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.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.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"]]

[["dc.bibliographiccitation.firstpage","1394"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Journal of Allergy and Clinical Immunology"],["dc.bibliographiccitation.lastpage","+"],["dc.bibliographiccitation.volume","130"],["dc.contributor.author","Gogishvili, Tea"],["dc.contributor.author","Luehder, Fred"],["dc.contributor.author","Kirstein, Frank"],["dc.contributor.author","Nieuwenhuizen, Natalie E."],["dc.contributor.author","Goebbels, Sandra"],["dc.contributor.author","Beer-Hammer, Sandra"],["dc.contributor.author","Pfeffer, Klaus"],["dc.contributor.author","Reuter, Sebastian"],["dc.contributor.author","Taube, Christian"],["dc.contributor.author","Brombacher, Frank"],["dc.contributor.author","Huenig, Thomas"],["dc.date.accessioned","2018-11-07T09:02:49Z"],["dc.date.available","2018-11-07T09:02:49Z"],["dc.date.issued","2012"],["dc.description.abstract","Background: Allergic asthma is a T(H)2-promoted hyperreactivity with an immediate, IgE, and mast cell-dependent response followed by eosinophil-dominated inflammation and airway obstruction. Objective: Because costimulation by CD28 is essential for T(H)2 but not T(H)1 responses, we investigated the effect of selective interference with this pathway in mice using the models of ovalbumin and house dust mite-induced airway inflammation. Methods: To study the role of CD28 in the effector phase of allergic airway inflammation, we developed an inducibly CD28-deleting mouse strain or alternatively used a CD28 ligand-binding site-specific mouse anti-mouse mAb blocking CD28 engagement. Results: We show that even after systemic sensitization to the allergen, interruption of CD28-mediated costimulation is highly effective in preventing airway inflammation during challenge. In addition to improving airway resistance and histopathologic presentation and reducing inflammatory infiltrates, antibody treatment during allergen challenge resulted in a marked relative increase in regulatory T-cell numbers among the CD4 T-cell subset of the challenged lung. Conclusion: Selective interference with CD28-mediated costimulation during allergen exposure might be an attractive therapeutic concept for allergic asthma. (J Allergy Clin Immunol 2012;130:1394-403.)"],["dc.identifier.doi","10.1016/j.jaci.2012.08.049"],["dc.identifier.isi","000311641100021"],["dc.identifier.pmid","23102920"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/24769"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Mosby-elsevier"],["dc.relation.issn","0091-6749"],["dc.title","Interruption of CD28-mediated costimulation during allergen challenge protects mice from allergic airway disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1473"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Cerebral Cortex"],["dc.bibliographiccitation.lastpage","1486"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Agarwal, Amit"],["dc.contributor.author","Dibaj, Payam"],["dc.contributor.author","Kassmann, Celia M."],["dc.contributor.author","Goebbels, Sandra"],["dc.contributor.author","Nave, Klaus-Armin"],["dc.contributor.author","Schwab, Markus H."],["dc.date.accessioned","2021-06-01T10:51:16Z"],["dc.date.available","2021-06-01T10:51:16Z"],["dc.date.issued","2011"],["dc.identifier.doi","10.1093/cercor/bhr214"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/86951"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation.eissn","1460-2199"],["dc.relation.issn","1047-3211"],["dc.title","In Vivo Imaging and Noninvasive Ablation of Pyramidal Neurons in Adult NEX-CreERT2 Mice"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","13205"],["dc.bibliographiccitation.issue","36"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","13210"],["dc.bibliographiccitation.volume","111"],["dc.contributor.author","Hsia, Hung-En"],["dc.contributor.author","Kumar, Rohit"],["dc.contributor.author","Luca, Rossella"],["dc.contributor.author","Takeda, Michiko"],["dc.contributor.author","Courchet, Julien"],["dc.contributor.author","Nakashima, Jonathan"],["dc.contributor.author","Wu, Shumin"],["dc.contributor.author","Goebbels, Sandra"],["dc.contributor.author","An, Wenlin"],["dc.contributor.author","Eickholt, Britta J."],["dc.contributor.author","Polleux, Franck"],["dc.contributor.author","Rotin, Daniela"],["dc.contributor.author","Wu, Hong"],["dc.contributor.author","Rossner, Moritz J."],["dc.contributor.author","Bagni, Claudia"],["dc.contributor.author","Rhee, Jeong-Seop"],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Kawabe, Hiroshi"],["dc.date.accessioned","2017-09-07T11:45:33Z"],["dc.date.available","2017-09-07T11:45:33Z"],["dc.date.issued","2014"],["dc.description.abstract","Protein ubiquitination is a core regulatory determinant of neural development. Previous studies have indicated that the Nedd4-family E3 ubiquitin ligases Nedd4-1 and Nedd4-2 may ubiquitinate phosphatase and tensin homolog (PTEN) and thereby regulate axonal growth in neurons. Using conditional knockout mice, we show here that Nedd4-1 and Nedd4-2 are indeed required for axonal growth in murine central nervous system neurons. However, in contrast to previously published data, we demonstrate that PTEN is not a substrate of Nedd4-1 and Nedd4-2, and that aberrant PTEN ubiquitination is not involved in the impaired axon growth upon deletion of Nedd4-1 and Nedd4-2. Rather, PTEN limits Nedd4-1 protein levels by modulating the activity of mTORC1, a protein complex that controls protein synthesis and cell growth. Our data demonstrate that Nedd4-family E3 ligases promote axonal growth and branching in the developing mammalian brain, where PTEN is not a relevant substrate. Instead, PTEN controls neurite growth by regulating Nedd4-1 expression."],["dc.identifier.doi","10.1073/pnas.1400737111"],["dc.identifier.gro","3142055"],["dc.identifier.isi","000341625600056"],["dc.identifier.pmid","25157163"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4045"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0027-8424"],["dc.title","Ubiquitin E3 ligase Nedd4-1 acts as a downstream target of PI3K/PTEN-mTORC1 signaling to promote neurite growth"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Pieper, Alexander"],["dc.contributor.author","Rudolph, Stephanie"],["dc.contributor.author","Wieser, Georg L."],["dc.contributor.author","Götze, Tilmann"],["dc.contributor.author","Mießner, Hendrik"],["dc.contributor.author","Yonemasu, Tomoko"],["dc.contributor.author","Yan, Kuo"],["dc.contributor.author","Tzvetanova, Iva"],["dc.contributor.author","Castillo, Bettina Duverge"],["dc.contributor.author","Goebbels, Sandra"],["dc.date.accessioned","2021-06-01T10:50:41Z"],["dc.date.available","2021-06-01T10:50:41Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1038/s41598-018-37850-7"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/86749"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation.eissn","2045-2322"],["dc.title","NeuroD2 controls inhibitory circuit formation in the molecular layer of the cerebellum"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]