Werner, Hauke B.

[["dc.bibliographiccitation.firstpage","764"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Journal of Neurochemistry"],["dc.bibliographiccitation.lastpage","783"],["dc.bibliographiccitation.volume","147"],["dc.contributor.author","Myllykoski, Matti"],["dc.contributor.author","Eichel, Maria A."],["dc.contributor.author","Jung, Ramona B."],["dc.contributor.author","Kelm, Sørge"],["dc.contributor.author","Werner, Hauke B."],["dc.contributor.author","Kursula, Petri"],["dc.date.accessioned","2020-12-10T18:29:01Z"],["dc.date.available","2020-12-10T18:29:01Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1111/jnc.14598"],["dc.identifier.issn","0022-3042"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/76493"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","High-affinity heterotetramer formation between the large myelin-associated glycoprotein and the dynein light chain DYNLL1"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Frontiers in Cell and Developmental Biology"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Siems, Sophie B."],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Hoodless, Laura J."],["dc.contributor.author","Jung, Ramona B."],["dc.contributor.author","Hesse, Dörte"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Czopka, Tim"],["dc.contributor.author","Werner, Hauke B."],["dc.date.accessioned","2022-03-01T11:44:21Z"],["dc.date.available","2022-03-01T11:44:21Z"],["dc.date.issued","2021"],["dc.description.abstract","The velocity of nerve conduction along vertebrate axons depends on their ensheathment with myelin. Myelin membranes comprise specialized proteins well characterized in mice. Much less is known about the protein composition of myelin in non-mammalian species. Here, we assess the proteome of myelin biochemically purified from the brains of adult zebrafish ( Danio rerio ), considering its increasing popularity as model organism for myelin biology. Combining gel-based and gel-free proteomic approaches, we identified > 1,000 proteins in purified zebrafish myelin, including all known constituents. By mass spectrometric quantification, the predominant Ig-CAM myelin protein zero (MPZ/P0), myelin basic protein (MBP), and the short-chain dehydrogenase 36K constitute 12%, 8%, and 6% of the total myelin protein, respectively. Comparison with previously established mRNA-abundance profiles shows that expression of many myelin-related transcripts coincides with the maturation of zebrafish oligodendrocytes. Zebrafish myelin comprises several proteins that are not present in mice, including 36K, CLDNK, and ZWI. However, a surprisingly large number of ortholog proteins is present in myelin of both species, indicating partial evolutionary preservation of its constituents. Yet, the relative abundance of CNS myelin proteins can differ markedly as exemplified by the complement inhibitor CD59 that constitutes 5% of the total zebrafish myelin protein but is a low-abundant myelin component in mice. Using novel transgenic reporter constructs and cryo-immuno electron microscopy, we confirm the incorporation of CD59 into myelin sheaths. These data provide the first proteome resource of zebrafish CNS myelin and demonstrate both similarities and heterogeneity of myelin composition between teleost fish and rodents."],["dc.description.abstract","The velocity of nerve conduction along vertebrate axons depends on their ensheathment with myelin. Myelin membranes comprise specialized proteins well characterized in mice. Much less is known about the protein composition of myelin in non-mammalian species. Here, we assess the proteome of myelin biochemically purified from the brains of adult zebrafish ( Danio rerio ), considering its increasing popularity as model organism for myelin biology. Combining gel-based and gel-free proteomic approaches, we identified > 1,000 proteins in purified zebrafish myelin, including all known constituents. By mass spectrometric quantification, the predominant Ig-CAM myelin protein zero (MPZ/P0), myelin basic protein (MBP), and the short-chain dehydrogenase 36K constitute 12%, 8%, and 6% of the total myelin protein, respectively. Comparison with previously established mRNA-abundance profiles shows that expression of many myelin-related transcripts coincides with the maturation of zebrafish oligodendrocytes. Zebrafish myelin comprises several proteins that are not present in mice, including 36K, CLDNK, and ZWI. However, a surprisingly large number of ortholog proteins is present in myelin of both species, indicating partial evolutionary preservation of its constituents. Yet, the relative abundance of CNS myelin proteins can differ markedly as exemplified by the complement inhibitor CD59 that constitutes 5% of the total zebrafish myelin protein but is a low-abundant myelin component in mice. Using novel transgenic reporter constructs and cryo-immuno electron microscopy, we confirm the incorporation of CD59 into myelin sheaths. These data provide the first proteome resource of zebrafish CNS myelin and demonstrate both similarities and heterogeneity of myelin composition between teleost fish and rodents."],["dc.identifier.doi","10.3389/fcell.2021.640169"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103004"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","2296-634X"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Proteome Profile of Myelin in the Zebrafish Brain"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Eichel, Maria A."],["dc.contributor.author","Gargareta, Vasiliki-Ilya"],["dc.contributor.author","D’Este, Elisa"],["dc.contributor.author","Fledrich, Robert"],["dc.contributor.author","Kungl, Theresa"],["dc.contributor.author","Buscham, Tobias J."],["dc.contributor.author","Lüders, Katja A."],["dc.contributor.author","Miracle, Cristina"],["dc.contributor.author","Jung, Ramona B."],["dc.contributor.author","Distler, Ute"],["dc.contributor.author","Kusch, Kathrin"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Hülsmann, Swen"],["dc.contributor.author","Tenzer, Stefan"],["dc.contributor.author","Nave, Klaus-Armin"],["dc.contributor.author","Werner, Hauke B."],["dc.date.accessioned","2021-04-14T08:23:13Z"],["dc.date.available","2021-04-14T08:23:13Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1038/s41467-020-18172-7"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/80831"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","2041-1723"],["dc.title","CMTM6 expressed on the adaxonal Schwann cell surface restricts axonal diameters in peripheral nerves"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","37"],["dc.bibliographiccitation.lastpage","63"],["dc.bibliographiccitation.seriesnr","1936"],["dc.contributor.author","Erwig, Michelle S."],["dc.contributor.author","Hesse, Dörte"],["dc.contributor.author","Jung, Ramona B."],["dc.contributor.author","Uecker, Marina"],["dc.contributor.author","Kusch, Kathrin"],["dc.contributor.author","Tenzer, Stefan"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Werner, Hauke B."],["dc.contributor.editor","Lyons, David A."],["dc.contributor.editor","Kegel, Linde"],["dc.date.accessioned","2021-06-02T10:44:26Z"],["dc.date.available","2021-06-02T10:44:26Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1007/978-1-4939-9072-6_3"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/87040"],["dc.notes.intern","DOI-Import GROB-425"],["dc.publisher","Springer New York"],["dc.publisher.place","New York, NY"],["dc.relation.crisseries","Methods in Molecular Biology"],["dc.relation.eisbn","978-1-4939-9072-6"],["dc.relation.isbn","978-1-4939-9070-2"],["dc.relation.ispartof","Methods in Molecular Biology"],["dc.relation.ispartof","Oligodendrocytes : Methods and Protocols"],["dc.relation.ispartofseries","Methods in Molecular Biology; 1936"],["dc.title","Myelin: Methods for Purification and Proteome Analysis"],["dc.type","book_chapter"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","634"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Glia"],["dc.bibliographiccitation.lastpage","649"],["dc.bibliographiccitation.volume","67"],["dc.contributor.author","Lüders, Katja A."],["dc.contributor.author","Nessler, Stefan"],["dc.contributor.author","Kusch, Kathrin"],["dc.contributor.author","Patzig, Julia"],["dc.contributor.author","Jung, Ramona B."],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Nave, Klaus-Armin"],["dc.contributor.author","Werner, Hauke B."],["dc.date.accessioned","2022-03-01T11:45:39Z"],["dc.date.available","2022-03-01T11:45:39Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1002/glia.23549"],["dc.identifier.issn","0894-1491"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103401"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0894-1491"],["dc.title","Maintenance of high proteolipid protein level in adult central nervous system myelin is required to preserve the integrity of myelin and axons"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]