Sloan, Katherine E.

[["dc.bibliographiccitation.firstpage","2004"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","EMBO reports"],["dc.bibliographiccitation.lastpage","2014"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","Warda, Ahmed S"],["dc.contributor.author","Kretschmer, Jens"],["dc.contributor.author","Hackert, Philipp"],["dc.contributor.author","Lenz, Christof"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Höbartner, Claudia"],["dc.contributor.author","Sloan, Katherine E"],["dc.contributor.author","Bohnsack, Markus T"],["dc.date.accessioned","2020-12-10T18:42:38Z"],["dc.date.available","2020-12-10T18:42:38Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.15252/embr.201744940"],["dc.identifier.eissn","1469-3178"],["dc.identifier.issn","1469-221X"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78032"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Human METTL16 is a N 6 ‐methyladenosine (m 6 A) methyltransferase that targets pre‐mRNAs and various non‐coding RNAs"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","237"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Cell Reports"],["dc.bibliographiccitation.lastpage","247"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Bohnsack, Markus T."],["dc.contributor.author","Watkins, Nicholas J."],["dc.date.accessioned","2018-11-07T09:19:15Z"],["dc.date.available","2018-11-07T09:19:15Z"],["dc.date.issued","2013"],["dc.description.abstract","Several proto-oncogenes and tumor suppressors regulate the production of ribosomes. Ribosome biogenesis is a major consumer of cellular energy, and defects result in p53 activation via repression of mouse double minute 2 (MDM2) homolog by the ribosomal proteins RPL5 and RPL11. Here, we report that RPL5 and RPL11 regulate p53 from the context of a ribosomal subcomplex, the 5S ribonucleoprotein particle (RNP). We provide evidence that the third component of this complex, the 5S rRNA, is critical for p53 regulation. In addition, we show that the 5S RNP is essential for the activation of p53 by p14(ARF), a protein that is activated by oncogene overexpression. Our data show that the abundance of the 5S RNP, and therefore p53 levels, is determined by factors regulating 5S complex formation and ribosome integration, including the tumor suppressor PICT1. The 5S RNP therefore emerges as the critical coordinator of signaling pathways that couple cell proliferation with ribosome production."],["dc.identifier.doi","10.1016/j.celrep.2013.08.049"],["dc.identifier.isi","000326152100024"],["dc.identifier.pmid","24120868"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10667"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28592"],["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 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/3.0"],["dc.title","The 5S RNP Couples p53 Homeostasis to Ribosome Biogenesis and Nucleolar Stress"],["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","4796"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Nucleic Acids Research"],["dc.bibliographiccitation.lastpage","4809"],["dc.bibliographiccitation.volume","45"],["dc.contributor.author","Wells, Graeme R."],["dc.contributor.author","Weichmann, Franziska"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Colvin, David"],["dc.contributor.author","Watkins, Nicholas J."],["dc.contributor.author","Schneider, Claudia"],["dc.date.accessioned","2018-11-07T10:23:54Z"],["dc.date.available","2018-11-07T10:23:54Z"],["dc.date.issued","2017"],["dc.description.abstract","Two proteins with PIN endonuclease domains, yUtp24(Fcf1)/hUTP24 and yUtp23/hUTP23 are essential for early pre-ribosomal (r) RNA cleavages at sites A0, A1/1 and A2/2a in yeast and humans. The yUtp24/hUTP24 PIN endonuclease is proposed to cleave at sites A1/1 and A2/2a, but the enzyme cleaving at site A0 is not known. Yeast yUtp23 contains a degenerate, non-essential PIN domain and functions together with the snR30 snoRNA, while human hUTP23 is associated with U17, the human snR30 counterpart. Using in vivo RNA-protein crosslinking and gel shift experiments, we reveal that yUtp23/hUTP23 makes direct contacts with expansion sequence 6 (ES6) in the 18S rRNA sequence and that yUtp23 interacts with the 3' half of the snR30 snoRNA. Protein-protein interaction studies further demonstrated that yeast yUtp23 and human hUTP23 directly interact with the H/ACA snoRNP protein yNhp2/hNHP2, the RNA helicase yRok1/hROK1(DDX52), the ribosome biogenesis factor yRrp7/hRRP7 and yUtp24/hUTP24. yUtp23/hUTP23 could therefore be central to the coordinated integration and release of ES6 binding factors and likely plays a pivotal role in remodeling this pre-rRNA region in both yeast and humans. Finally, studies using RNAi-rescue systems in human cells revealed that intact PIN domain and Zinc finger motifs in human hUTP23 are essential for 18S rRNA maturation."],["dc.identifier.doi","10.1093/nar/gkw1344"],["dc.identifier.isi","000400578600049"],["dc.identifier.pmid","28082392"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14964"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/42551"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Oxford Univ Press"],["dc.relation.issn","1362-4962"],["dc.relation.issn","0305-1048"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","The ribosome biogenesis factor yUtp23/hUTP23 coordinates key interactions in the yeast and human pre-40S particle and hUTP23 contains an essential PIN domain"],["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","209"],["dc.bibliographiccitation.journal","FEBS Journal"],["dc.bibliographiccitation.lastpage","210"],["dc.bibliographiccitation.volume","282"],["dc.contributor.author","Heininger, A. U."],["dc.contributor.author","Hackert, Philipp"],["dc.contributor.author","Andreou, Alexandra-Zoi"],["dc.contributor.author","Boon, K.-L."],["dc.contributor.author","Prior, M."],["dc.contributor.author","Schmidt, B."],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Schleiff, Enrico"],["dc.contributor.author","Deckers, Markus"],["dc.contributor.author","Lührmann, Reinhard"],["dc.contributor.author","Enderlein, Jörg"],["dc.contributor.author","Klostermeier, Dagmar"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2018-11-07T09:54:51Z"],["dc.date.available","2018-11-07T09:54:51Z"],["dc.date.issued","2015"],["dc.identifier.isi","000362570603174"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/36625"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.eventlocation","Berlin, GERMANY"],["dc.relation.issn","1742-4658"],["dc.relation.issn","1742-464X"],["dc.title","Sequestering and protein cofactor competition regulate a multifunctional RNA helicase in different pathways"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","18"],["dc.bibliographiccitation.journal","Nucleic Acids Research"],["dc.bibliographiccitation.volume","44"],["dc.contributor.author","Wells, Graeme R."],["dc.contributor.author","Weichmann, Franziska"],["dc.contributor.author","Colvin, David"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Kudla, Grzegorz"],["dc.contributor.author","Tollervey, David"],["dc.contributor.author","Watkins, Nicholas J."],["dc.contributor.author","Schneider, Claudia"],["dc.date.accessioned","2018-11-07T10:07:02Z"],["dc.date.available","2018-11-07T10:07:02Z"],["dc.date.issued","2016"],["dc.format.extent","9016"],["dc.identifier.doi","10.1093/nar/gkw645"],["dc.identifier.isi","000386945000043"],["dc.identifier.pmid","27418679"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39207"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Oxford Univ Press"],["dc.relation.issn","1362-4962"],["dc.relation.issn","0305-1048"],["dc.title","The PIN domain endonuclease Utp24 cleaves pre-ribosomal RNA at two coupled sites in yeast and humans (vol 44, pg 5399, 2016)"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1339"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","RNA"],["dc.bibliographiccitation.lastpage","1350"],["dc.bibliographiccitation.volume","24"],["dc.contributor.author","Kretschmer, Jens"],["dc.contributor.author","Rao, Harita"],["dc.contributor.author","Hackert, Philipp"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Höbartner, Claudia"],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2020-12-10T18:41:55Z"],["dc.date.available","2020-12-10T18:41:55Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1261/rna.064238.117"],["dc.identifier.eissn","1469-9001"],["dc.identifier.issn","1355-8382"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/77730"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","The m 6 A reader protein YTHDC2 interacts with the small ribosomal subunit and the 5′–3′ exoribonuclease XRN1"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1265"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Biological Chemistry"],["dc.bibliographiccitation.lastpage","1276"],["dc.bibliographiccitation.volume","399"],["dc.contributor.author","Bohnsack, Markus T."],["dc.contributor.author","Sloan, Katherine E."],["dc.date.accessioned","2020-12-10T18:42:22Z"],["dc.date.available","2020-12-10T18:42:22Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1515/hsz-2018-0205"],["dc.identifier.eissn","1437-4315"],["dc.identifier.issn","1431-6730"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/77914"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Modifications in small nuclear RNAs and their roles in spliceosome assembly and function"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","237"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Trends in Biochemical Sciences"],["dc.bibliographiccitation.lastpage","250"],["dc.bibliographiccitation.volume","43"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2020-12-10T15:21:34Z"],["dc.date.available","2020-12-10T15:21:34Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1016/j.tibs.2018.02.001"],["dc.identifier.issn","0968-0004"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/73074"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Unravelling the Mechanisms of RNA Helicase Regulation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","259"],["dc.bibliographiccitation.lastpage","268"],["dc.bibliographiccitation.seriesnr","1562"],["dc.contributor.author","Haag, Sara"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Höbartner, Claudia"],["dc.contributor.author","Bohnsack, Markus T."],["dc.contributor.editor","Lusser, Alexandra"],["dc.date.accessioned","2021-06-02T10:44:25Z"],["dc.date.available","2021-06-02T10:44:25Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.1007/978-1-4939-6807-7_17"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/87031"],["dc.notes.intern","DOI-Import GROB-425"],["dc.publisher","Springer New York"],["dc.publisher.place","New York, NY"],["dc.relation.crisseries","Methods in Molecular Biology"],["dc.relation.eisbn","978-1-4939-6807-7"],["dc.relation.isbn","978-1-4939-6805-3"],["dc.relation.ispartof","Methods in Molecular Biology"],["dc.relation.ispartof","RNA Methylation : Methods and Protocols"],["dc.relation.ispartofseries","Methods in Molecular Biology; 1562"],["dc.title","In Vitro Assays for RNA Methyltransferase Activity"],["dc.type","book_chapter"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","553"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nucleic Acids Research"],["dc.bibliographiccitation.lastpage","564"],["dc.bibliographiccitation.volume","43"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Leisegang, Matthias S."],["dc.contributor.author","Doebele, Carmen"],["dc.contributor.author","Ramirez, Ana S."],["dc.contributor.author","Simm, Stefan"],["dc.contributor.author","Safferthal, Charlotta"],["dc.contributor.author","Kretschmer, Jens"],["dc.contributor.author","Schorge, Tobias"],["dc.contributor.author","Markoutsa, Stavroula"],["dc.contributor.author","Haag, Sara"],["dc.contributor.author","Karas, Michael"],["dc.contributor.author","Ebersberger, Ingo"],["dc.contributor.author","Schleiff, Enrico"],["dc.contributor.author","Watkins, Nicholas J."],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2018-11-07T10:03:32Z"],["dc.date.available","2018-11-07T10:03:32Z"],["dc.date.issued","2015"],["dc.description.abstract","Translation fidelity and efficiency require multiple ribosomal (r)RNA modifications that are mostly mediated by small nucleolar (sno)RNPs during ribosome production. Overlapping basepairing of snoRNAs with pre-rRNAs often necessitates sequential and efficient association and dissociation of the snoRNPs, however, how such hierarchy is established has remained unknown so far. Here, we identify several late-acting snoRNAs that bind pre-40S particles in human cells and show that their association and function in pre-40S complexes is regulated by the RNA helicase DDX21. We map DDX21 crosslinking sites on pre-rRNAs and show their overlap with the basepairing sites of the affected snoRNAs. While DDX21 activity is required for recruitment of the late-acting snoRNAs SNORD56 and SNORD68, earlier snoRNAs are not affected by DDX21 depletion. Together, these observations provide an understanding of the timing and ordered hierarchy of snoRNP action in pre-40S maturation and reveal a novel mode of regulation of snoRNP function by an RNA helicase in human cells."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2014"],["dc.identifier.doi","10.1093/nar/gku1291"],["dc.identifier.isi","000350207100052"],["dc.identifier.pmid","25477391"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11460"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38490"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","1362-4962"],["dc.relation.issn","0305-1048"],["dc.rights","CC BY-NC 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc/4.0"],["dc.title","The association of late-acting snoRNPs with human pre-ribosomal complexes requires the RNA helicase DDX21"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]