Wienken, Magdalena

[["dc.bibliographiccitation.issue","9-10"],["dc.bibliographiccitation.journal","Neuromuscular Disorders"],["dc.bibliographiccitation.volume","24"],["dc.contributor.author","Schmidt, K."],["dc.contributor.author","Wienken, Magdalena"],["dc.contributor.author","Keller, C."],["dc.contributor.author","Schmidt, J."],["dc.date.accessioned","2018-11-07T09:34:34Z"],["dc.date.available","2018-11-07T09:34:34Z"],["dc.date.issued","2014"],["dc.format.extent","813"],["dc.identifier.doi","10.1016/j.nmd.2014.06.076"],["dc.identifier.isi","000342870200073"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/32199"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Pergamon-elsevier Science Ltd"],["dc.publisher.place","Oxford"],["dc.relation.conference","19th International Congress of the World-Muscle-Society"],["dc.relation.eventlocation","Berlin, GERMANY"],["dc.relation.issn","1873-2364"],["dc.relation.issn","0960-8966"],["dc.title","Molecular cell stress mechanisms in an in vitro model of IBM"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2740"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Cell Death and Differentiation"],["dc.bibliographiccitation.lastpage","2757"],["dc.bibliographiccitation.volume","26"],["dc.contributor.author","Wildung, Merit"],["dc.contributor.author","Esser, Tilman Uli"],["dc.contributor.author","Grausam, Katie Baker"],["dc.contributor.author","Wiedwald, Cornelia"],["dc.contributor.author","Volceanov-Hahn, Larisa"],["dc.contributor.author","Riedel, Dietmar"],["dc.contributor.author","Beuermann, Sabine"],["dc.contributor.author","Li, Li"],["dc.contributor.author","Zylla, Jessica"],["dc.contributor.author","Guenther, Ann-Kathrin"],["dc.contributor.author","Wienken, Magdalena"],["dc.contributor.author","Ercetin, Evrim"],["dc.contributor.author","Han, Zhiyuan"],["dc.contributor.author","Bremmer, Felix"],["dc.contributor.author","Shomroni, Orr"],["dc.contributor.author","Andreas, Stefan"],["dc.contributor.author","Zhao, Haotian"],["dc.contributor.author","Lizé, Muriel"],["dc.date.accessioned","2020-12-10T18:09:42Z"],["dc.date.available","2020-12-10T18:09:42Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1038/s41418-019-0332-7"],["dc.identifier.eissn","1476-5403"],["dc.identifier.issn","1350-9047"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/73732"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Transcription factor TAp73 and microRNA-449 complement each other to support multiciliogenesis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","68"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Molecular Cell"],["dc.bibliographiccitation.lastpage","83"],["dc.bibliographiccitation.volume","61"],["dc.contributor.author","Wienken, Magdalena"],["dc.contributor.author","Dickmanns, Antje"],["dc.contributor.author","Nemajerova, Alice"],["dc.contributor.author","Kramer, Daniela"],["dc.contributor.author","Najafova, Zeynab"],["dc.contributor.author","Weiss, Miriam"],["dc.contributor.author","Karpiuk, Oleksandra"],["dc.contributor.author","Kassem, Moustapha"],["dc.contributor.author","Zhang, Y."],["dc.contributor.author","Lozano, Guillermina"],["dc.contributor.author","Johnsen, Steven A."],["dc.contributor.author","Moll, Ute M."],["dc.contributor.author","Zhang, X."],["dc.contributor.author","Dobbelstein, Matthias"],["dc.date.accessioned","2018-11-07T10:19:27Z"],["dc.date.available","2018-11-07T10:19:27Z"],["dc.date.issued","2016"],["dc.description.abstract","The MDM2 oncoprotein ubiquitinates and antagonizes p53 but may also carry out p53-independent functions. Here we report that MDM2 is required for the efficient generation of induced pluripotent stem cells (iPSCs) from murine embryonic fibroblasts, in the absence of p53. Similarly, MDM2 depletion in the context of p53 deficiency also promoted the differentiation of human mesenchymal stem cells and diminished clonogenic survival of cancer cells. Most of the MDM2-controlled genes also responded to the inactivation of the Polycomb Repressor Complex 2 (PRC2) and its catalytic component EZH2. MDM2 physically associated with EZH2 on chromatin, enhancing the trimethylation of histone 3 at lysine 27 and the ubiquitination of histone 2A at lysine 119 (H2AK119) at its target genes. Removing MDM2 simultaneously with the H2AK119 E3 ligase Ring1B/RNF2 further induced these genes and synthetically arrested cell proliferation. In conclusion, MDM2 supports the Polycomb-mediated repression of lineage-specific genes, independent of p53."],["dc.identifier.doi","10.1016/j.molcel.2015.12.008"],["dc.identifier.isi","000372324500007"],["dc.identifier.pmid","26748827"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/41663"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.relation.issn","1097-4164"],["dc.relation.issn","1097-2765"],["dc.title","MDM2 Associates with Polycomb Repressor Complex 2 and Enhances Stemness-Promoting Chromatin Modifications Independent of p53"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","5470831"],["dc.bibliographiccitation.journal","Mediators of Inflammation"],["dc.contributor.author","Schmidt, Karsten"],["dc.contributor.author","Wienken, Magdalena"],["dc.contributor.author","Keller, Christian W."],["dc.contributor.author","Balcarek, Peter"],["dc.contributor.author","Münz, Christian"],["dc.contributor.author","Schmidt, Jens"],["dc.date.accessioned","2018-11-07T10:29:09Z"],["dc.date.available","2018-11-07T10:29:09Z"],["dc.date.issued","2017"],["dc.description.abstract","The pathology of inclusion body myositis (IBM) involves an inflammatory response and beta-amyloid deposits in muscle fibres. It is believed that MAP kinases such as the ERK signalling pathway mediate the inflammatory signalling in cells. Further, there is evidence that autophagic activity plays a crucial role in the pathogenesis of IBM. Using a well established in vitro model of IBM, the autophagic pathway, MAP kinases, and accumulation of beta-amyloid were examined. We demonstrate that stimulation of muscle cells with IL-1 beta and IFN-gamma led to an increased phosphorylation of ERK. The ERK inhibitor PD98059 diminished the expression of proinflammatory markers as well as the accumulation of beta-amyloid. In addition, IL-1 beta and IFN-gamma led to an increase of autophagic activity, upregulation of APP, and subsequent accumulation of beta-sheet aggregates. Taken together, the data demonstrate that the ERK pathway contributes to formation of beta-amyloid and regulation of autophagic activity in muscle cells exposed to proinflammatory cell stress. This suggests that ERK serves as an important mediator between inflammatory mechanisms and protein deposition in skeletal muscle and is a crucial element of the pathology of IBM."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2016"],["dc.identifier.doi","10.1155/2017/5470831"],["dc.identifier.isi","000394098400001"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14140"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/43582"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Hindawi Ltd"],["dc.relation.issn","1466-1861"],["dc.relation.issn","0962-9351"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","IL-1 beta-Induced Accumulation of Amyloid: Macroautophagy in Skeletal Muscle Depends on ERK"],["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","1845"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Cell Reports"],["dc.bibliographiccitation.lastpage","1857"],["dc.bibliographiccitation.volume","17"],["dc.contributor.author","Klusmann, Ina"],["dc.contributor.author","Rodewald, Sabrina"],["dc.contributor.author","Mueller, Leonie"],["dc.contributor.author","Friedrich, Mascha"],["dc.contributor.author","Wienken, Magdalena"],["dc.contributor.author","Li, Yizhu"],["dc.contributor.author","Schulz-Heddergott, Ramona"],["dc.contributor.author","Dobbelstein, Matthias"],["dc.date.accessioned","2018-11-07T10:05:50Z"],["dc.date.available","2018-11-07T10:05:50Z"],["dc.date.issued","2016"],["dc.description.abstract","p53 induces cell death upon DNA damage, but this may not confer all of its tumor suppressor activity. Wereport that p53 activation enhances the processivity of DNA replication, as monitored by multi-label fiber assays, whereas removal of p53 reduces fork progression. This is observed in tumor-derived U2OS cells but also in murine embryonic fibroblasts with heterozygous or homozygous p53 deletion and in freshly isolated thymocytes frommice with differential p53 status. Mdm2, a p53-inducible gene product, similarly supports DNA replication even in p53-deficient cells, suggesting that sustained Mdm2-expression is at least one of the mechanisms allowing p53 to prevent replicative stress. Thus, p53 helps to protect the genome during S phase, by preventing the occurrence of stalled or collapsed replication forks. These results expand p53's tumor-suppressive functions, adding to the ex-post model (elimination of damaged cells) an ex-ante activity; i.e., the prevention of DNA damage during replication."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2016"],["dc.identifier.doi","10.1016/j.celrep.2016.10.036"],["dc.identifier.isi","000390545900014"],["dc.identifier.pmid","27829155"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14102"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38979"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.relation.issn","2211-1247"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","p53 Activity Results in DNA Replication Fork Processivity"],["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","31623"],["dc.bibliographiccitation.issue","22"],["dc.bibliographiccitation.journal","Oncotarget"],["dc.bibliographiccitation.lastpage","31638"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Sriraman, Anusha"],["dc.contributor.author","Radovanovic, Marija"],["dc.contributor.author","Wienken, Magdalena"],["dc.contributor.author","Najafova, Zeynab"],["dc.contributor.author","Li, Yizhu"],["dc.contributor.author","Dobbelstein, Matthias"],["dc.date.accessioned","2018-11-07T10:14:02Z"],["dc.date.available","2018-11-07T10:14:02Z"],["dc.date.issued","2016"],["dc.description.abstract","Targeting the Mdm2 oncoprotein by drugs has the potential of re-establishing p53 function and tumor suppression. However, Mdm2-antagonizing drug candidates, e.g. Nutlin-3a, often fail to abolish cancer cell growth sustainably. To overcome these limitations, we inhibited Mdm2 and simultaneously a second negative regulator of p53, the phosphatase Wip1/PPM1D. When combining Nutlin-3a with the Wip1 inhibitor GSK2830371 in the treatment of p53-proficient but not p53-deficient cells, we observed enhanced phosphorylation (Ser 15) and acetylation (Lys 382) of p53, increased expression of p53 target gene products, and synergistic inhibition of cell proliferation. Surprisingly, when testing the two compounds individually, largely distinct sets of genes were induced, as revealed by deep sequencing analysis of RNA. In contrast, the combination of both drugs led to an expression signature that largely comprised that of Nutlin-3a alone. Moreover, the combination of drugs, or the combination of Nutlin-3a with Wip1-depletion by siRNA, activated p53-responsive genes to a greater extent than either of the compounds alone. Simultaneous inhibition of Mdm2 and Wip1 enhanced cell senescence and G2/M accumulation. Taken together, the inhibition of Wip1 might fortify p53-mediated tumor suppression by Mdm2 antagonists."],["dc.identifier.doi","10.18632/oncotarget.9302"],["dc.identifier.isi","000377748500002"],["dc.identifier.pmid","27183917"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14134"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/40550"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Impact Journals Llc"],["dc.relation.issn","1949-2553"],["dc.rights","CC BY 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/3.0"],["dc.title","Cooperation of Nutlin-3a and a Wip1 inhibitor to induce p53 activity"],["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","1300"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Genes & Development"],["dc.bibliographiccitation.lastpage","1312"],["dc.bibliographiccitation.volume","30"],["dc.contributor.author","Nemajerova, Alice"],["dc.contributor.author","Kramer, Daniela"],["dc.contributor.author","Siller, Saul S."],["dc.contributor.author","Herr, Christian"],["dc.contributor.author","Shomroni, Orr"],["dc.contributor.author","Pena, Tonatiuh"],["dc.contributor.author","Suazo, Cristina Gallinas"],["dc.contributor.author","Glaser, Katharina"],["dc.contributor.author","Wildung, Merit"],["dc.contributor.author","Steffen, Henrik"],["dc.contributor.author","Sriraman, Anusha"],["dc.contributor.author","Oberle, Fabian"],["dc.contributor.author","Wienken, Magdalena"],["dc.contributor.author","Hennion, Magali"],["dc.contributor.author","Vidal, Ramon"],["dc.contributor.author","Royen, Bettina"],["dc.contributor.author","Alevra, Mihai"],["dc.contributor.author","Schild, Detlev"],["dc.contributor.author","Bals, Robert"],["dc.contributor.author","Doenitz, Juergen"],["dc.contributor.author","Riedel, Dietmar"],["dc.contributor.author","Bonn, Stefan"],["dc.contributor.author","Takemaru, Ken-Ichi"],["dc.contributor.author","Moll, Ute M."],["dc.contributor.author","Lize, Muriel"],["dc.date.accessioned","2018-11-07T10:13:24Z"],["dc.date.available","2018-11-07T10:13:24Z"],["dc.date.issued","2016"],["dc.description.abstract","Motile multiciliated cells (MCCs) have critical roles in respiratory health and disease and are essential for cleaning inhaled pollutants and pathogens from airways. Despite their significance for human disease, the transcriptional control that governs multiciliogenesis remains poorly understood. Here we identify TP73, a p53 homolog, as governing the program for airway multiciliogenesis. Mice with TP73 deficiency suffer from chronic respiratory tract infections due to profound defects in ciliogenesis and complete loss of mucociliary clearance. Organotypic airway cultures pinpoint TAp73 as necessary and sufficient for basal body docking, axonemal extension, and motility during the differentiation of MCC progenitors. Mechanistically, cross-species genomic analyses and complete ciliary rescue of knockout MCCs identify TAp73 as the conserved central transcriptional integrator of multiciliogenesis. TAp73 directly activates the key regulators FoxJ1, Rfx2, Rfx3, and miR34bc plus nearly 50 structural and functional ciliary genes, some of which are associated with human ciliopathies. Our results position TAp73 as a novel central regulator of MCC differentiation."],["dc.identifier.doi","10.1101/gad.279836.116"],["dc.identifier.isi","000378084000006"],["dc.identifier.pmid","27257214"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/40428"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cold Spring Harbor Lab Press, Publications Dept"],["dc.relation.issn","1549-5477"],["dc.relation.issn","0890-9369"],["dc.title","TAp73 is a central transcriptional regulator of airway multiciliogenesis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","74"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Molecular Cell Biology"],["dc.bibliographiccitation.lastpage","80"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Wienken, Magdalena"],["dc.contributor.author","Moll, Ute M."],["dc.contributor.author","Dobbelstein, Matthias"],["dc.date.accessioned","2018-11-07T10:27:51Z"],["dc.date.available","2018-11-07T10:27:51Z"],["dc.date.issued","2017"],["dc.description.abstract","Mdm2 is the key negative regulator of the tumour suppressor p53, making it an attractive target for anti-cancer drug design. We recently identified a new role of Mdm2 in gene repression through its direct interaction with several proteins of the polycomb group (PcG) family. PcG proteins form polycomb repressive complexes PRC1 and PRC2. PRC2 (via EZH2) mediates histone 3 lysine 27 (H3K27) trimethylation, and PRC1 (via RING1B) mediates histone 2A lysine 119 (H2AK119) monoubiquitination. Both PRCs mostly support a compact and transcriptionally silent chromatin structure. We found that Mdm2 regulates a gene expression profile similar to that of PRC2 independent of p53. Moreover, Mdm2 promotes the stemness of murine induced pluripotent stem cells and human mesenchymal stem cells, and supports the survival of tumour cells. Mdm2 is recruited to target gene promoters by the PRC2 member and histone methyltransferase EZH2, and enhances PRC-dependent repressive chromatin modifications, specifically H3K27me3 and H2AK119ub1. Mdm2 also cooperates in gene repression with the PRC1 protein RING1B, a H2AK119 ubiquitin ligase. Here we discuss the possible implications of these p53-independent functions of Mdm2 in chromatin dynamics and in the stem cell phenotype. We propose that the p53-independent functions of Mdm2 should be taken into account for cancer drug design. So far, the majority of clinically tested Mdm2 inhibitors target its binding to p53 but do not affect the new functions of Mdm2 described here. However, when targeting the E3 ligase activity of Mdm2, a broader spectrum of its oncogenic activities might become druggable."],["dc.description.sponsorship","Else Kroner-Fresenius-Foundation; Studienstiftung des Deutschen Volkes"],["dc.identifier.doi","10.1093/jmcb/mjw046"],["dc.identifier.isi","000397087600010"],["dc.identifier.pmid","27927750"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/43308"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Oxford Univ Press"],["dc.relation.issn","1759-4685"],["dc.relation.issn","1674-2788"],["dc.title","Mdm2 as a chromatin modifier"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]