<?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%">Phan, Isabelle Q. H.</style></author><author><style face="normal" font="default" size="100%">Davies, Douglas R.</style></author><author><style face="normal" font="default" size="100%">Moretti, Nilmar Silvio</style></author><author><style face="normal" font="default" size="100%">Shanmugam, Dhanasekaran</style></author><author><style face="normal" font="default" size="100%">Cestari, Igor</style></author><author><style face="normal" font="default" size="100%">Anupama, Atashi</style></author><author><style face="normal" font="default" size="100%">Fairman, James W.</style></author><author><style face="normal" font="default" size="100%">Edwards, Thomas E.</style></author><author><style face="normal" font="default" size="100%">Stuart, Kenneth</style></author><author><style face="normal" font="default" size="100%">Schenkman, Sergio</style></author><author><style face="normal" font="default" size="100%">Myler, Peter J.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Iron superoxide dismutases in eukaryotic pathogens: new insights from apicomplexa and trypanosoma structures</style></title><secondary-title><style face="normal" font="default" size="100%">Acta Crystallographica Section F-Structural Biology Communications</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Apicomplexa</style></keyword><keyword><style  face="normal" font="default" size="100%">iron superoxide dismutase</style></keyword><keyword><style  face="normal" font="default" size="100%">Trypanosoma</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%">MAY</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">5, 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%">71</style></volume><pages><style face="normal" font="default" size="100%">615-621</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Prior studies have highlighted the potential of superoxide dismutases as drug targets in eukaryotic pathogens. This report presents the structures of three iron-dependent superoxide dismutases (FeSODs) from Trypanosoma cruzi, Leishmania major and Babesia bovis. Comparison with existing structures from Plasmodium and other trypanosome isoforms shows a very conserved overall fold with subtle differences. In particular, structural data suggest that B. bovis FeSOD may display similar resistance to peroxynitrite-mediated inactivation via an intramolecular electron-transfer pathway as previously described in T. cruzi FeSOD isoform B, thus providing valuable information for structure-based drug design. Furthermore, lysine-acetylation results in T. cruzi indicate that acetylation occurs at a position close to that responsible for the regulation of acetylation-mediated activity in the human enzyme.&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%">0.647</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%">Jachak, Gorakhnath R.</style></author><author><style face="normal" font="default" size="100%">Elizebath, Drishya</style></author><author><style face="normal" font="default" size="100%">Shukla, Anurag</style></author><author><style face="normal" font="default" size="100%">Shanmugam, Dhanasekaran</style></author><author><style face="normal" font="default" size="100%">Reddy, D. Srinivasa</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Synthesis and biological evaluation of hoshionolactam-based compounds</style></title><secondary-title><style face="normal" font="default" size="100%">European Journal of Organic Chemistry</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Hoshinolactam</style></keyword><keyword><style  face="normal" font="default" size="100%">Ozonolysis</style></keyword><keyword><style  face="normal" font="default" size="100%">Parasitic diseases</style></keyword><keyword><style  face="normal" font="default" size="100%">Trypanosoma</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%">APR </style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">2021</style></volume><pages><style face="normal" font="default" size="100%">2212-2218</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">In search of novel antitrypanosomal agents based on hoshinolactam (IC50=3.9 nM), we disclose the synthesis and biological evaluations of 14 different analogues of the natural product using combinations of different acids and lactams. Antitrypanosomal activity assays revealed that the synthesized analogues were less potent than the parent natural product.</style></abstract><issue><style face="normal" font="default" size="100%">15</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%">3.021</style></custom4></record></records></xml>