<?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%">Lo, Wing-Sze</style></author><author><style face="normal" font="default" size="100%">Gardiner, Elisabeth</style></author><author><style face="normal" font="default" size="100%">Xu, Zhiwen</style></author><author><style face="normal" font="default" size="100%">Lau, Ching-Fun</style></author><author><style face="normal" font="default" size="100%">Wang, Feng</style></author><author><style face="normal" font="default" size="100%">Zhou, Jie J</style></author><author><style face="normal" font="default" size="100%">Mendlein, John D</style></author><author><style face="normal" font="default" size="100%">Nangle, Leslie A</style></author><author><style face="normal" font="default" size="100%">Chiang, Kyle P</style></author><author><style face="normal" font="default" size="100%">Yang, Xiang-Lei</style></author><author><style face="normal" font="default" size="100%">Au, Kin-Fai</style></author><author><style face="normal" font="default" size="100%">Wong, Wing Hung</style></author><author><style face="normal" font="default" size="100%">Guo, Min</style></author><author><style face="normal" font="default" size="100%">Zhang, Mingjie</style></author><author><style face="normal" font="default" size="100%">Schimmel, Paul</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Human tRNA synthetase catalytic nulls with diverse functions.</style></title><secondary-title><style face="normal" font="default" size="100%">Science</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Science</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Alternative Splicing</style></keyword><keyword><style  face="normal" font="default" size="100%">Amino Acyl-tRNA Synthetases</style></keyword><keyword><style  face="normal" font="default" size="100%">Catalysis</style></keyword><keyword><style  face="normal" font="default" size="100%">Catalytic Domain</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Isoenzymes</style></keyword><keyword><style  face="normal" font="default" size="100%">Organ Specificity</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Isoforms</style></keyword><keyword><style  face="normal" font="default" size="100%">Recombinant Proteins</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2014</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2014 Jul 18</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/25035493</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">345</style></volume><pages><style face="normal" font="default" size="100%">328-32</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Genetic efficiency in higher organisms depends on mechanisms to create multiple functions from single genes. To investigate this question for an enzyme family, we chose aminoacyl tRNA synthetases (AARSs). They are exceptional in their progressive and accretive proliferation of noncatalytic domains as the Tree of Life is ascended. Here we report discovery of a large number of natural catalytic nulls (CNs) for each human AARS. Splicing events retain noncatalytic domains while ablating the catalytic domain to create CNs with diverse functions. Each synthetase is converted into several new signaling proteins with biological activities &quot;orthogonal&quot; to that of the catalytic parent. We suggest that splice variants with nonenzymatic functions may be more general, as evidenced by recent findings of other catalytically inactive splice-variant enzymes.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">6194</style></issue><notes><style face="normal" font="default" size="100%">http://www.sciencemag.org/content/345/6194/328.full?sid=dc3468b3-3acc-4a40-9d25-481cc130f5d4</style></notes><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/25035493?dopt=Abstract</style></custom1></record></records></xml>