<?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%">Changeux, J. P.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">The concept of allosteric interaction and its consequences for the chemistry of the brain</style></title><secondary-title><style face="normal" font="default" size="100%">J Biol Chem</style></secondary-title><alt-title><style face="normal" font="default" size="100%">The Journal of biological chemistry</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">20th Century</style></keyword><keyword><style  face="normal" font="default" size="100%">21st Century</style></keyword><keyword><style  face="normal" font="default" size="100%">Allosteric Regulation/physiology</style></keyword><keyword><style  face="normal" font="default" size="100%">Biological</style></keyword><keyword><style  face="normal" font="default" size="100%">Brain Chemistry/ physiology</style></keyword><keyword><style  face="normal" font="default" size="100%">History</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Models</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Dynamics Simulation</style></keyword><keyword><style  face="normal" font="default" size="100%">Nerve Tissue Proteins/ metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Portraits as Topic</style></keyword><keyword><style  face="normal" font="default" size="100%">Prokaryotic Cells/physiology</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2013</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Sep 20</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/23878193</style></url></web-urls></urls><number><style face="normal" font="default" size="100%">38</style></number><edition><style face="normal" font="default" size="100%">2013/07/24</style></edition><volume><style face="normal" font="default" size="100%">288</style></volume><pages><style face="normal" font="default" size="100%">26969-86</style></pages><isbn><style face="normal" font="default" size="100%">1083-351X (Electronic)00</style></isbn><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Throughout this Reflections article, I have tried to follow up on the genesis in the 1960s and subsequent evolution of the concept of allosteric interaction and to examine its consequences within the past decades, essentially in the field of the neuroscience. The main conclusion is that allosteric mechanisms built on similar structural principles operate in bacterial regulatory enzymes, gene repressors (and the related nuclear receptors), rhodopsin, G-protein-coupled receptors, neurotransmitter receptors, ion channels, and so on from prokaryotes up to the human brain yet with important features of their own. Thus, future research on these basic cybernetic sensors is expected to develop in two major directions: at the elementary level, toward the atomic structure and molecular dynamics of the conformational changes involved in signal recognition and transduction, but also at a higher level of organization, the contribution of allosteric mechanisms to the modulation of brain functions.&lt;/p&gt;
</style></abstract><accession-num><style face="normal" font="default" size="100%">23878193</style></accession-num><notes><style face="normal" font="default" size="100%">&lt;p&gt;J Biol Chem. 2013 Sep 20;288(38):26969-86. doi: 10.1074/jbc.X113.503375. Epub 2013 Jul PMCID: PMC3779700 [Available on 2014/9/20].&lt;/p&gt;
</style></notes><custom2><style face="normal" font="default" size="100%">3779700</style></custom2><auth-address><style face="normal" font="default" size="100%">From the College de France, 75005 Paris and the Institut Pasteur, 75724 Paris Cedex 15, France.</style></auth-address><remote-database-provider><style face="normal" font="default" size="100%">NLM</style></remote-database-provider></record></records></xml>