Dannenberg, Julia

[["dc.bibliographiccitation.artnumber","385"],["dc.bibliographiccitation.journal","Frontiers in Physiology"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Huelsmann, Swen"],["dc.contributor.author","Mesuret, Guillaume"],["dc.contributor.author","Dannenberg, Julia"],["dc.contributor.author","Arnoldt, Mauricio"],["dc.contributor.author","Niebert, Marcus"],["dc.date.accessioned","2018-11-07T10:08:36Z"],["dc.date.available","2018-11-07T10:08:36Z"],["dc.date.issued","2016"],["dc.description.abstract","Mutations in methyl-CpG-binding protein 2 (MECP2) gene have been shown to manifest in a neurodevelopmental disorder that is called Rett syndrome. A typical problem that occurs during development is a disturbance of breathing. To address the role of inhibitory neurons, we generated a mouse line that restores MECP2 in inhibitory neurons in the brainstem by crossbreeding a mouse line that expresses the Cre-recombinase (Cre) in inhibitory neurons under the control of the glycine transporter 2 (GIyT2, slc6a5) promotor(GlyT2-Cre) with a mouse line that has a floxed-stop mutation of the Mecp2 gene (Mecp2(stop/y)). Unrestrained whole-body-plethysmography at postnatal day P60 revealed a low respiratory rate and prolonged respiratory pauses in Mecp2(stop/y) mice. In contrast, G/yT2-Cre positive Mecp2(stop/y) mice (Cre; Mecp2(stop/y)) showed greatly improved respiration and were indistinguishable from wild type littermates. These data support the concept that alterations in inhibitory neurons are important for the development of the respiratory phenotype in Rett syndrome."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2016"],["dc.identifier.doi","10.3389/fphys.2016.00385"],["dc.identifier.isi","000382923200001"],["dc.identifier.pmid","27672368"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13673"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39494"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.eissn","1664-042X"],["dc.relation.issn","1664-042X"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","GlyT2-Dependent Preservation of MECP2-Expression in Inhibitory Neurons Improves Early Respiratory Symptoms but Does Not Rescue Survival in a Mouse Model of Rett Syndrome"],["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","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","902"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","RNA"],["dc.bibliographiccitation.lastpage","915"],["dc.bibliographiccitation.volume","19"],["dc.contributor.author","Ohrt, Thomas"],["dc.contributor.author","Odenwälder, Peter"],["dc.contributor.author","Dannenberg, Julia"],["dc.contributor.author","Prior, Mira"],["dc.contributor.author","Warkocki, Zbigniew"],["dc.contributor.author","Schmitzová, Jana"],["dc.contributor.author","Karaduman, Ramazan"],["dc.contributor.author","Gregor, Ingo"],["dc.contributor.author","Enderlein, Jörg"],["dc.contributor.author","Fabrizio, Patrizia"],["dc.contributor.author","Lührmann, Reinhard"],["dc.date.accessioned","2018-04-23T11:49:29Z"],["dc.date.available","2018-04-23T11:49:29Z"],["dc.date.issued","2013"],["dc.description.abstract","Step 2 catalysis of pre-mRNA splicing entails the excision of the intron and ligation of the 5′ and 3′ exons. The tasks of the splicing factors Prp16, Slu7, Prp18, and Prp22 in the formation of the step 2 active site of the spliceosome and in exon ligation, and the timing of their recruitment, remain poorly understood. Using a purified yeast in vitro splicing system, we show that only the DEAH-box ATPase Prp16 is required for formation of a functional step 2 active site and for exon ligation. Efficient docking of the 3′ splice site (3′SS) to the active site requires only Slu7/Prp18 but not Prp22. Spliceosome remodeling by Prp16 appears to be subtle as only the step 1 factor Cwc25 is dissociated prior to step 2 catalysis, with its release dependent on docking of the 3′SS to the active site and Prp16 action. We show by fluorescence cross-correlation spectroscopy that Slu7/Prp18 and Prp16 bind early to distinct, low-affinity binding sites on the step-1-activated B spliceosome, which are subsequently converted into high-affinity sites. Our results shed new light on the factor requirements for step 2 catalysis and the dynamics of step 1 and 2 factors during the catalytic steps of splicing."],["dc.identifier.doi","10.1261/rna.039024.113"],["dc.identifier.gro","3142126"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13707"],["dc.language.iso","en"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.status","final"],["dc.relation.doi","10.1261/rna.039024.113"],["dc.relation.issn","1355-8382"],["dc.title","Molecular dissection of step 2 catalysis of yeast pre-mRNA splicing investigated in a purified system"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1244"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","RNA"],["dc.bibliographiccitation.lastpage","1256"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","Ohrt, Thomas"],["dc.contributor.author","Prior, Mira"],["dc.contributor.author","Dannenberg, Julia"],["dc.contributor.author","Odenwälder, Peter"],["dc.contributor.author","Dybkov, Olexandr"],["dc.contributor.author","Rasche, Nicolas"],["dc.contributor.author","Schmitzová, Jana"],["dc.contributor.author","Gregor, Ingo"],["dc.contributor.author","Fabrizio, Patrizia"],["dc.contributor.author","Enderlein, Jörg"],["dc.contributor.author","Lührmann, Reinhard"],["dc.date.accessioned","2018-04-23T11:49:30Z"],["dc.date.available","2018-04-23T11:49:30Z"],["dc.date.issued","2012"],["dc.description.abstract","The compositional and conformational changes during catalytic activation of the spliceosome promoted by the DEAH box ATPase Prp2 are only poorly understood. Here, we show by dual-color fluorescence cross-correlation spectroscopy (dcFCCS) that the binding affinity of several proteins is significantly changed during the Prp2-mediated transition of precatalytic Bact spliceosomes to catalytically activated B spliceosomes from Saccharomyces cerevisiae. During this step, several proteins, including the zinc-finger protein Cwc24, are quantitatively displaced from the B complex. Consistent with this, we show that Cwc24 is required for step 1 but not for catalysis per se. The U2-associated SF3a and SF3b proteins Prp11 and Cus1 remain bound to the B spliceosome under near-physiological conditions, but their binding is reduced at high salt. Conversely, high-affinity binding sites are created for Yju2 and Cwc25 during catalytic activation, consistent with their requirement for step 1 catalysis. Our results suggest high cooperativity of multiple Prp2-mediated structural rearrangements at the spliceosome's catalytic core. Moreover, dcFCCS represents a powerful tool ideally suited to study quantitatively spliceosomal protein dynamics in equilibrium."],["dc.identifier.doi","10.1261/rna.033316.112"],["dc.identifier.gro","3142132"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13714"],["dc.language.iso","en"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.status","final"],["dc.relation.doi","10.1261/rna.033316.112"],["dc.relation.issn","1355-8382"],["dc.relation.issn","1355-8382"],["dc.title","Prp2-mediated protein rearrangements at the catalytic core of the spliceosome as revealed by dcFCCS"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","43"],["dc.bibliographiccitation.journal","Respiratory Physiology & Neurobiology"],["dc.bibliographiccitation.lastpage","47"],["dc.bibliographiccitation.volume","248"],["dc.contributor.author","Mesuret, Guillaume"],["dc.contributor.author","Dannenberg, Julia"],["dc.contributor.author","Arnoldt, Mauricio"],["dc.contributor.author","Grützner, Anja-Annett"],["dc.contributor.author","Niebert, Marcus"],["dc.contributor.author","Hülsmann, Swen"],["dc.date.accessioned","2020-12-10T15:21:04Z"],["dc.date.available","2020-12-10T15:21:04Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1016/j.resp.2017.11.011"],["dc.identifier.issn","1569-9048"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/72907"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Breathing disturbances in a model of Rett syndrome: A potential involvement of the glycine receptor α3 subunit?"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]