Stark, Holger

[["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","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","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","1237"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Nature Structural & Molecular Biology"],["dc.bibliographiccitation.lastpage","U50"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Warkocki, Zbigniew"],["dc.contributor.author","Odenwaelder, Peter"],["dc.contributor.author","Schmitzova, Jana"],["dc.contributor.author","Platzmann, Florian"],["dc.contributor.author","Stark, Holger"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Fabrizio, Patrizia"],["dc.contributor.author","Luehrmann, Reinhard"],["dc.date.accessioned","2017-09-07T11:46:45Z"],["dc.date.available","2017-09-07T11:46:45Z"],["dc.date.issued","2009"],["dc.description.abstract","The spliceosome is a ribonucleoprotein machine that removes introns from pre-mRNA in a two-step reaction. To investigate the catalytic steps of splicing, we established an in vitro splicing complementation system. Spliceosomes stalled before step 1 of this process were purified to near-homogeneity from a temperature-sensitive mutant of the RNA helicase Prp2, compositionally defined, and shown to catalyze efficient step 1 when supplemented with recombinant Prp2, Spp2 and Cwc25, thereby demonstrating that Cwc25 has a previously unknown role in promoting step 1. Step 2 catalysis additionally required Prp16, Slu7, Prp18 and Prp22. Our data further suggest that Prp2 facilitates catalytic activation by remodeling the spliceosome, including destabilizing the SF3a and SF3b proteins, likely exposing the branch site before step 1. Remodeling by Prp2 was confirmed by negative stain EM and image processing. This system allows future mechanistic analyses of spliceosome activation and catalysis."],["dc.identifier.doi","10.1038/nsmb.1729"],["dc.identifier.gro","3143021"],["dc.identifier.isi","000272609200010"],["dc.identifier.pmid","19935684"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/489"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1545-9993"],["dc.title","Reconstitution of both steps of Saccharomyces cerevisiae splicing with purified spliceosomal components"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","296"],["dc.bibliographiccitation.issue","7871"],["dc.bibliographiccitation.journal","Nature"],["dc.bibliographiccitation.lastpage","300"],["dc.bibliographiccitation.volume","596"],["dc.contributor.author","Zhang, Zhenwei"],["dc.contributor.author","Rigo, Norbert"],["dc.contributor.author","Dybkov, Olexandr"],["dc.contributor.author","Fourmann, Jean-Baptiste"],["dc.contributor.author","Will, Cindy L."],["dc.contributor.author","Kumar, Vinay"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Stark, Holger"],["dc.contributor.author","Lührmann, Reinhard"],["dc.date.accessioned","2021-09-01T06:42:22Z"],["dc.date.available","2021-09-01T06:42:22Z"],["dc.date.issued","2021"],["dc.description.abstract","Abstract During the splicing of introns from precursor messenger RNAs (pre-mRNAs), the U2 small nuclear ribonucleoprotein (snRNP) must undergo stable integration into the spliceosomal A complex—a poorly understood, multistep process that is facilitated by the DEAD-box helicase Prp5 (refs. 1–4 ). During this process, the U2 small nuclear RNA (snRNA) forms an RNA duplex with the pre-mRNA branch site (the U2–BS helix), which is proofread by Prp5 at this stage through an unclear mechanism 5 . Here, by deleting the branch-site adenosine (BS-A) or mutating the branch-site sequence of an actin pre-mRNA, we stall the assembly of spliceosomes in extracts from the yeast Saccharomyces cerevisiae directly before the A complex is formed. We then determine the three-dimensional structure of this newly identified assembly intermediate by cryo-electron microscopy. Our structure indicates that the U2–BS helix has formed in this pre-A complex, but is not yet clamped by the HEAT domain of the Hsh155 protein (Hsh155 HEAT ), which exhibits an open conformation. The structure further reveals a large-scale remodelling/repositioning of the U1 and U2 snRNPs during the formation of the A complex that is required to allow subsequent binding of the U4/U6.U5 tri-snRNP, but that this repositioning is blocked in the pre-A complex by the presence of Prp5. Our data suggest that binding of Hsh155 HEAT to the bulged BS-A of the U2–BS helix triggers closure of Hsh155 HEAT , which in turn destabilizes Prp5 binding. Thus, Prp5 proofreads the branch site indirectly, hindering spliceosome assembly if branch-site mutations prevent the remodelling of Hsh155 HEAT . Our data provide structural insights into how a spliceosomal helicase enhances the fidelity of pre-mRNA splicing."],["dc.description.abstract","Abstract During the splicing of introns from precursor messenger RNAs (pre-mRNAs), the U2 small nuclear ribonucleoprotein (snRNP) must undergo stable integration into the spliceosomal A complex—a poorly understood, multistep process that is facilitated by the DEAD-box helicase Prp5 (refs. 1–4 ). During this process, the U2 small nuclear RNA (snRNA) forms an RNA duplex with the pre-mRNA branch site (the U2–BS helix), which is proofread by Prp5 at this stage through an unclear mechanism 5 . Here, by deleting the branch-site adenosine (BS-A) or mutating the branch-site sequence of an actin pre-mRNA, we stall the assembly of spliceosomes in extracts from the yeast Saccharomyces cerevisiae directly before the A complex is formed. We then determine the three-dimensional structure of this newly identified assembly intermediate by cryo-electron microscopy. Our structure indicates that the U2–BS helix has formed in this pre-A complex, but is not yet clamped by the HEAT domain of the Hsh155 protein (Hsh155 HEAT ), which exhibits an open conformation. The structure further reveals a large-scale remodelling/repositioning of the U1 and U2 snRNPs during the formation of the A complex that is required to allow subsequent binding of the U4/U6.U5 tri-snRNP, but that this repositioning is blocked in the pre-A complex by the presence of Prp5. Our data suggest that binding of Hsh155 HEAT to the bulged BS-A of the U2–BS helix triggers closure of Hsh155 HEAT , which in turn destabilizes Prp5 binding. Thus, Prp5 proofreads the branch site indirectly, hindering spliceosome assembly if branch-site mutations prevent the remodelling of Hsh155 HEAT . Our data provide structural insights into how a spliceosomal helicase enhances the fidelity of pre-mRNA splicing."],["dc.identifier.doi","10.1038/s41586-021-03789-5"],["dc.identifier.pii","3789"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/89039"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-455"],["dc.relation.eissn","1476-4687"],["dc.relation.issn","0028-0836"],["dc.title","Structural insights into how Prp5 proofreads the pre-mRNA branch site"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["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.artnumber","M110.005371"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Molecular & Cellular Proteomics"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Nikolov, Miroslav"],["dc.contributor.author","Stuetzer, Alexandra"],["dc.contributor.author","Mosch, Kerstin"],["dc.contributor.author","Krasauskas, Andrius"],["dc.contributor.author","Soeroes, Szabolcs"],["dc.contributor.author","Stark, Holger"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Fischle, Wolfgang"],["dc.date.accessioned","2018-11-07T08:50:32Z"],["dc.date.available","2018-11-07T08:50:32Z"],["dc.date.issued","2011"],["dc.description.abstract","DNA and histone modifications direct the functional state of chromatin and thereby the readout of the genome. Candidate approaches and histone peptide affinity purification experiments have identified several proteins that bind to chromatin marks. However, the complement of factors that is recruited by individual and combinations of DNA and histone modifications has not yet been defined. Here, we present a strategy based on recombinant, uniformly modified chromatin templates used in affinity purification experiments in conjunction with SILAC-based quantitative mass spectrometry for this purpose. On the prototypic H3K4me3 and H3K9me3 histone modification marks we compare our method with a histone N-terminal peptide affinity purification approach. Our analysis shows that only some factors associate with both, chromatin and peptide matrices but that a surprisingly large number of proteins differ in their association with these templates. Global analysis of the proteins identified implies specific domains mediating recruitment to the chromatin marks. Our proof-of-principle studies show that chromatin templates with defined modification patterns can be used to decipher how the histone code is read and translated. Molecular & Cellular Proteomics 10: 10.1074/mcp.M110.005371, 1-16, 2011."],["dc.identifier.doi","10.1074/mcp.M110.005371"],["dc.identifier.isi","000296759400009"],["dc.identifier.pmid","21836164"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/21717"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Biochemistry Molecular Biology Inc"],["dc.relation.issn","1535-9484"],["dc.relation.issn","1535-9476"],["dc.title","Chromatin Affinity Purification and Quantitative Mass Spectrometry Defining the Interactome of Histone Modification Patterns"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e11349"],["dc.bibliographiccitation.journal","eLife"],["dc.bibliographiccitation.volume","4"],["dc.contributor.author","Pleiner, Tino"],["dc.contributor.author","Bates, Mark"],["dc.contributor.author","Trakhanov, Sergei"],["dc.contributor.author","Lee, Chung-Tien"],["dc.contributor.author","Schliep, Jan Erik"],["dc.contributor.author","Chug, Hema"],["dc.contributor.author","Boehning, Marc"],["dc.contributor.author","Stark, Holger"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Goerlich, Dirk"],["dc.date.accessioned","2018-11-07T09:47:38Z"],["dc.date.available","2018-11-07T09:47:38Z"],["dc.date.issued","2015"],["dc.description.abstract","Nanobodies are single-domain antibodies of camelid origin. We generated nanobodies against the vertebrate nuclear pore complex (NPC) and used them in STORM imaging to locate individual NPC proteins with <2 nm epitope-label displacement. For this, we introduced cysteines at specific positions in the nanobody sequence and labeled the resulting proteins with fluorophore-maleimides. As nanobodies are normally stabilized by disulfide-bonded cysteines, this appears counterintuitive. Yet, our analysis showed that this caused no folding problems. Compared to traditional NHS ester-labeling of lysines, the cysteine-maleimide strategy resulted in far less background in fluorescence imaging, it better preserved epitope recognition and it is site-specific. We also devised a rapid epitope-mapping strategy, which relies on crosslinking mass spectrometry and the introduced ectopic cysteines. Finally, we used different anti-nucleoporin nanobodies to purify the major NPC building blocks - each in a single step, with native elution and, as demonstrated, in excellent quality for structural analysis by electron microscopy. The presented strategies are applicable to any nanobody and nanobody-target."],["dc.description.sponsorship","Dutsche Forschungsgemeinschaft"],["dc.identifier.doi","10.7554/eLife.11349"],["dc.identifier.isi","000373951200001"],["dc.identifier.pmid","26633879"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13260"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/35156"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["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","Nanobodies: site-specific labeling for super-resolution imaging, rapid epitope-mapping and native protein complex isolation"],["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","454"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Cell"],["dc.bibliographiccitation.lastpage","464.e11"],["dc.bibliographiccitation.volume","172"],["dc.contributor.author","Haselbach, David"],["dc.contributor.author","Komarov, Ilya"],["dc.contributor.author","Agafonov, Dmitry E."],["dc.contributor.author","Hartmuth, Klaus"],["dc.contributor.author","Graf, Benjamin"],["dc.contributor.author","Dybkov, Olexandr"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Kastner, Berthold"],["dc.contributor.author","Lührmann, Reinhard"],["dc.contributor.author","Stark, Holger"],["dc.date.accessioned","2020-12-10T14:22:58Z"],["dc.date.available","2020-12-10T14:22:58Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1016/j.cell.2018.01.010"],["dc.identifier.issn","0092-8674"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/71792"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Structure and Conformational Dynamics of the Human Spliceosomal Bact Complex"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]