<HashMap><database>biostudies-literature</database><scores/><additional><submitter>de Haan N</submitter><funding>Danmarks Grundforskningsfond</funding><funding>European Research Council</funding><funding>Horizon 2020 Framework Programme</funding><funding>Friis Foundation</funding><funding>A.P. M?ller og Hustru Chastine Mc-Kinney M?llers Fond til almene Formaal</funding><funding>Lundbeck Foundation</funding><funding>Michelsen Foundation</funding><pagination>4343-4351</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8928149</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>94(10)</volume><pubmed_abstract>&lt;i>O&lt;/i>-Glycosylation is an omnipresent modification of the human proteome affecting many cellular functions, including protein cleavage, protein folding, and cellular signaling, interactions, and trafficking. The functions are governed by differentially regulated &lt;i>O&lt;/i>-glycan types and terminal structures. It is therefore essential to develop analytical methods that facilitate the annotation of &lt;i>O&lt;/i>-glycans in biological material. While various successful strategies for the in-depth profiling of released &lt;i>O&lt;/i>-glycans have been reported, these methods are often limitedly accessible to the nonspecialist or challenged by the high abundance of &lt;i>O&lt;/i>-glycan structural isomers. Here, we developed a high-throughput sample preparation approach for the nonreductive release and chara</pubmed_abstract><journal>Analytical chemistry</journal><pubmed_title>In-Depth Profiling of &lt;i>O&lt;/i>-Glycan Isomers in Human Cells Using C18 Nanoliquid Chromatography-Mass Spectrometry and Glycogenomics.</pubmed_title><pmcid>PMC8928149</pmcid><funding_grant_id>313-2019-869</funding_grant_id><funding_grant_id>R313-2019-869</funding_grant_id><funding_grant_id>772735</funding_grant_id><funding_grant_id>DNRF107</funding_grant_id><pubmed_authors>Larsen ISB</pubmed_authors><pubmed_authors>Wandall HH</pubmed_authors><pubmed_authors>Koed Moller Aasted M</pubmed_authors><pubmed_authors>Dabelsteen S</pubmed_authors><pubmed_authors>de Haan N</pubmed_authors><pubmed_authors>Vakhrushev SY</pubmed_authors><pubmed_authors>Marinova IN</pubmed_authors><pubmed_authors>Narimatsu Y</pubmed_authors></additional><is_claimable>false</is_claimable><name>In-Depth Profiling of &lt;i>O&lt;/i>-Glycan Isomers in Human Cells Using C18 Nanoliquid Chromatography-Mass Spectrometry and Glycogenomics.</name><description>&lt;i>O&lt;/i>-Glycosylation is an omnipresent modification of the human proteome affecting many cellular functions, including protein cleavage, protein folding, and cellular signaling, interactions, and trafficking. The functions are governed by differentially regulated &lt;i>O&lt;/i>-glycan types and terminal structures. It is therefore essential to develop analytical methods that facilitate the annotation of &lt;i>O&lt;/i>-glycans in biological material. While various successful strategies for the in-depth profiling of released &lt;i>O&lt;/i>-glycans have been reported, these methods are often limitedly accessible to the nonspecialist or challenged by the high abundance of &lt;i>O&lt;/i>-glycan structural isomers. Here, we developed a high-throughput sample preparation approach for the nonreductive release and chara</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Mar</publication><modification>2025-04-26T03:57:15.123Z</modification><creation>2025-04-06T10:58:26.536Z</creation></dates><accession>S-EPMC8928149</accession><cross_references><pubmed>35245040</pubmed><doi>10.1021/acs.analchem.1c05068</doi></cross_references></HashMap>