Göbbels, Sandra

[["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","647"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Experimental Dermatology"],["dc.bibliographiccitation.lastpage","649"],["dc.bibliographiccitation.volume","25"],["dc.contributor.author","Schiller, Stina A."],["dc.contributor.author","Seebode, Christina"],["dc.contributor.author","Wieser, Georg L."],["dc.contributor.author","Goebbels, Sandra"],["dc.contributor.author","Ruhwedel, Torben"],["dc.contributor.author","Horowitz, Mia"],["dc.contributor.author","Rapaport, Debora"],["dc.contributor.author","Sarig, Ofer"],["dc.contributor.author","Sprecher, Eli"],["dc.contributor.author","Emmert, Steffen"],["dc.date.accessioned","2018-11-07T10:11:12Z"],["dc.date.available","2018-11-07T10:11:12Z"],["dc.date.issued","2016"],["dc.identifier.doi","10.1111/exd.13050"],["dc.identifier.isi","000380705500016"],["dc.identifier.pmid","27095090"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/40000"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1600-0625"],["dc.relation.issn","0906-6705"],["dc.title","Non-keratinocyte SNAP29 influences epidermal differentiation and hair follicle formation in mice"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["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","225"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Neuroscience"],["dc.bibliographiccitation.lastpage","233"],["dc.bibliographiccitation.volume","31"],["dc.contributor.author","Reich, Arno"],["dc.contributor.author","Spering, Christopher"],["dc.contributor.author","Gertz, Karen"],["dc.contributor.author","Harms, Christoph"],["dc.contributor.author","Gerhardt, Ellen"],["dc.contributor.author","Kronenberg, Golo"],["dc.contributor.author","Nave, Klaus A."],["dc.contributor.author","Schwab, Markus"],["dc.contributor.author","Tauber, Simone C."],["dc.contributor.author","Drinkut, Anja"],["dc.contributor.author","Harms, Kristian"],["dc.contributor.author","Beier, Chrstioph P."],["dc.contributor.author","Voigt, Aaron"],["dc.contributor.author","Goebbels, Sandra"],["dc.contributor.author","Endres, Matthias"],["dc.contributor.author","Schulz, Joerg B."],["dc.date.accessioned","2018-11-07T09:00:08Z"],["dc.date.available","2018-11-07T09:00:08Z"],["dc.date.issued","2011"],["dc.description.abstract","Death receptor (DR) signaling has a major impact on the outcome of numerous neurological diseases, including ischemic stroke. DRs mediate not only cell death signals, but also proinflammatory responses and cell proliferation. Identification of regulatory proteins that control the switch between apoptotic and alternative DR signaling opens new therapeutic opportunities. Fas apoptotic inhibitory molecule 2 (Faim2) is an evolutionary conserved, neuron-specific inhibitor of Fas/CD95-mediated apoptosis. To investigate its role during development and in disease models, we generated Faim2-deficient mice. The ubiquitous null mutation displayed a viable and fertile phenotype without overt deficiencies. However, lack of Faim2 caused an increase in susceptibility to combined oxygen-glucose deprivation in primary neurons in vitro as well as in caspase-associated cell death, stroke volume, and neurological impairment after cerebral ischemia in vivo. These processes were rescued by lentiviral Faim2 gene transfer. In summary, we provide evidence that Faim2 is a novel neuroprotective molecule in the context of cerebral ischemia."],["dc.identifier.doi","10.1523/JNEUROSCI.2188-10.2011"],["dc.identifier.isi","000285915100026"],["dc.identifier.pmid","21209208"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/24077"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Soc Neuroscience"],["dc.relation.issn","0270-6474"],["dc.title","Fas/CD95 Regulatory Protein Faim2 Is Neuroprotective after Transient Brain Ischemia"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Molecular Psychiatry"],["dc.contributor.author","Butt, Umer Javed"],["dc.contributor.author","Steixner-Kumar, Agnes A."],["dc.contributor.author","Depp, Constanze"],["dc.contributor.author","Sun, Ting"],["dc.contributor.author","Hassouna, Imam"],["dc.contributor.author","Wüstefeld, Liane"],["dc.contributor.author","Arinrad, Sahab"],["dc.contributor.author","Zillmann, Matthias R."],["dc.contributor.author","Schopf, Nadine"],["dc.contributor.author","Fernandez Garcia-Agudo, Laura"],["dc.contributor.author","Mohrmann, Leonie"],["dc.contributor.author","Bode, Ulli"],["dc.contributor.author","Ronnenberg, Anja"],["dc.contributor.author","Hindermann, Martin"],["dc.contributor.author","Goebbels, Sandra"],["dc.contributor.author","Bonn, Stefan"],["dc.contributor.author","Katschinski, Dörthe M."],["dc.contributor.author","Miskowiak, Kamilla W."],["dc.contributor.author","Nave, Klaus-Armin"],["dc.contributor.author","Ehrenreich, Hannelore"],["dc.date.accessioned","2021-04-14T08:28:40Z"],["dc.date.available","2021-04-14T08:28:40Z"],["dc.date.issued","2021"],["dc.description.abstract","Physical activity and cognitive challenge are established non-invasive methods to induce comprehensive brain activation and thereby improve global brain function including mood and emotional well-being in healthy subjects and in patients. However, the mechanisms underlying this experimental and clinical observation and broadly exploited therapeutic tool are still widely obscure. Here we show in the behaving brain that physiological (endogenous) hypoxia is likely a respective lead mechanism, regulating hippocampal plasticity via adaptive gene expression. A refined transgenic approach in mice, utilizing the oxygen-dependent degradation (ODD) domain of HIF-1α fused to CreERT2 recombinase, allows us to demonstrate hypoxic cells in the performing brain under normoxia and motor-cognitive challenge, and spatially map them by light-sheet microscopy, all in comparison to inspiratory hypoxia as strong positive control. We report that a complex motor-cognitive challenge causes hypoxia across essentially all brain areas, with hypoxic neurons particularly abundant in the hippocampus. These data suggest an intriguing model of neuroplasticity, in which a specific task-associated neuronal activity triggers mild hypoxia as a local neuron-specific as well as a brain-wide response, comprising indirectly activated neurons and non-neuronal cells."],["dc.identifier.doi","10.1038/s41380-020-00988-w"],["dc.identifier.pmid","33564132"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/82678"],["dc.identifier.url","https://rdp.sfb274.de/literature/publications/31"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/104"],["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 | C01: Oligodendroglial NMDA receptors and NMDAR1 autoantibodies as determinants of axonal integrity in neuropsychiatric disease"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | Z02: Integrative Datenanalyse und -interpretation. Generierung einer synaptisch-integrativen Datenstrategie (SynIDs)"],["dc.relation.eissn","1476-5578"],["dc.relation.issn","1359-4184"],["dc.relation.workinggroup","RG Ehrenreich (Clinical Neuroscience)"],["dc.relation.workinggroup","RG Nave (Neurogenetics)"],["dc.relation.workinggroup","RG Bonn"],["dc.rights","CC BY 4.0"],["dc.title","Hippocampal neurons respond to brain activity with functional hypoxia"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","486"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","EMBO Molecular Medicine"],["dc.bibliographiccitation.lastpage","499"],["dc.bibliographiccitation.volume","4"],["dc.contributor.author","Goebbels, Sandra"],["dc.contributor.author","Oltrogge, Jan H."],["dc.contributor.author","Wolfer, Susanne"],["dc.contributor.author","Wieser, Georg L."],["dc.contributor.author","Nientiedt, Tobias"],["dc.contributor.author","Pieper, Alexander"],["dc.contributor.author","Ruhwedel, Torben"],["dc.contributor.author","Groszer, Matthias"],["dc.contributor.author","Sereda, Michael W."],["dc.contributor.author","Nave, Klaus-Armin"],["dc.date.accessioned","2018-11-07T09:09:46Z"],["dc.date.available","2018-11-07T09:09:46Z"],["dc.date.issued","2012"],["dc.description.abstract","Tomacula and myelin outfoldings are striking neuropathological features of a diverse group of inherited demyelinating neuropathies. Whereas the underlying genetic defects are well known, the molecular mechanisms of tomacula formation have remained obscure. We hypothesized that they are caused by uncontrolled, excessive myelin membrane growth, a process, which is regulated in normal development by neuregulin-1/ErbB2, PI3 Kinase signalling and ERK/MAPK signalling. Here, we demonstrate by targeted disruption of Pten in Schwann cells that hyperactivation of the endogenous PI3 Kinase pathway causes focal hypermyelination, myelin outfoldings and tomacula, even when induced in adult animals by tamoxifen, and is associated with progressive peripheral neuropathy. Activated AKT kinase is associated with PtdIns(3,4,5)P3 at paranodal loops and SchmidtLanterman incisures. This striking myelin pathology, with features of human CMT type 4B1 and HNPP, is dependent on AKT/mTOR signalling, as evidenced by a significant amelioration of the pathology in mice treated with rapamycin. We suggest that regions of non-compact myelin are under lifelong protection by PTEN against abnormal membrane outgrowth, and that dysregulated phosphoinositide levels play a critical role in the pathology of tomaculous neuropathies."],["dc.identifier.doi","10.1002/emmm.201200227"],["dc.identifier.isi","000304767900007"],["dc.identifier.pmid","22488882"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7777"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/26338"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1757-4676"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Genetic disruption of Pten in a novel mouse model of tomaculous neuropathy"],["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","247"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","genesis"],["dc.bibliographiccitation.lastpage","252"],["dc.bibliographiccitation.volume","42"],["dc.contributor.author","Goebbels, Sandra"],["dc.contributor.author","Bode, Ulli"],["dc.contributor.author","Pieper, Alexander"],["dc.contributor.author","Funfschilling, Ursula"],["dc.contributor.author","Schwab, Markus H."],["dc.contributor.author","Nave, Klaus-Armin"],["dc.date.accessioned","2021-06-01T10:50:23Z"],["dc.date.available","2021-06-01T10:50:23Z"],["dc.date.issued","2005"],["dc.identifier.doi","10.1002/gene.20138"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/86642"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation.eissn","1526-968X"],["dc.relation.issn","1526-954X"],["dc.title","Cre/loxP-mediated inactivation of the bHLH transcription factor gene NeuroD/BETA2"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","528"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","EMBO Molecular Medicine"],["dc.bibliographiccitation.lastpage","539"],["dc.bibliographiccitation.volume","4"],["dc.contributor.author","Hagemeyer, Nora"],["dc.contributor.author","Goebbels, Sandra"],["dc.contributor.author","Papiol, Sergi"],["dc.contributor.author","Kästner, Anne"],["dc.contributor.author","Hofer, Sabine"],["dc.contributor.author","Begemann, Martin"],["dc.contributor.author","Gerwig, Ulrike C."],["dc.contributor.author","Boretius, Susann"],["dc.contributor.author","Wieser, Georg L."],["dc.contributor.author","Ronnenberg, Anja"],["dc.contributor.author","Gurvich, Artem"],["dc.contributor.author","Heckers, Stephan H."],["dc.contributor.author","Frahm, Jens"],["dc.contributor.author","Nave, Klaus-Armin"],["dc.contributor.author","Ehrenreich, Hannelore"],["dc.date.accessioned","2017-08-25T10:14:17Z"],["dc.date.available","2017-08-25T10:14:17Z"],["dc.date.issued","2012"],["dc.description.abstract","Severe mental illnesses have been linked to white matter abnormalities, documented by postmortem studies. However, cause and effect have remained difficult to distinguish. CNP (2',3'-cyclic nucleotide 3'-phosphodiesterase) is among the oligodendrocyte/myelin-associated genes most robustly reduced on mRNA and protein level in brains of schizophrenic, bipolar or major depressive patients. This suggests that CNP reduction might be critical for a more general disease process and not restricted to a single diagnostic category. We show here that reduced expression of CNP is the primary cause of a distinct behavioural phenotype, seen only upon aging as an additional 'pro-inflammatory hit'. This phenotype is strikingly similar in Cnp heterozygous mice and patients with mental disease carrying the AA genotype at CNP SNP rs2070106. The characteristic features in both species with their partial CNP 'loss-of-function' genotype are best described as 'catatonia-depression' syndrome. As a consequence of perturbed CNP expression, mice show secondary low-grade inflammation/neurodegeneration. Analogously, in man, diffusion tensor imaging points to axonal loss in the frontal corpus callosum. To conclude, subtle white matter abnormalities inducing neurodegenerative changes can cause/amplify psychiatric diseases."],["dc.identifier.doi","10.1002/emmm.201200230"],["dc.identifier.gro","3150560"],["dc.identifier.pmid","22473874"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7776"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7334"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","A myelin gene causative of a catatonia-depression syndrome upon aging"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","6125"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Molecular Psychiatry"],["dc.bibliographiccitation.lastpage","6148"],["dc.bibliographiccitation.volume","26"],["dc.contributor.author","Runge, Karen"],["dc.contributor.author","Mathieu, Rémi"],["dc.contributor.author","Bugeon, Stéphane"],["dc.contributor.author","Lafi, Sahra"],["dc.contributor.author","Beurrier, Corinne"],["dc.contributor.author","Sahu, Surajit"],["dc.contributor.author","Schaller, Fabienne"],["dc.contributor.author","Loubat, Arthur"],["dc.contributor.author","Herault, Leonard"],["dc.contributor.author","Gaillard, Stéphane"],["dc.contributor.author","Pallesi-Pocachard, Emilie"],["dc.contributor.author","Montheil, Aurélie"],["dc.contributor.author","Bosio, Andreas"],["dc.contributor.author","Rosenfeld, Jill A"],["dc.contributor.author","Hudson, Eva"],["dc.contributor.author","Lindstrom, Kristin"],["dc.contributor.author","Mercimek-Andrews, Saadet"],["dc.contributor.author","Jeffries, Lauren"],["dc.contributor.author","van Haeringen, Arie"],["dc.contributor.author","Vanakker, Olivier"],["dc.contributor.author","Van Hecke, Audrey"],["dc.contributor.author","Amrom, Dina"],["dc.contributor.author","Küry, Sebastien"],["dc.contributor.author","Ratner, Chana"],["dc.contributor.author","Jethva, Reena"],["dc.contributor.author","Gamble, Candace"],["dc.contributor.author","Jacq, Bernard"],["dc.contributor.author","Fasano, Laurent"],["dc.contributor.author","Santpere, Gabriel"],["dc.contributor.author","Lorente-Galdos, Belen"],["dc.contributor.author","Sestan, Nenad"],["dc.contributor.author","Gelot, Antoinette"],["dc.contributor.author","Giacuzz, Sylvie"],["dc.contributor.author","Goebbels, Sandra"],["dc.contributor.author","Represa, Alfonso"],["dc.contributor.author","Cardoso, Carlos"],["dc.contributor.author","Cremer, Harold"],["dc.contributor.author","de Chevigny, Antoine"],["dc.date.accessioned","2022-08-09T12:22:40Z"],["dc.date.available","2022-08-09T12:22:40Z"],["dc.date.issued","2021"],["dc.description.abstract","While the transcription factor NEUROD2 has recently been associated with epilepsy, its precise role during nervous system development remains unclear. Using a multi-scale approach, we set out to understand how Neurod2 deletion affects the development of the cerebral cortex in mice. In Neurod2 KO embryos, cortical projection neurons over-migrated, thereby altering the final size and position of layers. In juvenile and adults, spine density and turnover were dysregulated in apical but not basal compartments in layer 5 neurons. Patch-clamp recordings in layer 5 neurons of juvenile mice revealed increased intrinsic excitability. Bulk RNA sequencing showed dysregulated expression of many genes associated with neuronal excitability and synaptic function, whose human orthologs were strongly associated with autism spectrum disorders (ASD). At the behavior level, Neurod2 KO mice displayed social interaction deficits, stereotypies, hyperactivity, and occasionally spontaneous seizures. Mice heterozygous for Neurod2 had similar defects, indicating that Neurod2 is haploinsufficient. Finally, specific deletion of Neurod2 in forebrain excitatory neurons recapitulated cellular and behavioral phenotypes found in constitutive KO mice, revealing the region-specific contribution of dysfunctional Neurod2 in symptoms. Informed by these neurobehavioral features in mouse mutants, we identified eleven patients from eight families with a neurodevelopmental disorder including intellectual disability and ASD associated with NEUROD2 pathogenic mutations. Our findings demonstrate crucial roles for Neurod2 in neocortical development, whose alterations can cause neurodevelopmental disorders including intellectual disability and ASD."],["dc.identifier.doi","10.1038/s41380-021-01179-x"],["dc.identifier.pmid","34188164"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/112704"],["dc.language.iso","en"],["dc.relation.eissn","1476-5578"],["dc.relation.haserratum","/handle/2/88325"],["dc.relation.issn","1359-4184"],["dc.relation.issn","1476-5578"],["dc.rights","CC BY 4.0"],["dc.title","Disruption of NEUROD2 causes a neurodevelopmental syndrome with autistic features via cell-autonomous defects in forebrain glutamatergic neurons"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Experimental Dermatology"],["dc.bibliographiccitation.volume","23"],["dc.contributor.author","Schiller, S."],["dc.contributor.author","Seebode, Christina"],["dc.contributor.author","Wieser, Georg L."],["dc.contributor.author","Goebbels, Sandra"],["dc.contributor.author","Bennemann, A."],["dc.contributor.author","Schoen, Michael Peter"],["dc.contributor.author","Sprecher, Eli"],["dc.contributor.author","Nave, K."],["dc.contributor.author","Emmert, Steffen"],["dc.date.accessioned","2018-11-07T09:43:02Z"],["dc.date.available","2018-11-07T09:43:02Z"],["dc.date.issued","2014"],["dc.format.extent","E22"],["dc.identifier.isi","000332335500147"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/34090"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.conference","41st Annual Meeting of the Arbeitsgemeinschaft-Dermatologische-Forschung (ADF)"],["dc.relation.eventlocation","Cologne, GERMANY"],["dc.relation.issn","1600-0625"],["dc.relation.issn","0906-6705"],["dc.title","A novel mouse model reveals the pivotal role of SNAP29 in epidermal differentiation"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]