<?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%">Altheide, T. K.</style></author><author><style face="normal" font="default" size="100%">Hayakawa, T.</style></author><author><style face="normal" font="default" size="100%">Mikkelsen, T. S.</style></author><author><style face="normal" font="default" size="100%">Diaz, S.</style></author><author><style face="normal" font="default" size="100%">Nissi M Varki</style></author><author><style face="normal" font="default" size="100%">Ajit Varki</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">System-wide genomic and biochemical comparisons of sialic acid biology among primates and rodents: Evidence for two modes of rapid evolution</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%">*Genome</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%">Antigens</style></keyword><keyword><style  face="normal" font="default" size="100%">Biological Evolution</style></keyword><keyword><style  face="normal" font="default" size="100%">CD/biosynthesis</style></keyword><keyword><style  face="normal" font="default" size="100%">Differentiation</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">Myelomonocytic/biosynthesis</style></keyword><keyword><style  face="normal" font="default" size="100%">N-Acetylneuraminic Acid/*chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Oligosaccharides/chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Pan trog</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2006</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Sep 1</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/16769723</style></url></web-urls></urls><number><style face="normal" font="default" size="100%">35</style></number><edition><style face="normal" font="default" size="100%">2006/06/14</style></edition><volume><style face="normal" font="default" size="100%">281</style></volume><pages><style face="normal" font="default" size="100%">25689-702</style></pages><isbn><style face="normal" font="default" size="100%">0021-9258 (Print)0021-92</style></isbn><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Numerous vertebrate genes are involved in the biology of the oligosaccharide chains attached to glycoconjugates. These genes fall into diverse groups within the conventional Gene Ontology classification. However, they should be evaluated together from functional and evolutionary perspectives in a &amp;quot;biochemical systems&amp;quot; approach, considering each monosaccharide unit&#039;s biosynthesis, activation, transport, modification, transfer, recycling, degradation, and recognition. Sialic acid (Sia) residues are monosaccharides at the outer end of glycans on the cell-surface and secreted molecules of vertebrates, mediating recognition by intrinsic or extrinsic (pathogen) receptors. The availability of multiple genome sequences allows a system-wide comparison among primates and rodents of all genes directly involved in Sia biology. Taking this approach, we present further evidence for accelerated evolution in Sia-binding domains of CD33-related Sia-recognizing Ig-like lectins. Other gene classes are more conserved, including those encoding the sialyltransferases that attach Sia residues to glycans. Despite this conservation, tissue sialylation patterns are shown to differ widely among these species, presumably because of rapid evolution of sialyltransferase expression patterns. Analyses of N- and O-glycans of erythrocyte and plasma glycopeptides from these and other mammalian taxa confirmed this phenomenon. Sia modifications on these glycopeptides also appear to be undergoing rapid evolution. This rapid evolution of the sialome presumably results from the ongoing need of organisms to evade microbial pathogens that use Sia residues as receptors. The rapid evolution of Sia-binding domains of the inhibitory CD33-related Sia-recognizing Ig-like lectins is likely to be a secondary consequence, as these inhibitory receptors presumably need to keep up with recognition of the rapidly evolving &amp;quot;self&amp;quot;-sialome.&lt;/p&gt;</style></abstract><work-type><style face="normal" font="default" size="100%">Research Support, N.I.H., ExtramuralResearch Support, Non-U.S. Gov&#039;t</style></work-type><accession-num><style face="normal" font="default" size="100%">16769723 PMID</style></accession-num><notes><style face="normal" font="default" size="100%">&lt;p&gt;J Biol Chem. 2006 Sep 1;281(35):25689-702. Epub 2006 Jun 12&lt;/p&gt;</style></notes><auth-address><style face="normal" font="default" size="100%">Glycobiology Research and Training Center, Department of Cellular and Molecular Medicine, University of California San Diego, La Jolla, California 92093-0687, USA.</style></auth-address></record></records></xml>