Kessel, Michael

[["dc.bibliographiccitation.firstpage","4737"],["dc.bibliographiccitation.issue","13"],["dc.bibliographiccitation.journal","Molecular and Cellular Biology"],["dc.bibliographiccitation.lastpage","4744"],["dc.bibliographiccitation.volume","27"],["dc.contributor.author","Luo, Lingfei"],["dc.contributor.author","Uerlings, Yvonne"],["dc.contributor.author","Happel, Nicole"],["dc.contributor.author","Asli, Naisana S."],["dc.contributor.author","Knoetgen, Hendrik"],["dc.contributor.author","Kessel, Michael"],["dc.date.accessioned","2018-11-07T11:01:10Z"],["dc.date.available","2018-11-07T11:01:10Z"],["dc.date.issued","2007"],["dc.description.abstract","The geminin protein functions both as a DNA rereplication inhibitor through association with Cdtl and as a repressor of Hox gene transcription through the polycomb pathway. Here, we report that the functions of avian geminin are coordinated with and regulated by cell cycle-dependent nuclear-cytoplasmic shuttling. In S phase, geminin enters nuclei and inhibits both loading of the minichromosome maintenance (MCM) complex onto chromatin and Hox gene transcription. At the end of mitosis, geminin is exported from nuclei by the exportin protein Crm1 and is unavailable in the nucleus during the next G(1) phase, thus ensuring proper chromatin loading of the MCM complex and Hox gene transcription. This mechanism for regulating the functions of geminin adds to distinct mechanisms, such as protein degradation and ubiquitination, applied in other vertebrates."],["dc.identifier.doi","10.1128/MCB.00123-07"],["dc.identifier.isi","000247569200012"],["dc.identifier.pmid","17470552"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/51087"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Microbiology"],["dc.relation.issn","0270-7306"],["dc.title","Regulation of geminin functions by cell cycle-dependent nuclear-cytoplasmic shuttling"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","16"],["dc.bibliographiccitation.journal","BMC Biochemistry"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Pitulescu, Mara E."],["dc.contributor.author","Teichmann, Martin"],["dc.contributor.author","Luo, Lingfei"],["dc.contributor.author","Kessel, Michael"],["dc.date.accessioned","2019-07-09T11:52:37Z"],["dc.date.available","2019-07-09T11:52:37Z"],["dc.date.issued","2009"],["dc.description.abstract","Background The re-replication inhibitor Geminin binds to several transcription factors including homeodomain proteins, and to members of the polycomb and the SWI/SNF complexes. Results Here we describe the TATA-binding protein-like factor-interacting protein (TIPT) isoform 2, as a strong binding partner of Geminin. TIPT2 is widely expressed in mouse embryonic and adult tissues, residing both in cyto- and nucleoplasma, and enriched in the nucleolus. Like Geminin, also TIPT2 interacts with several polycomb factors, with the general transcription factor TBP (TATA box binding protein), and with the related protein TBPL1 (TRF2). TIPT2 synergizes with geminin and TBP in the activation of TATA box-containing promoters, and with TBPL1 and geminin in the activation of the TATA-less NF1 promoter. Geminin and TIPT2 were detected in the chromatin near TBP/TBPL1 binding sites. Conclusion Together, our study introduces a novel transcriptional regulator and its function in cooperation with chromatin associated factors and the basal transcription machinery."],["dc.identifier.doi","10.1186/1471-2091-10-16"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/60240"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.rights","CC BY 2.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.0"],["dc.subject.ddc","610"],["dc.subject.ddc","573"],["dc.subject.ddc","573.8"],["dc.subject.ddc","612"],["dc.subject.ddc","612.8"],["dc.title","TIPT2 and geminin interact with basal transcription factors to synergize in transcriptional regulation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1596"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Cell Cycle"],["dc.bibliographiccitation.lastpage","1610"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Pirouz, Mehdi"],["dc.contributor.author","Rahjouei, Ali"],["dc.contributor.author","Shamsi, Farnaz"],["dc.contributor.author","Eckermann, Kolja Neil"],["dc.contributor.author","Salinas-Riester, Gabriela"],["dc.contributor.author","Pommerenke, Claudia"],["dc.contributor.author","Kessel, Michael"],["dc.date.accessioned","2018-11-07T09:57:10Z"],["dc.date.available","2018-11-07T09:57:10Z"],["dc.date.issued","2015"],["dc.description.abstract","The induction and maintenance of pluripotency requires the expression of several core factors at appropriate levels (Oct4, Sox2, Klf4, Prdm14). A subset of these proteins (Oct4, Sox2, Prdm14) also plays crucial roles for the establishment of primordial germ cells (PGCs). Here we demonstrate that the Mad2l2 (MAD2B, Rev7) gene product is not only required by PGCs, but also by pluripotent embryonic stem cells (ESCs), depending on the growth conditions. Mad2l2(-/-) ESCs were unstable in LIF/serum medium, and differentiated into primitive endoderm. However, they could be stably propagated using small molecule inhibitors of MAPK signaling. Several components of the MAPK cascade were up- or downregulated even in undifferentiated Mad2l2(-/-) ESCs. Global levels of repressive histone H3 variants were increased in mutant ESCs, and the epigenetic signatures on pluripotency-, primitive endoderm-, and MAPK-related loci differed. Thus, H3K9me2 repressed the Nanog promoter, while the promoter of Gata4 lost H3K27me3 and became de-repressed in LIF/serum condition. Promoters associated with genes involved in MAPK signaling also showed misregulation of these histone marks. Such epigenetic modifications could be indirect consequences of mutating Mad2l2. However, our previous observations suggested the histone methyltransferases as direct (G9a) or indirect (Ezh2) targets of Mad2l2. In effect, the intricate balance necessary for pluripotency becomes perturbed in the absence of Mad2l2."],["dc.identifier.doi","10.1080/15384101.2015.1026485"],["dc.identifier.isi","000354877800017"],["dc.identifier.pmid","25928475"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/37104"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Taylor & Francis Inc"],["dc.relation.issn","1551-4005"],["dc.relation.issn","1538-4101"],["dc.title","Destabilization of pluripotency in the absence of Mad2l2"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1842"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Cell Reports"],["dc.bibliographiccitation.lastpage","1854"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Narayanan, Ramanathan"],["dc.contributor.author","Pirouz, Mehdi"],["dc.contributor.author","Kerimoglu, Cemil"],["dc.contributor.author","Pham, Linh"],["dc.contributor.author","Wagener, Robin J."],["dc.contributor.author","Kiszka, Kamila A."],["dc.contributor.author","Rosenbusch, Joachim"],["dc.contributor.author","Seong, Rho H."],["dc.contributor.author","Kessel, Michael"],["dc.contributor.author","Fischer, Andre"],["dc.contributor.author","Stoykova, Anastassia"],["dc.contributor.author","Staiger, Jochen F."],["dc.contributor.author","Tuoc, Tran"],["dc.date.accessioned","2017-09-07T11:54:50Z"],["dc.date.available","2017-09-07T11:54:50Z"],["dc.date.issued","2015"],["dc.description.abstract","BAF (Brg/Brm-associated factors) complexes play important roles in development and are linked to chromatin plasticity at selected genomic loci. Nevertheless, a full understanding of their role in development and chromatin remodeling has been hindered by the absence of mutants completely lacking BAF complexes. Here, we report that the loss of BAF155/BAF170 in double-conditional knockout (dcKO) mice eliminates all known BAF subunits, resulting in an overall reduction in active chromatin marks (H3K9Ac), a global increase in repressive marks (H3K27me2/3), and downregulation of gene expression. We demonstrate that BAF complexes interact with H3K27 demethylases (JMJD3 and UTX) and potentiate their activity. Importantly, BAF complexes are indispensable for forebrain development, including proliferation, differentiation, and cell survival of neural progenitor cells. Our findings reveal a molecular mechanism mediated by BAF complexes that controls the global transcriptional program and chromatin state in development."],["dc.description.sponsorship","Open-Access Publikationsfonds 2015"],["dc.identifier.doi","10.1016/j.celrep.2015.10.046"],["dc.identifier.gro","3141775"],["dc.identifier.isi","000366047000012"],["dc.identifier.pmid","26655900"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12641"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/935"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Cell Press"],["dc.relation.issn","2211-1247"],["dc.rights","CC BY-NC-ND 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/4.0"],["dc.title","Loss of BAF (mSWI/SNF) Complexes Causes Global Transcriptional and Chromatin State Changes in Forebrain Development"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","753"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Journal of Molecular Medicine"],["dc.bibliographiccitation.lastpage","761"],["dc.bibliographiccitation.volume","90"],["dc.contributor.author","Pirouz, Mehdi"],["dc.contributor.author","Klimke, Alexander"],["dc.contributor.author","Kessel, Michael"],["dc.date.accessioned","2021-06-01T10:49:04Z"],["dc.date.available","2021-06-01T10:49:04Z"],["dc.date.issued","2012"],["dc.identifier.doi","10.1007/s00109-012-0912-1"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/86158"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation.eissn","1432-1440"],["dc.relation.issn","0946-2716"],["dc.title","The reciprocal relationship between primordial germ cells and pluripotent stem cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e73826"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","PLOS ONE"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Tabrizi, Golnaz A."],["dc.contributor.author","Böse, Kerstin"],["dc.contributor.author","Reimann, Yvonne"],["dc.contributor.author","Kessel, Michael"],["dc.contributor.editor","Cooney, Austin John"],["dc.date.accessioned","2018-11-23T08:47:00Z"],["dc.date.available","2018-11-23T08:47:00Z"],["dc.date.issued","2013"],["dc.description.abstract","Pluripotency requires the expression of the three core transcriptions factors Oct4, Sox2 and Nanog, as well as further, complementary proteins. The geminin protein is part of this network, and was shown to play a role in the regulation of DNA replication, the control of the cell cycle, and the acquisition of neural fate. It is highly expressed in the early embryo, in particular the epiblast and the early neural ectoderm, and also in pluripotent embryonic stem cells. The genetic inactivation of geminin resulted in lethality after the first few cell divisions, and thus prohibited the outgrowth of pluripotent cells. We established embryonic stem cells allowing the deletion of the geminin gene by induction of of Cre-recombinase with tamoxifen. Here, we show that geminin deficiency quickly leads to a loss of pluripotency, and to differentiation into the mesendodermal direction with high Oct4/low Sox2 levels. Simultaneous loss of geminin and induction of the neural lineage resulted in immediate apoptosis. These results suggested that in early development geminin functions via the co-expressed Sox2 gene. We found that the stem cell enhancer SRR2 of Sox2 is occupied by the activating esBAF complex in the presence of geminin, but becomes epigenetically repressed in its absence by the Polycomb repressive complex PRC2. The importance of geminin for Sox2 expression also explains the absolute requirement for geminin during the induction of pluripotency by OSKM viruses. In summary, geminin is required for Sox2 expression, and thus for the maintenance of totipotency, pluripotency and the early neural lineage."],["dc.identifier.doi","10.1371/journal.pone.0073826"],["dc.identifier.pmid","24069236"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/56957"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1932-6203"],["dc.title","Geminin is required for the maintenance of pluripotency"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","European Journal of Cancer"],["dc.bibliographiccitation.volume","50"],["dc.contributor.author","Suazo, C. Gallinas"],["dc.contributor.author","Klimke, Alexander"],["dc.contributor.author","Lize, M."],["dc.contributor.author","Kessel, Michael"],["dc.contributor.author","Dobbelstein, Matthias"],["dc.date.accessioned","2018-11-07T09:37:50Z"],["dc.date.available","2018-11-07T09:37:50Z"],["dc.date.issued","2014"],["dc.format.extent","S84"],["dc.identifier.isi","000351589700308"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/32930"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Sci Ltd"],["dc.publisher.place","Oxford"],["dc.relation.issn","1879-0852"],["dc.relation.issn","0959-8049"],["dc.title","microRNA-449 acts as a barrier to stemness"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","115"],["dc.bibliographiccitation.issue","7503"],["dc.bibliographiccitation.journal","Nature"],["dc.bibliographiccitation.lastpage","+"],["dc.bibliographiccitation.volume","510"],["dc.contributor.author","Song, Rui"],["dc.contributor.author","Walentek, Peter"],["dc.contributor.author","Sponer, Nicole"],["dc.contributor.author","Klimke, Alexander"],["dc.contributor.author","Lee, Joon Sub"],["dc.contributor.author","Dixon, Gary"],["dc.contributor.author","Harland, Richard"],["dc.contributor.author","Wan, Ying"],["dc.contributor.author","Lishko, Polina"],["dc.contributor.author","Lize, Muriel"],["dc.contributor.author","Kessel, Michael"],["dc.contributor.author","He, Lin"],["dc.date.accessioned","2018-11-07T09:38:59Z"],["dc.date.available","2018-11-07T09:38:59Z"],["dc.date.issued","2014"],["dc.description.abstract","The mir-34/449 family consists of six homologous miRNAs at three genomic loci. Redundancy of miR-34/449 miRNAs and their dominant expression in multiciliated epithelia suggest a functional significance in ciliogenesis. Here we report that mice deficient for all miR-34/449 miRNAs exhibited postnatal mortality, infertility and strong respiratory dysfunction caused by defective mucociliary clearance. In both mouse and Xenopus, miR-34/449-deficient multiciliated cells (MCCs) exhibited a significant decrease in cilia length and number, due to defective basal body maturation and apical docking. The effect of miR-34/449 on ciliogenesis was mediated, at least in part, by post-transcriptional repression of Cp110, a centriolar protein suppressing cilia assembly. Consistent with this, cp110 knockdown in miR-34/449-deficient MCCs restored ciliogenesis by rescuing basal body maturation and docking. Altogether, our findings elucidate conserved cellular and molecular mechanisms through which miR-34/449 regulate motile ciliogenesis."],["dc.identifier.doi","10.1038/nature13413"],["dc.identifier.isi","000336768900039"],["dc.identifier.pmid","24899310"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/33182"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","1476-4687"],["dc.relation.issn","0028-0836"],["dc.title","miR-34/449 miRNAs are required for motile ciliogenesis by repressing cp110"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","European Heart Journal"],["dc.bibliographiccitation.volume","34"],["dc.contributor.author","Gogiraju, R."],["dc.contributor.author","Steinbrecher, Julia H."],["dc.contributor.author","Lehnart, Stephan E."],["dc.contributor.author","Kessel, Michael"],["dc.contributor.author","Dobbelstein, Matthias"],["dc.contributor.author","Schaefer, K."],["dc.date.accessioned","2018-11-07T09:21:34Z"],["dc.date.available","2018-11-07T09:21:34Z"],["dc.date.issued","2013"],["dc.format.extent","319"],["dc.identifier.isi","000327744602072"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29138"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Oxford Univ Press"],["dc.publisher.place","Oxford"],["dc.relation.eventlocation","Amsterdam, NETHERLANDS"],["dc.relation.issn","1522-9645"],["dc.relation.issn","0195-668X"],["dc.title","Importance of tumor suppressor gene p53-mediated endothelial cell apoptosis for cardiac angiogenesis and hypertrophy"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e001770"],["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Journal of the American Heart Association"],["dc.bibliographiccitation.lastpage","21"],["dc.bibliographiccitation.volume","4"],["dc.contributor.author","Gogiraju, Rajinikanth"],["dc.contributor.author","Xu, Xingbo"],["dc.contributor.author","Bochenek, Magdalena L."],["dc.contributor.author","Steinbrecher, Julia H."],["dc.contributor.author","Lehnart, Stephan E."],["dc.contributor.author","Wenzel, Philip"],["dc.contributor.author","Kessel, Michael"],["dc.contributor.author","Zeisberg, Elisabeth M."],["dc.contributor.author","Dobbelstein, Matthias"],["dc.contributor.author","Schäfer, Katrin"],["dc.date.accessioned","2018-05-07T11:17:45Z"],["dc.date.available","2018-05-07T11:17:45Z"],["dc.date.issued","2015"],["dc.description.abstract","Cardiac dysfunction developing in response to chronic pressure overload is associated with apoptotic cell death and myocardial vessel rarefaction. We examined whether deletion of tumor suppressor p53 in endothelial cells may prevent the transition from cardiac hypertrophy to heart failure."],["dc.identifier.doi","10.1161/JAHA.115.001770"],["dc.identifier.gro","3142397"],["dc.identifier.pmid","25713289"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12727"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/14615"],["dc.identifier.url","https://sfb1002.med.uni-goettingen.de/production/literature/publications/81"],["dc.language.iso","en"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation","SFB 1002: Modulatorische Einheiten bei Herzinsuffizienz"],["dc.relation","SFB 1002 | C01: Epigenetische Kontrolle der Herzfibrose"],["dc.relation","SFB 1002 | C06: Mechanismen und Regulation der koronaren Gefäßneubildung"],["dc.relation.eissn","2047-9980"],["dc.relation.issn","2047-9980"],["dc.relation.issn","2047-9980"],["dc.relation.workinggroup","RG Lehnart (Cellular Biophysics and Translational Cardiology Section)"],["dc.relation.workinggroup","RG Schäfer (Translationale Vaskuläre Biologie)"],["dc.relation.workinggroup","RG E. Zeisberg (Kardiales Stroma)"],["dc.rights","CC BY-NC 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc/4.0"],["dc.title","Endothelial p53 deletion improves angiogenesis and prevents cardiac fibrosis and heart failure induced by pressure overload in mice"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]