<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Munkley J</submitter><funding>Prostate Cancer UK</funding><pagination>4248</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9454432</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>14(17)</volume><pubmed_abstract>The surface of every eukaryotic cell is coated in a thick layer of glycans that acts as a key interface with the extracellular environment. Cancer cells have a different 'glycan coat' to healthy cells and aberrant glycosylation is a universal feature of cancer cells linked to all of the cancer hallmarks. This means glycans hold huge potential for the development of new diagnostic and therapeutic strategies. One key change in tumour glycosylation is increased sialylation, both on &lt;i>N&lt;/i>-glycans and &lt;i>O&lt;/i&gt;-glycans, which leads to a dense forest of sialylated structures covering the cell surface. This hypersialylation has far-reaching consequences for cancer cells, and sialylated glycans are fundamental in tumour growth, metastasis, immune evasion and drug resistance. The development of s</pubmed_abstract><journal>Cancers</journal><pubmed_title>Aberrant Sialylation in Cancer: Therapeutic Opportunities.</pubmed_title><pmcid>PMC9454432</pmcid><funding_grant_id>RIA16-ST2-011</funding_grant_id><pubmed_authors>Munkley J</pubmed_authors></additional><is_claimable>false</is_claimable><name>Aberrant Sialylation in Cancer: Therapeutic Opportunities.</name><description>The surface of every eukaryotic cell is coated in a thick layer of glycans that acts as a key interface with the extracellular environment. Cancer cells have a different 'glycan coat' to healthy cells and aberrant glycosylation is a universal feature of cancer cells linked to all of the cancer hallmarks. This means glycans hold huge potential for the development of new diagnostic and therapeutic strategies. One key change in tumour glycosylation is increased sialylation, both on &lt;i>N&lt;/i>-glycans and &lt;i>O&lt;/i&gt;-glycans, which leads to a dense forest of sialylated structures covering the cell surface. This hypersialylation has far-reaching consequences for cancer cells, and sialylated glycans are fundamental in tumour growth, metastasis, immune evasion and drug resistance. The development of s</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Aug</publication><modification>2025-05-29T16:11:31.555Z</modification><creation>2025-04-04T18:43:37.385Z</creation></dates><accession>S-EPMC9454432</accession><cross_references><pubmed>36077781</pubmed><doi>10.3390/cancers14174248</doi></cross_references></HashMap>