Werner, Hauke B.

[["dc.bibliographiccitation.artnumber","dev.200597"],["dc.bibliographiccitation.journal","Development"],["dc.contributor.author","de Faria, Joana Paes"],["dc.contributor.author","Vale-Silva, Raquel S."],["dc.contributor.author","Fässler, Reinhard"],["dc.contributor.author","Werner, Hauke B."],["dc.contributor.author","Relvas, João B."],["dc.date.accessioned","2022-06-01T09:39:44Z"],["dc.date.available","2022-06-01T09:39:44Z"],["dc.date.issued","2022"],["dc.description.abstract","The extensive morphological changes of oligodendrocytes during axon ensheathment and myelination involve assembly of the Ilk-Parvin-Pinch (IPP) heterotrimeric complex of proteins to relay essential mechanical and biochemical signals between integrins and the actin cytoskeleton. Binding of Pinch 1 and 2 isoforms to Ilk is mutually exclusive and allows the formation of distinct IPP complexes with specific signaling properties. Using tissue-specific conditional gene ablation in mice, we reveal an essential role for Pinch2 during central nervous system myelination. Unlike Pinch1-gene ablation, loss of Pinch2 in oligodendrocytes results in hypermyelination and in the formation of pathological myelin outfoldings in white matter regions. These structural changes concurred with inhibition of Rho GTPases RhoA and Cdc42 activities and phenocopied aspects of myelin pathology observed in corresponding mouse mutants. We propose a dual role for Pinch2 in preventing excess of myelin wraps through RhoA-dependent control of membrane growth and in fostering myelin stability via Cdc42-dependent organization of cytoskeletal septins. Together, these findings indicate that IPP-containing Pinch2 is a novel critical cell-autonomous molecular hub ensuring synchronous control of key signaling networks during developmental myelination."],["dc.identifier.doi","10.1242/dev.200597"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/108547"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-572"],["dc.relation.eissn","1477-9129"],["dc.relation.issn","0950-1991"],["dc.title","Pinch2 is a novel regulator of myelination in the central nervous system"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3465"],["dc.bibliographiccitation.issue","15"],["dc.bibliographiccitation.journal","Journal of Neuroscience Research"],["dc.bibliographiccitation.lastpage","3479"],["dc.bibliographiccitation.volume","87"],["dc.contributor.author","Schardt, Anke"],["dc.contributor.author","Brinkmann, Bastian G."],["dc.contributor.author","Mitkovski, Miso"],["dc.contributor.author","Sereda, Michael W."],["dc.contributor.author","Werner, Hauke B."],["dc.contributor.author","Nave, Klaus-Armin"],["dc.date.accessioned","2018-11-07T11:22:05Z"],["dc.date.available","2018-11-07T11:22:05Z"],["dc.date.issued","2009"],["dc.description.abstract","During myelin formation, vast amounts of specialized membrane proteins and lipids are trafficked toward the growing sheath in cell surface-directed transport vesicles. Soluble N-ethylmaleimide-sensitive factor (NSF) attachment proteins (SNAPs) are important components of molecular complexes required for membrane fusion. We have analyzed the expression profile and molecular interactions of SNAP-29 in the nervous system. In addition to its known enrichment in neuronal synapses, SNAP-29 is abundant in oligodendrocytes during myelination and in noncompact myelin of the peripheral nervous system. By yeast two-hybrid screen and coimmunoprecipitation, we found that the GTPases Rab3A, Rab24, and septin 4 bind to the N-terminal domain of SNAP-29. The interaction with Rab24 or septin 4 was GTP independent. In contrast, interaction between SNAP-29 and Rab3A was GTP dependent, and colocalization was extensive both in synapses and in myelinating glia. In HEK293 cells, cytoplasmic SNAP-29 pools were redistributed upon coexpression with Rab3A, and surface-directed trafficking of myelin proteolipid protein was enhanced by overexpression of SNAP-29 and Rab3A. Interestingly, the abundance of SNAP-29 in sciatic nerves was increased during remyelination and in a rat model of Charcot-Marie-Tooth disease, two pathological situations with increased myelin membrane biogenesis. We suggest that Rab3A may regulate SNAP-29-mediated membrane fusion during myelination. (C) 2009 Wiley-Liss, Inc."],["dc.description.sponsorship","DFG [SFB 523]; BMBF (Leukonet)"],["dc.identifier.doi","10.1002/jnr.22005"],["dc.identifier.isi","000270843400023"],["dc.identifier.pmid","19170188"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/55921"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","0360-4012"],["dc.title","The SNARE Protein SNAP-29 Interacts With the GTPase Rab3A: Implications for Membrane Trafficking in Myelinating Glia"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","533"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","The American Journal of Human Genetics"],["dc.bibliographiccitation.lastpage","546"],["dc.bibliographiccitation.volume","94"],["dc.contributor.author","Prukop, Thomas"],["dc.contributor.author","Epplen, Dirk B."],["dc.contributor.author","Nientiedt, Tobias"],["dc.contributor.author","Wichert, Sven P."],["dc.contributor.author","Fledrich, Robert"],["dc.contributor.author","Stassart, Ruth Martha"],["dc.contributor.author","Rossner, Moritz J."],["dc.contributor.author","Edgar, Julia M."],["dc.contributor.author","Werner, Hauke B."],["dc.contributor.author","Nave, Klaus-Armin"],["dc.contributor.author","Sereda, Michael W."],["dc.date.accessioned","2018-11-07T09:41:24Z"],["dc.date.available","2018-11-07T09:41:24Z"],["dc.date.issued","2014"],["dc.description.abstract","Pelizaeus-Merzbacher disease (PMD) is a severe hypomyelinating disease, characterized by ataxia, intellectual disability, epilepsy, and premature death. In the majority of cases, PMD is caused by duplication of PLP1 that is expressed in myelinating oligodendrocytes. Despite detailed knowledge of PLP1, there is presently no curative therapy for PMD. We used a Plp1 transgenic PMD mouse model to test the therapeutic effect of Lonaprisan, an antagonist of the nuclear progesterone receptor, in lowering Plp1 mRNA overexpression. We applied placebo-controlled Lonaprisan therapy to PMD mice for 10 weeks and performed the grid slip analysis to assess the clinical phenotype. Additionally, mRNA expression and protein accumulation as well as histological analysis of the central nervous system were performed. Although Plp1 mRNA levels are increased 1.8-fold in PMD mice compared to wild-type controls, daily Lonaprisan treatment reduced overexpression at the RNA level to about 1.5-fold, which was sufficient to significantly improve the poor motor phenotype. Electron microscopy confirmed a 25% increase in the number of myelinated axons in the corticospinal tract when compared to untreated PMD mice. Microarray analysis revealed the upregulation of proapoptotic genes in PMD mice that could be partially rescued by Lonaprisan treatment, which also reduced microgliosis, astrogliosis, and lymphocyte infiltration."],["dc.identifier.doi","10.1016/j.ajhg.2014.03.001"],["dc.identifier.isi","000333765300005"],["dc.identifier.pmid","24680886"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/33720"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.relation.issn","1537-6605"],["dc.relation.issn","0002-9297"],["dc.title","Progesterone Antagonist Therapy in a Pelizaeus-Merzbacher Mouse Model"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","111"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Neuron Glia Biology"],["dc.bibliographiccitation.lastpage","127"],["dc.bibliographiccitation.volume","4"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Patzig, Julia"],["dc.contributor.author","Nave, Klaus-Armin"],["dc.contributor.author","Werner, Hauke B."],["dc.date.accessioned","2022-03-01T11:45:38Z"],["dc.date.available","2022-03-01T11:45:38Z"],["dc.date.issued","2009"],["dc.description.abstract","The protein composition of myelin in the central nervous system (CNS) has changed at the evolutionary transition from fish to tetrapods, when a lipid-associated transmembrane-tetraspan (proteolipid protein, PLP) replaced an adhesion protein of the immunoglobulin superfamily (P0) as the most abundant constituent. Here, we review major steps of proteolipid evolution. Three paralog proteolipids (PLP/DM20/DMα, M6B/DMγ and the neuronal glycoprotein M6A/DMβ) exist in vertebrates from cartilaginous fish to mammals, and one (M6/CG7540) can be traced in invertebrate bilaterians including the planktonic copepod Calanus finmarchicus that possess a functional myelin equivalent. In fish, DMα and DMγ are coexpressed in oligodendrocytes but are not major myelin components. PLP emerged at the root of tetrapods by the acquisition of an enlarged cytoplasmic loop in the evolutionary older DMα/DM20. Transgenic experiments in mice suggest that this loop enhances the incorporation of PLP into myelin. The evolutionary recruitment of PLP as the major myelin protein provided oligodendrocytes with the competence to support long-term axonal integrity. We suggest that the molecular shift from P0 to PLP also correlates with the concentration of adhesive forces at the radial component, and that the new balance between membrane adhesion and dynamics was favorable for CNS myelination."],["dc.description.abstract","The protein composition of myelin in the central nervous system (CNS) has changed at the evolutionary transition from fish to tetrapods, when a lipid-associated transmembrane-tetraspan (proteolipid protein, PLP) replaced an adhesion protein of the immunoglobulin superfamily (P0) as the most abundant constituent. Here, we review major steps of proteolipid evolution. Three paralog proteolipids (PLP/DM20/DMα, M6B/DMγ and the neuronal glycoprotein M6A/DMβ) exist in vertebrates from cartilaginous fish to mammals, and one (M6/CG7540) can be traced in invertebrate bilaterians including the planktonic copepod Calanus finmarchicus that possess a functional myelin equivalent. In fish, DMα and DMγ are coexpressed in oligodendrocytes but are not major myelin components. PLP emerged at the root of tetrapods by the acquisition of an enlarged cytoplasmic loop in the evolutionary older DMα/DM20. Transgenic experiments in mice suggest that this loop enhances the incorporation of PLP into myelin. The evolutionary recruitment of PLP as the major myelin protein provided oligodendrocytes with the competence to support long-term axonal integrity. We suggest that the molecular shift from P0 to PLP also correlates with the concentration of adhesive forces at the radial component, and that the new balance between membrane adhesion and dynamics was favorable for CNS myelination."],["dc.identifier.doi","10.1017/S1740925X0900009X"],["dc.identifier.pii","S1740925X0900009X"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103398"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1741-0533"],["dc.relation.issn","1740-925X"],["dc.title","Phylogeny of proteolipid proteins: divergence, constraints, and the evolution of novel functions in myelination and neuroprotection"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","567"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Glia"],["dc.bibliographiccitation.lastpage","586"],["dc.bibliographiccitation.volume","61"],["dc.contributor.author","Werner, Hauke B."],["dc.contributor.author","Kraemer-Albers, Eva-Maria"],["dc.contributor.author","Strenzke, Nicola"],["dc.contributor.author","Saher, Gesine"],["dc.contributor.author","Tenzer, Stefan"],["dc.contributor.author","Ohno-Iwashita, Yoshiko"],["dc.contributor.author","Monasterio-Schrader, Patricia de"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Moser, Tobias"],["dc.contributor.author","Griffiths, Ian R."],["dc.contributor.author","Nave, Klaus-Armin"],["dc.date.accessioned","2017-09-07T11:47:44Z"],["dc.date.available","2017-09-07T11:47:44Z"],["dc.date.issued","2013"],["dc.description.abstract","The formation of central nervous system myelin by oligodendrocytes requires sterol synthesis and is associated with a significant enrichment of cholesterol in the myelin membrane. However, it is unknown how oligodendrocytes concentrate cholesterol above the level found in nonmyelin membranes. Here, we demonstrate a critical role for proteolipids in cholesterol accumulation. Mice lacking the most abundant myelin protein, proteolipid protein (PLP), are fully myelinated, but PLP-deficient myelin exhibits a reduced cholesterol content. We therefore hypothesized that high cholesterol is not essential in the myelin sheath itself but is required for an earlier step of myelin biogenesis that is fully compensated for in the absence of PLP. We also found that a PLP-homolog, glycoprotein M6B, is a myelin component of low abundance. By targeting the Gpm6b-gene and crossbreeding, we found that single-mutant mice lacking either PLP or M6B are fully myelinated, while double mutants remain severely hypomyelinated, with enhanced neurodegeneration and premature death. As both PLP and M6B bind membrane cholesterol and associate with the same cholesterol-rich oligodendroglial membrane microdomains, we suggest a model in which proteolipids facilitate myelination by sequestering cholesterol. While either proteolipid can maintain a threshold level of cholesterol in the secretory pathway that allows myelin biogenesis, lack of both proteolipids results in a severe molecular imbalance of prospective myelin membrane. However, M6B is not efficiently sorted into mature myelin, in which it is 200-fold less abundant than PLP. Thus, only PLP contributes to the high cholesterol content of myelin by association and co-transport. (c) 2013 Wiley Periodicals, Inc."],["dc.identifier.doi","10.1002/glia.22456"],["dc.identifier.gro","3142368"],["dc.identifier.isi","000314981400010"],["dc.identifier.pmid","23322581"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7508"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: BMBF; European Commission"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","0894-1491"],["dc.title","A critical role for the cholesterol-associated proteolipids PLP and M6B in myelination of the central nervous system"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.journal","Brain Research"],["dc.bibliographiccitation.lastpage","12"],["dc.bibliographiccitation.volume","1197"],["dc.contributor.author","Cooper, Ben"],["dc.contributor.author","Werner, Hauke B."],["dc.contributor.author","Flügge, Gabriele"],["dc.date.accessioned","2022-10-06T13:33:00Z"],["dc.date.available","2022-10-06T13:33:00Z"],["dc.date.issued","2008"],["dc.identifier.doi","10.1016/j.brainres.2007.11.066"],["dc.identifier.pii","S0006899307028429"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/115519"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-602"],["dc.relation.issn","0006-8993"],["dc.relation.orgunit","Deutsches Primatenzentrum"],["dc.title","Glycoprotein M6a is present in glutamatergic axons in adult rat forebrain and cerebellum"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["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","4111"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Cerebral Cortex"],["dc.bibliographiccitation.lastpage","4125"],["dc.bibliographiccitation.volume","25"],["dc.contributor.author","Mita, Sakura"],["dc.contributor.author","de Monasterio-Schrader, Patricia"],["dc.contributor.author","Fünfschilling, Ursula"],["dc.contributor.author","Kawasaki, Takahiko"],["dc.contributor.author","Mizuno, Hidenobu"],["dc.contributor.author","Iwasato, Takuji"],["dc.contributor.author","Nave, Klaus-Armin"],["dc.contributor.author","Werner, Hauke B."],["dc.contributor.author","Hirata, Tatsumi"],["dc.date.accessioned","2021-06-01T10:51:16Z"],["dc.date.available","2021-06-01T10:51:16Z"],["dc.date.issued","2014"],["dc.identifier.doi","10.1093/cercor/bhu129"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/86952"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation.eissn","1460-2199"],["dc.relation.issn","1047-3211"],["dc.title","Transcallosal Projections Require Glycoprotein M6-Dependent Neurite Growth and Guidance"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e77019"],["dc.bibliographiccitation.journal","eLife"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Gargareta, Vasiliki-Ilya"],["dc.contributor.author","Reuschenbach, Josefine"],["dc.contributor.author","Siems, Sophie B"],["dc.contributor.author","Sun, Ting"],["dc.contributor.author","Piepkorn, Lars"],["dc.contributor.author","Mangana, Carolina"],["dc.contributor.author","Späte, Erik"],["dc.contributor.author","Goebbels, Sandra"],["dc.contributor.author","Huitinga, Inge"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Werner, Hauke B"],["dc.date.accessioned","2022-06-01T09:40:04Z"],["dc.date.available","2022-06-01T09:40:04Z"],["dc.date.issued","2022"],["dc.description.abstract","Human myelin disorders are commonly studied in mouse models. Since both clades evolutionarily diverged approximately 85 million years ago, it is critical to know to what extent the myelin protein composition has remained similar. Here, we use quantitative proteomics to analyze myelin purified from human white matter and find that the relative abundance of the structural myelin proteins PLP, MBP, CNP, and SEPTIN8 correlates well with that in C57Bl/6N mice. Conversely, multiple other proteins were identified exclusively or predominantly in human or mouse myelin. This is exemplified by peripheral myelin protein 2 (PMP2), which was specific to human central nervous system myelin, while tetraspanin-2 (TSPAN2) and connexin-29 (CX29/GJC3) were confined to mouse myelin. Assessing published scRNA-seq-datasets, human and mouse oligodendrocytes display well-correlating transcriptome profiles but divergent expression of distinct genes, including Pmp2, Tspan2, and Gjc3 . A searchable web interface is accessible via www.mpinat.mpg.de/myelin . Species-dependent diversity of oligodendroglial mRNA expression and myelin protein composition can be informative when translating from mouse models to humans."],["dc.description.abstract","Like the electrical wires in our homes, the processes of nerve cells – the axons, thin extensions that project from the cell bodies – need to be insulated to work effectively. This insulation takes the form of layers of a membrane called myelin, which is made of proteins and fats and produced by specialized cells called oligodendrocytes in the brain and the spinal cord. If this layer of insulation becomes damaged, the electrical impulses travelling along the nerves slow down, affecting the ability to walk, speak, see or think. This is the cause of several illnesses, including multiple sclerosis and a group of rare genetic diseases known as leukodystrophies. A lot of the research into myelin, oligodendrocytes and the diseases caused by myelin damage uses mice as an experimental model for humans. Using mice for this type of research is appropriate because of the ethical and technical limitations of experiments on humans. This approach can be highly effective because mice and humans share a large proportion of their genes. However, there are many obvious physical differences between the two species, making it important to determine whether the results of experiments performed in mice are applicable to humans. To do this, it is necessary to understand how myelin differs between these two species at the molecular level. Gargareta, Reuschenbach, Siems, Sun et al. approached this problem by studying the proteins found in myelin isolated from the brains of people who had passed away and donated their organs for scientific research. They used a technique called mass spectrometry, which identifies molecules based on their weight, to produce a list of proteins in human myelin that could then be compared to existing data from mouse myelin. This analysis showed that myelin is very similar in both species, but some proteins only appear in humans or in mice. Gargareta, Reuschenbach, Siems, Sun et al. then compared which genes are turned on in the oligodendrocytes making the myelin. The results of this comparison reflected most of the differences and similarities seen in the myelin proteins. Despite the similarities identified by Gargareta, Reuschenbach, Siems, Sun et al., it became evident that there are unexpected differences between the myelin of humans and mice that will need to be considered when applying results from mice research to humans. To enable this endeavor, Gargareta, Reuschenbach, Siems, Sun et al. have created a searchable web interface of the proteins in myelin and the genes expressed in oligodendrocytes in the two species."],["dc.description.sponsorship"," Deutsche Forschungsgemeinschaft"],["dc.description.sponsorship"," Deutsche Forschungsgemeinschaft"],["dc.description.sponsorship"," Deutsche Forschungsgemeinschaft"],["dc.description.sponsorship"," European Research Council"],["dc.identifier.doi","10.7554/eLife.77019"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/108629"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-572"],["dc.relation.eissn","2050-084X"],["dc.rights.uri","http://creativecommons.org/licenses/by/4.0/"],["dc.title","Conservation and divergence of myelin proteome and oligodendrocyte transcriptome profiles between humans and mice"],["dc.type","journal_article"],["dc.type.internalPublication","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"]]