<?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%">Kumar, Santosh</style></author><author><style face="normal" font="default" size="100%">Maiti, Souvik</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Effect of different arginine methylations on the thermodynamics of tat peptide binding to HIV-1 TAR RNA</style></title><secondary-title><style face="normal" font="default" size="100%">Biochimie</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">HIV-1</style></keyword><keyword><style  face="normal" font="default" size="100%">Post-translational modification</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein methylation</style></keyword><keyword><style  face="normal" font="default" size="100%">RNA-protein interaction</style></keyword><keyword><style  face="normal" font="default" size="100%">Thermodynamics</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2013</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%">ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER</style></publisher><pub-location><style face="normal" font="default" size="100%">23 RUE LINOIS, 75724 PARIS, FRANCE</style></pub-location><volume><style face="normal" font="default" size="100%">95</style></volume><pages><style face="normal" font="default" size="100%">1422-1431</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;RNA-binding proteins are an important class of mediators that regulate cell function and differentiation. Methylation of arginine, a post-translational modification (PTM) found in these proteins, can modulate their function. Arginine can be monomethylated or dimethylated, depending on the type of methyl transferases involved. This paper describes a comparative study of the thermodynamics of unmodified and modified Tat peptide interaction with TAR RNA, where the peptide is methylated at epsilon (epsilon) and eta (eta) nitrogen atoms of guanidinium group of arginine side chain at position 52 or 53. The results indicate that monomethylation of arginine at epsilon (epsilon) nitrogen atom enhances binding affinity, owing to a more favourable enthalpy component which overrides the less favourable entropy change. In contrast, monomethylation of arginine residue at eta nitrogen results in reduced binding affinity originating exclusively from a less favourable enthalpy change leaving entropic component unaffected. However, in case of simultaneous methylation at epsilon and eta positions, the binding parameters remain almost unaffected, when compared to the unmodified peptide. In case of symmetric dimethylation at eta position the observed enthalpy change of the binding was found to be smaller than the values obtained for the unmodified peptide. Asymmetric dimethylation at eta position showed the most reduced binding affinities owing to less favourable enthalpy changes. These results provide insights that enable elucidation of the biological outcome of arginine methylation as PTMs that regulate protein function, and will contribute to our understanding of how these PTMs are established in vitro and in vivo. (C) 2013 Elsevier Masson SAS. All rights reserved.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">7</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">3.123
</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%">Kumar, Santosh</style></author><author><style face="normal" font="default" size="100%">Maiti, Souvik</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Effect of N-acetylation and N-methylation of lysine residue of tat peptide on its interaction with HIV-1 TAR RNA</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%">2013</style></year><pub-dates><date><style  face="normal" font="default" size="100%">OCT</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">10</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%">8</style></volume><pages><style face="normal" font="default" size="100%">UNSP e77595</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Post-translational modification (PTM) of RNA binding proteins (RBPs) play a very important role in determining their binding to cognate RNAs and therefore regulate the downstream effects. Lysine can undergo various PTMs and thereby contribute to the regulation of different cellular processes. It can be reversibly acetylated and methylated using a pool of respective enzymes, to act as a switch for controlling the binding efficiency of RBPs. Here we have delineated the thermodynamic and kinetic effects of N-acetylation and N-monomethylation of lysine on interaction between HIV-1 TAR RNA and its cognate binder Tat peptide (a model system). Our results indicate that acetylation of lysine 50 (K50), leads to eight-fold reduction in binding affinity, originating exclusively from entropy changes whereas, lysine 51 (K51) acetylation resulted only in three fold decrease with large enthalpy-entropy compensation. The measurement of kinetic parameters indicated major change (4.5 fold) in dissociation rate in case of K50 acetylation however, K51 acetylation showed similar effect on both association and dissociation rates. In contrast, lysine methylation did not affect the binding affinity of Tat peptide to TAR RNA at K50, nonetheless three fold enhancement in binding affinity was observed at K51 position. In spite of large enthalpy-entropy compensation, lysine methylation seems to have more pronounced position specific effect on the kinetic parameters. In case of K50 methylation, simultaneous increase was observed in the rate of association and dissociation leaving binding affinity unaffected. The increased binding affinity for methylated Tat at K51 stems from faster association rate with slightly slower dissociation rate.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">10</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">3.534
</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%">Kumar, Dhiraj</style></author><author><style face="normal" font="default" size="100%">Haldar, Saikat</style></author><author><style face="normal" font="default" size="100%">Gorain, Mahadeo</style></author><author><style face="normal" font="default" size="100%">Kumar, Santosh</style></author><author><style face="normal" font="default" size="100%">Mulani, Fayaj A.</style></author><author><style face="normal" font="default" size="100%">Yadav, Amit S.</style></author><author><style face="normal" font="default" size="100%">Miele, Lucio</style></author><author><style face="normal" font="default" size="100%">Thulasiram, Hirekodathakallu V.</style></author><author><style face="normal" font="default" size="100%">Kundu, Gopal C.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Epoxyazadiradione suppresses breast tumor growth through mitochondrial depolarization and caspase-dependent apoptosis by targeting PI3K/Akt pathway</style></title><secondary-title><style face="normal" font="default" size="100%">BMC Cancer</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Angiogenesis</style></keyword><keyword><style  face="normal" font="default" size="100%">Apoptosis</style></keyword><keyword><style  face="normal" font="default" size="100%">Breast cancer</style></keyword><keyword><style  face="normal" font="default" size="100%">Limonoids</style></keyword><keyword><style  face="normal" font="default" size="100%">Metastasis</style></keyword><keyword><style  face="normal" font="default" size="100%">PI3K</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%">JAN</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">18</style></volume><pages><style face="normal" font="default" size="100%">52</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: Breast cancer is one of the most commonly diagnosed invasive cancers among women around the world. Among several subtypes, triple negative breast cancer (TNBC) is highly aggressive and chemoresistant. Treatment of TNBC patients has been challenging due to heterogeneity and devoid of well-defined molecular targets. Thus, identification of novel effective and selective agents against TNBC is essential. Methods: We used epoxyazadiradione to assess the cell viability, mitochondrial potential, ROS level, cell migration, apoptosis and protein expression in cell culture models of TNBC MDA-MB-231 and ER+MCF-7 breast cancer cells. The molecular mechanism was examined in two different type of breast cancer cells in response to epoxyazadiradione. We have also analyzed the effect of epoxyazadiradione on breast tumor growth using in vivo mice model. Results: In this study, we for the first time investigated that out of 10 major limonoids isolated from Azadirachta indica, epoxyazadiradione exhibits most potent anti-cancer activity in both TNBC and ER+breast cancer cells. Epoxyazadiradione induces apoptosis and inhibits PI3K/Akt-mediated mitochondrial potential, cell viability, migration and angiogenesis. It also inhibits the expression of pro-angiogenic and pro-metastatic genes such as Cox2, OPN, VEGF and MMP-9 in these cells. Furthermore, epoxyazadiradione attenuates PI3K/Akt- mediated AP-1 activation. Our in vivo data revealed that epoxyazadiradione suppresses breast tumor growth and angiogenesis in orthotopic NOD/SCID mice model. Conclusion: Our findings demonstrate that epoxyazadiradione inhibits PI3K/Akt-dependent mitochondrial depolarisation, induces apoptosis and attenuates cell migration, angiogenesis and breast tumor growth suggesting that this compound may act as a potent therapeutic agent for the management of breast cancer.&lt;/p&gt;</style></abstract><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%">3.288</style></custom4></record></records></xml>