><pub-location><style face="normal" font="default" size="100%">525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA</style></pub-location><volume><style face="normal" font="default" size="100%">419</style></volume><pages><style face="normal" font="default" size="100%">490-494</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;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.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">3</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">2.406
</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%">Sacheti, Poonam</style></author><author><style face="normal" font="default" size="100%">Bhonsle, Hemangi S.</style></author><author><style face="normal" font="default" size="100%">Patil, Rajendra</style></author><author><style face="normal" font="default" size="100%">Kulkarni, Mahesh J.</style></author><author><style face="normal" font="default" size="100%">Srikanth, Rapole</style></author><author><style face="normal" font="default" size="100%">Gade, Wasudeo N.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Arsenomics of exiguobacterium sp PS (NCIM 5463)</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%">2013</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%">25</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%">3</style></volume><pages><style face="normal" font="default" size="100%">9705-9713</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;In the present study, arsenate [As(V)] tolerant organisms were isolated from a metal contaminated site, and identified by 16S rDNA sequencing as Exiguobacterium sp. Arsenomics (omics of arsenic response) in Exiguobacterium sp. PS via two-dimensional gel electrophoresis (2-DGE) coupled with identification of proteins using MALDI-TOF MS, MALDI-TOF MS/MS and LC/MSE are studied vide this paper. Out of 2460 Coomassie stained proteins, 270 were differentially expressed (p &amp;lt; 0.05). Considering the resolution and abundance level, 45 spots (proteins) were subjected to MALDI-TOF MS/MS, MALDI-TOF/TOF and LC/MSE. Out of these, 33 were identified and categorized into several functional categories (including both known and novel/putative stress responsive proteins) viz., carbohydrate and energy metabolism, stress response, motility, amino acid, and purine and protein synthesis. The identifications of unique proteins, phosphate ABC transporter ATPase subunit and pyridine nucleotide disulfide oxidoreductase, are the significant findings of the present study which may be used as markers of As(V) stress in Exiguobacterium sp. PS. The absence of As(V) reductase activity and non-amplification of the arsC gene of the ars operon suggests that the classical mechanism of As(V) resistance may not be operating in Exiguobacterium sp. PS. Lastly, considering the fact that proteomic studies under As(V) stress were performed only in Gram negative organisms, this study is the first comprehensive endeavour to explore the mechanism of As(V) response in Gram positive organisms, Exiguobacterium sp. PS at the proteomic level.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">25</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">3.708
</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%">Tiwari, Shalbha</style></author><author><style face="normal" font="default" size="100%">Botahle, Manish</style></author><author><style face="normal" font="default" size="100%">Hasan, Imtiaz</style></author><author><style face="normal" font="default" size="100%">Kulkarni, Mahesh J.</style></author><author><style face="normal" font="default" size="100%">Sayyad, Mehmood G.</style></author><author><style face="normal" font="default" size="100%">Basu, Rita</style></author><author><style face="normal" font="default" size="100%">Basu, Ananda</style></author><author><style face="normal" font="default" size="100%">Unnikrishnan A. G.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Association between serum albumin and glycated hemoglobin in Asian Indian subjects</style></title><secondary-title><style face="normal" font="default" size="100%">Indian Journal of Endocrinology and Metabolism</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%">JAN</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">19</style></volume><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Protein glycation plays a significant role in diabetic complications. Glycated hemoglobin (HbA1c) is a known predictor of diabetes and its complications. Albumin, found to be profoundly glycated in diabetes, and its level could regulate plasma protein as well as hemoglobin glycation. We aimed to evaluate the association between variations in albumin level with HbA1c in the Asian Indian population. We screened data of 929 subjects who have had a simultaneous measurement of fasting plasma glucose (FPG), HbA1c and albumin levels via the same blood collection. Data were analyzed by SPSS for 610 subjects who met the study criteria. There was a significant negative correlation between HbA1c and albumin concentration (r = -0.284; P &amp;lt; 0.001). Univariate analysis showed the statistically significant decrease of average HbA1c but not for fasting plasma glucose (FPG) across increasing tertiles of albumin. Stepwise multiple regression model showed a significant correlation between HbA1c and serum albumin (P &amp;lt; 0.05), FPG (P &amp;lt; 0.001), hemoglobin (Hb) (P &amp;lt; 0.001) and serum globulin (P &amp;lt; 0.05). FPG was the strongest predictor (63.4%) of variation of HbA1c. The albumin concentration (r = -0.114) accounted for 0.3% (P &amp;lt; 0.05) of the total variance in HbA1c independent of age, body mass index, FPG, Hb, creatinine, total protein and globulin. It was also observed that HbA1c decreases with increasing albumin concentration in those having FPG between 100 to &amp;lt;126 mg/dl. Serum albumin negatively correlates with HbA1c in Asian Indians independent of other variables. This study suggests that predicting diabetes and its complication based on the HbA1c needs to be further investigated in Indian subjects.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">1</style></issue><custom3><style face="normal" font="default" size="100%">&lt;p&gt;Indian&lt;/p&gt;</style></custom3><custom4><style face="normal" font="default" size="100%">2.644</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%">Bhat, Shweta</style></author><author><style face="normal" font="default" size="100%">Jagadeeshaprasad, Mashanipalya G.</style></author><author><style face="normal" font="default" size="100%">Venkatasubramani, Vinashya</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%">Abundance matters: role of albumin in diabetes, a proteomics perspective</style></title><secondary-title><style face="normal" font="default" size="100%">Expert Review of Proteomics</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2017</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JUL</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">14</style></volume><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Introduction: Human serum albumin (HSA) is a multifaceted protein with vital physiological functions. It is the most abundant plasma protein with inherent capability to bind to diverse ligands, and thus susceptible to various post-translational modifications (PTMs) which alter its structure and functions. One such PTM is glycation, a non-enzymatic reaction between reducing sugar and protein leading to formation of heterogeneous advanced glycation end products (AGEs). Glycated albumin (GA) concentration increases significantly in diabetes and is implicated in development of secondary complications. Areas covered: In this review, we discuss in depth formation of GA and its consequences, approaches used for characterization and quantification of GA, milestones in GA proteomics, clinical relevance of GA as a biomarker, significance of maintaining abundant levels of albumin and future perspectives. Expert commentary: Elevated GA levels are associated with development of insulin resistance as well as secondary complications, in healthy and diabetic individuals respectively. Mass spectrometry (MS) based approaches aid in precise characterization and quantification of GA including early and advanced glycated peptides, which can be useful in prediction of the disease status. Thus GA has evolved to be one of the best candidates in the pursuit of diagnostic markers for prediction of prediabetes and diabetic complications.</style></abstract><issue><style face="normal" font="default" size="100%">8</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">3.465</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</style></author><author><style face="normal" font="default" size="100%">Godbole, Rashmi</style></author><author><style face="normal" font="default" size="100%">Banarjee, Reema</style></author><author><style face="normal" font="default" size="100%">Kassaar, Omar</style></author><author><style face="normal" font="default" size="100%">Williams, Robert J.</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%">Advanced glycation end products modulate amyloidogenic APP processing and tau phosphorylation: a mechanistic link between glycation and the development of alzheimer's disease</style></title><secondary-title><style face="normal" font="default" size="100%">ACS Chemical Neuroscience</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2018</style></year><pub-dates><date><style  face="normal" font="default" size="100%">MAY</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">9</style></volume><pages><style face="normal" font="default" size="100%">988-1000</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Advanced glycation end products (AGEs) are implicated in the pathology of Alzheimer's disease (AD), as they induce neurodegeneration following interaction with the receptor for AGE (RAGE). This study aimed to establish a mechanistic link between AGE-RAGE signaling and AD pathology. AGE-induced changes in the neuro2a proteome were monitored by SWATH-MS. Western blotting and cell-based reporter assays were used to investigate AGE-RAGE regulated APP processing and tau phosphorylation in primary cortical neurons. Selected protein expression was validated in brain samples affected by AD. The AGE-RAGE axis altered proteome included increased expression of cathepsin B and asparagine endopeptidase (AEP), which mediated an increase in A beta(1-)(42) formation and tau phosphorylation, respectively. Elevated cathepsin B, AEP, RAGE, and pTau levels were found in human AD brain, coincident with enhanced AGEs. This study demonstrates that the AGE-RAGE axis regulates A beta(1-)(42) formation and tau phosphorylation via increased cathepsin B and AEP, providing a new molecular link between AGEs and AD pathology.</style></abstract><issue><style face="normal" font="default" size="100%">5</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">3.883</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%">Venkatasubramani, Vinashya</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%"> Albumin abundance and its glycation Status determine hemoglobin glycation</style></title><secondary-title><style face="normal" font="default" size="100%">ACS Omega</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2018</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%">3</style></volume><pages><style face="normal" font="default" size="100%">12999-13008</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Diabetes diagnosis and management majorly depend upon the measurement of glycated hemoglobin (HbAlc) levels. Various factors influence HbAlc levels such as the use of various analytical methods and the presence of various clinical conditions. Plasma albumin levels were known to be negatively associated with HbAlc. However, the precise mechanism by which they affect HbAlc is not well' understood. Therefore, we have studied the influence of albumin levels and its glycation status on hemoglobin glycation using erythrocyte culture experiments. Erythrocytes maintained at low albumin concentration exhibited relatively increased albumin and hemoglobin glycation as compared to that in those maintained at higher albumin concentration. Increase in albumin glycation may decrease its ability to protect hemoglobin glycation. This was demonstrated by treatment of erythrocytes with N(epsilon-(carboxymethyl)lysine-modified serum albumin (CMSA), which failed to protect hemoglobin glycation; instead, it increased hemoglobin glycation. The inability of CMSA to reduce hemoglobin glycation was due to the lack of free lysine residues of albumin, which was corroborated by using N(epsilon-(acetyI)lysine serum albumin (AcSA) and clinical diabetic plasma. This is the first study which demonstrates that the modification of lysine residues of albumin impairs its ability to inhibit hemoglobin glycation. Furthermore, correlation studies between HbAlc and albumin levels or relative albumin fructosamine from clinical subjects supported our experimental finding that albumin abundance and its glycation status influence hemoglobin glycation. Therefore, we propose albumin level and its glycation status to be quantified in conjunction with HbAlc for better management of diabetes.</style></abstract><issue><style face="normal" font="default" size="100%">10</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">0.75</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%">Joshi, Rakesh S.</style></author><author><style face="normal" font="default" size="100%">Giri, Ashok P.</style></author><author><style face="normal" font="default" size="100%">Kulkarni, Mahesh J.</style></author><author><style face="normal" font="default" size="100%">Gupta, Mahesh</style></author><author><style face="normal" font="default" size="100%">Verma, Savita</style></author><author><style face="normal" font="default" size="100%">Chaudhry, Dhruva</style></author><author><style face="normal" font="default" size="100%">Deshmukh, Narendra</style></author><author><style face="normal" font="default" size="100%">Chugh, Anita</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Antiviral drugs prioritization for COVID-19 management based on rational selection</style></title><secondary-title><style face="normal" font="default" size="100%">Current Science</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Drug repurposing</style></keyword><keyword><style  face="normal" font="default" size="100%">hACE-2</style></keyword><keyword><style  face="normal" font="default" size="100%">main protease</style></keyword><keyword><style  face="normal" font="default" size="100%">RNA dependent RNA polymerase</style></keyword><keyword><style  face="normal" font="default" size="100%">SARS-CoV-2</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2021</style></year><pub-dates><date><style  face="normal" font="default" size="100%">MAY </style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">120</style></volume><pages><style face="normal" font="default" size="100%">1464-1470</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 SARS-CoV-2 infection has resulted in COVID-19 pandemic worldwide. It has infected around 0.1 billion individuals and caused 2 million fatalities across the globe till mid-January 2021. Drug repurposing has been utilized as the most preferred therapeutic intervention for COVID-19 mitigation due to its necessity and feasibility. To prioritize therapeutic regime against COVID-19, we used 61 antiviral drugs and their combinations. Selected molecules were subjected to virtual screening against: (i) human angiotensin-converting enzyme 2 receptor binding domain (hACE-2) which serves as an anchor for virus attachment and entry, (ii) SARS-CoV-2 RNA dependent RNA polymerase (RdRp) responsible for viral RNA replication, and (iii) SARS-CoV-2 main protease (M-Pro) needed for viral polyprotein slab proteolytic processing. Based on docking score, pharmacodynamic and pharmacokinetic parameters, combinations of Daclatasvir, Elbasvir, Indinavir, Ledipasvir, Paritaprevir and Rilpivirine were analysed further. Our analysis suggested Sofosbuvir in combination with Ledipasvir and Daclatasvir as potential therapeutic agents for SARS-CoV-2. The combined score suggests that these combinations have superior anti-SARS-CoV-2 potential than Remdesivir and other investigational drugs. The present work provides a rationale-based approach to select drugs with possible anti-SARS-CoV-2 activity for further clinical evaluation.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">9</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;Indian&lt;/p&gt;</style></custom3><custom4><style face="normal" font="default" size="100%">1.102</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%">Patil, Yugendra R.</style></author><author><style face="normal" font="default" size="100%">Tiwari, Shalbha</style></author><author><style face="normal" font="default" size="100%">Momin, Abdulrahaman A.</style></author><author><style face="normal" font="default" size="100%">Unnikrishnan, A. 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%">Autoantibodies against Nε-carboxymethyl lysine and methylglyoxal modified albumin are associated with cardiovascular risk in type 2 diabetes</style></title><secondary-title><style face="normal" font="default" size="100%">International Journal of Diabetes in Developing Countries</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">AGE</style></keyword><keyword><style  face="normal" font="default" size="100%">Atherosclerosis</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%">Immune response</style></keyword><keyword><style  face="normal" font="default" size="100%">ROC</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2025</style></year><pub-dates><date><style  face="normal" font="default" size="100%">DEC</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">45</style></volume><pages><style face="normal" font="default" size="100%">1104-1110</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 Albumin is an abundant plasma protein which gets modified with advanced glycation end products (AGEs) predominantly in diabetic condition. AGE modification induces immune response and autoantibodies are generated which play an important role in disease pathology. Objective This study aimed to illustrate the role of autoantibodies against N epsilon-carboxymethyl lysine (CML) and methylglyoxal (MG) modified albumin in diabetic cardiovascular complications. MethodsType-2 diabetes subjects were enrolled and further grouped into stress test positive or stress test negative based on treadmill stress test (TMT). Autoantibody titer was quantified by ELISA assay for CML-modified albumin (stress test positive&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">4</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;Foreign&lt;/p&gt;
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