Cretu, Constantin

[["dc.bibliographiccitation.firstpage","307"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Molecular Cell"],["dc.bibliographiccitation.lastpage","319"],["dc.bibliographiccitation.volume","64"],["dc.contributor.author","Cretu, Constantin"],["dc.contributor.author","Schmitzova, Jana"],["dc.contributor.author","Ponce-Salvatierra, Almudena"],["dc.contributor.author","Dybkov, Olexandr"],["dc.contributor.author","De laurentiis, Evelina I."],["dc.contributor.author","Sharma, Kundan"],["dc.contributor.author","Will, Cindy L."],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Lührmann, Reinhard"],["dc.contributor.author","Pena, Vladimir"],["dc.date.accessioned","2018-11-07T10:06:55Z"],["dc.date.available","2018-11-07T10:06:55Z"],["dc.date.issued","2016"],["dc.description.abstract","SF3b is a heptameric protein complex of the U2 small nuclear ribonucleoprotein (snRNP) that is essential for pre-mRNA splicing. Mutations in the largest SF3b subunit, SF3B1/SF3b155, are linked to cancer and lead to alternative branch site (BS) selection. Here we report the crystal structure of a human SF3b core complex, revealing how the distinctive conformation of SF3b155's HEAT domain is maintained by multiple contacts with SF3b130, SF3b10, and SF3b14b. Protein-protein crosslinking enabled the localization of the BS-binding proteins p14 and U2AF65 within SF3b155's HEAT-repeat superhelix, which together with SF3b14b forms a composite RNA-binding platform. SF3b155 residues, the mutation of which leads to cancer, contribute to the tertiary structure of the HEAT superhelix and its surface properties in the proximity of p14 and U2AF65. The molecular architecture of SF3b reveals the spatial organization of cancer-related SF3b155 mutations and advances our understanding of their effects on SF3b structure and function."],["dc.identifier.doi","10.1016/j.molcel.2016.08.036"],["dc.identifier.isi","000389515000011"],["dc.identifier.pmid","27720643"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39188"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","1097-4164"],["dc.relation.issn","1097-2765"],["dc.title","Molecular Architecture of SF3b and Structural Consequences of Its Cancer-Related Mutations"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","979"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Molecular Cell"],["dc.bibliographiccitation.lastpage","992.e6"],["dc.bibliographiccitation.volume","69"],["dc.contributor.author","de Moura, Tales Rocha"],["dc.contributor.author","Mozaffari-Jovin, Sina"],["dc.contributor.author","Szabó, Csaba Zoltán Kibédi"],["dc.contributor.author","Schmitzová, Jana"],["dc.contributor.author","Dybkov, Olexandr"],["dc.contributor.author","Cretu, Constantin"],["dc.contributor.author","Kachala, Michael"],["dc.contributor.author","Svergun, Dmitri"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Lührmann, Reinhard"],["dc.contributor.author","Pena, Vladimir"],["dc.date.accessioned","2020-12-10T15:20:22Z"],["dc.date.available","2020-12-10T15:20:22Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1016/j.molcel.2018.02.022"],["dc.identifier.issn","1097-2765"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/72647"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Prp19/Pso4 Is an Autoinhibited Ubiquitin Ligase Activated by Stepwise Assembly of Three Splicing Factors"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","265"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Molecular Cell"],["dc.bibliographiccitation.lastpage","273.e8"],["dc.bibliographiccitation.volume","70"],["dc.contributor.author","Cretu, Constantin"],["dc.contributor.author","Agrawal, Anant A."],["dc.contributor.author","Cook, Andrew"],["dc.contributor.author","Will, Cindy L."],["dc.contributor.author","Fekkes, Peter"],["dc.contributor.author","Smith, Peter G."],["dc.contributor.author","Lührmann, Reinhard"],["dc.contributor.author","Larsen, Nicholas"],["dc.contributor.author","Buonamici, Silvia"],["dc.contributor.author","Pena, Vladimir"],["dc.date.accessioned","2022-11-07T07:41:02Z"],["dc.date.available","2022-11-07T07:41:02Z"],["dc.date.issued","2018"],["dc.description.abstract","SF3B is a multi-protein complex essential for branch site (BS) recognition and selection during pre-mRNA splicing. Several splicing modulators with antitumor activity bind SF3B and thereby modulate splicing. Here we report the crystal structure of a human SF3B core in complex with pladienolide B (PB), a macrocyclic splicing modulator and potent inhibitor of tumor cell proliferation. PB stalls SF3B in an open conformation by acting like a wedge within a hinge, modulating SF3B's transition to the closed conformation needed to form the BS adenosine-binding pocket and stably accommodate the BS/U2 duplex. This work explains the structural basis for the splicing modulation activity of PB and related compounds, and reveals key interactions between SF3B and a common pharmacophore, providing a framework for future structure-based drug design."],["dc.identifier.doi","10.1016/j.molcel.2018.03.011"],["dc.identifier.pmid","29656923"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/116954"],["dc.language.iso","en"],["dc.relation.eissn","1097-4164"],["dc.relation.issn","1097-2765"],["dc.relation.orgunit","Max-Planck-Institut für biophysikalische Chemie"],["dc.title","Structural Basis of Splicing Modulation by Antitumor Macrolide Compounds"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]