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	<title>Center for Biomedical Mass Spectrometry</title>
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		<title>New Glycomics Review!</title>
		<link>http://www.bumc.bu.edu/bucbm/2008/09/25/new-glycomics-review/</link>
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		<pubDate>Thu, 25 Sep 2008 17:59:40 +0000</pubDate>
		<dc:creator>jzaia</dc:creator>
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		<description><![CDATA[Mass spectrometry and the emerging field of glycomics.
Chem Biol. 2008 Sep 22;15(9):881-92.
Zaia, J
Deptartment of Biochemistry, Boston University, 670 Albany Street, Room 509, Boston, MA 02118, USA.
The biological significance of protein and lipid glycosylation is well established. For example, cells respond to environmental stimuli by altering glycan structures on their surfaces, and cancer cells evade normal [...]]]></description>
			<content:encoded><![CDATA[<p><span style="font-size: medium"><strong>Mass spectrometry and the emerging field of glycomics.<br />
</strong><span title="Chemistry &amp; biology.">Chem Biol.</span> 2008 Sep 22;15(9):881-92.<br />
</span><strong>Zaia, J</strong></p>
<p>Deptartment of Biochemistry, Boston University, 670 Albany Street, Room 509, Boston, MA 02118, USA.</p>
<p>The biological significance of protein and lipid glycosylation is well established. For example, cells respond to environmental stimuli by altering glycan structures on their surfaces, and cancer cells evade normal growth regulation in part by remodeling their surface glycans. In general, glycan chemical properties differ significantly from those of proteins, lipids, nucleic acids, and small molecule metabolites. Thus, advances in glycomics, a comprehensive study to identify all glycans in an organism, rely on the development of specialized analytical methods. Mass spectrometry (MS) is emerging as an enabling technology in the field of glycomics. This review summarizes recent developments in mass spectrometric analysis methods for protein-based glycomics and glycoproteomics workflows.</p>
<p><a href="http://www.ncbi.nlm.nih.gov/pubmed/18804025?dopt=Citation">Link to Citation</a></p>
<p><a href="http://www.bumc.bu.edu/bucbm/files/2008/09/zaia-chem-bio-08.pdf">Free Pubmed Central Version</a></p>
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		<title>Prof. Costello wins 2008 HUPO Discovery Award!</title>
		<link>http://www.bumc.bu.edu/bucbm/2008/09/12/prof-costello-wins-2008-hupo-discovery-award/</link>
		<comments>http://www.bumc.bu.edu/bucbm/2008/09/12/prof-costello-wins-2008-hupo-discovery-award/#comments</comments>
		<pubDate>Fri, 12 Sep 2008 17:17:23 +0000</pubDate>
		<dc:creator>jzaia</dc:creator>
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		<description><![CDATA[Prof. Catherine Costello, Director of the Center of Biomedical Mass Spectrometry and Professor of Biochemistry, was given the 2008 Proteomics Discovery Award at the Human Proteome Organization international conference in Amsterdam, The Netherlands, in August.
The award recognizes Prof. Costello&#8217;s contributions to proteomics.  Here are links to some of Prof. Costello&#8217;s proteomics publications:

Zhao, C.; Xie, [...]]]></description>
			<content:encoded><![CDATA[<p>Prof. Catherine Costello, Director of the Center of Biomedical Mass Spectrometry and Professor of Biochemistry, was given the 2008 Proteomics Discovery Award at the Human Proteome Organization international conference in Amsterdam, The Netherlands, in August.</p>
<p>The award recognizes Prof. Costello&#8217;s contributions to proteomics.  Here are links to some of Prof. Costello&#8217;s proteomics publications:</p>
<ul>
<LI>Zhao, C.; Xie, B.; Chan, S. Y.; Costello, C. E.; O&#8217;Connor, P. B. Collisionally activated dissociation and electron capture dissociation provide complementary structural information for branched permethylated oligosaccharides. <em>J Am Soc Mass Spectrom</em> <strong>2008</strong>, <em>19</em>, 138-50.<A HREF="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;db=PubMed&amp;dopt=Citation&amp;list_uids=18063385" target="blank"> Link</A></LI><br />
<LI>Lavatelli, F.; Perlman, D. H.; Spencer, B.; Prokaeva, T.; McComb, M. E.; Theberge, R.; Connors, L. H.; Bellotti, V.; Seldin, D. C.; Merlini, G.; Skinner, M.; Costello, C. E. Amyloidogenic and associated proteins in systemic amyloidosis proteome of adipose tissue. <em>Mol Cell Proteomics</em> <strong>2008</strong>, <em>7</em>, 1570-83.<A HREF="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;db=PubMed&amp;dopt=Citation&amp;list_uids=18474516" target="blank"> Link</A></LI><br />
<LI>Sethuraman, M.; Clavreul, N.; Huang, H.; McComb, M. E.; Costello, C. E.; Cohen, R. A. Quantification of oxidative posttranslational modifications of cysteine thiols of p21ras associated with redox modulation of activity using isotope-coded affinity tags and mass spectrometry. <em>Free radical biology &amp; medicine</em> <strong>2007</strong>, <em>42</em>, 823-9.<A HREF="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;db=PubMed&amp;dopt=Citation&amp;list_uids=17320764" target="blank"> Link</A></LI><br />
<LI>Saba, J. A.; McComb, M. E.; Potts, D. L.; Costello, C. E.; Amar, S. Proteomic Mapping of Stimulus-Specific Signaling Pathways Involved in THP-1 Cells Exposed to …. <em>J. Proteome Res</em> <strong>2007</strong>, <em>6</em>, 2195-2204.<A HREF="http://pubs.acs.org/cgi-bin/abstract.cgi/jprobs/2007/6/i06/abs/pr0700347.html" target="blank"> Link</A></LI><br />
<LI>Perlman, D. H.; Huang, H.; Dauly, C.; Costello, C. E.; McComb, M. E. Coupling of protein HPLC to MALDI-TOF MS using an on-target device for fraction collection, concentration, digestion, desalting, and matrix/analyte cocrystallization. <em>Anal. Chem.</em> <strong>2007</strong>, <em>79</em>, 2058-66.<A HREF="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;db=PubMed&amp;dopt=Citation&amp;list_uids=17256876" target="blank"> Link</A></LI></p>
</ul>
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