<?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%">Tokhunts, Robert</style></author><author><style face="normal" font="default" size="100%">Singh, Samer</style></author><author><style face="normal" font="default" size="100%">Chu, Tehyen</style></author><author><style face="normal" font="default" size="100%">D'Angelo, Gisela</style></author><author><style face="normal" font="default" size="100%">Baubet, Valerie</style></author><author><style face="normal" font="default" size="100%">Goetz, John A</style></author><author><style face="normal" font="default" size="100%">Huang, Zhen</style></author><author><style face="normal" font="default" size="100%">Yuan, Ziqiang</style></author><author><style face="normal" font="default" size="100%">Ascano, Manuel</style></author><author><style face="normal" font="default" size="100%">Zavros, Yana</style></author><author><style face="normal" font="default" size="100%">Thérond, Pascal P</style></author><author><style face="normal" font="default" size="100%">Kunes, Sam</style></author><author><style face="normal" font="default" size="100%">Dahmane, Nadia</style></author><author><style face="normal" font="default" size="100%">Robbins, David J</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">The full-length unprocessed hedgehog protein is an active signaling molecule.</style></title><secondary-title><style face="normal" font="default" size="100%">The Journal of biological chemistry</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Biol. Chem.</style></alt-title></titles><dates><year><style  face="normal" font="default" size="100%">2010</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2010 Jan 22</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">285</style></volume><pages><style face="normal" font="default" size="100%">2562-8</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 hedgehog (HH) family of ligands plays an important instructional role in metazoan development. HH proteins are initially produced as approximately 45-kDa full-length proteins, which undergo an intramolecular cleavage to generate an amino-terminal product that subsequently becomes cholesterol-modified (HH-Np). It is well accepted that this cholesterol-modified amino-terminal cleavage product is responsible for all HH-dependent signaling events. Contrary to this model we show here that full-length forms of HH proteins are able to traffic to the plasma membrane and participate directly in cell-cell signaling, both in vitro and in vivo. We were also able to rescue a Drosophila eye-specific hh loss of function phenotype by expressing a full-length form of hh that cannot be processed into HH-Np. These results suggest that in some physiological contexts full-length HH proteins may participate directly in HH signaling and that this novel activity of full-length HH may be evolutionarily conserved.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">4</style></issue><notes><style face="normal" font="default" size="100%">&lt;p&gt;n/a&lt;/p&gt;
</style></notes><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/19920144?dopt=Abstract</style></custom1></record></records></xml>