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.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"]]

[["dc.bibliographiccitation.artnumber","11997"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Boesler, Carsten"],["dc.contributor.author","Rigo, Norbert"],["dc.contributor.author","Anokhina, Maria M."],["dc.contributor.author","Tauchert, Marcel J."],["dc.contributor.author","Agafonov, Dmitry E."],["dc.contributor.author","Kastner, Berthold"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Will, Cindy L."],["dc.contributor.author","Luehrmann, Reinhard"],["dc.date.accessioned","2017-09-07T11:44:49Z"],["dc.date.available","2017-09-07T11:44:49Z"],["dc.date.issued","2016"],["dc.description.abstract","The precise role of the spliceosomal DEAD-box protein Prp28 in higher eukaryotes remains unclear. We show that stable tri-snRNP association during pre-catalytic spliceosomal B complex formation is blocked by a dominant-negative hPrp28 mutant lacking ATPase activity. Complexes formed in the presence of ATPase-deficient hPrp28 represent a novel assembly intermediate, the pre-B complex, that contains U1, U2 and loosely associated tri-snRNP and is stalled before disruption of the U1/5'ss base pairing interaction, consistent with a role for hPrp28 in the latter. Pre-B and B complexes differ structurally, indicating that stable tri-snRNP integration is accompanied by substantial rearrangements in the spliceosome. Disruption of the U1/5'ss interaction alone is not sufficient to bypass the block by ATPase-deficient hPrp28, suggesting hPrp28 has an additional function at this stage of splicing. Our data provide new insights into the function of Prp28 in higher eukaryotes, and the requirements for stable tri-snRNP binding during B complex formation."],["dc.identifier.doi","10.1038/ncomms11997"],["dc.identifier.gro","3141654"],["dc.identifier.isi","000380044600001"],["dc.identifier.pmid","27377154"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13548"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/5787"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft (DFG) [LU 294/15-1, SFB860, TP A02]"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","2041-1723"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","A spliceosome intermediate with loosely associated tri-snRNP accumulates in the absence of Prp28 ATPase activity"],["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"]]