Lührmann, Reinhard

[["dc.bibliographiccitation.firstpage","278"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","BIOspektrum"],["dc.bibliographiccitation.lastpage","282"],["dc.bibliographiccitation.volume","24"],["dc.contributor.author","Dybkov, Olexandr"],["dc.contributor.author","Stützer, Alexandra"],["dc.contributor.author","Bertram, Karl"],["dc.contributor.author","Kastner, Berthold"],["dc.contributor.author","Stark, Holger"],["dc.contributor.author","Lührmann, Reinhard"],["dc.contributor.author","Urlaub, Henning"],["dc.date.accessioned","2018-11-15T12:52:38Z"],["dc.date.accessioned","2021-10-27T13:12:42Z"],["dc.date.available","2018-11-15T12:52:38Z"],["dc.date.available","2021-10-27T13:12:42Z"],["dc.date.issued","2018"],["dc.description.abstract","Cryo-electron microscopy (cryo-EM) can solve structures of highly dynamic macromolecular complexes. To characterize less well defined regions in cryo-EM images, cross-linking coupled with mass spectrometry (CX-MS) provides valuable information on the arrangement of domains and amino acids. CX-MS involves covalent linkage of protein residues close to each other and identifying these connections by mass spectrometry. Here, we summarise the advances of CX-MS and its integration with cryo-EM for structural reconstruction."],["dc.identifier.doi","10.1007/s12268-018-0909-6"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15570"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/91715"],["dc.language.iso","de"],["dc.notes.intern","Migrated from goescholar"],["dc.relation.issn","1868-6249"],["dc.relation.issn","0947-0867"],["dc.relation.orgunit","Fakultät für Chemie"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Protein-Cross-Linking zur Aufklärung von komplexen Strukturen"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","267"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Molecular Cell"],["dc.bibliographiccitation.lastpage","278"],["dc.bibliographiccitation.volume","24"],["dc.contributor.author","Sander, Bjoern"],["dc.contributor.author","Golas, Monika M."],["dc.contributor.author","Makarov, Evgeny M."],["dc.contributor.author","Brahms, Hero"],["dc.contributor.author","Kastner, Berthold"],["dc.contributor.author","Lührmann, Reinhard"],["dc.contributor.author","Stark, Holger"],["dc.date.accessioned","2021-03-05T08:58:09Z"],["dc.date.available","2021-03-05T08:58:09Z"],["dc.date.issued","2006"],["dc.identifier.doi","10.1016/j.molcel.2006.08.021"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/80026"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-393"],["dc.relation.issn","1097-2765"],["dc.title","Organization of Core Spliceosomal Components U5 snRNA Loop I and U4/U6 Di-snRNP within U4/U6.U5 Tri-snRNP as Revealed by Electron Cryomicroscopy"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","5528"],["dc.bibliographiccitation.issue","14"],["dc.bibliographiccitation.journal","Molecular and Cellular Biology"],["dc.bibliographiccitation.lastpage","5543"],["dc.bibliographiccitation.volume","26"],["dc.contributor.author","Deckert, Jochen"],["dc.contributor.author","Hartmuth, Klaus"],["dc.contributor.author","Boehringer, Daniel"],["dc.contributor.author","Behzadnia, Nastaran"],["dc.contributor.author","Will, Cindy L."],["dc.contributor.author","Kastner, Berthold"],["dc.contributor.author","Stark, Holger"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Lührmann, Reinhard"],["dc.date.accessioned","2021-03-05T08:59:02Z"],["dc.date.available","2021-03-05T08:59:02Z"],["dc.date.issued","2006"],["dc.identifier.doi","10.1128/MCB.00582-06"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/80332"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-393"],["dc.relation.eissn","1098-5549"],["dc.relation.issn","0270-7306"],["dc.title","Protein Composition and Electron Microscopy Structure of Affinity-Purified Human Spliceosomal B Complexes Isolated under Physiological Conditions"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","593"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Molecular Cell"],["dc.bibliographiccitation.lastpage","608"],["dc.bibliographiccitation.volume","36"],["dc.contributor.author","Fabrizio, Patrizia"],["dc.contributor.author","Dannenberg, Julia"],["dc.contributor.author","Dube, Prakash"],["dc.contributor.author","Kastner, Berthold"],["dc.contributor.author","Stark, Holger"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Lührmann, Reinhard"],["dc.date.accessioned","2018-11-07T11:21:51Z"],["dc.date.available","2018-11-07T11:21:51Z"],["dc.date.issued","2009"],["dc.description.abstract","Metazoan spliceosomes exhibit an elaborate protein composition required for canonical and alternative splicing. Thus, the minimal set of proteins essential for activation and catalysis remains elusive. We therefore purified in vitro assembled, precatalytic spliceosomal complex B, activated Bact, and step 1 complex C from the simple eukaryote Saccharomyces cerevisiae. Mass spectrometry revealed that yeast spliceosomes contain fewer proteins than metazoans and that each functional stage is very homogeneous. Dramatic compositional changes convert B to Bact, which is composed of similar to 40 evolutionarily conserved proteins that organize the catalytic core. Additional remodeling occurs concomitant with step 1, during which nine proteins are recruited to form complex C. The moderate number of proteins recruited to complex C will allow investigations of the chemical reactions in a fully defined system. Electron microscopy reveals high-quality images of yeast spliceosomes at defined functional stages, indicating that they are well-suited for three-dimensional structure analyses."],["dc.description.sponsorship","European Commission [EURASNET-518238]; Ernst Jung Stiftung"],["dc.identifier.doi","10.1016/j.molcel.2009.09.040"],["dc.identifier.isi","000272534800008"],["dc.identifier.pmid","19941820"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/55879"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.relation.issn","1097-2765"],["dc.title","The Evolutionarily Conserved Core Design of the Catalytic Activation Step of the Yeast Spliceosome"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","463"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Nature Structural & Molecular Biology"],["dc.bibliographiccitation.lastpage","468"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Boehringer, Daniel"],["dc.contributor.author","Makarov, Evgeny M."],["dc.contributor.author","Sander, Bjoern"],["dc.contributor.author","Makarova, Olga V."],["dc.contributor.author","Kastner, Berthold"],["dc.contributor.author","Lührmann, Reinhard"],["dc.contributor.author","Stark, Holger"],["dc.date.accessioned","2021-03-05T08:58:30Z"],["dc.date.available","2021-03-05T08:58:30Z"],["dc.date.issued","2004"],["dc.identifier.doi","10.1038/nsmb761"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/80158"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-393"],["dc.relation.eissn","1545-9985"],["dc.relation.issn","1545-9993"],["dc.title","Three-dimensional structure of a pre-catalytic human spliceosomal complex B"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","53"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Methods"],["dc.bibliographiccitation.lastpage","55"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Kastner, Berthold"],["dc.contributor.author","Fischer, Niels"],["dc.contributor.author","Golas, Monika Mariola"],["dc.contributor.author","Sander, Bjoern"],["dc.contributor.author","Dube, Prakash"],["dc.contributor.author","Boehringer, Daniel"],["dc.contributor.author","Hartmuth, Klaus"],["dc.contributor.author","Deckert, Jochen"],["dc.contributor.author","Hauer, Florian"],["dc.contributor.author","Wolf, Elmar"],["dc.contributor.author","Uchtenhagen, Hannes"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Herzog, Franz"],["dc.contributor.author","Peters, Jan Michael"],["dc.contributor.author","Poerschke, Dietmar"],["dc.contributor.author","Lührmann, Reinhard"],["dc.contributor.author","Stark, Holger"],["dc.date.accessioned","2021-03-05T08:58:29Z"],["dc.date.available","2021-03-05T08:58:29Z"],["dc.date.issued","2007"],["dc.identifier.doi","10.1038/nmeth1139"],["dc.identifier.pii","BFnmeth1139"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/80155"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-393"],["dc.relation.eissn","1548-7105"],["dc.relation.issn","1548-7091"],["dc.title","GraFix: sample preparation for single-particle electron cryomicroscopy"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","318"],["dc.bibliographiccitation.issue","7641"],["dc.bibliographiccitation.journal","Nature"],["dc.bibliographiccitation.volume","542"],["dc.contributor.author","Bertram, Karl"],["dc.contributor.author","Agafonov, Dmitry E."],["dc.contributor.author","Liu, Wen-Ti"],["dc.contributor.author","Dybkov, Olexandr"],["dc.contributor.author","Will, Cindy L."],["dc.contributor.author","Hartmuth, Klaus"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Kastner, Berthold"],["dc.contributor.author","Stark, Holger"],["dc.contributor.author","Lührmann, Reinhard"],["dc.date.accessioned","2018-11-07T10:27:23Z"],["dc.date.available","2018-11-07T10:27:23Z"],["dc.date.issued","2017"],["dc.description.abstract","Spliceosome rearrangements facilitated by RNA helicase PRP16 before catalytic step two of splicing are poorly understood. Here we report a 3D cryo-electron microscopy structure of the human spliceosomal C complex stalled directly after PRP16 action (C ). The architecture of the catalytic U2-U6 ribonucleoprotein (RNP) core of the human C spliceosome is very similar to that of the yeast pre-Prp16 C complex. However, in C the branched intron region is separated from the catalytic centre by approximately 20 angstrom, and its position close to the U6 small nuclear RNA ACAGA box is stabilized by interactions with the PRP8 RNase H-like and PRP17 WD40 domains. RNA helicase PRP22 is located about 100 angstrom from the catalytic centre, suggesting that it destabilizes the spliced mRNA after step two from a distance. Comparison of the structure of the yeast C and human C complexes reveals numerous RNP rearrangements that are likely to be facilitated by PRP16, including a large-scale movement of the U2 small nuclear RNP."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft [SFB 860]"],["dc.identifier.doi","10.1038/nature21079"],["dc.identifier.isi","000394451600030"],["dc.identifier.pmid","28076346"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/43225"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","1476-4687"],["dc.relation.issn","0028-0836"],["dc.title","Cryo-EM structure of a human spliceosome activated for step 2 of splicing"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2528"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","RNA"],["dc.bibliographiccitation.lastpage","2537"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Karaduman, Ramazan"],["dc.contributor.author","Dube, Prakash"],["dc.contributor.author","Stark, Holger"],["dc.contributor.author","Fabrizio, Patrizia"],["dc.contributor.author","Kastner, Berthold"],["dc.contributor.author","Lührmann, Reinhard"],["dc.date.accessioned","2018-11-07T11:08:52Z"],["dc.date.available","2018-11-07T11:08:52Z"],["dc.date.issued","2008"],["dc.description.abstract","Protein components of the U6 snRNP (Prp24p and LSm2-8) are thought to act cooperatively in facilitating the annealing of U6 and U4 snRNAs during U4/U6 di-snRNP formation. To learn more about the spatial arrangement of these proteins in S. cerevisiae U6 snRNPs, we investigated the structure of this particle by electron microscopy. U6 snRNPs, purified by affinity chromatography and gradient centrifugation, and then immediately adsorbed to the carbon film support, revealed an open form in which the Prp24 protein and the ring formed by the LSm proteins were visible as two separate morphological domains, while particles stabilized by chemical cross-linking in solution under mild conditions before binding to the carbon film exhibited a compact form, with the two domains in close proximity to one another. In the open form, individual LSm proteins were located by a novel approach employing C-terminal genetic tagging of the LSm proteins with yECitrine. These studies show the Prp24 protein at defined distances from each subunit of the LSm ring, which in turn suggests that the LSm ring is positioned in a consistent manner on the U6 RNA. Furthermore, in agreement with the EM observations, UV cross-linking revealed U6 RNA in contact with the LSm2 protein at the interface between Prp24p and the LSm ring. Further, LSmp-Prp24p interactions may be restricted to the closed form, which appears to represent the solution structure of the U6 snRNP particle."],["dc.identifier.doi","10.1261/rna.1369808"],["dc.identifier.isi","000261398400010"],["dc.identifier.pmid","18971323"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/52888"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cold Spring Harbor Lab Press, Publications Dept"],["dc.relation.issn","1355-8382"],["dc.title","Structure of yeast U6 snRNPs: Arrangement of Prp24p and the LSm complex as revealed by electron microscopy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2283"],["dc.bibliographiccitation.issue","15"],["dc.bibliographiccitation.journal","The EMBO Journal"],["dc.bibliographiccitation.lastpage","2292"],["dc.bibliographiccitation.volume","28"],["dc.contributor.author","Wolf, Elmar"],["dc.contributor.author","Kastner, Berthold"],["dc.contributor.author","Deckert, Jochen"],["dc.contributor.author","Merz, Christian"],["dc.contributor.author","Stark, Holger"],["dc.contributor.author","Lührmann, Reinhard"],["dc.date.accessioned","2021-03-05T08:58:27Z"],["dc.date.available","2021-03-05T08:58:27Z"],["dc.date.issued","2009"],["dc.identifier.doi","10.1038/emboj.2009.171"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/80139"],["dc.notes.intern","DOI Import GROB-393"],["dc.relation.eissn","1460-2075"],["dc.relation.issn","0261-4189"],["dc.title","Exon, intron and splice site locations in the spliceosomal B complex"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e23533"],["dc.bibliographiccitation.journal","eLife"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Sidarovich, Anzhalika"],["dc.contributor.author","Will, Cindy L."],["dc.contributor.author","Anokhina, Maria M."],["dc.contributor.author","Ceballos, Javier"],["dc.contributor.author","Sievers, Sonja"],["dc.contributor.author","Agafonov, Dmitry E."],["dc.contributor.author","Samatov, Timur"],["dc.contributor.author","Bao, Penghui"],["dc.contributor.author","Kastner, Berthold"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Waldmann, Herbert"],["dc.contributor.author","Luehrmann, Reinhard"],["dc.date.accessioned","2018-11-07T10:26:11Z"],["dc.date.available","2018-11-07T10:26:11Z"],["dc.date.issued","2017"],["dc.description.abstract","Small molecule inhibitors of pre-mRNA splicing are important tools for identifying new spliceosome assembly intermediates, allowing a finer dissection of spliceosome dynamics and function. Here, we identified a small molecule that inhibits human pre-mRNA splicing at an intermediate stage during conversion of pre-catalytic spliceosomal B complexes into activated B-act complexes. Characterization of the stalled complexes (designated B-028) revealed that U4/U6 snRNP proteins are released during activation before the U6 Lsm and B-specific proteins, and before recruitment and/or stable incorporation of Prp19/CDC5L complex and other B-act complex proteins. The U2/U6 RNA network in B-028 complexes differs from that of the Bact complex, consistent with the idea that the catalytic RNA core forms stepwise during the B to B-act transition and is likely stabilized by the Prp19/CDC5L complex and related proteins. Taken together, our data provide new insights into the RNP rearrangements and extensive exchange of proteins that occurs during spliceosome activation."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft [LU 294/15-1]"],["dc.identifier.doi","10.7554/eLife.23533"],["dc.identifier.isi","000397628000001"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14442"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/42985"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Elife Sciences Publications Ltd"],["dc.relation.issn","2050-084X"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Identification of a small molecule inhibitor that stalls splicing at an early step of spliceosome activation"],["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"]]