<?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%">Lacruz, R. S.</style></author><author><style face="normal" font="default" size="100%">Lakshminarayanan, R.</style></author><author><style face="normal" font="default" size="100%">Bromley, K. M.</style></author><author><style face="normal" font="default" size="100%">Hacia, J. G.</style></author><author><style face="normal" font="default" size="100%">Bromage, T. G.</style></author><author><style face="normal" font="default" size="100%">Snead, M. L.</style></author><author><style face="normal" font="default" size="100%">Moradian-Oldak, J.</style></author><author><style face="normal" font="default" size="100%">Paine, M. L.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Structural analysis of a repetitive protein sequence motif in strepsirrhine primate amelogenin</style></title><secondary-title><style face="normal" font="default" size="100%">PLoS One</style></secondary-title><alt-title><style face="normal" font="default" size="100%">PloS one</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Amelogenin/*chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Amino Acid Motifs</style></keyword><keyword><style  face="normal" font="default" size="100%">Amino Acid Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Circular Dichroism</style></keyword><keyword><style  face="normal" font="default" size="100%">Cloning</style></keyword><keyword><style  face="normal" font="default" size="100%">Exons/genetics</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydrogen-Ion Concentration</style></keyword><keyword><style  face="normal" font="default" size="100%">Kinetics</style></keyword><keyword><style  face="normal" font="default" size="100%">Light</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">Pr</style></keyword><keyword><style  face="normal" font="default" size="100%">Primates/*metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Refolding</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2011</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/21437261</style></url></web-urls></urls><number><style face="normal" font="default" size="100%">3</style></number><edition><style face="normal" font="default" size="100%">2011/03/26</style></edition><volume><style face="normal" font="default" size="100%">6</style></volume><pages><style face="normal" font="default" size="100%">e18028</style></pages><isbn><style face="normal" font="default" size="100%">1932-6203 (Electronic)19</style></isbn><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Strepsirrhines are members of a primate suborder that has a distinctive set of features associated with the development of the dentition. Amelogenin (AMEL), the better known of the enamel matrix proteins, forms 90% of the secreted organic matrix during amelogenesis. Although AMEL has been sequenced in numerous mammalian lineages, the only reported strepsirrhine AMEL sequences are those of the ring-tailed lemur and galago, which contain a set of additional proline-rich tandem repeats absent in all other primates species analyzed to date, but present in some non-primate mammals. Here, we first determined that these repeats are present in AMEL from three additional lemur species and thus are likely to be widespread throughout this group. To evaluate the functional relevance of these repeats in strepsirrhines, we engineered a mutated murine amelogenin sequence containing a similar proline-rich sequence to that of Lemur catta. In the monomeric form, the MQP insertions had no influence on the secondary structure or refolding properties, whereas in the assembled form, the insertions increased the hydrodynamic radii. We speculate that increased AMEL nanosphere size may influence enamel formation in strepsirrhine primates.&lt;/p&gt;</style></abstract><work-type><style face="normal" font="default" size="100%">Research Support, N.I.H., Extramural</style></work-type><notes><style face="normal" font="default" size="100%">&lt;p&gt;&lt;span role=&quot;menubar&quot;&gt;PLoS One.&lt;/span&gt;&amp;nbsp;2011 Mar 18;6(3):e18028. doi: 10.1371/journal.pone.0018028.&lt;/p&gt;</style></notes><custom2><style face="normal" font="default" size="100%">3060920</style></custom2><auth-address><style face="normal" font="default" size="100%">Center for Craniofacial Molecular Biology, Herman Ostrow School of Dentistry, University of Southern California, Los Angeles, California, United States of America. rodrigo@usc.edu</style></auth-address></record></records></xml>