{"doi":"10.1002/biof.1076","title":"Myelin‐specific proteins: A structurally diverse group of membrane‐interacting molecules","abstract":"<jats:title>Abstract</jats:title><jats:p>The myelin sheath is a multilayered membrane in the nervous system, which has unique biochemical properties. Myelin carries a set of specific high‐abundance proteins, the structure and function of which are still poorly understood. The proteins of the myelin sheath are involved in a number of neurological diseases, including autoimmune diseases and inherited neuropathies. In this review, we briefly discuss the structural properties and functions of selected myelin‐specific proteins (P0, myelin oligodendrocyte glycoprotein, myelin‐associated glycoprotein, myelin basic protein, myelin‐associated oligodendrocytic basic protein, P2, proteolipid protein, peripheral myelin protein of 22 kDa, 2′,3′‐cyclic nucleotide 3′‐phosphodiesterase, and periaxin); such properties include, for example, interactions with lipid bilayers and the presence of large intrinsically disordered regions in some myelin proteins. A detailed understanding of myelin protein structure and function at the molecular level will be required to fully grasp their physiological roles in the myelin sheath. © 2013 BioFactors, 2013</jats:p>","journal":"BioFactors","year":2013,"id":630898,"datarank":0.6782682865573562,"base_score":4.5217885770490405,"endowment":4.5217885770490405,"self_citation_contribution":0.6782682865573562,"citation_network_contribution":0.0,"self_endowment_contribution":0.6782682865573562,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":91,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1634683,"name":"Matti Myllykoski","orcid":null,"position":1,"is_corresponding":false},{"id":1634686,"name":"Salla Ruskamo","orcid":null,"position":2,"is_corresponding":false},{"id":1634687,"name":"Chaozhan Wang","orcid":null,"position":3,"is_corresponding":false},{"id":630647,"name":"Petri Kursula","orcid":"0000-0001-8529-3751","position":4,"is_corresponding":false},{"id":942981,"name":"Huijong Han","orcid":"0000-0002-1197-3014","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Myelin‐specific proteins: A structurally diverse group of membrane‐interacting molecules","abstract":"<jats:title>Abstract</jats:title><jats:p>The myelin sheath is a multilayered membrane in the nervous system, which has unique biochemical properties. Myelin carries a set of specific high‐abundance proteins, the structure and function of which are still poorly understood. The proteins of the myelin sheath are involved in a number of neurological diseases, including autoimmune diseases and inherited neuropathies. In this review, we briefly discuss the structural properties and functions of selected myelin‐specific proteins (P0, myelin oligodendrocyte glycoprotein, myelin‐associated glycoprotein, myelin basic protein, myelin‐associated oligodendrocytic basic protein, P2, proteolipid protein, peripheral myelin protein of 22 kDa, 2′,3′‐cyclic nucleotide 3′‐phosphodiesterase, and periaxin); such properties include, for example, interactions with lipid bilayers and the presence of large intrinsically disordered regions in some myelin proteins. A detailed understanding of myelin protein structure and function at the molecular level will be required to fully grasp their physiological roles in the myelin sheath. © 2013 BioFactors, 2013</jats:p>","is_dataset_classified":null,"base_score":0.0,"endowment":0.0,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"23780694","pmcid":null,"openalex_id":null,"authors":[],"funders":[],"total_grants":0,"fwci":null,"citation_percentile":null,"influential_citations":0,"citation_trend":[],"oa_status":"closed","license":"http://onlinelibrary.wiley.com/termsAndConditions#vor","oa_locations":[{"url":"https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbiof.1076","host_type":"publisher"},{"url":"https://iubmb.onlinelibrary.wiley.com/doi/pdf/10.1002/biof.1076","host_type":"publisher"}],"fields_of_study":[],"mesh_terms":["Humans","Myelin Proteolipid Protein","Myelin-Associated Glycoprotein","Membrane Proteins","Myelin Proteins","Myelin Basic Protein","Myelin-Oligodendrocyte Glycoprotein"],"keywords":[],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-05T22:23:25.986926Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}