{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Garapati K"],"funding":["DBT/Wellcome Trust India Alliance entitled \"Center for Rare Disease Diagnosis, Research, and Training\"","DBT/Wellcome Trust India Alliance entitled “Center for Rare Disease Diagnosis, Research, and Training”","DBT/Wellcome Trust India Alliance","Wellcome Trust"],"pagination":["cwae076"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7617596"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["34(11)"],"pubmed_abstract":["SRD5A3-CDG is a congenital disorder of glycosylation (CDG) resulting from pathogenic variants in SRD5A3 and follows an autosomal recessive inheritance pattern. The enzyme encoded by SRD5A3, polyprenal reductase, plays a crucial role in synthesizing lipid precursors essential for N-linked glycosylation. Despite insights from functional studies into its enzymatic function, there remains a gap in understanding global changes in patient cells. We sought to identify N-glycoproteomic and proteomic signatures specific to SRD5A3-CDG, potentially aiding in biomarker discovery and advancing our understanding of disease mechanisms. Using tandem mass tag (TMT)-based relative quantitation, we analyzed fibroblasts derived from five patients along with control fibroblasts. N-glycoproteomics analysis by l"],"journal":["Glycobiology"],"pubmed_title":["N-glycoproteomic and proteomic alterations in SRD5A3-deficient fibroblasts."],"pmcid":["PMC7617596"],"funding_grant_id":["IA/CRC/20/1/600002"],"pubmed_authors":["Garapati K","Joshi N","Sabu S","Morava E","Preston G","Ranatunga W","Budhraja R","Pandey A","Kantautas KA","Perlstein EO","Kozicz T"],"additional_accession":[]},"is_claimable":false,"name":"N-glycoproteomic and proteomic alterations in SRD5A3-deficient fibroblasts.","description":"SRD5A3-CDG is a congenital disorder of glycosylation (CDG) resulting from pathogenic variants in SRD5A3 and follows an autosomal recessive inheritance pattern. The enzyme encoded by SRD5A3, polyprenal reductase, plays a crucial role in synthesizing lipid precursors essential for N-linked glycosylation. Despite insights from functional studies into its enzymatic function, there remains a gap in understanding global changes in patient cells. We sought to identify N-glycoproteomic and proteomic signatures specific to SRD5A3-CDG, potentially aiding in biomarker discovery and advancing our understanding of disease mechanisms. Using tandem mass tag (TMT)-based relative quantitation, we analyzed fibroblasts derived from five patients along with control fibroblasts. N-glycoproteomics analysis by l","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Sep","modification":"2026-05-22T03:15:35.907Z","creation":"2025-07-12T03:04:38.139Z"},"accession":"S-EPMC7617596","cross_references":{"pubmed":["39360848"],"doi":["10.1093/glycob/cwae076"]}}