Dobbelstein, Matthias

[["dc.bibliographiccitation.artnumber","S0168170221001763"],["dc.bibliographiccitation.firstpage","198469"],["dc.bibliographiccitation.journal","Virus Research"],["dc.bibliographiccitation.volume","302"],["dc.contributor.author","Stegmann, Kim M."],["dc.contributor.author","Dickmanns, Antje"],["dc.contributor.author","Gerber, Sabrina"],["dc.contributor.author","Nikolova, Vella"],["dc.contributor.author","Klemke, Luisa"],["dc.contributor.author","Manzini, Valentina"],["dc.contributor.author","Schlösser, Denise"],["dc.contributor.author","Bierwirth, Cathrin"],["dc.contributor.author","Freund, Julia"],["dc.contributor.author","Dobbelstein, Matthias"],["dc.date.accessioned","2021-07-05T15:00:26Z"],["dc.date.available","2021-07-05T15:00:26Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1016/j.virusres.2021.198469"],["dc.identifier.pii","S0168170221001763"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/87826"],["dc.language.iso","en"],["dc.notes.intern","DOI Import DOI-Import GROB-441"],["dc.relation.issn","0168-1702"],["dc.title","The folate antagonist methotrexate diminishes replication of the coronavirus SARS-CoV-2 and enhances the antiviral efficacy of remdesivir in cell culture models"],["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.firstpage","580"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Cell Cycle"],["dc.bibliographiccitation.lastpage","587"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Drewelus, Isabella"],["dc.contributor.author","Göpfert, Constanze"],["dc.contributor.author","Hippel, Cathrin"],["dc.contributor.author","Dickmanns, Antje"],["dc.contributor.author","Damianitsch, Katharina"],["dc.contributor.author","Pieler, Tomas"],["dc.contributor.author","Dobbelstein, Matthias"],["dc.date.accessioned","2022-03-01T11:44:31Z"],["dc.date.available","2022-03-01T11:44:31Z"],["dc.date.issued","2010"],["dc.description.abstract","The p53 homologue p63/TP73L is required for the proper development of squamous epithelia, mammary glands and limb buds, with some of these tissues also displaying strong canonical Wnt signalling activity. It was previously suggested that Delta Np63 alpha, the predominant isoform of p63 in epithelia, positively regulates beta-Catenin through inhibition of GSK3 beta. Results reported in this communication show that, upon transient overexpression, Delta Np63 alpha indeed promotes Wnt-inducible reporter gene activity in human cells, as well as secondary axis formation in Xenopus embryos. However, in apparent contradiction to these observations, siRNA-mediated knockdown of endogenous p63 equally enhanced the expression of Wnt-responsive genes. While p63 knockdown did not detectably affect beta-Catenin levels or phosphorylation, Delta Np63 alpha was found in a complex with members of the TCF/LEF family of Wnt-responsive transcription factors. On the basis of these findings, we propose that Delta Np63 alpha has a function in recruiting transcriptional repressors to Wnt-responsive genes. Overexpression of p63 may lead to sequestration of such repressors (squelching), resulting in a similar effect like siRNA-mediated removal of p63, i.e., activation of Wnt-responsive genes. The role of p63 as a negative Wnt-regulator thus matches with the frequently observed downregulation of p63 during tumor progression, when cancer cells adopt a more mesenchymal, invasive phenotype."],["dc.identifier.isi","000274140000038"],["dc.identifier.pmid","20107313"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103040"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Landes Bioscience"],["dc.relation.eissn","1551-4005"],["dc.relation.issn","1538-4101"],["dc.title","p63 antagonizes Wnt-induced transcription"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","5765"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Journal of Clinical Investigation"],["dc.bibliographiccitation.lastpage","5781"],["dc.bibliographiccitation.volume","130"],["dc.contributor.author","Müller, Anne"],["dc.contributor.author","Dickmanns, Antje"],["dc.contributor.author","Resch, Claudia"],["dc.contributor.author","Schäkel, Knut"],["dc.contributor.author","Hailfinger, Stephan"],["dc.contributor.author","Dobbelstein, Matthias"],["dc.contributor.author","Schulze-Osthoff, Klaus"],["dc.contributor.author","Kramer, Daniela"],["dc.date.accessioned","2021-04-14T08:31:22Z"],["dc.date.available","2021-04-14T08:31:22Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1172/JCI134217"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83571"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","1558-8238"],["dc.relation.issn","0021-9738"],["dc.title","The CDK4/6-EZH2 pathway is a potential therapeutic target for psoriasis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]