<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>14</volume><submitter>Xu Y</submitter><funding>National Key Research and Development Program of China</funding><pubmed_abstract>&lt;h4>Objectives&lt;/h4>Hashimoto's thyroiditis (HT) is one of the most common autoimmune disorders; however, its underlying pathological mechanisms remain unclear. Although aberrant glycosylation has been implicated in the N-glycome of immunoglobulin G (IgG), changes in serum proteins have not been comprehensively characterized. This study aimed to investigate glycosylation profiles in serum samples depleted of highly abundant proteins from patients with HT and propose the potential functions of glycoproteins for further studies on the pathological mechanisms of HT.&lt;h4>Methods&lt;/h4>A lectin microarray containing 70 lectins was used to detect and analyze glycosylation of serum proteins using serum samples (N=27 HT; N=26 healthy control [HC]) depleted of abundant proteins. Significant differences</pubmed_abstract><journal>Frontiers in immunology</journal><pagination>1182842</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC10348014</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Altered profile of glycosylated proteins in serum samples obtained from patients with Hashimoto's thyroiditis following depletion of highly abundant proteins.</pubmed_title><pmcid>PMC10348014</pmcid><pubmed_authors>Nie R</pubmed_authors><pubmed_authors>Huo J</pubmed_authors><pubmed_authors>Liu J</pubmed_authors><pubmed_authors>Wu L</pubmed_authors><pubmed_authors>Qin X</pubmed_authors><pubmed_authors>Ge L</pubmed_authors><pubmed_authors>Meng Y</pubmed_authors><pubmed_authors>Xie C</pubmed_authors><pubmed_authors>Xu Y</pubmed_authors></additional><is_claimable>false</is_claimable><name>Altered profile of glycosylated proteins in serum samples obtained from patients with Hashimoto's thyroiditis following depletion of highly abundant proteins.</name><description>&lt;h4>Objectives&lt;/h4>Hashimoto's thyroiditis (HT) is one of the most common autoimmune disorders; however, its underlying pathological mechanisms remain unclear. Although aberrant glycosylation has been implicated in the N-glycome of immunoglobulin G (IgG), changes in serum proteins have not been comprehensively characterized. This study aimed to investigate glycosylation profiles in serum samples depleted of highly abundant proteins from patients with HT and propose the potential functions of glycoproteins for further studies on the pathological mechanisms of HT.&lt;h4>Methods&lt;/h4>A lectin microarray containing 70 lectins was used to detect and analyze glycosylation of serum proteins using serum samples (N=27 HT; N=26 healthy control [HC]) depleted of abundant proteins. Significant differences</description><dates><release>2023-01-01T00:00:00Z</release><publication>2023</publication><modification>2026-04-15T03:29:00.034Z</modification><creation>2025-07-12T03:04:45.202Z</creation></dates><accession>S-EPMC10348014</accession><cross_references><pubmed>37457741</pubmed><doi>10.3389/fimmu.2023.1182842</doi></cross_references></HashMap>