<?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%">Gunjal, Anita D.</style></author><author><style face="normal" font="default" size="100%">Fernandes, Moneesha</style></author><author><style face="normal" font="default" size="100%">Erande, Namrata D.</style></author><author><style face="normal" font="default" size="100%">Rajamohanan, P. R.</style></author><author><style face="normal" font="default" size="100%">Kumar, Vaijayanti A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Functional isoDNA aptamers: modified thrombin binding aptamers with a 2'-5'-linked sugarphosphate backbone (isoTBA)</style></title><secondary-title><style face="normal" font="default" size="100%">Chemical Communications</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%">NOV</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">5</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%">50</style></volume><pages><style face="normal" font="default" size="100%">605-607</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 regioisomeric 3'-deoxy-2'-5'-linked thrombin binding DNA aptamers (isoTBAs) were chemically synthesized and their ability to form unimolecular anti-parallel G-quadruplexes in the presence of K+ ions was evaluated. These modified sequences retain the function of the native thrombin binding aptamer (TBA), exhibit better stability against exonuclease and are capable of slowing down the process of blood clotting.&lt;/p&gt;</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%">7.00</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%">Awachat, Ragini</style></author><author><style face="normal" font="default" size="100%">Wagh, Atish A.</style></author><author><style face="normal" font="default" size="100%">Aher, Manisha</style></author><author><style face="normal" font="default" size="100%">Fernandes, Moneesha</style></author><author><style face="normal" font="default" size="100%">Kumar, Vaijayanti A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Favorable 2 '-substitution in the loop region of a thrombin-binding DNA aptamer</style></title><secondary-title><style face="normal" font="default" size="100%">Bioorganic &amp; Medicinal Chemistry Letters</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%">JUN</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">28</style></volume><pages><style face="normal" font="default" size="100%">1765-1768</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Simple 2'-OMe-chemical modification in the loop region of the 15mer G-rich DNA sequence GGTTGGTGTGGTTGG is reported. The G-quadruplex structure of this thrombin-binding aptamer (TBA), is stabilized by single modifications (T -&gt; 2'-OMe-U), depending on the position of the modification. The structural stability also renders significantly increased inhibition of thrombin-induced fibrin polymerization, a process closely associated with blood-clotting. (C) 2018 Elsevier Ltd. All rights reserved.</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%">2.454</style></custom4></record></records></xml>