<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Lev, Avital</style></author><author><style face="normal" font="default" size="100%">Princiotta, Michael F</style></author><author><style face="normal" font="default" size="100%">Zanker, Damian</style></author><author><style face="normal" font="default" size="100%">Takeda, Kazuyo</style></author><author><style face="normal" font="default" size="100%">Gibbs, James S</style></author><author><style face="normal" font="default" size="100%">Kumagai, Chiharu</style></author><author><style face="normal" font="default" size="100%">Waffarn, Elizabeth</style></author><author><style face="normal" font="default" size="100%">Dolan, Brian P</style></author><author><style face="normal" font="default" size="100%">Burgevin, Anne</style></author><author><style face="normal" font="default" size="100%">Van Endert, Peter</style></author><author><style face="normal" font="default" size="100%">Chen, Weisan</style></author><author><style face="normal" font="default" size="100%">Bennink, Jack R</style></author><author><style face="normal" font="default" size="100%">Yewdell, Jonathan W</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Compartmentalized MHC class I antigen processing enhances immunosurveillance by circumventing the law of mass action.</style></title><secondary-title><style face="normal" font="default" size="100%">Proceedings of the National Academy of Sciences of the United States of America</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Proc. Natl. Acad. Sci. U.S.A.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Antigen Presentation</style></keyword><keyword><style  face="normal" font="default" size="100%">Binding, Competitive</style></keyword><keyword><style  face="normal" font="default" size="100%">CD8-Positive T-Lymphocytes</style></keyword><keyword><style  face="normal" font="default" size="100%">Cytosol</style></keyword><keyword><style  face="normal" font="default" size="100%">Flow Cytometry</style></keyword><keyword><style  face="normal" font="default" size="100%">Genes, MHC Class I</style></keyword><keyword><style  face="normal" font="default" size="100%">Histocompatibility Antigens Class I</style></keyword><keyword><style  face="normal" font="default" size="100%">Kinetics</style></keyword><keyword><style  face="normal" font="default" size="100%">Ligands</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice</style></keyword><keyword><style  face="normal" font="default" size="100%">Models, Biological</style></keyword><keyword><style  face="normal" font="default" size="100%">Monitoring, Immunologic</style></keyword><keyword><style  face="normal" font="default" size="100%">Peptides</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Binding</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2010</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2010 Apr 13</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">107</style></volume><pages><style face="normal" font="default" size="100%">6964-9</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">MHC class I molecules function to display peptides generated from cellular and pathogen gene products for immune surveillance by CD8(+) T cells. Cells typically express approximately 100,000 class I molecules, or approximately 1 per 30,000 cellular proteins. Given &quot;one protein, one peptide&quot; representation, immunosurveillance would be heavily biased toward the most abundant cell proteins. Cells use several mechanisms to prevent this, including the predominant use of defective ribosomal products (DRiPs) to generate peptides from nascent proteins and, as we show here, compartmentalization of DRiP peptide generation to prevent competition from abundant cytosolic peptides. This provides an explanation for the exquisite ability of T cells to recognize peptides generated from otherwise undetected gene products.</style></abstract><issue><style face="normal" font="default" size="100%">15</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/20351281?dopt=Abstract</style></custom1></record></records></xml>