<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Leymarie N</submitter><funding>NIDCR NIH HHS</funding><funding>NCRR NIH HHS</funding><funding>NIAID NIH HHS</funding><funding>NHLBI NIH HHS</funding><funding>NIGMS NIH HHS</funding><funding>PHS HHS</funding><funding>NIH HHS</funding><pagination>2935-51</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3790302</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>12(10)</volume><pubmed_abstract>One of the principal goals of glycoprotein research is to correlate glycan structure and function. Such correlation is necessary in order for one to understand the mechanisms whereby glycoprotein structure elaborates the functions of myriad proteins. The accurate comparison of glycoforms and quantification of glycosites are essential steps in this direction. Mass spectrometry has emerged as a powerful analytical technique in the field of glycoprotein characterization. Its sensitivity, high dynamic range, and mass accuracy provide both quantitative and sequence/structural information. As part of the 2012 ABRF Glycoprotein Research Group study, we explored the use of mass spectrometry and ancillary methodologies to characterize the glycoforms of two sources of human prostate specific antigen</pubmed_abstract><journal>Molecular &amp; cellular proteomics : MCP</journal><pubmed_title>Interlaboratory study on differential analysis of protein glycosylation by mass spectrometry: the ABRF glycoprotein research multi-institutional study 2012.</pubmed_title><pmcid>PMC3790302</pmcid><funding_grant_id>S10 RR 020946</funding_grant_id><funding_grant_id>S10 OD010731</funding_grant_id><funding_grant_id>R01 AI094797</funding_grant_id><funding_grant_id>R01 GM103547</funding_grant_id><funding_grant_id>S10 RR 015942</funding_grant_id><funding_grant_id>S10 RR 025082</funding_grant_id><funding_grant_id>S10 RR020946</funding_grant_id><funding_grant_id>R01 098050</funding_grant_id><funding_grant_id>P41 P41GM104603</funding_grant_id><funding_grant_id>N01 HV 00239</funding_grant_id><funding_grant_id>S10 RR025082</funding_grant_id><funding_grant_id>R01 DE020925</funding_grant_id><funding_grant_id>P41 GM104603</funding_grant_id><pubmed_authors>Horn DM</pubmed_authors><pubmed_authors>Watson M</pubmed_authors><pubmed_authors>Jonscher K</pubmed_authors><pubmed_authors>Wuhrer M</pubmed_authors><pubmed_authors>Brown KJ</pubmed_authors><pubmed_authors>Zaia J</pubmed_authors><pubmed_authors>Aguilan J</pubmed_authors><pubmed_authors>Resemann A</pubmed_authors><pubmed_authors>Whittal R</pubmed_authors><pubmed_authors>Wada Y</pubmed_authors><pubmed_authors>Goldman R</pubmed_authors><pubmed_authors>Ball LE</pubmed_authors><pubmed_authors>Nyalwidhe JO</pubmed_authors><pubmed_authors>Schweiger-Hufnagel U</pubmed_authors><pubmed_authors>Meyer B</pubmed_authors><pubmed_authors>McComb M</pubmed_authors><pubmed_authors>Moginger U</pubmed_authors><pubmed_authors>Schulz JM</pubmed_authors><pubmed_authors>Windwarder M</pubmed_authors><pubmed_authors>Basumallick L</pubmed_authors><pubmed_authors>Rohrer JS</pubmed_authors><pubmed_authors>Behnken H</pubmed_authors><pubmed_authors>Alley WR</pubmed_authors><pubmed_authors>Cairo CW</pubmed_authors><pubmed_authors>Ly M</pubmed_authors><pubmed_authors>Daneshfar R</pubmed_authors><pubmed_authors>Sanda M</pubmed_authors><pubmed_authors>Cipollo JF</pubmed_authors><pubmed_authors>Pompach P</pubmed_authors><pubmed_authors>Hurum D</pubmed_authors><pubmed_authors>Zhu Y</pubmed_authors><pubmed_authors>Desaire H</pubmed_authors><pubmed_authors>Nilsson J</pubmed_authors><pubmed_authors>Reiz B</pubmed_authors><pubmed_authors>Zou C</pubmed_authors><pubmed_authors>Tang H</pubmed_authors><pubmed_authors>Bazemore-Walker CR</pubmed_authors><pubmed_authors>Halim A</pubmed_authors><pubmed_authors>Kolarich D</pubmed_authors><pubmed_authors>Jabs W</pubmed_authors><pubmed_authors>Marx K</pubmed_authors><pubmed_authors>Valmu L</pubmed_authors><pubmed_authors>Go EP</pubmed_authors><pubmed_authors>Bunz SC</pubmed_authors><pubmed_authors>Thaysen-Andersen M</pubmed_authors><pubmed_authors>An Y</pubmed_authors><pubmed_authors>Neusuβ C</pubmed_authors><pubmed_authors>Drake RR</pubmed_authors><pubmed_authors>Gruber C</pubmed_authors><pubmed_authors>Sihlbom C</pubmed_authors><pubmed_authors>Griffin PJ</pubmed_authors><pubmed_authors>Packer NH</pubmed_authors><pubmed_authors>Viner RI</pubmed_authors><pubmed_authors>Novotny MV</pubmed_authors><pubmed_authors>Leymarie N</pubmed_authors><pubmed_authors>Song E</pubmed_authors><pubmed_authors>Mechref Y</pubmed_authors><pubmed_authors>Hensbergen PJ</pubmed_authors><pubmed_authors>Ruthenbeck A</pubmed_authors><pubmed_authors>Blank MA</pubmed_authors><pubmed_authors>Staples GO</pubmed_authors><pubmed_authors>Hathout Y</pubmed_authors><pubmed_authors>Mann BF</pubmed_authors><pubmed_authors>Larson G</pubmed_authors><pubmed_authors>Orlando R</pubmed_authors><pubmed_authors>Suckau D</pubmed_authors><pubmed_authors>Altmann F</pubmed_authors></additional><is_claimable>false</is_claimable><name>Interlaboratory study on differential analysis of protein glycosylation by mass spectrometry: the ABRF glycoprotein research multi-institutional study 2012.</name><description>One of the principal goals of glycoprotein research is to correlate glycan structure and function. Such correlation is necessary in order for one to understand the mechanisms whereby glycoprotein structure elaborates the functions of myriad proteins. The accurate comparison of glycoforms and quantification of glycosites are essential steps in this direction. Mass spectrometry has emerged as a powerful analytical technique in the field of glycoprotein characterization. Its sensitivity, high dynamic range, and mass accuracy provide both quantitative and sequence/structural information. As part of the 2012 ABRF Glycoprotein Research Group study, we explored the use of mass spectrometry and ancillary methodologies to characterize the glycoforms of two sources of human prostate specific antigen</description><dates><release>2013-01-01T00:00:00Z</release><publication>2013 Oct</publication><modification>2026-05-01T15:13:37.485Z</modification><creation>2026-04-07T16:59:56.18Z</creation></dates><accession>S-EPMC3790302</accession><cross_references><pubmed>23764502</pubmed><doi>10.1074/mcp.m113.030643</doi><doi>10.1074/mcp.M113.030643</doi></cross_references></HashMap>