{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ji Y"],"funding":["HHS | NIH | National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)","HHS | NIH | National Institute of General Medical Sciences (NIGMS)"],"pagination":["e2505249122"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12403103"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["122(34)"],"pubmed_abstract":["Sialic acids (Sias) are a diverse family of nine-carbon backbone monosaccharides occupying terminal positions on cell surface and secreted glycans and are abundant at mucosal surfaces. Sias can be modified with <i>O</i>-acetyl esters on the side chain (C7 to C9) hydroxyls. Structural analysis and functional studies of these modifications are challenging due to chemical lability and variable resistance to sialidases. For in-depth analysis of the expression and functions of <i>O</i>-acetyl Sia modifications, we used a unique set of sialoglycan-recognizing probes, HPLC analysis of DMB-derivatized Sias and mice lacking the first known sialate <i>O</i>-acetyltransferase, CASD1. C7/C9-<i>O</i>-acetylated Sias are most abundant in the colon, with lower levels in the heart, brain, and spleen, and "],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Loss of sialic acid side-chain &lt;i&gt;O&lt;/i&gt;-acetylation exacerbates colitis."],"pmcid":["PMC12403103"],"funding_grant_id":["GM032373","DK120515"],"pubmed_authors":["Srivastava S","Varki A","Parashar S","Varki N","Eckmann L","Lewis AL","Ji Y","Miyamoto Y"],"additional_accession":[]},"is_claimable":false,"name":"Loss of sialic acid side-chain &lt;i&gt;O&lt;/i&gt;-acetylation exacerbates colitis.","description":"Sialic acids (Sias) are a diverse family of nine-carbon backbone monosaccharides occupying terminal positions on cell surface and secreted glycans and are abundant at mucosal surfaces. Sias can be modified with <i>O</i>-acetyl esters on the side chain (C7 to C9) hydroxyls. Structural analysis and functional studies of these modifications are challenging due to chemical lability and variable resistance to sialidases. For in-depth analysis of the expression and functions of <i>O</i>-acetyl Sia modifications, we used a unique set of sialoglycan-recognizing probes, HPLC analysis of DMB-derivatized Sias and mice lacking the first known sialate <i>O</i>-acetyltransferase, CASD1. C7/C9-<i>O</i>-acetylated Sias are most abundant in the colon, with lower levels in the heart, brain, and spleen, and ","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Aug","modification":"2026-07-16T06:36:30.633Z","creation":"2026-07-09T10:40:17.353Z"},"accession":"S-EPMC12403103","cross_references":{"pubmed":["40828018"],"doi":["10.1073/pnas.2505249122"]}}