Werner, Hauke B.

[["dc.bibliographiccitation.firstpage","e3000943"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","PLoS Biology"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","Trevisiol, Andrea"],["dc.contributor.author","Kusch, Kathrin"],["dc.contributor.author","Steyer, Anna M."],["dc.contributor.author","Gregor, Ingo"],["dc.contributor.author","Nardis, Christos"],["dc.contributor.author","Winkler, Ulrike"],["dc.contributor.author","Köhler, Susanne"],["dc.contributor.author","Restrepo, Alejandro"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Werner, Hauke B."],["dc.contributor.author","Nave, Klaus-Armin"],["dc.contributor.author","Hirrlinger, Johannes"],["dc.date.accessioned","2021-04-14T08:31:16Z"],["dc.date.available","2021-04-14T08:31:16Z"],["dc.date.issued","2020"],["dc.description.abstract","In several neurodegenerative disorders, axonal pathology may originate from impaired oligodendrocyte-to-axon support of energy substrates. We previously established transgenic mice that allow measuring axonal ATP levels in electrically active optic nerves. Here, we utilize this technique to explore axonal ATP dynamics in the Plpnull/y mouse model of spastic paraplegia. Optic nerves from Plpnull/y mice exhibited lower and more variable basal axonal ATP levels and reduced compound action potential (CAP) amplitudes, providing a missing link between axonal pathology and a role of oligodendrocytes in brain energy metabolism. Surprisingly, when Plpnull/y optic nerves are challenged with transient glucose deprivation, both ATP levels and CAP decline slower, but recover faster upon reperfusion of glucose. Structurally, myelin sheaths display an increased frequency of cytosolic channels comprising glucose and monocarboxylate transporters, possibly facilitating accessibility of energy substrates to the axon. These data imply that complex metabolic alterations of the axon–myelin unit contribute to the phenotype of Plpnull/y mice."],["dc.identifier.doi","10.1371/journal.pbio.3000943"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83539"],["dc.identifier.url","https://for2848.gwdguser.de/literature/publications/20"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","FOR 2848: Architektur und Heterogenität der inneren mitochondrialen Membran auf der Nanoskala"],["dc.relation","FOR 2848 | P08: Strukturelle und funktionale Veränderungen der inneren mitochondrialen Membran axonaler Mitochondrien in vivo in einem dymyelinisierenden Mausmodell"],["dc.relation.eissn","1545-7885"],["dc.relation.workinggroup","RG Möbius"],["dc.rights","CC BY 4.0"],["dc.title","Structural myelin defects are associated with low axonal ATP levels but rapid recovery from energy deprivation in a mouse model of spastic paraplegia"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Glia"],["dc.bibliographiccitation.volume","65"],["dc.contributor.author","Kusch, Kathrin"],["dc.contributor.author","Uecker, Martin"],["dc.contributor.author","Liepold, Thomas"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Werner, Hauke B."],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Nave, Klaus-Armin"],["dc.date.accessioned","2018-11-07T10:23:03Z"],["dc.date.available","2018-11-07T10:23:03Z"],["dc.date.issued","2017"],["dc.identifier.isi","000403071700600"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/42387"],["dc.language.iso","en"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Wiley"],["dc.publisher.place","Hoboken"],["dc.relation.conference","13th European Meeting on Glial Cells in Health and Disease"],["dc.relation.eventlocation","Edinburgh, Scotland"],["dc.title","SIRT2 as a genetic modifier of axonal degeneration in white matter tracts"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1832"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Glia"],["dc.bibliographiccitation.lastpage","1847"],["dc.bibliographiccitation.volume","61"],["dc.contributor.author","de Monasterio-Schrader, Patricia"],["dc.contributor.author","Patzig, Julia"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Barrette, Benoit"],["dc.contributor.author","Wagner, Tadzio L."],["dc.contributor.author","Kusch, Kathrin"],["dc.contributor.author","Edgar, Julia M."],["dc.contributor.author","Brophy, Peter J."],["dc.contributor.author","Werner, Hauke B."],["dc.date.accessioned","2022-03-01T11:45:36Z"],["dc.date.available","2022-03-01T11:45:36Z"],["dc.date.issued","2013"],["dc.identifier.doi","10.1002/glia.22561"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103390"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0894-1491"],["dc.title","Uncoupling of neuroinflammation from axonal degeneration in mice lacking the myelin protein tetraspanin-2"],["dc.title.alternative","Tspan2-Deficient Myelin Induces Neuroinflammation"],["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","3"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Proteomes"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Kusch, Kathrin"],["dc.contributor.author","Uecker, Marina"],["dc.contributor.author","Liepold, Thomas"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Hoffmann, Christian"],["dc.contributor.author","Neumann, Heinz"],["dc.contributor.author","Werner, Hauke"],["dc.contributor.author","Jahn, Olaf"],["dc.date.accessioned","2020-12-10T18:47:19Z"],["dc.date.available","2020-12-10T18:47:19Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.3390/proteomes5010003"],["dc.identifier.eissn","2227-7382"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78723"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.publisher","MDPI"],["dc.relation.eissn","2227-7382"],["dc.rights","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Partial Immunoblotting of 2D-Gels: A Novel Method to Identify Post-Translationally Modified Proteins Exemplified for the Myelin Acetylome"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","eLife"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Patzig, Julia"],["dc.contributor.author","Erwig, Michelle S"],["dc.contributor.author","Tenzer, Stefan"],["dc.contributor.author","Kusch, Kathrin"],["dc.contributor.author","Dibaj, Payam"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Goebbels, Sandra"],["dc.contributor.author","Schaeren-Wiemers, Nicole"],["dc.contributor.author","Nave, Klaus-Armin"],["dc.contributor.author","Werner, Hauke B"],["dc.date.accessioned","2021-06-01T10:48:59Z"],["dc.date.available","2021-06-01T10:48:59Z"],["dc.date.issued","2016"],["dc.description.abstract","Myelination of axons facilitates rapid impulse propagation in the nervous system. The axon/myelin-unit becomes impaired in myelin-related disorders and upon normal aging. However, the molecular cause of many pathological features, including the frequently observed myelin outfoldings, remained unknown. Using label-free quantitative proteomics, we find that the presence of myelin outfoldings correlates with a loss of cytoskeletal septins in myelin. Regulated by phosphatidylinositol-(4,5)-bisphosphate (PI(4,5)P2)-levels, myelin septins (SEPT2/SEPT4/SEPT7/SEPT8) and the PI(4,5)P2-adaptor anillin form previously unrecognized filaments that extend longitudinally along myelinated axons. By confocal microscopy and immunogold-electron microscopy, these filaments are localized to the non-compacted adaxonal myelin compartment. Genetic disruption of these filaments in Sept8-mutant mice causes myelin outfoldings as a very specific neuropathology. Septin filaments thus serve an important function in scaffolding the axon/myelin-unit, evidently a late stage of myelin maturation. We propose that pathological or aging-associated diminishment of the septin/anillin-scaffold causes myelin outfoldings that impair the normal nerve conduction velocity."],["dc.description.abstract","Normal communication within the brain or between the brain and other parts of the body requires information to flow quickly around the nervous system. This information travels along nerve cells in the form of electrical signals. To speed up the signals, a part of the nerve cell called the axon is frequently wrapped in an electrically insulating sheath made up of a membrane structure called myelin. The myelin sheath becomes impaired as a result of disease or ageing. In order to understand what might produce these changes, Patzig et al. have used biochemical and microscopy techniques to study mice that had similar defects in their myelin sheaths. The study reveals that forming a normal myelin sheath around an axon requires a newly identified ‘scaffold’ made of a group of proteins called the septins. Combining with another protein called anillin, septins assemble into filaments in the myelin sheath. These filaments then knit together into a scaffold that grows lengthways along the myelin-wrapped axon. Without this scaffold, the myelin sheath grew defects known as outfoldings. Axons transmitted electrical signals much more slowly than normal when the septin scaffold was missing from the myelin sheath. Future studies are needed to understand the factors that control how the septin scaffold forms. This could help to reveal ways of reversing the changes that alter the myelin sheath during ageing and disease."],["dc.identifier.doi","10.7554/eLife.17119"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13756"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/86124"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.notes.intern","Merged from goescholar"],["dc.relation.eissn","2050-084X"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Septin/anillin filaments scaffold central nervous system myelin to accelerate nerve conduction"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["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","155"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Glia"],["dc.bibliographiccitation.lastpage","174"],["dc.bibliographiccitation.volume","64"],["dc.contributor.author","Patzig, Julia"],["dc.contributor.author","Kusch, Kathrin"],["dc.contributor.author","Fledrich, Robert"],["dc.contributor.author","Eichel, Maria A."],["dc.contributor.author","Lueders, Katja A."],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Sereda, Michael W."],["dc.contributor.author","Nave, Klaus-Armin"],["dc.contributor.author","Martini, Rudolf"],["dc.contributor.author","Werner, Hauke B."],["dc.date.accessioned","2018-11-07T10:21:33Z"],["dc.date.available","2018-11-07T10:21:33Z"],["dc.date.issued","2016"],["dc.description.abstract","Protein zero (P0) is the major structural component of peripheral myelin. Lack of this adhesion protein from Schwann cells causes a severe dysmyelinating neuropathy with secondary axonal degeneration in humans with the neuropathy Dejerine-Sottas syndrome (DSS) and in the corresponding mouse model (P0(null)-mice). In the mammalian CNS, the tetraspan-membrane protein PLP is the major structural myelin constituent and required for the long-term preservation of myelinated axons, which fails in hereditary spastic paraplegia (SPG type-2) and the relevant mouse model (Plp(null)-mice). The Plp-gene is also expressed in Schwann cells but PLP is of very low abundance in normal peripheral myelin; its function has thus remained enigmatic. Here we show that the abundance of PLP but not of other tetraspan myelin proteins is strongly increased in compact peripheral myelin of P0(null)-mice. To determine the functional relevance of PLP expression in the absence of P0, we generated P0(null star) Plp(null)-double-mutant mice. Compared with either single-mutant, P0(null star) Plp(null)-mice display impaired nerve conduction, reduced motor functions, and premature death. At the morphological level, axonal segments were frequently non-myelinated but in a one-to-one relationship with a hypertrophic Schwann cell. Importantly, axonal numbers were reduced in the vital phrenic nerve of P0(null star) Plp(null)-mice. In the absence of P0, thus, PLP also contributes to myelination by Schwann cells and to the preservation of peripheral axons. These data provide a link between the Schwann cell-dependent support of peripheral axons and the oligodendrocyte-dependent support of central axons."],["dc.identifier.doi","10.1002/glia.22922"],["dc.identifier.isi","000367677600011"],["dc.identifier.pmid","26393339"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/42116"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1098-1136"],["dc.relation.issn","0894-1491"],["dc.title","Proteolipid Protein Modulates Preservation of Peripheral Axons and Premature Death when Myelin Protein Zero is Lacking"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","eLife"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Erwig, Michelle S."],["dc.contributor.author","Patzig, Julia"],["dc.contributor.author","Steyer, Anna M."],["dc.contributor.author","Dibaj, Payam"],["dc.contributor.author","Heilmann, Mareike"],["dc.contributor.author","Heilmann, Ingo"],["dc.contributor.author","Jung, Ramona B."],["dc.contributor.author","Kusch, Kathrin"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Nave, Klaus-Armin"],["dc.contributor.author","Werner, Hauke B."],["dc.date.accessioned","2019-08-02T06:29:41Z"],["dc.date.available","2019-08-02T06:29:41Z"],["dc.date.issued","2019"],["dc.description.abstract","Myelin serves as an axonal insulator that facilitates rapid nerve conduction along axons. By transmission electron microscopy, a healthy myelin sheath comprises compacted membrane layers spiraling around the cross-sectioned axon. Previously we identified the assembly of septin filaments in the innermost non-compacted myelin layer as one of the latest steps of myelin maturation in the central nervous system (CNS) (Patzig et al., 2016). Here we show that loss of the cytoskeletal adaptor protein anillin (ANLN) from oligodendrocytes disrupts myelin septin assembly, thereby causing the emergence of pathological myelin outfoldings. Since myelin outfoldings are a poorly understood hallmark of myelin disease and brain aging we assessed axon/myelin-units in Anln-mutant mice by focused ion beam-scanning electron microscopy (FIB-SEM); myelin outfoldings were three-dimensionally reconstructed as large sheets of multiple compact membrane layers. We suggest that anillin-dependent assembly of septin filaments scaffolds mature myelin sheaths, facilitating rapid nerve conduction in the healthy CNS."],["dc.identifier.doi","10.7554/eLife.43888"],["dc.identifier.pmid","30672734"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15932"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/62262"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation.eissn","2050-084X"],["dc.relation.issn","2050-084X"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Anillin facilitates septin assembly to prevent pathological outfoldings of central nervous system myelin"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["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"]]