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.bibliographiccitation.firstpage","33"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Cell and Tissue Research"],["dc.bibliographiccitation.lastpage","47"],["dc.bibliographiccitation.volume","352"],["dc.contributor.author","Schneider, Anja"],["dc.contributor.author","Simons, Mikael"],["dc.date.accessioned","2019-07-09T11:39:48Z"],["dc.date.available","2019-07-09T11:39:48Z"],["dc.date.issued","2012"],["dc.description.abstract","The intercellular transfer of misfolded proteins has received increasing attention in various neurodegenerative diseases characterized by the aggregation of specific proteins, as observed in Alzheimer’s, Parkinson’s and Huntington’s disease. One hypothesis holds that intercellular dissemination of these aggregates within the central nervous system results in the seeded assembly of the cognate soluble protein in target cells, similar to that proposed for transmissible prion diseases. The molecular mechanisms underlying the intercellular transfer of these proteinaceous aggregates are poorly understood. Various transfer modes of misfolded proteins including continuous cell-cell contacts such as nanotubes, unconventional secretion or microvesicle/exosome-associated dissemination have been suggested. Cells can release proteins, lipids and nucleic acids by vesicular exocytosis pathways destined for horizontal transfer. Encapsulation into microvesicular/exosomal vehicles not only protects these molecules from degradation and dilution in the extracellular space but also facilitates delivery over large distances, e.g. within the blood flow or interstitial fluid. Specific surface ligands might allow the highly efficient and targeted uptake of these vesicles by recipient cells. In this review, we focus on the cell biology and function of neuronal microvesicles/exosomes and discuss the evidence for pathogenic intercellular protein transfer mediated by vesicular carriers."],["dc.identifier.doi","10.1007/s00441-012-1428-2"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10314"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/58038"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.publisher","Springer"],["dc.publisher.place","Berlin/Heidelberg"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Exosomes: vesicular carriers for intercellular communication in neurodegenerative disorders"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","2123"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","4"],["dc.contributor.author","Grapp, Marcel"],["dc.contributor.author","Wrede, Arne"],["dc.contributor.author","Schweizer, Michaela"],["dc.contributor.author","Huewel, Sabine"],["dc.contributor.author","Galla, Hans-Joachim"],["dc.contributor.author","Snaidero, Nicolas"],["dc.contributor.author","Simons, Mikael"],["dc.contributor.author","Bueckers, Johanna"],["dc.contributor.author","Low, Philip S."],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Gärtner, Jutta"],["dc.contributor.author","Steinfeld, Robert"],["dc.date.accessioned","2017-09-07T11:47:39Z"],["dc.date.available","2017-09-07T11:47:39Z"],["dc.date.issued","2013"],["dc.description.abstract","Loss of folate receptor-alpha function is associated with cerebral folate transport deficiency and childhood-onset neurodegeneration. To clarify the mechanism of cerebral folate transport at the blood-cerebrospinal fluid barrier, we investigate the transport of 5-methyltetrahydrofolate in polarized cells. Here we identify folate receptor-alpha-positive intralumenal vesicles within multivesicular bodies and demonstrate the directional cotransport of human folate receptor-alpha, and labelled folate from the basolateral to the apical membrane in rat choroid plexus cells. Both the apical medium of folate receptor-alpha-transfected rat choroid plexus cells and human cerebrospinal fluid contain folate receptor-alpha-positive exosomes. Loss of folate receptor-alpha-expressing cerebrospinal fluid exosomes correlates with severely reduced 5-methyltetrahydrofolate concentration, corroborating the importance of the folate receptor-alpha-mediated folate transport in the cerebrospinal fluid. Intraventricular injections of folate receptor-alpha-positive and -negative exosomes into mouse brains demonstrate folate receptor-alpha-dependent delivery of exosomes into the brain parenchyma. Our results unravel a new pathway of folate receptor-alpha-dependent exosome-mediated folate delivery into the brain parenchyma and opens new avenues for cerebral drug targeting."],["dc.identifier.doi","10.1038/ncomms3123"],["dc.identifier.gro","3142330"],["dc.identifier.isi","000323715900003"],["dc.identifier.pmid","23828504"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/9774"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7086"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","2041-1723"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Choroid plexus transcytosis and exosome shuttling deliver folate into brain parenchyma"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","submitted_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","13275"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Romanelli, Elisa"],["dc.contributor.author","Merkler, Doron"],["dc.contributor.author","Mezydlo, Aleksandra"],["dc.contributor.author","Weil, Marie-Theres"],["dc.contributor.author","Weber, Martin S."],["dc.contributor.author","Nikic, Ivana"],["dc.contributor.author","Potz, Stephanie"],["dc.contributor.author","Meinl, Edgar"],["dc.contributor.author","Matznick, Florian E. H."],["dc.contributor.author","Kreutzfeldt, Mario"],["dc.contributor.author","Ghanem, Alexander"],["dc.contributor.author","Conzelmann, Karl-Klaus"],["dc.contributor.author","Metz, Imke"],["dc.contributor.author","Brueck, Wolfgang"],["dc.contributor.author","Routh, Matthew"],["dc.contributor.author","Simons, Mikael"],["dc.contributor.author","Bishop, Derron"],["dc.contributor.author","Misgeld, Thomas"],["dc.contributor.author","Kerschensteiner, Martin"],["dc.date.accessioned","2018-11-07T10:05:43Z"],["dc.date.available","2018-11-07T10:05:43Z"],["dc.date.issued","2016"],["dc.description.abstract","Oligodendrocyte damage is a central event in the pathogenesis of the common neuro-inflammatory condition, multiple sclerosis (MS). Where and how oligodendrocyte damage is initiated in MS is not completely understood. Here, we use a combination of light and electron microscopy techniques to provide a dynamic and highly resolved view of oligodendrocyte damage in neuroinflammatory lesions. We show that both in MS and in its animal model structural damage is initiated at the myelin sheaths and only later spreads to the oligodendrocyte cell body. Early myelin damage itself is characterized by the formation of local myelin out-foldings-'myelinosomes'-, which are surrounded by phagocyte processes and promoted in their formation by anti-myelin antibodies and complement. The presence of myelinosomes in actively demyelinating MS lesions suggests that oligodendrocyte damage follows a similar pattern in the human disease, where targeting demyelination by therapeutic interventions remains a major open challenge."],["dc.identifier.doi","10.1038/ncomms13275"],["dc.identifier.isi","000387837900001"],["dc.identifier.pmid","27848954"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13963"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38953"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","2041-1723"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Myelinosome formation represents an early stage of oligodendrocyte damage in multiple sclerosis and its animal model"],["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","512"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Current Opinion in Cell Biology"],["dc.bibliographiccitation.lastpage","519"],["dc.bibliographiccitation.volume","25"],["dc.contributor.author","Simons, Mikael"],["dc.contributor.author","Lyons, David A."],["dc.date.accessioned","2018-11-07T09:21:50Z"],["dc.date.available","2018-11-07T09:21:50Z"],["dc.date.issued","2013"],["dc.description.abstract","The formation of myelin in the central nervous system is a multistep process that involves coordinated cell cell interactions and dramatic changes in plasma membrane architecture. First, oligodendrocytes send our numerous highly ramified processes to sample the axonal environment and decide which axon(s) to select for myelination. After this decision is made and individual axon to oligodendrocyte contact has been established, the exploratory process of the oligodendrocyte is converted into a flat sheath that spreads and winds along and around its associated axon to generate a multilayered membrane stack. By compaction of the opposing extracellular layers of membrane and extrusion of almost all cytoplasm from the intracellular domain of the sheath, the characteristic membrane-rich multi-lamellar structure of myelin is formed. Here we highlight recent advances in identifying biophysical and signalling based mechanisms that are involved in axonal selection and myelin sheath generation by oligodendrocytes. A thorough understanding of the mechanisms underlying these events is a prerequisite for the design of novel myelin repair strategies in demyelinating and dysmyelinating diseases."],["dc.identifier.doi","10.1016/j.ceb.2013.04.007"],["dc.identifier.isi","000323084700017"],["dc.identifier.pmid","23707197"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29201"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Current Biology Ltd"],["dc.relation.issn","0955-0674"],["dc.title","Axonal selection and myelin sheath generation 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","937"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","The Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","948"],["dc.bibliographiccitation.volume","172"],["dc.contributor.author","Trajkovic, K."],["dc.contributor.author","Dhaunchak, A. S."],["dc.contributor.author","Goncalves, J. T."],["dc.contributor.author","Wenzel, D."],["dc.contributor.author","Schneider, Anja"],["dc.contributor.author","Bunt, Gertrude"],["dc.contributor.author","Nave, K. A."],["dc.contributor.author","Simons, Mikael"],["dc.date.accessioned","2018-11-07T10:06:22Z"],["dc.date.available","2018-11-07T10:06:22Z"],["dc.date.issued","2006"],["dc.description.abstract","During vertebrate brain development, axons are enwrapped by myelin, an insulating membrane produced by oligodendrocytes. Neuron-derived signaling molecules are temporally and spatially required to coordinate oligodendrocyte differentiation. In this study, we show that neurons regulate myelin membrane trafficking in oligodendrocytes. In the absence of neurons, the major myelin membrane protein, the proteolipid protein (PLP), is internalized and stored in late endosomes/lysosomes (LEs/Ls) by a cholesterol-dependent and clathrin-independent endocytosis pathway that requires actin and the RhoA guanosine triphosphatase. Upon maturation, the rate of endocytosis is reduced, and a cAMP-dependent neuronal signal triggers the transport of PLP from LEs/Ls to the plasma membrane. These findings reveal a fundamental and novel role of LEs/Ls in oligodendrocytes: to store and release PLP in a regulated fashion. The release of myelin membrane from LEs/Ls by neuronal signals may represent a mechanism to control myelin membrane growth."],["dc.identifier.doi","10.1083/jcb.200509022"],["dc.identifier.isi","000235971900018"],["dc.identifier.pmid","16520383"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39080"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Rockefeller Univ Press"],["dc.relation.issn","0021-9525"],["dc.title","Neuron to glia signaling triggers myelin membrane exocytosis from endosomal storage sites"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","856"],["dc.bibliographiccitation.issue","6518"],["dc.bibliographiccitation.journal","Science"],["dc.bibliographiccitation.lastpage","860"],["dc.bibliographiccitation.volume","370"],["dc.contributor.author","Cantuti-Castelvetri, Ludovico"],["dc.contributor.author","Ojha, Ravi"],["dc.contributor.author","Pedro, Liliana D."],["dc.contributor.author","Djannatian, Minou"],["dc.contributor.author","Franz, Jonas"],["dc.contributor.author","Kuivanen, Suvi"],["dc.contributor.author","van der Meer, Franziska"],["dc.contributor.author","Kallio, Katri"],["dc.contributor.author","Kaya, Tuğberk"],["dc.contributor.author","Anastasina, Maria"],["dc.contributor.author","Smura, Teemu"],["dc.contributor.author","Levanov, Lev"],["dc.contributor.author","Szirovicza, Leonora"],["dc.contributor.author","Tobi, Allan"],["dc.contributor.author","Kallio-Kokko, Hannimari"],["dc.contributor.author","Österlund, Pamela"],["dc.contributor.author","Joensuu, Merja"],["dc.contributor.author","Meunier, Frédéric A."],["dc.contributor.author","Butcher, Sarah J."],["dc.contributor.author","Winkler, Martin Sebastian"],["dc.contributor.author","Mollenhauer, Brit"],["dc.contributor.author","Helenius, Ari"],["dc.contributor.author","Gokce, Ozgun"],["dc.contributor.author","Teesalu, Tambet"],["dc.contributor.author","Hepojoki, Jussi"],["dc.contributor.author","Vapalahti, Olli"],["dc.contributor.author","Stadelmann, Christine"],["dc.contributor.author","Balistreri, Giuseppe"],["dc.contributor.author","Simons, Mikael"],["dc.date.accessioned","2021-04-14T08:31:26Z"],["dc.date.available","2021-04-14T08:31:26Z"],["dc.date.issued","2020"],["dc.description.abstract","The causative agent of coronavirus disease 2019 (COVID-19) is the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). For many viruses, tissue tropism is determined by the availability of virus receptors and entry cofactors on the surface of host cells. In this study, we found that neuropilin-1 (NRP1), known to bind furin-cleaved substrates, significantly potentiates SARS-CoV-2 infectivity, an effect blocked by a monoclonal blocking antibody against NRP1. A SARS-CoV-2 mutant with an altered furin cleavage site did not depend on NRP1 for infectivity. Pathological analysis of olfactory epithelium obtained from human COVID-19 autopsies revealed that SARS-CoV-2 infected NRP1-positive cells facing the nasal cavity. Our data provide insight into SARS-CoV-2 cell infectivity and define a potential target for antiviral intervention."],["dc.identifier.doi","10.1126/science.abd2985"],["dc.identifier.pmid","33082293"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83594"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/73"],["dc.identifier.url","https://rdp.sfb274.de/literature/publications/8"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","TRR 274: Checkpoints of Central Nervous System Recovery"],["dc.relation","TRR 274 | A06: The role of lipid-sensing nuclear receptors as checkpoints in regulating phagocyte function during recovery from demyelinating injury"],["dc.relation.eissn","1095-9203"],["dc.relation.issn","0036-8075"],["dc.relation.workinggroup","RG Stadelmann-Nessler"],["dc.relation.workinggroup","RG Cantuti"],["dc.relation.workinggroup","RG Gokce (Systems Neuroscience – Cell Diversity)"],["dc.relation.workinggroup","RG Simons (The Biology of Glia in Development and Disease)"],["dc.rights","CC BY 4.0"],["dc.title","Neuropilin-1 facilitates SARS-CoV-2 cell entry and infectivity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["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","132"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Cell Biology"],["dc.bibliographiccitation.lastpage","+"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","Baskin, Jeremy M."],["dc.contributor.author","Wu, X."],["dc.contributor.author","Christiano, Romain"],["dc.contributor.author","Oh, Michael S."],["dc.contributor.author","Schauder, Curtis M."],["dc.contributor.author","Gazzerro, Elisabetta"],["dc.contributor.author","Messa, Mirko"],["dc.contributor.author","Baldassari, Simona"],["dc.contributor.author","Assereto, Stefania"],["dc.contributor.author","Biancheri, Roberta"],["dc.contributor.author","Zara, Federico"],["dc.contributor.author","Minetti, Carlo"],["dc.contributor.author","Raimondi, Andrea"],["dc.contributor.author","Simons, Mikael"],["dc.contributor.author","Walther, Tobias C."],["dc.contributor.author","Reinisch, Karin M."],["dc.contributor.author","De Camilli, Pietro"],["dc.date.accessioned","2018-11-07T10:21:43Z"],["dc.date.available","2018-11-07T10:21:43Z"],["dc.date.issued","2016"],["dc.description.abstract","Genetic defects in myelin formation and maintenance cause leukodystrophies, a group of white matter diseases whose mechanistic underpinnings are poorly understood(1,2). Hypomyelination and congenital cataract (HCC), one of these disorders, is caused by mutations in FAM126A, a gene of unknown function(3). We show that FAM126A, also known as hyccin, regulates the synthesis of phosphatidylinositol 4-phosphate (PtdIns(4)P), a determinant of plasma membrane identity(4-6). HCC patient fibroblasts exhibit reduced PtdIns(4)P levels. FAM126A is an intrinsic component of the plasma membrane phosphatidylinositol 4-kinase complex that comprises PI4KIII alpha and its adaptors TTC7 and EFR3 (refs 5,7). A FAM126A TTC7 alpha-crystal structure reveals an all-alpha-helical heterodimer with a large protein protein interface and a conserved surface that may mediate binding to PI4KIII alpha. Absence of FAM126A, the predominant FAM126 isoform in oligodendrocytes, destabilizes the PI4KIII alpha complex in mouse brain and patient fibroblasts. We propose that HCC pathogenesis involves defects in PtdIns(4)P production in oligodendrocytes, whose specialized function requires massive plasma membrane expansion and thus generation of PtdIns(4)P and downstream phosphoinositides(8-11). Our results point to a role for FAM126A in supporting myelination, an important process in development and also following acute exacerbations in multiple sclerosis(12-14)."],["dc.identifier.doi","10.1038/ncb3271"],["dc.identifier.isi","000367030900006"],["dc.identifier.pmid","26571211"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/42143"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","1476-4679"],["dc.relation.issn","1465-7392"],["dc.title","The leukodystrophy protein FAM126A (hyccin) regulates PtdIns(4)P synthesis at the plasma membrane"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","101141"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","STAR Protocols"],["dc.bibliographiccitation.volume","3"],["dc.contributor.author","Bosch-Queralt, Mar"],["dc.contributor.author","Tiwari, Vini"],["dc.contributor.author","Damkou, Alkmini"],["dc.contributor.author","Vaculčiaková, Lenka"],["dc.contributor.author","Alexopoulos, Ioannis"],["dc.contributor.author","Simons, Mikael"],["dc.date.accessioned","2022-08-19T07:37:21Z"],["dc.date.available","2022-08-19T07:37:21Z"],["dc.date.issued","2022"],["dc.description.abstract","Lysolecithin injections into the white matter tracts of the central nervous system are a valuable tool to study remyelination, but evaluating the resulting demyelinating lesion size is challenging. Here, we present a protocol to consistently measure the volume of demyelination and remyelination in mice following brain lysolecithin injections. We describe serial sectioning of the lesion, followed by the evaluation of the demyelinated area in two-dimensional images. We then detail the computation of the volume using our own automated iPython script. For complete details on the use and execution of this profile, please refer to Bosch-Queralt et al. (2021)."],["dc.identifier.doi","10.1016/j.xpro.2022.101141"],["dc.identifier.pmid","35141565"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/113022"],["dc.identifier.url","https://rdp.sfb274.de/literature/publications/57"],["dc.language.iso","en"],["dc.relation","TRR 274: Checkpoints of Central Nervous System Recovery"],["dc.relation.eissn","2666-1667"],["dc.relation.workinggroup","RG Simons (The Biology of Glia in Development and Disease)"],["dc.title","A fluorescence microscopy-based protocol for volumetric measurement of lysolecithin lesion-associated de- and re-myelination in mouse brain"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]