<?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></records></xml>