<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Bartels MF</submitter><funding>Bundesministerium für Bildung und Forschung</funding><funding>Ministerium für Innovation, Wissenschaft und Forschung des Landes Nordrhein-Westfalen</funding><funding>Deutsche Forschungsgemeinschaft</funding><funding>Wellcome Trust</funding><funding>Senatsverwaltung für Wirtschaft, Technologie und Forschung des Landes Berlin</funding><pagination>e0166119</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC5094735</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>11(11)</volume><pubmed_abstract>Protein O-mannosylation is a post-translational modification essential for correct development of mammals. In humans, deficient O-mannosylation results in severe congenital muscular dystrophies often associated with impaired brain and eye development. Although various O-mannosylated proteins have been identified in the recent years, the distribution of O-mannosyl glycans in the mammalian brain and target proteins are still not well defined. In the present study, rabbit monoclonal antibodies directed against the O-mannosylated peptide YAT(α1-Man)AV were generated. Detailed characterization of clone RKU-1-3-5 revealed that this monoclonal antibody recognizes O-linked mannose also in different peptide and protein contexts. Using this tool, we observed that mono-O-mannosyl glycans occur ubiqui</pubmed_abstract><journal>PloS one</journal><pubmed_title>Protein O-Mannosylation in the Murine Brain: Occurrence of Mono-O-Mannosyl Glycans and Identification of New Substrates.</pubmed_title><pmcid>PMC5094735</pmcid><funding_grant_id>Sonderforschungsbereich 1036, project 11</funding_grant_id><funding_grant_id>WT099197MA</funding_grant_id><funding_grant_id>WT093378MA, WT099197MA and 108430/Z/15/Z</funding_grant_id><funding_grant_id>108430/Z/15/Z</funding_grant_id><funding_grant_id>WT093378MA</funding_grant_id><pubmed_authors>Liu Y</pubmed_authors><pubmed_authors>Feizi T</pubmed_authors><pubmed_authors>Strahl S</pubmed_authors><pubmed_authors>Winterhalter PR</pubmed_authors><pubmed_authors>Mohrlen F</pubmed_authors><pubmed_authors>Hu H</pubmed_authors><pubmed_authors>Bartels MF</pubmed_authors><pubmed_authors>Westerlind U</pubmed_authors><pubmed_authors>Ruppert T</pubmed_authors><pubmed_authors>Lommel M</pubmed_authors><pubmed_authors>Yu J</pubmed_authors></additional><is_claimable>false</is_claimable><name>Protein O-Mannosylation in the Murine Brain: Occurrence of Mono-O-Mannosyl Glycans and Identification of New Substrates.</name><description>Protein O-mannosylation is a post-translational modification essential for correct development of mammals. In humans, deficient O-mannosylation results in severe congenital muscular dystrophies often associated with impaired brain and eye development. Although various O-mannosylated proteins have been identified in the recent years, the distribution of O-mannosyl glycans in the mammalian brain and target proteins are still not well defined. In the present study, rabbit monoclonal antibodies directed against the O-mannosylated peptide YAT(α1-Man)AV were generated. Detailed characterization of clone RKU-1-3-5 revealed that this monoclonal antibody recognizes O-linked mannose also in different peptide and protein contexts. Using this tool, we observed that mono-O-mannosyl glycans occur ubiqui</description><dates><release>2016-01-01T00:00:00Z</release><publication>2016</publication><modification>2026-05-02T02:25:53.91Z</modification><creation>2019-03-26T22:51:10Z</creation></dates><accession>S-EPMC5094735</accession><cross_references><pubmed>27812179</pubmed><doi>10.1371/journal.pone.0166119</doi></cross_references></HashMap>