Simons, Mikael

[["dc.bibliographiccitation.firstpage","277"],["dc.bibliographiccitation.issue","1-2"],["dc.bibliographiccitation.journal","Cell"],["dc.bibliographiccitation.lastpage","290"],["dc.bibliographiccitation.volume","156"],["dc.contributor.author","Snaidero, Nicolas"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Czopka, Tim"],["dc.contributor.author","Hekking, Liesbeth H. P."],["dc.contributor.author","Mathisen, Cliff"],["dc.contributor.author","Verkleij, Dick"],["dc.contributor.author","Goebbels, Sandra"],["dc.contributor.author","Edgar, Julia M."],["dc.contributor.author","Merkler, Doron"],["dc.contributor.author","Lyons, David A."],["dc.contributor.author","Nave, Klaus-Armin"],["dc.contributor.author","Simons, Mikael"],["dc.date.accessioned","2018-11-07T09:45:05Z"],["dc.date.available","2018-11-07T09:45:05Z"],["dc.date.issued","2014"],["dc.description.abstract","Central nervous system myelin is a multilayered membrane sheath generated by oligodendrocytes for rapid impulse propagation. However, the underlying mechanisms of myelin wrapping have remained unclear. Using an integrative approach of live imaging, electron microscopy, and genetics, we show that new myelin membranes are incorporated adjacent to the axon at the innermost tongue. Simultaneously, newly formed layers extend laterally, ultimately leading to the formation of a set of closely apposed paranodal loops. An elaborated system of cytoplasmic channels within the growing myelin sheath enables membrane trafficking to the leading edge. Most of these channels close with ongoing development but can be reopened in adults by experimentally raising phosphatidylinositol-(3,4,5)-triphosphate levels, which reinitiates myelin growth. Our model can explain assembly of myelin as a multilayered structure, abnormal myelin outfoldings in neurological disease, and plasticity of myelin biogenesis observed in adult life."],["dc.identifier.doi","10.1016/j.cell.2013.11.044"],["dc.identifier.isi","000329912200027"],["dc.identifier.pmid","24439382"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/34540"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.relation.issn","1097-4172"],["dc.relation.issn","0092-8674"],["dc.title","Myelin Membrane Wrapping of CNS Axons by PI(3,4,5) P3-Dependent Polarized Growth at the Inner Tongue"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.contributor.author","Djannatian, Minou"],["dc.contributor.author","Weikert, Ulrich"],["dc.contributor.author","Safaiyan, Shima"],["dc.contributor.author","Wrede, Christoph"],["dc.contributor.author","Deichsel, Cassandra"],["dc.contributor.author","Kislinger, Georg"],["dc.contributor.author","Ruhwedel, Torben"],["dc.contributor.author","Campbell, Douglas S."],["dc.contributor.author","van Ham, Tjakko"],["dc.contributor.author","Schmid, Bettina"],["dc.contributor.author","Hegermann, Jan"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Schifferer, Martina"],["dc.contributor.author","Simons, Mikael"],["dc.date.accessioned","2022-08-19T08:17:44Z"],["dc.date.available","2022-08-19T08:17:44Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1101/2021.02.02.429485"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/113031"],["dc.identifier.url","https://rdp.sfb274.de/literature/publications/14"],["dc.relation","TRR 274: Checkpoints of Central Nervous System Recovery"],["dc.relation","TRR 274 | B01: The role of inflammatory cytokine signaling for efficient remyelination in multiple sclerosis"],["dc.relation.workinggroup","RG Schifferer"],["dc.relation.workinggroup","RG Simons (The Biology of Glia in Development and Disease)"],["dc.title","Myelin biogenesis is associated with pathological ultrastructure that is resolved by microglia during development"],["dc.type","preprint"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","47"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Neuroscience"],["dc.bibliographiccitation.lastpage","60"],["dc.bibliographiccitation.volume","24"],["dc.contributor.author","Berghoff, Stefan A."],["dc.contributor.author","Spieth, Lena"],["dc.contributor.author","Sun, Ting"],["dc.contributor.author","Hosang, Leon"],["dc.contributor.author","Schlaphoff, Lennart"],["dc.contributor.author","Depp, Constanze"],["dc.contributor.author","Düking, Tim"],["dc.contributor.author","Winchenbach, Jan"],["dc.contributor.author","Neuber, Jonathan"],["dc.contributor.author","Ewers, David"],["dc.contributor.author","Scholz, Patricia"],["dc.contributor.author","van der Meer, Franziska"],["dc.contributor.author","Cantuti-Castelvetri, Ludovico"],["dc.contributor.author","Sasmita, Andrew O."],["dc.contributor.author","Meschkat, Martin"],["dc.contributor.author","Ruhwedel, Torben"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Sankowski, Roman"],["dc.contributor.author","Prinz, Marco"],["dc.contributor.author","Huitinga, Inge"],["dc.contributor.author","Sereda, Michael W."],["dc.contributor.author","Odoardi, Francesca"],["dc.contributor.author","Ischebeck, Till"],["dc.contributor.author","Simons, Mikael"],["dc.contributor.author","Stadelmann-Nessler, Christine"],["dc.contributor.author","Edgar, Julia M."],["dc.contributor.author","Nave, Klaus-Armin"],["dc.contributor.author","Saher, Gesine"],["dc.date.accessioned","2021-04-14T08:27:05Z"],["dc.date.available","2021-04-14T08:27:05Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1038/s41593-020-00757-6"],["dc.identifier.pmid","33349711"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/82162"],["dc.identifier.url","https://rdp.sfb274.de/literature/publications/11"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","TRR 274: Checkpoints of Central Nervous System Recovery"],["dc.relation","TRR 274 | A04: The role of the meninges in the resolution of acute autoimmune CNS lesions"],["dc.relation.eissn","1546-1726"],["dc.relation.issn","1097-6256"],["dc.relation.workinggroup","RG Cantuti"],["dc.relation.workinggroup","RG Nave (Neurogenetics)"],["dc.relation.workinggroup","RG Odoardi (Echtzeitdarstellung neuroimmunologischer Prozesse)"],["dc.relation.workinggroup","RG Simons (The Biology of Glia in Development and Disease)"],["dc.relation.workinggroup","RG Stadelmann-Nessler"],["dc.title","Microglia facilitate repair of demyelinated lesions via post-squalene sterol synthesis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","314"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Cell Reports"],["dc.bibliographiccitation.lastpage","323"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","Snaidero, Nicolas"],["dc.contributor.author","Velte, Caroline"],["dc.contributor.author","Myllykoski, Matti"],["dc.contributor.author","Raasakka, Arne"],["dc.contributor.author","Ignatev, Alexander"],["dc.contributor.author","Werner, Hauke B."],["dc.contributor.author","Erwig, Michelle S."],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Kursula, Petri"],["dc.contributor.author","Nave, Klaus-Armin"],["dc.contributor.author","Simons, Mikael"],["dc.date.accessioned","2019-07-09T11:43:19Z"],["dc.date.available","2019-07-09T11:43:19Z"],["dc.date.issued","2017"],["dc.description.abstract","The myelin sheath is a multilamellar plasma membrane extension of highly specialized glial cells laid down in regularly spaced segments along axons. Recent studies indicate that myelin is metabolically active and capable of communicating with the underlying axon. To be functionally connected to the neuron, oligodendrocytes maintain non-compacted myelin as cytoplasmic nanochannels. Here, we used high-pressure freezing for electron microscopy to study these cytoplasmic regions within myelin close to their native state. We identified 2,030-cyclic nucleotide 30-phosphodiesterase (CNP), an oligodendrocyte- specific protein previously implicated in the maintenance of axonal integrity, as an essential factor in generating and maintaining cytoplasm within the myelin compartment. We provide evidence that CNP directly associates with and organizes the actin cytoskeleton, thereby providing an intracellular strut that counteracts membrane compaction by myelin basic protein (MBP). Our study provides amolecular and structural framework for understanding how myelin maintains its cytoplasm to function as an active axon-glial unit."],["dc.identifier.doi","10.1016/j.celrep.2016.12.053"],["dc.identifier.pmid","28076777"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14431"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/58862"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation","info:eu-repo/grantAgreement/EC/FP7/647168/EU/Cell biology of myelin wrapping, plasticity and turnover/Myelination"],["dc.relation","info:eu-repo/grantAgreement/EC/FP7/269020/EU/The role of myelinating glia in preserving axon function/AXOGLIA"],["dc.relation","info:eu-repo/grantAgreement/EC/FP7/671048/EU/Myelinic nanochannels in neurodegenerative diseases/MyeliNANO"],["dc.relation.issn","2211-1247"],["dc.rights","CC BY-NC-ND 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/4.0"],["dc.title","Antagonistic Functions of MBP and CNP Establish Cytosolic Channels in CNS Myelin"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","223"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","The Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","232"],["dc.bibliographiccitation.volume","189"],["dc.contributor.author","Hsu, Chieh"],["dc.contributor.author","Morohashi, Yuichi"],["dc.contributor.author","Yoshimura, Shin-ichiro"],["dc.contributor.author","Manrique-Hoyos, Natalia"],["dc.contributor.author","Jung, SangYong"],["dc.contributor.author","Lauterbach, Marcel A."],["dc.contributor.author","Bakhti, Mostafa"],["dc.contributor.author","Gronborg, Mads"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Rhee, JeongSeop"],["dc.contributor.author","Barr, Francis A."],["dc.contributor.author","Simons, Mikael"],["dc.date.accessioned","2018-11-07T08:44:01Z"],["dc.date.available","2018-11-07T08:44:01Z"],["dc.date.issued","2010"],["dc.description.abstract","Oligodendrocytes secrete vesicles into the extracellular space, where they might play a role in neuron-glia communication. These exosomes are small vesicles with a diameter of 50-100 nm that are formed within multivesicular bodies and are released after fusion with the plasma membrane. The intracellular pathways that generate exosomes are poorly defined. Because Rab family guanosine triphosphatases (GTPases) together with their regulators are important membrane trafficking organizers, we investigated which Rab GTPase-activating proteins interfere with exosome release. We find that TBC1D10A-C regulate exosome secretion in a catalytic activity-dependent manner. We show that Rab35 is the target of TBC1D10A-C and that the inhibition of Rab35 function leads to intracellular accumulation of endosomal vesicles and impairs exosome secretion. Rab35 localizes to the surface of oligodendroglia in a GTP-dependent manner, where it increases the density of vesicles, suggesting a function in docking or tethering. These findings provide a basis for understanding the biogenesis and function of exosomes in the central nervous system."],["dc.identifier.doi","10.1083/jcb.200911018"],["dc.identifier.isi","000276825200007"],["dc.identifier.pmid","20404108"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/20111"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Rockefeller Univ Press"],["dc.relation.issn","0021-9525"],["dc.title","Regulation of exosome secretion by Rab35 and its GTPase-activating proteins TBC1D10A-C"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","26279"],["dc.bibliographiccitation.issue","34"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","26288"],["dc.bibliographiccitation.volume","285"],["dc.contributor.author","Strauss, Katrin"],["dc.contributor.author","Goebel, Cornelia"],["dc.contributor.author","Runz, Heiko"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Weiss, Sievert"],["dc.contributor.author","Feussner, Ivo"],["dc.contributor.author","Simons, Mikael"],["dc.contributor.author","Schneider, Anja"],["dc.date.accessioned","2018-11-07T08:40:18Z"],["dc.date.available","2018-11-07T08:40:18Z"],["dc.date.issued","2010"],["dc.description.abstract","Niemann-Pick type C1 disease is an autosomal-recessive lysosomal storage disorder. Loss of function of the npc1 gene leads to abnormal accumulation of free cholesterol and sphingolipids within the late endosomal and lysosomal compartments resulting in progressive neurodegeneration and dysmyelination. Here, we show that oligodendroglial cells secrete cholesterol by exosomes when challenged with cholesterol or U18666A, which induces late endosomal cholesterol accumulation. Up-regulation of exosomal cholesterol release was also observed after siRNA-mediated knockdown of NPC1 and in fibroblasts derived from NPC1 patients and could be reversed by expression of wild-type NPC1. We provide evidence that exosomal cholesterol secretion depends on the presence of flotillin. Our findings indicate that exosomal release of cholesterol may serve as a cellular mechanism to partially bypass the traffic block that results in the toxic lysosomal cholesterol accumulation in Niemann-Pick type C1 disease. Furthermore, we suggest that secretion of cholesterol by exosomes contributes to maintain cellular cholesterol homeostasis."],["dc.identifier.doi","10.1074/jbc.M110.134775"],["dc.identifier.isi","000280921000045"],["dc.identifier.pmid","20554533"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/19200"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Biochemistry Molecular Biology Inc"],["dc.relation.issn","0021-9258"],["dc.title","Exosome Secretion Ameliorates Lysosomal Storage of Cholesterol in Niemann-Pick Type C Disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","314"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Cell Reports"],["dc.bibliographiccitation.lastpage","322"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Weil, Marie-Theres"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Winkler, Anne"],["dc.contributor.author","Ruhwedel, Torben"],["dc.contributor.author","Wrzos, Claudia"],["dc.contributor.author","Romanelli, Elisa"],["dc.contributor.author","Bennett, Jeffrey L."],["dc.contributor.author","Enz, Lukas"],["dc.contributor.author","Goebels, Norbert"],["dc.contributor.author","Nave, Klaus-Armin"],["dc.contributor.author","Kerschensteiner, Martin"],["dc.contributor.author","Schaeren-Wiemers, Nicole"],["dc.contributor.author","Stadelmann, Christine"],["dc.contributor.author","Simons, Mikael"],["dc.date.accessioned","2018-11-07T10:11:38Z"],["dc.date.available","2018-11-07T10:11:38Z"],["dc.date.issued","2016"],["dc.description.abstract","Breakdown of myelin sheaths is a pathological hallmark of several autoimmune diseases of the nervous system. We employed autoantibody-mediated animal models of demyelinating diseases, including a rat model of neuromyelitis optica (NMO), to target myelin and found that myelin lamellae are broken down into vesicular structures at the innermost region of the myelin sheath. We demonstrated that myelin basic proteins (MBP), which form a polymer in between the myelin membrane layers, are targeted in these models. Elevation of intracellular Ca2+ levels resulted in MBP network disassembly and myelin vesiculation. We propose that the aberrant phase transition of MBP molecules from their cohesive to soluble and non-adhesive state is a mechanism triggering myelin breakdown in NMO and possibly in other demyelinating diseases."],["dc.identifier.doi","10.1016/j.celrep.2016.06.008"],["dc.identifier.isi","000380262300005"],["dc.identifier.pmid","27346352"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13675"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/40088"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.relation.issn","2211-1247"],["dc.rights","CC BY-NC-ND 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/4.0"],["dc.title","Loss of Myelin Basic Protein Function Triggers Myelin Breakdown in Models of Demyelinating Diseases"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3143"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences of the United States of America"],["dc.bibliographiccitation.lastpage","3148"],["dc.bibliographiccitation.volume","110"],["dc.contributor.author","Bakhti, Mostafa"],["dc.contributor.author","Snaidero, Nicolas"],["dc.contributor.author","Schneider, David"],["dc.contributor.author","Aggarwal, Shweta"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Eckhardt, Matthias"],["dc.contributor.author","Nave, Klaus-Armin"],["dc.contributor.author","Simons, Mikael"],["dc.date.accessioned","2018-11-07T09:28:05Z"],["dc.date.available","2018-11-07T09:28:05Z"],["dc.date.issued","2013"],["dc.description.abstract","During the development of the central nervous system (CNS), oligodendrocytes wrap their plasma membrane around axons to form a multilayered stack of tightly attached membranes. Although in-tracellular myelin compaction and the role of myelin basic protein has been investigated, the forces that mediate the close interaction of myelin membranes at their external surfaces are poorly understood. Such extensive bilayer-bilayer interactions are usually prevented by repulsive forces generated by the glycocalyx, a dense and confluent layer of large and negatively charged oligosaccharides. Here we investigate the molecular mechanisms underlying myelin adhesion and compaction in the CNS. We revisit the role of the proteolipid protein and analyze the contribution of oligosaccharides using cellular assays, biophysical tools, and transgenic mice. We observe that differentiation of oligodendrocytes is accompanied by a striking down-regulation of components of their glycocalyx. Both in vitro and in vivo experiments indicate that the adhesive properties of the proteolipid protein, along with the reduction of sialic acid residues from the cell surface, orchestrate myelin membrane adhesion and compaction in the CNS. We suggest that loss of electrostatic cell-surface repulsion uncovers weak and unspecific attractive forces in the bilayer that bring the extracellular surfaces of a membrane into close contact over long distances."],["dc.identifier.doi","10.1073/pnas.1220104110"],["dc.identifier.isi","000315954400104"],["dc.identifier.pmid","23382229"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/30690"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Natl Acad Sciences"],["dc.relation.issn","0027-8424"],["dc.title","Loss of electrostatic cell-surface repulsion mediates myelin membrane adhesion and compaction in the central nervous system"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","5037"],["dc.bibliographiccitation.issue","21"],["dc.bibliographiccitation.journal","EMBO Journal"],["dc.bibliographiccitation.lastpage","5048"],["dc.bibliographiccitation.volume","25"],["dc.contributor.author","Fitzner, Dirk"],["dc.contributor.author","Schneider, Anja"],["dc.contributor.author","Kippert, Angelika"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Willig, Katrin I."],["dc.contributor.author","Hell, Stefan"],["dc.contributor.author","Bunt, Gertrude"],["dc.contributor.author","Gaus, Katharina"],["dc.contributor.author","Simons, Mikael"],["dc.date.accessioned","2017-09-07T11:52:27Z"],["dc.date.available","2017-09-07T11:52:27Z"],["dc.date.issued","2006"],["dc.description.abstract","During vertebrate development, oligodendrocytes wrap their plasma membrane around axons to produce myelin, a specialized membrane highly enriched in galactosylceramide (GalC) and cholesterol. Here, we studied the formation of myelin membrane sheets in a neuron-glia co-culture system. We applied different microscopy techniques to visualize lipid packing and dynamics in the oligodendroglial plasma membrane. We used the fluorescent dye Laurdan to examine the lipid order with two-photon microscopy and observed that neurons induce a dramatic lipid condensation of the oligodendroglial membrane. On a nanoscale resolution, using stimulated emission depletion and fluorescence resonance energy transfer microscopy, we demonstrated a neuronal-dependent clustering of GalC in oligodendrocytes. Most importantly these changes in lipid organization of the oligodendroglial plasma membrane were not observed in shiverer mice that do not express the myelin basic protein. Our data demonstrate that neurons induce the condensation of the myelin-forming bilayer in oligodendrocytes and that MBP is involved in this process of plasma membrane rearrangement. We propose that this mechanism is essential for myelin to perform its insulating function during nerve conduction."],["dc.identifier.doi","10.1038/sj.emboj.7601376"],["dc.identifier.gro","3143596"],["dc.identifier.isi","000242214900001"],["dc.identifier.pmid","17036049"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1128"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0261-4189"],["dc.title","Myelin basic protein-dependent plasma membrane reorganization in the formation of myelin"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","684"],["dc.bibliographiccitation.issue","6376"],["dc.bibliographiccitation.journal","Science"],["dc.bibliographiccitation.lastpage","688"],["dc.bibliographiccitation.volume","359"],["dc.contributor.author","Cantuti-Castelvetri, Ludovico"],["dc.contributor.author","Fitzner, Dirk"],["dc.contributor.author","Bosch-Queralt, Mar"],["dc.contributor.author","Weil, Marie-Theres"],["dc.contributor.author","Su, Minhui"],["dc.contributor.author","Sen, Paromita"],["dc.contributor.author","Ruhwedel, Torben"],["dc.contributor.author","Mitkovski, Miso"],["dc.contributor.author","Trendelenburg, George"],["dc.contributor.author","Lütjohann, Dieter"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Simons, Mikael"],["dc.date.accessioned","2020-12-10T18:36:42Z"],["dc.date.available","2020-12-10T18:36:42Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1126/science.aan4183"],["dc.identifier.eissn","1095-9203"],["dc.identifier.issn","0036-8075"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/76715"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Defective cholesterol clearance limits remyelination in the aged central nervous system"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]