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.bibliographiccitation.firstpage","2520"],["dc.bibliographiccitation.issue","17"],["dc.bibliographiccitation.journal","FEBS Letters"],["dc.bibliographiccitation.lastpage","2533"],["dc.bibliographiccitation.volume","591"],["dc.contributor.author","Wagner, Jonathan"],["dc.contributor.author","Schaffer, Miroslava"],["dc.contributor.author","Fernández Busnadiego, Rubén"],["dc.date.accessioned","2022-03-01T11:44:38Z"],["dc.date.available","2022-03-01T11:44:38Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.1002/1873-3468.12757"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103073"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0014-5793"],["dc.title","Cryo-electron tomography-the cell biology that came in from the cold"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Journal of Cell Biology"],["dc.bibliographiccitation.volume","220"],["dc.contributor.author","Eisenberg-Bord, Michal"],["dc.contributor.author","Zung, Naama"],["dc.contributor.author","Collado, Javier"],["dc.contributor.author","Drwesh, Layla"],["dc.contributor.author","Fenech, Emma J."],["dc.contributor.author","Fadel, Amir"],["dc.contributor.author","Dezorella, Nili"],["dc.contributor.author","Bykov, Yury S."],["dc.contributor.author","Rapaport, Doron"],["dc.contributor.author","Fernández Busnadiego, Rubén"],["dc.contributor.author","Schuldiner, Maya"],["dc.date.accessioned","2021-12-01T09:21:03Z"],["dc.date.available","2021-12-01T09:21:03Z"],["dc.date.issued","2021"],["dc.description.abstract","Mitochondrial functions are tightly regulated by nuclear activity, requiring extensive communication between these organelles. One way by which organelles can communicate is through contact sites, areas of close apposition held together by tethering molecules. While many contacts have been characterized in yeast, the contact between the nucleus and mitochondria was not previously identified. Using fluorescence and electron microscopy in S. cerevisiae, we demonstrate specific areas of contact between the two organelles. Using a high-throughput screen, we uncover a role for the uncharacterized protein Ybr063c, which we have named Cnm1 (contact nucleus mitochondria 1), as a molecular tether on the nuclear membrane. We show that Cnm1 mediates contact by interacting with Tom70 on mitochondria. Moreover, Cnm1 abundance is regulated by phosphatidylcholine, enabling the coupling of phospholipid homeostasis with contact extent. The discovery of a molecular mechanism that allows mitochondrial crosstalk with the nucleus sets the ground for better understanding of mitochondrial functions in health and disease."],["dc.identifier.doi","10.1083/jcb.202104100"],["dc.identifier.pmid","34694322"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/94334"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/365"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/162"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-478"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P11: Zuordnung zellulärer Kontaktstellen und deren Zusammenspiel"],["dc.relation.eissn","1540-8140"],["dc.relation.issn","0021-9525"],["dc.relation.workinggroup","RG Fernández-Busnadiego (Structural Cell Biology)"],["dc.relation.workinggroup","RG Schuldiner (Functional Genomics of Organelles)"],["dc.rights","CC BY 4.0"],["dc.title","Cnm1 mediates nucleus–mitochondria contact site formation in response to phospholipid levels"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","161"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Cell Reports"],["dc.bibliographiccitation.lastpage","173"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","Vargas, Karina J."],["dc.contributor.author","Schrod, Nikolas"],["dc.contributor.author","Davis, Taylor"],["dc.contributor.author","Fernández Busnadiego, Rubén"],["dc.contributor.author","Taguchi, Yumiko V."],["dc.contributor.author","Laugks, Ulrike"],["dc.contributor.author","Lucic, Vladan"],["dc.contributor.author","Chandra, Sreeganga S."],["dc.date.accessioned","2022-03-01T11:45:05Z"],["dc.date.available","2022-03-01T11:45:05Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.1016/j.celrep.2016.12.023"],["dc.identifier.pii","S2211124716317132"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103203"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","2211-1247"],["dc.rights.uri","https://www.elsevier.com/tdm/userlicense/1.0/"],["dc.title","Synucleins Have Multiple Effects on Presynaptic Architecture"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["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.bibliographiccitation.firstpage","227"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Huntington's Disease"],["dc.bibliographiccitation.lastpage","242"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Seefelder, Manuel"],["dc.contributor.author","Klein, Fabrice A.C."],["dc.contributor.author","Landwehrmeyer, Bernhard"],["dc.contributor.author","Fernández-Busnadiego, Rubén"],["dc.contributor.author","Kochanek, Stefan"],["dc.date.accessioned","2022-09-01T09:51:05Z"],["dc.date.available","2022-09-01T09:51:05Z"],["dc.date.issued","2022"],["dc.description.abstract","Since the discovery of the mutation causing Huntington’s disease (HD) in 1993, it has been debated whether an expanded polyglutamine (polyQ) stretch affects the properties of the huntingtin (HTT) protein and thus contributes to the pathological mechanisms responsible for HD. Here we review the current knowledge about the structure of HTT, alone (apo-HTT) or in a complex with Huntingtin-Associated Protein 40 (HAP40), the influence of polyQ-length variation on apo-HTT and the HTT-HAP40 complex, and the biology of HAP40. Phylogenetic analyses suggest that HAP40 performs essential functions. Highlighting the relevance of its interaction with HTT, HAP40 is one of the most abundant partners copurifying with HTT and is rapidly degraded, when HTT levels are reduced. As the levels of both proteins decrease during disease progression, HAP40 could also be a biomarker for HD. Whether declining HAP40 levels contribute to disease etiology is an open question. Structural studies have shown that the conformation of apo-HTT is less constrained but resembles that adopted in the HTT-HAP40 complex, which is exceptionally stable because of extensive interactions between HAP40 and the three domains of HTT. The complex— and to some extent apo-HTT— resists fragmentation after limited proteolysis. Unresolved regions of apo-HTT, constituting about 25% of the protein, are the main sites of post-translational modifications and likely have major regulatory functions. PolyQ elongation does not substantially alter the structure of HTT, alone or when associated with HAP40. Particularly, polyQ above the disease length threshold does not induce drastic conformational changes in full-length HTT. Therefore, models of HD pathogenesis stating that polyQ expansion drastically alters HTT properties should be reconsidered."],["dc.identifier.doi","10.3233/JHD-220543"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/113880"],["dc.notes.intern","DOI-Import GROB-597"],["dc.relation.eissn","1879-6400"],["dc.relation.issn","1879-6397"],["dc.title","Huntingtin and Its Partner Huntingtin-Associated Protein 40: Structural and Functional Considerations in Health and Disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","534"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biochemical Society Transactions"],["dc.bibliographiccitation.lastpage","540"],["dc.bibliographiccitation.volume","44"],["dc.contributor.author","Fernández Busnadiego, Rubén"],["dc.date.accessioned","2022-03-01T11:46:16Z"],["dc.date.available","2022-03-01T11:46:16Z"],["dc.date.issued","2016"],["dc.description.abstract","The endoplasmic reticulum (ER) forms membrane contact sites (MCS) with most other cellular organelles and the plasma membrane (PM). These ER–PM MCS, where the membranes of the ER and PM are closely apposed, were discovered in the early days of electron microscopy (EM), but only recently are we starting to understand their functional and structural diversity. ER–PM MCS are nowadays known to mediate excitation–contraction coupling (ECC) in striated muscle cells and to play crucial roles in Ca2+ and lipid homoeostasis in all metazoan cells. A common feature across ER–PM MCS specialized in different functions is the preponderance of cooperative phenomena that result in the formation of large supramolecular assemblies. Therefore, characterizing the supramolecular architecture of ER–PM MCS is critical to understand their mechanisms of function. Cryo-electron tomography (cryo-ET) is a powerful EM technique uniquely positioned to address this issue, as it allows 3D imaging of fully hydrated, unstained cellular structures at molecular resolution. In this review I summarize our current structural knowledge on the molecular organization of ER–PM MCS and its functional implications, with special emphasis on the emerging contributions of cryo-ET."],["dc.description.abstract","The endoplasmic reticulum (ER) forms membrane contact sites (MCS) with most other cellular organelles and the plasma membrane (PM). These ER–PM MCS, where the membranes of the ER and PM are closely apposed, were discovered in the early days of electron microscopy (EM), but only recently are we starting to understand their functional and structural diversity. ER–PM MCS are nowadays known to mediate excitation–contraction coupling (ECC) in striated muscle cells and to play crucial roles in Ca2+ and lipid homoeostasis in all metazoan cells. A common feature across ER–PM MCS specialized in different functions is the preponderance of cooperative phenomena that result in the formation of large supramolecular assemblies. Therefore, characterizing the supramolecular architecture of ER–PM MCS is critical to understand their mechanisms of function. Cryo-electron tomography (cryo-ET) is a powerful EM technique uniquely positioned to address this issue, as it allows 3D imaging of fully hydrated, unstained cellular structures at molecular resolution. In this review I summarize our current structural knowledge on the molecular organization of ER–PM MCS and its functional implications, with special emphasis on the emerging contributions of cryo-ET."],["dc.identifier.doi","10.1042/BST20150279"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103612"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1470-8752"],["dc.relation.issn","0300-5127"],["dc.title","Supramolecular architecture of endoplasmic reticulum–plasma membrane contact sites"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","fnw169"],["dc.bibliographiccitation.issue","18"],["dc.bibliographiccitation.journal","FEMS Microbiology Letters"],["dc.bibliographiccitation.volume","363"],["dc.contributor.author","Nagy, István"],["dc.contributor.author","Knispel, Roland Wilhelm"],["dc.contributor.author","Kofler, Christine"],["dc.contributor.author","Orsini, Massimiliano"],["dc.contributor.author","Boicu, Marius"],["dc.contributor.author","Varga, Sándor"],["dc.contributor.author","Weyher-Stingl, Elisabeth"],["dc.contributor.author","Sun, Na"],["dc.contributor.author","Fernández Busnadiego, Rubén"],["dc.contributor.author","Kukolya, József"],["dc.contributor.editor","Moracci, Marco"],["dc.date.accessioned","2022-03-01T11:46:44Z"],["dc.date.available","2022-03-01T11:46:44Z"],["dc.date.issued","2016"],["dc.identifier.doi","10.1093/femsle/fnw169"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103783"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1574-6968"],["dc.title","Lipoprotein-like particles in a prokaryote: quinone droplets of Thermoplasma acidophilum"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]