<?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%">Yadav, Amit Kumar</style></author><author><style face="normal" font="default" size="100%">Dey, Namit</style></author><author><style face="normal" font="default" size="100%">Chattopadhyay, Sabyasachi</style></author><author><style face="normal" font="default" size="100%">Ganguli, Munia</style></author><author><style face="normal" font="default" size="100%">Fernandes, Moneesha</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Dendrimeric amide- and carbamate-linked lysine-based efficient molecular transporters</style></title><secondary-title><style face="normal" font="default" size="100%">Organic &amp; Biomolecular Chemistry</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%">DEC</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">15</style></volume><pages><style face="normal" font="default" size="100%">9579-9584</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Amide- and carbamate-linked dendrimeric oligomers are reported as molecular transporters. They effectively complex with pDNA and transport it into cells at an efficiency superior to Lipofectamine, when complexation is carried out by incubation overnight. The carbamate-linked K2C is superior to amide-linked K2A; their pDNA complexes have very low associated cytotoxicity.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">45</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%">3.559</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%">Saikhedkar, Nidhi S.</style></author><author><style face="normal" font="default" size="100%">Joshi, Rakesh S.</style></author><author><style face="normal" font="default" size="100%">Bhoite, Ashwini S.</style></author><author><style face="normal" font="default" size="100%">Mohandasan, Radhika</style></author><author><style face="normal" font="default" size="100%">Yadav, Amit Kumar</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%">Tripeptides derived from reactive centre loop of potato type II protease inhibitors preferentially inhibit midgut proteases of Helicoverpa armigera</style></title><secondary-title><style face="normal" font="default" size="100%">Insect Biochemistry and Molecular Biology </style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Helicoverpa armigera</style></keyword><keyword><style  face="normal" font="default" size="100%">Protease</style></keyword><keyword><style  face="normal" font="default" size="100%">protease inhibitor</style></keyword><keyword><style  face="normal" font="default" size="100%">Reactive centre loop peptides</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2018</style></year><pub-dates><date><style  face="normal" font="default" size="100%">APR </style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">95</style></volume><pages><style face="normal" font="default" size="100%">17-25</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Potato type II protease inhibitors (Pin-II PIs) impede the growth of lepidopteran insects by inhibiting serine protease-like enzymes in the larval gut. The three amino acid reactive centre loop (RCL) of these proteinaceous inhibitors is crucial for protease binding and is conserved across the Pin-II family. However, the molecular mechanism and inhibitory potential of the RCL tripeptides in isolation of the native protein has remained elusive. In this study, six peptides corresponding to the RCLs of the predominant Pin-II PIs were identified, synthesized and evaluated for in vitro and in vivo inhibitory activity against serine proteases of the polyphagous insect, Helicoverpa armigera. RCL peptides with sequences PRN, PRY and TRE were found to be potent inhibitors that adversely affected the growth and development of H. armigera. The binding mechanism and differential affinity of the RCL peptides with serine proteases was delineated by crystal structures of complexes of the RCL peptides with trypsin. Residues P1 and P2 of the inhibitors play a crucial role in the interaction and specificity of these inhibitors. Important features of RCL peptides like higher inhibition of insect proteases, enhanced efficacy at alkaline gut pH, longer retention and high stability in insect gut make them suitable molecules for the development of sustainable pest management strategies for crop protection.&lt;/p&gt;</style></abstract><work-type><style face="normal" font="default" size="100%">Journal 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;3.756&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%">Yadav, Amit Kumar</style></author><author><style face="normal" font="default" size="100%">Chilukuri, Harsha</style></author><author><style face="normal" font="default" size="100%">Kumari, Linthoinganbi Raj</style></author><author><style face="normal" font="default" size="100%">Karthikeyan, Muthukumarasamy</style></author><author><style face="normal" font="default" size="100%">Fernandes, Moneesha</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">p-Nitrophenylcarbonates: a new class of compounds for chemodosimetric colorimetric fluoride anion sensing detectable by the naked eye</style></title><secondary-title><style face="normal" font="default" size="100%">ChemistrySelect</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">colorimetric sensing</style></keyword><keyword><style  face="normal" font="default" size="100%">p-nitrophenyl carbonate</style></keyword><keyword><style  face="normal" font="default" size="100%">selective fluoride detection</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2019</style></year><pub-dates><date><style  face="normal" font="default" size="100%">FEB</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">4</style></volume><pages><style face="normal" font="default" size="100%">1830-1833</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;A new class of compounds containing the p-nitrophenylcarbonate motif is reported, that can selectively sense fluoride anions over other halide anions with a detection limit ranging from 0.29 to 0.48 mu M. The fluoride ion acts as nucleophile, leading to the liberation of p-nitrophenol, that is easily detectable and quantifiable colorimetrically.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">5</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;1.716&lt;/p&gt;
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