Sereda, Michael Werner

[["dc.bibliographiccitation.firstpage","1050"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Nature Neuroscience"],["dc.bibliographiccitation.lastpage","1059"],["dc.bibliographiccitation.volume","19"],["dc.contributor.author","Quintes, Susanne"],["dc.contributor.author","Brinkmann, Bastian G"],["dc.contributor.author","Ebert, Madlen"],["dc.contributor.author","Fröb, Franziska"],["dc.contributor.author","Kungl, Theresa"],["dc.contributor.author","Arlt, Friederike A"],["dc.contributor.author","Tarabykin, Victor"],["dc.contributor.author","Huylebroeck, Danny"],["dc.contributor.author","Meijer, Dies"],["dc.contributor.author","Suter, Ueli"],["dc.contributor.author","Wegner, Michael"],["dc.contributor.author","Sereda, Michael W"],["dc.contributor.author","Nave, Klaus-Armin"],["dc.date.accessioned","2020-12-10T18:09:31Z"],["dc.date.available","2020-12-10T18:09:31Z"],["dc.date.issued","2016"],["dc.identifier.doi","10.1038/nn.4321"],["dc.identifier.eissn","1546-1726"],["dc.identifier.issn","1097-6256"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/73679"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Zeb2 is essential for Schwann cell differentiation, myelination and nerve repair"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","282"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Annals of Neurology"],["dc.bibliographiccitation.lastpage","282"],["dc.bibliographiccitation.volume","61"],["dc.contributor.author","Meyer zu Horste, Gerd"],["dc.contributor.author","Prukop, Thomas"],["dc.contributor.author","Liebetanz, David"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Nave, Klaus-Armin"],["dc.contributor.author","Sereda, Michael W."],["dc.date.accessioned","2022-03-01T11:44:49Z"],["dc.date.available","2022-03-01T11:44:49Z"],["dc.date.issued","2007"],["dc.identifier.doi","10.1002/ana.21134"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103128"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1531-8249"],["dc.relation.iserratumof","/handle/2/52190"],["dc.relation.issn","0364-5134"],["dc.title","Correction"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.subtype","erratum_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Journal of the Peripheral Nervous System"],["dc.bibliographiccitation.volume","20"],["dc.contributor.author","Prukop, Thomas"],["dc.contributor.author","Milet, A."],["dc.contributor.author","Stenzel, J."],["dc.contributor.author","Cholet, N."],["dc.contributor.author","Nabirotchkin, S."],["dc.contributor.author","Hajj, R."],["dc.contributor.author","Nave, K-A"],["dc.contributor.author","Chumakov, I."],["dc.contributor.author","Cohen, Doron"],["dc.contributor.author","Sereda, Michael W."],["dc.date.accessioned","2018-11-07T09:56:13Z"],["dc.date.available","2018-11-07T09:56:13Z"],["dc.date.issued","2015"],["dc.format.extent","213"],["dc.identifier.isi","000360214600327"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/36911"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.conference","Biennial Meeting of the Peripheral-Nerve-Society"],["dc.relation.eventlocation","Quebec, CANADA"],["dc.relation.issn","1529-8027"],["dc.relation.issn","1085-9489"],["dc.title","AN EXPERIMENTAL TRIAL OF AN EARLY ONSET TREATMENT WITH A COMBINATIONAL DRUG (PXT3003) CONSISTING OF BACLOFEN, NALTREXONE AND SORBITOL IN THE CMT1A RAT MODEL"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

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

[["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","MULTIPLE SCLEROSIS"],["dc.bibliographiccitation.volume","15"],["dc.contributor.author","Merkler, Doron"],["dc.contributor.author","Klinker, Florian"],["dc.contributor.author","Juergens, T."],["dc.contributor.author","Glaser, Raoul"],["dc.contributor.author","Paulus, Walter J."],["dc.contributor.author","Brinkmann, Bastian G."],["dc.contributor.author","Sereda, Michael W."],["dc.contributor.author","Stadelmann, Christine"],["dc.contributor.author","Brueck, Wolfgang"],["dc.contributor.author","Liebetanz, David"],["dc.date.accessioned","2018-11-07T11:25:14Z"],["dc.date.available","2018-11-07T11:25:14Z"],["dc.date.issued","2009"],["dc.format.extent","S180"],["dc.identifier.isi","000269652500538"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/56580"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Sage Publications Ltd"],["dc.publisher.place","London"],["dc.relation.conference","25th Congress of the European-Committee-for-Treatment-and-Research-in-Multiple-Sclerosis"],["dc.relation.eventlocation","Dusseldorf, GERMANY"],["dc.relation.issn","1352-4585"],["dc.title","Propagation of cortical spreading depression inversely correlates with cortical myelin content"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3973"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA"],["dc.bibliographiccitation.lastpage","3978"],["dc.bibliographiccitation.volume","109"],["dc.contributor.author","Makoukji, Joelle"],["dc.contributor.author","Belle, Martin"],["dc.contributor.author","Meffre, Delphine"],["dc.contributor.author","Stassart, Ruth"],["dc.contributor.author","Grenier, Julien"],["dc.contributor.author","Shackleford, Ghjuvan'Ghjacumu"],["dc.contributor.author","Fledrich, Robert"],["dc.contributor.author","Fonte, Cosima"],["dc.contributor.author","Branchu, Julien"],["dc.contributor.author","Goulard, Marie"],["dc.contributor.author","de Waele, Catherine"],["dc.contributor.author","Charbonnier, Frederic"],["dc.contributor.author","Sereda, Michael W."],["dc.contributor.author","Baulieu, Etienne-Emile"],["dc.contributor.author","Schumacher, Michael"],["dc.contributor.author","Bernard, Sophie"],["dc.contributor.author","Massaad, Charbel"],["dc.date.accessioned","2018-11-07T09:12:24Z"],["dc.date.available","2018-11-07T09:12:24Z"],["dc.date.issued","2012"],["dc.description.abstract","Glycogen synthase kinase 3 beta (GSK3 beta) inhibitors, especially the mood stabilizer lithium chloride, are also used as neuroprotective or anti-inflammatory agents. We studied the influence of LiCl on the remyelination of peripheral nerves. We showed that the treatment of adult mice with LiCl after facial nerve crush injury stimulated the expression of myelin genes, restored the myelin structure, and accelerated the recovery of whisker movements. LiCl treatment also promoted remyelination of the sciatic nerve after crush. We also demonstrated that peripheral myelin gene MPZ and PMP22 promoter activities, transcripts, and protein levels are stimulated by GSK3 beta inhibitors (LiCl and SB216763) in Schwann cells as well as in sciatic and facial nerves. LiCl exerts its action in Schwann cells by increasing the amount of beta-catenin and provoking its nuclear localization. We showed by ChIP experiments that LiCl treatment drives beta-catenin to bind to T-cell factor/lymphoid-enhancer factor response elements identified in myelin genes. Taken together, our findings open perspectives in the treatment of nerve demyelination by administering GSK3 beta inhibitors such as lithium."],["dc.identifier.doi","10.1073/pnas.1121367109"],["dc.identifier.isi","000301117700073"],["dc.identifier.pmid","22355115"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/26939"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Natl Acad Sciences"],["dc.relation.issn","0027-8424"],["dc.title","Lithium enhances remyelination of peripheral nerves"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

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

[["dc.bibliographiccitation.firstpage","89"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","British Medical Bulletin"],["dc.bibliographiccitation.lastpage","113"],["dc.bibliographiccitation.volume","102"],["dc.contributor.author","Fledrich, Robert"],["dc.contributor.author","Stassart, Ruth Martha"],["dc.contributor.author","Sereda, Michael W."],["dc.date.accessioned","2018-11-07T09:09:45Z"],["dc.date.available","2018-11-07T09:09:45Z"],["dc.date.issued","2012"],["dc.description.abstract","Charcot-Marie-Tooth (CMT) disease represents a broad group of inherited motor and sensory neuropathies which can originate from various genetic aberrations, e.g. mutations, deletions and duplications. We performed a literature review on murine animal models of CMT disease with regard to experimental therapeutic approaches. Hereby, we focussed on the demyelinating subforms of CMT (CMT1). PubMed items were CMT, animal model, demyelination and therapy. Patients affected by CMT suffer from slowly progressive, distally pronounced muscle atrophy caused by an axonal loss. The disease severity is highly variable and impairments may result in wheelchair boundness. No therapy is available yet. Numerous rodent models for the various CMT subtypes are available today. The selection of the correct animal model for the specific CMT subtype provides an important prerequisite for the successful translation of experimental findings in patients. Despite more than 20 years of remarkable progress in CMT research, the disease is still left untreatable. There is a growing number of experimental therapeutic strategies that may be translated into future clinical trials in patients with CMT. The slow disease progression and insensitive outcome measures hamper clinical therapy trials in CMT. Biomarkers may provide powerful tools to monitor therapeutic efficacy. Recently, we have shown that transcriptional profiling can be utilized to assess and predict the disease severity in a transgenic rat model and in affected humans."],["dc.identifier.doi","10.1093/bmb/lds010"],["dc.identifier.isi","000304831300007"],["dc.identifier.pmid","22551516"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/26332"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Oxford Univ Press"],["dc.relation.issn","0007-1420"],["dc.title","Murine therapeutic models for Charcot-Marie-Tooth (CMT) disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","77"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Molecular Neuroscience"],["dc.bibliographiccitation.lastpage","88"],["dc.bibliographiccitation.volume","28"],["dc.contributor.author","Horste, GMZ"],["dc.contributor.author","Prukop, Thomas"],["dc.contributor.author","Nave, K. A."],["dc.contributor.author","Sereda, Michael W."],["dc.date.accessioned","2018-11-07T10:36:54Z"],["dc.date.available","2018-11-07T10:36:54Z"],["dc.date.issued","2006"],["dc.description.abstract","Charcot-Marie-Tooth (CMT) disease is a common hereditary neuropathy that causes progressive distally pronounced muscle weakness and can lead to life-long disability in patients. In most cases, the disorder has been associated with a partial duplication of human chromosome 17 (CMT1A), causing 1.5-fold overexpression of the peripheral myelin protein 22 kDa (PMP22). Increased PMP22 gene dosage results in demyelination, secondary axonal loss, and neurogenic muscle atrophy. Experimental therapeutic approaches based on the role of progesterone and ascorbic acid in myelin formation recently have reached preclinical proof-of-principle trials in rodents. It was shown that progesterone receptor antagonists can reduce PMP22 overexpression and clinical severity in a CMT1A rat model. Furthermore, ascorbic acid treatment reduced premature death and demyelination in a CMT1A mouse model. Thus, basic research has opened up new vistas for the understanding and treatment of hereditary neuropathies."],["dc.identifier.doi","10.1385/JMN:28:1:77"],["dc.identifier.isi","000236438000007"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/45435"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","0895-8696"],["dc.title","Myelin disorders causes and perspectives of Charcot-Marie-Tooth neuropathy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Glia"],["dc.bibliographiccitation.volume","61"],["dc.contributor.author","Kungl, Theresa"],["dc.contributor.author","Nientiedt, T."],["dc.contributor.author","Neufeld, K. J."],["dc.contributor.author","Sereda, Michael W."],["dc.contributor.author","Nave, K-A."],["dc.date.accessioned","2018-11-07T09:23:23Z"],["dc.date.available","2018-11-07T09:23:23Z"],["dc.date.issued","2013"],["dc.format.extent","S142"],["dc.identifier.isi","000320408400456"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29565"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.conference","11th European Meeting on Glial Cell Function in Health and Disease"],["dc.relation.eventlocation","Berlin, GERMANY"],["dc.relation.issn","0894-1491"],["dc.title","2 ',3 '-CYCLIC NUCLEOTIDE 3 '-PHOSPHODIESTERASE (CNP) DEFICIENCY CAUSES AXONAL LOSS AND HYPERMYELINATION IN THE SENSORY PERIPHERAL NERVOUS SYSTEM"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]