Dobbelstein, Matthias

[["dc.bibliographiccitation.firstpage","A665"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Gastroenterology"],["dc.bibliographiccitation.volume","118"],["dc.contributor.author","Roth, Judith C."],["dc.contributor.author","Koch, Philipp"],["dc.contributor.author","Contente, Ana"],["dc.contributor.author","Dobbelstein, Matthias"],["dc.date.accessioned","2022-03-01T11:45:28Z"],["dc.date.available","2022-03-01T11:45:28Z"],["dc.date.issued","2000"],["dc.identifier.doi","10.1016/S0016-5085(00)84796-4"],["dc.identifier.pii","S0016508500847964"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103338"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0016-5085"],["dc.title","Tumor-derived mutations within the DNA-binding domain of p53 that phenotypically resemble the deletion of the proline-rich domain"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","11"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Cell Cycle"],["dc.bibliographiccitation.lastpage","12"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Dobbelstein, Matthias"],["dc.date.accessioned","2018-11-07T09:30:38Z"],["dc.date.available","2018-11-07T09:30:38Z"],["dc.date.issued","2013"],["dc.identifier.doi","10.4161/cc.22917"],["dc.identifier.isi","000313414700006"],["dc.identifier.pmid","23255095"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/31354"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Landes Bioscience"],["dc.relation.issn","1538-4101"],["dc.title","Interchanging heads: p53 re-composes the DREAM/MMB complex to repress transcription"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","315"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Cell Cycle"],["dc.bibliographiccitation.lastpage","321"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Schumann, M."],["dc.contributor.author","Dobbelstein, Matthias"],["dc.date.accessioned","2018-11-07T10:21:13Z"],["dc.date.available","2018-11-07T10:21:13Z"],["dc.date.issued","2006"],["dc.description.abstract","Adenoviruses lacking their PKR-antagonizing VA RNAs replicate poorly in primary cells. It has been suggested that these virus recombinants still replicate efficiently in tumor cells with Ras mutations and might therefore be useful in tumor therapy. The ability of interferon-sensitive viruses to grow in Ras-mutant tumor cells is generally ascribed to a postulated inhibitory effect of mutant Ras on PKR. We have constructed a set of isogenic adenoviruses that lack either or both VA RNA species, and tested virus replication in a variety of cell species with different Ras status. In tendency, VA-less viruses replicated with higher efficiency in Ras-mutant cells, as compared to cell lines without Ras mutation. However, several exceptions to this rule were observed, arguing against a direct inhibition of PKR by mutant Ras. Phosphorylation of the PKR-substrate elF2 alpha was observed regardless of the Ras mutational status, upon infection with VA-less adenoviruses in the presence of interferon, but also upon addition of the PKR activator polyIC to cells. When comparing two isogenic cell lines that differ solely with regard to the presence or absence of mutant Ras, no difference was observed concerning the replication of VA-less adenoviruses or the phosphorylation of elF2 alpha. We conclude that mutant Ras does not directly affect elF2 alpha phosphorylation or the replication of interferon-sensitive adenoviruses. These results strongly suggest that the Ras mutational status is insufficient to predict the oncolytic effect of interferon-sensitive viruses. We propose that Ras mutations predispose tumor cells to undergo secondary changes that sometimes enable the replication of interferon-sensitive viruses."],["dc.identifier.doi","10.4161/cc.5.3.2411"],["dc.identifier.isi","000237246600018"],["dc.identifier.pmid","16434881"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/42047"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Landes Bioscience"],["dc.relation.issn","1538-4101"],["dc.title","Activating ras mutations fail to ensure efficient replication of adenovirus mutants lacking VA-RNA"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","780"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Cell Death and Differentiation"],["dc.bibliographiccitation.lastpage","780"],["dc.bibliographiccitation.volume","26"],["dc.contributor.author","Kramer, Daniela"],["dc.contributor.author","Stark, Nadine"],["dc.contributor.author","Schulz-Heddergott, Ramona"],["dc.contributor.author","Erytch, Norman"],["dc.contributor.author","Edmunds, Shelley"],["dc.contributor.author","Roßmann, Laura"],["dc.contributor.author","Bastians, Holger"],["dc.contributor.author","Concin, Nicole"],["dc.contributor.author","Moll, Ute M."],["dc.contributor.author","Dobbelstein, Matthias"],["dc.date.accessioned","2020-12-10T18:09:42Z"],["dc.date.available","2020-12-10T18:09:42Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1038/s41418-018-0190-8"],["dc.identifier.eissn","1476-5403"],["dc.identifier.issn","1350-9047"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/73731"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.relation.iserratumof","/handle/2/43281"],["dc.title","Correction: Strong antitumor synergy between DNA crosslinking and HSP90 inhibition causes massive premitotic DNA fragmentation in ovarian cancer cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","erratum_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","300"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Cell Death and Differentiation"],["dc.bibliographiccitation.lastpage","316"],["dc.bibliographiccitation.volume","24"],["dc.contributor.author","Kramer, Daniela"],["dc.contributor.author","Stark, Nadine"],["dc.contributor.author","Schulz-Heddergott, Ramona"],["dc.contributor.author","Erytch, Norman"],["dc.contributor.author","Edmunds, Shelley"],["dc.contributor.author","Rossmann, Laura"],["dc.contributor.author","Bastians, Holger"],["dc.contributor.author","Concin, Nicole"],["dc.contributor.author","Moll, Ute M."],["dc.contributor.author","Dobbelstein, Matthias"],["dc.date.accessioned","2018-11-07T10:27:41Z"],["dc.date.available","2018-11-07T10:27:41Z"],["dc.date.issued","2017"],["dc.description.abstract","All current regimens for treating ovarian cancer center around carboplatin as standard first line. The HSP90 inhibitor ganetespib is currently being assessed in advanced clinical oncology trials. Thus, we tested the combined effects of ganetespib and carboplatin on a panel of 15 human ovarian cancer lines. Strikingly, the two drugs strongly synergized in cytotoxicity in tumor cells lacking wild-type p53. Mechanistically, ganetespib and carboplatin in combination, but not individually, induced persistent DNA damage causing massive global chromosome fragmentation. Live-cell microscopy revealed chromosome fragmentation occurring to a dramatic degree when cells condensed their chromatin in preparation for mitosis, followed by cell death in mitosis or upon aberrant exit from mitosis. HSP90 inhibition caused the rapid decay of key components of the Fanconi anemia pathway required for repair of carboplatin-induced interstrand crosslinks (ICLs), as well as of cell cycle checkpoint mediators. Overexpressing FancA rescued the DNA damage induced by the drug combination, indicating that FancA is indeed a key client of Hsp90 that enables cancer cell survival in the presence of ICLs. Conversely, depletion of nuclease DNA2 prevented chromosomal fragmentation, pointing to an imbalance of defective repair in the face of uncontrolled nuclease activity as mechanistic basis for the observed premitotic DNA fragmentation. Importantly, the drug combination induced robust antitumor activity in xenograft models, again accompanied with depletion of FancA. In sum, our findings indicate that ganetespib strongly potentiates the antitumor efficacy of carboplatin by causing combined inhibition of DNA repair and cell cycle control mechanisms, thus triggering global chromosome disruption, aberrant mitosis and cell death."],["dc.identifier.doi","10.1038/cdd.2016.124"],["dc.identifier.isi","000395789500012"],["dc.identifier.pmid","27834954"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/43281"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Nature Publishing Group"],["dc.relation.haserratum","/handle/2/73731"],["dc.relation.issn","1476-5403"],["dc.relation.issn","1350-9047"],["dc.title","Strong antitumor synergy between DNA crosslinking and HSP90 inhibition causes massive premitotic DNA fragmentation in ovarian cancer cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","688"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Biochemical and Biophysical Research Communications"],["dc.bibliographiccitation.lastpage","693"],["dc.bibliographiccitation.volume","331"],["dc.contributor.author","Dobbelstein, Matthias"],["dc.contributor.author","Strano, Sabrina"],["dc.contributor.author","Roth, Judith"],["dc.contributor.author","Blandino, Giovanni"],["dc.date.accessioned","2022-03-01T11:44:47Z"],["dc.date.available","2022-03-01T11:44:47Z"],["dc.date.issued","2005"],["dc.identifier.doi","10.1016/j.bbrc.2005.03.155"],["dc.identifier.pii","S0006291X05006613"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103119"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0006-291X"],["dc.title","p73-induced apoptosis: A question of compartments and cooperation"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

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[["dc.bibliographiccitation.firstpage","5686"],["dc.bibliographiccitation.issue","36"],["dc.bibliographiccitation.journal","Oncogene"],["dc.bibliographiccitation.lastpage","5693"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Waltermann, Angelika"],["dc.contributor.author","Kartasheva, Natalia N"],["dc.contributor.author","Dobbelstein, Matthias"],["dc.date.accessioned","2022-03-01T11:46:06Z"],["dc.date.available","2022-03-01T11:46:06Z"],["dc.date.issued","2003"],["dc.identifier.doi","10.1038/sj.onc.1206859"],["dc.identifier.pii","BF1206859"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103562"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1476-5594"],["dc.relation.issn","0950-9232"],["dc.title","Differential regulation of p63 and p73 expression"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1609"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","EMBO Reports"],["dc.bibliographiccitation.lastpage","1623"],["dc.bibliographiccitation.volume","17"],["dc.contributor.author","Kari, Vijayalakshmi"],["dc.contributor.author","Mansour, Wael Yassin"],["dc.contributor.author","Raul, Sanjay Kumar"],["dc.contributor.author","Baumgart, Simon J."],["dc.contributor.author","Mund, Andreas"],["dc.contributor.author","Grade, Marian"],["dc.contributor.author","Sirma, Hueseyin"],["dc.contributor.author","Simon, Ronald"],["dc.contributor.author","Will, Hans"],["dc.contributor.author","Dobbelstein, Matthias"],["dc.contributor.author","Dikomey, Ekkehard"],["dc.contributor.author","Johnsen, Steven A."],["dc.date.accessioned","2018-11-07T10:06:25Z"],["dc.date.available","2018-11-07T10:06:25Z"],["dc.date.issued","2016"],["dc.description.abstract","The CHD1 gene, encoding the chromo-domain helicase DNA-binding protein-1, is one of the most frequently deleted genes in prostate cancer. Here, we examined the role of CHD1 in DNA double-strand break (DSB) repair in prostate cancer cells. We show that CHD1 is required for the recruitment of CtIP to chromatin and subsequent end resection during DNA DSB repair. Our data support a role for CHD1 in opening the chromatin around the DSB to facilitate the recruitment of homologous recombination (HR) proteins. Consequently, depletion of CHD1 specifically affects HR-mediated DNA repair but not non-homologous end joining. Together, we provide evidence for a previously unknown role of CHD1 in DNA DSB repair via HR and show that CHD1 depletion sensitizes cells to PARP inhibitors, which has potential therapeutic relevance. Our findings suggest that CHD1 deletion, like BRCA1/2 mutation in ovarian cancer, may serve as a marker for prostate cancer patient stratification and the utilization of targeted therapies such as PARP inhibitors, which specifically target tumors with HR defects."],["dc.identifier.doi","10.15252/embr.201642352"],["dc.identifier.isi","000387148700012"],["dc.identifier.pmid","27596623"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39090"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1469-3178"],["dc.relation.issn","1469-221X"],["dc.title","Loss of CHD1 causes DNA repair defects and enhances prostate cancer therapeutic responsiveness"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","315"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Nature Genetics"],["dc.bibliographiccitation.lastpage","320"],["dc.bibliographiccitation.volume","30"],["dc.contributor.author","Contente, Ana"],["dc.contributor.author","Dittmer, Alexandra"],["dc.contributor.author","Koch, Manuela C."],["dc.contributor.author","Roth, Judith"],["dc.contributor.author","Dobbelstein, Matthias"],["dc.date.accessioned","2022-03-01T11:45:52Z"],["dc.date.available","2022-03-01T11:45:52Z"],["dc.date.issued","2002"],["dc.identifier.doi","10.1038/ng836"],["dc.identifier.pii","BFng836z"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103481"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1546-1718"],["dc.relation.issn","1061-4036"],["dc.title","A polymorphic microsatellite that mediates induction of PIG3 by p53"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]