<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>13</volume><submitter>Takakura D</submitter><pubmed_abstract>Aberrant glycosylation is a prominent feature of cancer, that can be used as targets to improve the existing cancer biomarkers, and help to assess metastasis risks, and therapeutic effects. We developed a targeted O-glycoproteomics method using serum specimens, and evaluated its utility in identifying advanced colorectal cancer (CRC) markers. To this end, we combined consecutive lectin affinity purification using &lt;i>Maclura pomifera&lt;/i> lectin (MPL), jacalin, and &lt;i>Sambucus nigra&lt;/i> lectin, which have affinities for the following O-glycans, that have received attention as cancer-related antigens, Tn (GalNAc-Ser/Thr), Sialyl Tn (Siaα2-6GalNAc-Ser/Thr), T (Galβ1-3GalNAc-Ser/Thr), Sialyl T (Siaα2-3Galβ1-GalNAc-Ser/Thr), and di-Sialyl T (Siaα2-3Galβ1-3[Siaα2-6] GalNAc-Ser/Thr), with a unique</pubmed_abstract><journal>Frontiers in oncology</journal><pagination>1104936</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9948623</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Targeted O-glycoproteomics for the development of diagnostic markers for advanced colorectal cancer.</pubmed_title><pmcid>PMC9948623</pmcid><pubmed_authors>Tokuhisa M</pubmed_authors><pubmed_authors>Ichikawa Y</pubmed_authors><pubmed_authors>Kawasaki N</pubmed_authors><pubmed_authors>Takakura D</pubmed_authors><pubmed_authors>Kobayashi N</pubmed_authors><pubmed_authors>Ohashi S</pubmed_authors></additional><is_claimable>false</is_claimable><name>Targeted O-glycoproteomics for the development of diagnostic markers for advanced colorectal cancer.</name><description>Aberrant glycosylation is a prominent feature of cancer, that can be used as targets to improve the existing cancer biomarkers, and help to assess metastasis risks, and therapeutic effects. We developed a targeted O-glycoproteomics method using serum specimens, and evaluated its utility in identifying advanced colorectal cancer (CRC) markers. To this end, we combined consecutive lectin affinity purification using &lt;i>Maclura pomifera&lt;/i> lectin (MPL), jacalin, and &lt;i>Sambucus nigra&lt;/i> lectin, which have affinities for the following O-glycans, that have received attention as cancer-related antigens, Tn (GalNAc-Ser/Thr), Sialyl Tn (Siaα2-6GalNAc-Ser/Thr), T (Galβ1-3GalNAc-Ser/Thr), Sialyl T (Siaα2-3Galβ1-GalNAc-Ser/Thr), and di-Sialyl T (Siaα2-3Galβ1-3[Siaα2-6] GalNAc-Ser/Thr), with a unique</description><dates><release>2023-01-01T00:00:00Z</release><publication>2023</publication><modification>2025-04-29T10:47:46.387Z</modification><creation>2024-11-20T19:24:49.108Z</creation></dates><accession>S-EPMC9948623</accession><cross_references><pubmed>36845686</pubmed><doi>10.3389/fonc.2023.1104936</doi></cross_references></HashMap>