{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Li W"],"funding":["National Institute of Neurological Disorders and Stroke","Intramural NIH HHS","Eunice Kennedy Shriver National Institute of Child Health and Human Development","NINDS NIH HHS","National Niemann-Pick Disease Foundation"],"pagination":["e2200378"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10918788"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["23(11)"],"pubmed_abstract":["Niemann-Pick, type C1 (NPC1) is a fatal, neurodegenerative disease, which belongs to the family of lysosomal diseases. In NPC1, endo/lysosomal accumulation of unesterified cholesterol and sphingolipids arise from improper intracellular trafficking resulting in multi-organ dysfunction. With the proximity between the brain and cerebrospinal fluid (CSF), performing differential proteomics provides a means to shed light to changes occurring in the brain. In this study, CSF samples obtained from NPC1 individuals and unaffected controls were used for protein biomarker identification. A subset of these individuals with NPC1 are being treated with miglustat, a glycosphingolipid synthesis inhibitor. Of the 300 identified proteins, 71 proteins were altered in individuals with NPC1 compared to contro"],"journal":["Proteomics"],"pubmed_title":["A differential proteomics study of cerebrospinal fluid from individuals with Niemann-Pick disease, Type C1."],"pmcid":["PMC10918788"],"funding_grant_id":["R01 NS114413","ZIA GD008989","ZIA HD008989","R01 NS124784"],"pubmed_authors":["Picache JA","Wassif CA","Pergande MR","Burkert K","Yanjanin-Farhat NM","Searle BC","Li W","Porter FD","Cologna SM","Blank PS","Toth CL","Crutchfield CA","Backlund PS"],"additional_accession":[]},"is_claimable":false,"name":"A differential proteomics study of cerebrospinal fluid from individuals with Niemann-Pick disease, Type C1.","description":"Niemann-Pick, type C1 (NPC1) is a fatal, neurodegenerative disease, which belongs to the family of lysosomal diseases. In NPC1, endo/lysosomal accumulation of unesterified cholesterol and sphingolipids arise from improper intracellular trafficking resulting in multi-organ dysfunction. With the proximity between the brain and cerebrospinal fluid (CSF), performing differential proteomics provides a means to shed light to changes occurring in the brain. In this study, CSF samples obtained from NPC1 individuals and unaffected controls were used for protein biomarker identification. A subset of these individuals with NPC1 are being treated with miglustat, a glycosphingolipid synthesis inhibitor. Of the 300 identified proteins, 71 proteins were altered in individuals with NPC1 compared to contro","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jun","modification":"2025-04-04T12:58:37.454Z","creation":"2025-04-04T12:58:37.454Z"},"accession":"S-EPMC10918788","cross_references":{"pubmed":["36638187"],"doi":["10.1002/pmic.202200378"]}}