Fernández Busnadiego, Rubén

[["dc.bibliographiccitation.firstpage","296"],["dc.bibliographiccitation.issue","7794"],["dc.bibliographiccitation.journal","Nature"],["dc.bibliographiccitation.lastpage","300"],["dc.bibliographiccitation.volume","578"],["dc.contributor.author","Yasuda, Sayaka"],["dc.contributor.author","Tsuchiya, Hikaru"],["dc.contributor.author","Kaiho, Ai"],["dc.contributor.author","Guo, Qiang"],["dc.contributor.author","Ikeuchi, Ken"],["dc.contributor.author","Endo, Akinori"],["dc.contributor.author","Arai, Naoko"],["dc.contributor.author","Ohtake, Fumiaki"],["dc.contributor.author","Murata, Shigeo"],["dc.contributor.author","Inada, Toshifumi"],["dc.contributor.author","Baumeister, Wolfgang"],["dc.contributor.author","Fernández Busnadiego, Rubén"],["dc.contributor.author","Tanaka, Keiji"],["dc.contributor.author","Saeki, Yasushi"],["dc.date.accessioned","2020-12-10T18:10:02Z"],["dc.date.available","2020-12-10T18:10:02Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1038/s41586-020-1982-9"],["dc.identifier.pmid","32025036"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/73832"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/30"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.workinggroup","RG Fernández-Busnadiego (Structural Cell Biology)"],["dc.title","Stress- and ubiquitylation-dependent phase separation of the proteasome"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","e1007962"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","PLoS Computational Biology"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Salfer, Maria"],["dc.contributor.author","Collado, Javier F."],["dc.contributor.author","Baumeister, Wolfgang"],["dc.contributor.author","Fernández Busnadiego, Rubén"],["dc.contributor.author","Martínez-Sánchez, Antonio"],["dc.date.accessioned","2021-04-14T08:23:54Z"],["dc.date.available","2021-04-14T08:23:54Z"],["dc.date.issued","2020"],["dc.description.abstract","Curvature is a fundamental morphological descriptor of cellular membranes. Cryo-electron tomography (cryo-ET) is particularly well-suited to visualize and analyze membrane morphology in a close-to-native state and molecular resolution. However, current curvature estimation methods cannot be applied directly to membrane segmentations in cryo-ET, as these methods cannot cope with some of the artifacts introduced during image acquisition and membrane segmentation, such as quantization noise and open borders. Here, we developed and implemented a Python package for membrane curvature estimation from tomogram segmentations, which we named PyCurv. From a membrane segmentation, a signed surface (triangle mesh) is first extracted. The triangle mesh is then represented by a graph, which facilitates finding neighboring triangles and the calculation of geodesic distances necessary for local curvature estimation. PyCurv estimates curvature based on tensor voting. Beside curvatures, this algorithm also provides robust estimations of surface normals and principal directions. We tested PyCurv and three well-established methods on benchmark surfaces and biological data. This revealed the superior performance of PyCurv not only for cryo-ET, but also for data generated by other techniques such as light microscopy and magnetic resonance imaging. Altogether, PyCurv is a versatile open-source software to reliably estimate curvature of membranes and other surfaces in a wide variety of applications."],["dc.identifier.doi","10.1371/journal.pcbi.1007962"],["dc.identifier.pmid","32776920"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/81095"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/59"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.eissn","1553-7358"],["dc.relation.workinggroup","RG Fernández-Busnadiego (Structural Cell Biology)"],["dc.rights","CC BY 4.0"],["dc.title","Reliable estimation of membrane curvature for cryo-electron tomography"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.contributor.author","Saha, Itika"],["dc.contributor.author","Yuste-Checa, Patricia"],["dc.contributor.author","Silva Padilha, Miguel Da"],["dc.contributor.author","Guo, Qiang"],["dc.contributor.author","Körner, Roman"],["dc.contributor.author","Holthusen, Hauke"],["dc.contributor.author","Trinkaus, Victoria A."],["dc.contributor.author","Dudanova, Irina"],["dc.contributor.author","Fernández Busnadiego, Rubén"],["dc.contributor.author","Baumeister, Wolfgang"],["dc.contributor.author","Sanders, David W."],["dc.contributor.author","Gautam, Saurabh"],["dc.contributor.author","Diamond, Marc I."],["dc.contributor.author","Ulrich Hartl, F."],["dc.contributor.author","Hipp, Mark S."],["dc.date.accessioned","2022-04-06T12:10:37Z"],["dc.date.available","2022-04-06T12:10:37Z"],["dc.date.issued","2022"],["dc.identifier.doi","10.1101/2022.02.18.481043"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/106453"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/449"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.workinggroup","RG Fernández-Busnadiego (Structural Cell Biology)"],["dc.title","The AAA+ chaperone VCP disaggregates Tau fibrils and generates aggregate seeds"],["dc.type","preprint"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.contributor.author","Huang, Bin"],["dc.contributor.author","Guo, Qiang"],["dc.contributor.author","Niedermeier, Marie L."],["dc.contributor.author","Cheng, Jingdong"],["dc.contributor.author","Engler, Tatjana"],["dc.contributor.author","Maurer, Melanie"],["dc.contributor.author","Pautsch, Alexander"],["dc.contributor.author","Baumeister, Wolfgang"],["dc.contributor.author","Stengel, Florian"],["dc.contributor.author","Kochanek, Stefan"],["dc.contributor.author","Fernández Busnadiego, Rubén"],["dc.date.accessioned","2022-02-23T16:35:26Z"],["dc.date.available","2022-02-23T16:35:26Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1101/2021.02.02.429316"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/100375"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/231"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.workinggroup","RG Fernández-Busnadiego (Structural Cell Biology)"],["dc.title","PolyQ expansion does not alter the Huntingtin-HAP40 complex"],["dc.type","preprint"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.contributor.author","Riemenschneider, Henrick"],["dc.contributor.author","Guo, Qiang"],["dc.contributor.author","Bader, Jakob"],["dc.contributor.author","Frottin, Frédéric"],["dc.contributor.author","Farny, Daniel"],["dc.contributor.author","Kleinberger, Gernot"],["dc.contributor.author","Haass, Christian"],["dc.contributor.author","Mann, Matthias"],["dc.contributor.author","Hartl, F. Ulrich"],["dc.contributor.author","Baumeister, Wolfgang"],["dc.contributor.author","Hipp, Mark S."],["dc.contributor.author","Meissner, Felix"],["dc.contributor.author","Fernández Busnadiego, Rubén"],["dc.contributor.author","Edbauer, Dieter"],["dc.date.accessioned","2022-02-23T16:35:41Z"],["dc.date.available","2022-02-23T16:35:41Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1101/2021.03.15.435268"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/100379"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/288"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.workinggroup","RG Fernández-Busnadiego (Structural Cell Biology)"],["dc.title","Gel-like inclusions of C-terminal fragments of TDP-43 sequester and inhibit proteasomes in neurons"],["dc.type","preprint"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","951"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Trends in Cell Biology"],["dc.bibliographiccitation.lastpage","966"],["dc.bibliographiccitation.volume","30"],["dc.contributor.author","Bäuerlein, Felix J. B."],["dc.contributor.author","Fernández Busnadiego, Rubén"],["dc.contributor.author","Baumeister, Wolfgang"],["dc.date.accessioned","2021-04-14T08:28:14Z"],["dc.date.available","2021-04-14T08:28:14Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1016/j.tcb.2020.08.007"],["dc.identifier.pmid","32981805"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/82547"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/71"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.issn","0962-8924"],["dc.relation.workinggroup","RG Fernández-Busnadiego (Structural Cell Biology)"],["dc.rights","CC BY 4.0"],["dc.title","Investigating the Structure of Neurotoxic Protein Aggregates Inside Cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","overview_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","725"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","740"],["dc.bibliographiccitation.volume","201"],["dc.contributor.author","Fernández Busnadiego, Rubén"],["dc.contributor.author","Asano, Shoh"],["dc.contributor.author","Oprisoreanu, Ana-Maria"],["dc.contributor.author","Sakata, Eri"],["dc.contributor.author","Doengi, Michael"],["dc.contributor.author","Kochovski, Zdravko"],["dc.contributor.author","Zürner, Magdalena"],["dc.contributor.author","Stein, Valentin"],["dc.contributor.author","Schoch, Susanne"],["dc.contributor.author","Baumeister, Wolfgang"],["dc.contributor.author","Lučić, Vladan"],["dc.date.accessioned","2022-03-01T11:46:33Z"],["dc.date.available","2022-03-01T11:46:33Z"],["dc.date.issued","2013"],["dc.description.abstract","Synaptic vesicles are embedded in a complex filamentous network at the presynaptic terminal. Before fusion, vesicles are linked to the active zone (AZ) by short filaments (tethers). The identity of the molecules that form and regulate tethers remains unknown, but Rab3-interacting molecule (RIM) is a prominent candidate, given its central role in AZ organization. In this paper, we analyzed presynaptic architecture of RIM1α knockout (KO) mice by cryo–electron tomography. In stark contrast to previous work on dehydrated, chemically fixed samples, our data show significant alterations in vesicle distribution and AZ tethering that could provide a structural basis for the functional deficits of RIM1α KO synapses. Proteasome inhibition reversed these structural defects, suggesting a functional recovery confirmed by electrophysiological recordings. Altogether, our results not only point to the ubiquitin–proteasome system as an important regulator of presynaptic architecture and function but also show that the tethering machinery plays a critical role in exocytosis, converging into a structural model of synaptic vesicle priming by RIM1α."],["dc.description.abstract","Synaptic vesicles are embedded in a complex filamentous network at the presynaptic terminal. Before fusion, vesicles are linked to the active zone (AZ) by short filaments (tethers). The identity of the molecules that form and regulate tethers remains unknown, but Rab3-interacting molecule (RIM) is a prominent candidate, given its central role in AZ organization. In this paper, we analyzed presynaptic architecture of RIM1α knockout (KO) mice by cryo–electron tomography. In stark contrast to previous work on dehydrated, chemically fixed samples, our data show significant alterations in vesicle distribution and AZ tethering that could provide a structural basis for the functional deficits of RIM1α KO synapses. Proteasome inhibition reversed these structural defects, suggesting a functional recovery confirmed by electrophysiological recordings. Altogether, our results not only point to the ubiquitin–proteasome system as an important regulator of presynaptic architecture and function but also show that the tethering machinery plays a critical role in exocytosis, converging into a structural model of synaptic vesicle priming by RIM1α."],["dc.identifier.doi","10.1083/jcb.201206063"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103710"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1540-8140"],["dc.relation.issn","0021-9525"],["dc.title","Cryo–electron tomography reveals a critical role of RIM1α in synaptic vesicle tethering"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","179"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Cell"],["dc.bibliographiccitation.lastpage","187.e10"],["dc.bibliographiccitation.volume","171"],["dc.contributor.author","Bäuerlein, Felix J.B."],["dc.contributor.author","Saha, Itika"],["dc.contributor.author","Mishra, Archana"],["dc.contributor.author","Kalemanov, Maria"],["dc.contributor.author","Martínez-Sánchez, Antonio"],["dc.contributor.author","Klein, Rüdiger"],["dc.contributor.author","Dudanova, Irina"],["dc.contributor.author","Hipp, Mark S."],["dc.contributor.author","Hartl, F. Ulrich"],["dc.contributor.author","Baumeister, Wolfgang"],["dc.contributor.author","Fernández Busnadiego, Rubén"],["dc.date.accessioned","2022-03-01T11:45:03Z"],["dc.date.available","2022-03-01T11:45:03Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.1016/j.cell.2017.08.009"],["dc.identifier.pii","S0092867417309340"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103197"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0092-8674"],["dc.rights.uri","https://www.elsevier.com/tdm/userlicense/1.0/"],["dc.title","In Situ Architecture and Cellular Interactions of PolyQ Inclusions"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","145"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","156"],["dc.bibliographiccitation.volume","188"],["dc.contributor.author","Fernández Busnadiego, Rubén"],["dc.contributor.author","Zuber, Benoît"],["dc.contributor.author","Maurer, Ulrike Elisabeth"],["dc.contributor.author","Cyrklaff, Marek"],["dc.contributor.author","Baumeister, Wolfgang"],["dc.contributor.author","Lučić, Vladan"],["dc.date.accessioned","2022-03-01T11:46:33Z"],["dc.date.available","2022-03-01T11:46:33Z"],["dc.date.issued","2010"],["dc.description.abstract","The presynaptic terminal contains a complex network of filaments whose precise organization and functions are not yet understood. The cryoelectron tomography experiments reported in this study indicate that these structures play a prominent role in synaptic vesicle release. Docked synaptic vesicles did not make membrane to membrane contact with the active zone but were instead linked to it by tethers of different length. Our observations are consistent with an exocytosis model in which vesicles are first anchored by long (>5 nm) tethers that give way to multiple short tethers once vesicles enter the readily releasable pool. The formation of short tethers was inhibited by tetanus toxin, indicating that it depends on soluble N-ethyl-maleimide sensitive fusion protein attachment protein receptor complex assembly. Vesicles were extensively interlinked via a set of connectors that underwent profound rearrangements upon synaptic stimulation and okadaic acid treatment, suggesting a role of these connectors in synaptic vesicle mobilization and neurotransmitter release."],["dc.description.abstract","The presynaptic terminal contains a complex network of filaments whose precise organization and functions are not yet understood. The cryoelectron tomography experiments reported in this study indicate that these structures play a prominent role in synaptic vesicle release. Docked synaptic vesicles did not make membrane to membrane contact with the active zone but were instead linked to it by tethers of different length. Our observations are consistent with an exocytosis model in which vesicles are first anchored by long (>5 nm) tethers that give way to multiple short tethers once vesicles enter the readily releasable pool. The formation of short tethers was inhibited by tetanus toxin, indicating that it depends on soluble N-ethyl-maleimide sensitive fusion protein attachment protein receptor complex assembly. Vesicles were extensively interlinked via a set of connectors that underwent profound rearrangements upon synaptic stimulation and okadaic acid treatment, suggesting a role of these connectors in synaptic vesicle mobilization and neurotransmitter release."],["dc.identifier.doi","10.1083/jcb.200908082"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103709"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1540-8140"],["dc.relation.issn","0021-9525"],["dc.title","Quantitative analysis of the native presynaptic cytomatrix by cryoelectron tomography"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","503"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Structural Biology"],["dc.bibliographiccitation.lastpage","514"],["dc.bibliographiccitation.volume","196"],["dc.contributor.author","Lučić, Vladan"],["dc.contributor.author","Fernández Busnadiego, Rubén"],["dc.contributor.author","Laugks, Ulrike"],["dc.contributor.author","Baumeister, Wolfgang"],["dc.date.accessioned","2022-03-01T11:45:15Z"],["dc.date.available","2022-03-01T11:45:15Z"],["dc.date.issued","2016"],["dc.identifier.doi","10.1016/j.jsb.2016.10.004"],["dc.identifier.pii","S104784771630209X"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103267"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","1047-8477"],["dc.rights.uri","https://www.elsevier.com/tdm/userlicense/1.0/"],["dc.title","Hierarchical detection and analysis of macromolecular complexes in cryo-electron tomograms using Pyto software"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]