Options
Fischer, Niels
Loading...
Preferred name
Fischer, Niels
Official Name
Fischer, Niels
Alternative Name
Fischer, N.
Now showing 1 - 10 of 23
2013Journal Article [["dc.bibliographiccitation.firstpage","258a"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","104"],["dc.contributor.author","Vaiana, Andrea C."],["dc.contributor.author","Bock, Lars V."],["dc.contributor.author","Blau, Christian"],["dc.contributor.author","Schroeder, Gunnar F."],["dc.contributor.author","Fischer, Niels"],["dc.contributor.author","Stark, Holger"],["dc.contributor.author","Rodnina, Marina"],["dc.contributor.author","Grubmüller, Helmut"],["dc.date.accessioned","2022-03-01T11:44:56Z"],["dc.date.available","2022-03-01T11:44:56Z"],["dc.date.issued","2013"],["dc.identifier.doi","10.1016/j.bpj.2012.11.1447"],["dc.identifier.pii","S0006349512026938"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103165"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0006-3495"],["dc.title","Modulation of Intersubunit Interactions during tRNA Translocation through the Ribosome"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]Details DOI2016Conference Abstract [["dc.bibliographiccitation.firstpage","s45"],["dc.bibliographiccitation.issue","a1"],["dc.bibliographiccitation.journal","Acta Crystallographica Section A Foundations and Advances"],["dc.bibliographiccitation.lastpage","s45"],["dc.bibliographiccitation.volume","72"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Fischer, Niels"],["dc.contributor.author","Stark, Holger"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2018-05-30T11:09:47Z"],["dc.date.available","2018-05-30T11:09:47Z"],["dc.date.issued","2016"],["dc.identifier.doi","10.1107/S2053273316099307"],["dc.identifier.issn","2053-2733"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/14805"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.status","fcwi"],["dc.relation.eventend","2016-09-01"],["dc.relation.eventlocation","Basel, Switzerland"],["dc.relation.eventstart","2016-08-28"],["dc.relation.ispartof","Acta Crystallographica Section A, 72(Part a1)"],["dc.title","How reliable are atomic models based on cryo-EM reconstructions? Improvements in model fitting and validation"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]Details DOI2015Conference Abstract [["dc.bibliographiccitation.journal","European Biophysics Journal"],["dc.bibliographiccitation.volume","44"],["dc.contributor.author","Fischer, N."],["dc.contributor.author","Neumann, P."],["dc.contributor.author","Bock, L."],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Rodnina, Marina"],["dc.contributor.author","Stark, Holger"],["dc.date.accessioned","2018-11-07T09:55:31Z"],["dc.date.available","2018-11-07T09:55:31Z"],["dc.date.issued","2015"],["dc.format.extent","S46"],["dc.identifier.isi","000380001400013"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/36763"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","New york"],["dc.relation.eventlocation","Dresden, GERMANY"],["dc.relation.issn","1432-1017"],["dc.relation.issn","0175-7571"],["dc.title","Breaking the 3 angstrom resolution barrier in single particle cryo-EM"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details WOS2013Journal Article [["dc.bibliographiccitation.firstpage","663a"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","104"],["dc.contributor.author","Blau, Christian"],["dc.contributor.author","Bock, Lars V."],["dc.contributor.author","Schröder, Gunnar F."],["dc.contributor.author","Fischer, Niels"],["dc.contributor.author","Stark, Holger"],["dc.contributor.author","Rodnina, Marina V."],["dc.contributor.author","Vaiana, Andrea C."],["dc.contributor.author","Grubmüller, Helmut"],["dc.date.accessioned","2021-03-05T08:57:55Z"],["dc.date.available","2021-03-05T08:57:55Z"],["dc.date.issued","2013"],["dc.identifier.doi","10.1016/j.bpj.2012.11.3662"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/79932"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-393"],["dc.relation.issn","0006-3495"],["dc.title","Rate Estimates from Sampling Sparse Transitions: TRNA Motion Limits Transitions between Ribosomal Translocation Intermediates"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]Details DOI2007Journal Article [["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"]]Details DOI2020Journal Article [["dc.bibliographiccitation.firstpage","157"],["dc.bibliographiccitation.issue","7832"],["dc.bibliographiccitation.journal","Nature"],["dc.bibliographiccitation.lastpage","161"],["dc.bibliographiccitation.volume","587"],["dc.contributor.author","Yip, Ka Man"],["dc.contributor.author","Fischer, Niels"],["dc.contributor.author","Paknia, Elham"],["dc.contributor.author","Chari, Ashwin"],["dc.contributor.author","Stark, Holger"],["dc.date.accessioned","2022-03-01T11:46:00Z"],["dc.date.available","2022-03-01T11:46:00Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1038/s41586-020-2833-4"],["dc.identifier.pii","2833"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103527"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1476-4687"],["dc.relation.issn","0028-0836"],["dc.rights.uri","https://www.springer.com/tdm"],["dc.title","Atomic-resolution protein structure determination by cryo-EM"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]Details DOI2016Journal Article Research Paper [["dc.bibliographiccitation.firstpage","80"],["dc.bibliographiccitation.issue","7631"],["dc.bibliographiccitation.journal","Nature"],["dc.bibliographiccitation.lastpage","85"],["dc.bibliographiccitation.volume","540"],["dc.contributor.author","Fischer, Niels"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Bock, Lars V."],["dc.contributor.author","Maracci, Cristina"],["dc.contributor.author","Wang, Zhe"],["dc.contributor.author","Paleskava, Alena"],["dc.contributor.author","Konevega, Andrey L."],["dc.contributor.author","Schröder, Gunnar F."],["dc.contributor.author","Grubmüller, Helmut"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Rodnina, Marina V."],["dc.contributor.author","Stark, Holger"],["dc.date.accessioned","2017-09-07T11:44:31Z"],["dc.date.available","2017-09-07T11:44:31Z"],["dc.date.issued","2016"],["dc.description.abstract","In all domains of life, selenocysteine (Sec) is delivered to the ribosome by selenocysteine-specific tRNA (tRNA(Sec)) with the help of a specialized translation factor, SelB in bacteria. Sec-tRNA(Sec) recodes a UGA stop codon next to a downstream mRNA stem-loop. Here we present the structures of six intermediates on the pathway of UGA recoding in Escherichia coli by single-particle cryo-electron microscopy. The structures explain the specificity of Sec-tRNA(Sec) binding by SelB and show large-scale rearrangements of Sec-tRNA(Sec). Upon initial binding of SelB-Sec-tRNA(Sec) to the ribosome and codon reading, the 30S subunit adopts an open conformation with Sec-tRNA(Sec) covering the sarcin-ricin loop (SRL) on the 50S subunit. Subsequent codon recognition results in a local closure of the decoding site, which moves Sec-tRNA(Sec) away from the SRL and triggers a global closure of the 30S subunit shoulder domain. As a consequence, SelB docks on the SRL, activating the GTPase of SelB. These results reveal how codon recognition triggers GTPase activation in translational GTPases."],["dc.identifier.doi","10.1038/nature20560"],["dc.identifier.gro","3141595"],["dc.identifier.isi","000388916600051"],["dc.identifier.pmid","27842381"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1476-4687"],["dc.relation.issn","0028-0836"],["dc.title","The pathway to GTPase activation of elongation factor SelB on the ribosome"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS2005Journal Article [["dc.bibliographiccitation.firstpage","c99"],["dc.bibliographiccitation.issue","a1"],["dc.bibliographiccitation.journal","Acta Crystallographica Section A Foundations of Crystallography"],["dc.bibliographiccitation.lastpage","c99"],["dc.bibliographiccitation.volume","61"],["dc.contributor.author","Wahl, M. C."],["dc.contributor.author","Diaconu, M."],["dc.contributor.author","Kothe, U."],["dc.contributor.author","Schlünzen, F."],["dc.contributor.author","Fischer, N."],["dc.contributor.author","Harms, J."],["dc.contributor.author","Tonevitski, A. G."],["dc.contributor.author","Stark, Holger"],["dc.contributor.author","Rodnina, Marina V."],["dc.date.accessioned","2022-03-01T11:47:02Z"],["dc.date.available","2022-03-01T11:47:02Z"],["dc.date.issued","2005"],["dc.identifier.doi","10.1107/S0108767305095784"],["dc.identifier.pii","S0108767305095784"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103888"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0108-7673"],["dc.title","Structural analysis of the L7/12 ribosomal stalk"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]Details DOI2015Journal Article [["dc.bibliographiccitation.firstpage","1769"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Structure"],["dc.bibliographiccitation.lastpage","1775"],["dc.bibliographiccitation.volume","23"],["dc.contributor.author","Hauer, Florian"],["dc.contributor.author","Gerle, Christoph"],["dc.contributor.author","Fischer, Niels"],["dc.contributor.author","Oshima, Atsunori"],["dc.contributor.author","Shinzawa-Itoh, Kyoko"],["dc.contributor.author","Shimada, Satoru"],["dc.contributor.author","Yokoyama, Ken"],["dc.contributor.author","Fujiyoshi, Yoshinori"],["dc.contributor.author","Stark, Holger"],["dc.date.accessioned","2018-11-07T09:52:34Z"],["dc.date.available","2018-11-07T09:52:34Z"],["dc.date.issued","2015"],["dc.description.abstract","We developed a method, named GraDeR, which substantially improves the preparation of membrane protein complexes for structure determination by single-particle cryo-electron microscopy (cryo-EM). In GraDeR, glycerol gradient centrifugation is used for the mild removal of free detergent monomers and micelles from lauryl maltose-neopentyl glycol detergent stabilized membrane complexes, resulting in mono-disperse and stable complexes to which standard processes for water-soluble complexes can be applied. We demonstrate the applicability of the method on three different membrane complexes, including the mammalian FoF1 ATP synthase. For this highly dynamic and fragile rotary motor, we show that GraDeR allows visualizing the asymmetry of the F-1 domain, which matches the ground state structure of the isolated domain. Therefore, the present cryo-EM structure of FoF1 ATP synthase provides direct structural evidence for Boyer's binding change mechanism in the context of the intact enzyme."],["dc.identifier.doi","10.1016/j.str.2015.06.029"],["dc.identifier.isi","000361113000021"],["dc.identifier.pmid","26278176"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/36154"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.relation.issn","1878-4186"],["dc.relation.issn","0969-2126"],["dc.title","GraDeR: Membrane Protein Complex Preparation for Single-Particle Cryo-EM"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS2015Journal Article Research Paper [["dc.bibliographiccitation.firstpage","567"],["dc.bibliographiccitation.issue","7548"],["dc.bibliographiccitation.journal","Nature"],["dc.bibliographiccitation.lastpage","570"],["dc.bibliographiccitation.volume","520"],["dc.contributor.author","Fischer, Niels"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Konevega, Andrey L."],["dc.contributor.author","Bock, Lars V."],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Rodnina, Marina V."],["dc.contributor.author","Stark, Holger"],["dc.date.accessioned","2017-09-07T11:44:26Z"],["dc.date.available","2017-09-07T11:44:26Z"],["dc.date.issued","2015"],["dc.description.abstract","Single particle electron cryomicroscopy (cryo-EM) has recently made significant progress in high-resolution structure determination of macromolecular complexes due to improvements in electron microscopic instrumentation and computational image analysis. However, cryo-EM structures can be highly non-uniform in local resolution\" and all structures available to date have been limited to resolutions above 3 angstrom(3,4). Here we present the cryo-EM structure of the 70S ribosome from Escherichia coli in complex with elongation factor Tu, aminoacyl-tRNA and the antibiotic kirromycin at 2.65-2.9 angstrom resolution using spherical aberration (c)-corrected cryo-EM. Overall, the cryo-EM reconstruction at 2.9 angstrom resolution is comparable to the best-resolved X-ray structure of the E. coil 70S ribosome(5) (2.8 angstrom), but provides more detailed information (2.65 angstrom) at the functionally important ribosomal core. The cryo-EM map elucidates for the first time the structure of all 35 rRNA modifications in the bacterial ribosome, explaining their roles in fine-tuning ribosome structure and function and modulating the action of antibiotics. We also obtained atomic models for flexible parts of the ribosome such as ribosomal proteins L9 and L31. The refined cryo-EM -based model presents the currently most complete high-resolution structure of the E. coil ribosome, which demonstrates the power of cryo-EM in structure determination of large and dynamic macromolecular complexes."],["dc.identifier.doi","10.1038/nature14275"],["dc.identifier.gro","3141921"],["dc.identifier.isi","000353334500049"],["dc.identifier.pmid","25707802"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2555"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1476-4687"],["dc.relation.issn","0028-0836"],["dc.title","Structure of the E. coli ribosome-EF-Tu complex at <3 Å resolution by Cs-corrected cryo-EM"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS