{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Yoshikawa F"],"funding":["Tokyo University of Science","Hamaguchi Foundation for the Advancement of Biochemistry","Japan Society for the Promotion of Science","Exchange Program between Tokyo University of Science and the University of Strasbourg"],"pagination":["e0166732"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5113975"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11(11)"],"pubmed_abstract":["Opalin, a central nervous system-specific myelin protein phylogenetically unique to mammals, has been suggested to play a role in mammalian-specific myelin. To elucidate the role of Opalin in mammalian myelin, we disrupted the Opalin gene in mice and analyzed the impacts on myelination and behavior. Opalin-knockout (Opalin-/-) mice were born at a Mendelian ratio and had a normal body shape and weight. Interestingly, Opalin-/- mice had no obvious abnormalities in major myelin protein compositions, expression of oligodendrocyte lineage markers, or domain organization of myelinated axons compared with WT mice (Opalin+/+) mice. Electron microscopic observation of the optic nerves did not reveal obvious differences between Opalin+/+ and Opalin-/- mice in terms of fine structures of paranodal lo"],"journal":["PloS one"],"pubmed_title":["Mammalian-Specific Central Myelin Protein Opalin Is Redundant for Normal Myelination: Structural and Behavioral Assessments."],"pmcid":["PMC5113975"],"funding_grant_id":["Research Grant","KAKENHI 20300134, 23300137, 26290026, 15K14356"],"pubmed_authors":["Yoshikawa F","Ghandour MS","Furuse T","Sano Y","Wakana S","Furuichi T","Sato Y","Sadakata T","Shinoda Y","Tohyama K","Itohara S","Tanaka M","Hashikawa T","Akagi T"],"additional_accession":[]},"is_claimable":false,"name":"Mammalian-Specific Central Myelin Protein Opalin Is Redundant for Normal Myelination: Structural and Behavioral Assessments.","description":"Opalin, a central nervous system-specific myelin protein phylogenetically unique to mammals, has been suggested to play a role in mammalian-specific myelin. To elucidate the role of Opalin in mammalian myelin, we disrupted the Opalin gene in mice and analyzed the impacts on myelination and behavior. Opalin-knockout (Opalin-/-) mice were born at a Mendelian ratio and had a normal body shape and weight. Interestingly, Opalin-/- mice had no obvious abnormalities in major myelin protein compositions, expression of oligodendrocyte lineage markers, or domain organization of myelinated axons compared with WT mice (Opalin+/+) mice. Electron microscopic observation of the optic nerves did not reveal obvious differences between Opalin+/+ and Opalin-/- mice in terms of fine structures of paranodal lo","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016","modification":"2025-04-26T20:48:04.496Z","creation":"2019-03-26T22:48:50Z"},"accession":"S-EPMC5113975","cross_references":{"pubmed":["27855200"],"doi":["10.1371/journal.pone.0166732"]}}