Neumann, Piotr D.

[["dc.bibliographiccitation.firstpage","960"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","965"],["dc.bibliographiccitation.volume","110"],["dc.contributor.author","Monecke, Thomas"],["dc.contributor.author","Haselbach, David"],["dc.contributor.author","Voss, Bela"],["dc.contributor.author","Russek, Andreas"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Thomson, Emma"],["dc.contributor.author","Hurt, Ed"],["dc.contributor.author","Zachariae, Ulrich"],["dc.contributor.author","Stark, Holger"],["dc.contributor.author","Grubmüller, Helmut"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2017-09-07T11:48:18Z"],["dc.date.available","2017-09-07T11:48:18Z"],["dc.date.issued","2013"],["dc.description.abstract","In eukaryotes, the nucleocytoplasmic transport of macromolecules is mainly mediated by soluble nuclear transport receptors of the karyopherin-beta superfamily termed importins and exportins. The highly versatile exportin chromosome region maintenance 1 (CRM1) is essential for nuclear depletion of numerous structurally and functionally unrelated protein and ribonucleoprotein cargoes. CRM1 has been shown to adopt a toroidal structure in several functional transport complexes and was thought to maintain this conformation throughout the entire nucleocytoplasmic transport cycle. We solved crystal structures of free CRM1 from the thermophilic eukaryote Chaetomium thermophilum. Surprisingly, unbound CRM1 exhibits an overall extended and pitched superhelical conformation. The two regulatory regions, namely the acidic loop and the C-terminal a-helix, are dramatically repositioned in free CRM1 in comparison with the ternary CRM1-Ran-Snurportin1 export complex. Single-particle EM analysis demonstrates that, in a noncrystalline environment, free CRM1 exists in equilibrium between extended, superhelical and compact, ring-like conformations. Molecular dynamics simulations show that the C-terminal helix plays an important role in regulating the transition from an extended to a compact conformation and reveal how the binding site for nuclear export signals of cargoes is modulated by different CRM1 conformations. Combining these results, we propose a model for the cooperativity of CRM1 export complex assembly involving the long-range allosteric communication between the distant binding sites of GTP-bound Ran and cargo."],["dc.identifier.doi","10.1073/pnas.1215214110"],["dc.identifier.gro","3142406"],["dc.identifier.isi","000313909100042"],["dc.identifier.pmid","23277578"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7930"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0027-8424"],["dc.title","Structural basis for cooperativity of CRM1 export complex formation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Metje-Sprink, Janina"],["dc.contributor.author","Groffmann, Johannes"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Barg-Kues, Brigitte"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Kühnel, Karin"],["dc.contributor.author","Schalk, Amanda M."],["dc.contributor.author","Binotti, Beyenech"],["dc.date.accessioned","2021-04-14T08:24:26Z"],["dc.date.available","2021-04-14T08:24:26Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1038/s41598-020-69637-0"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/81283"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","2045-2322"],["dc.title","Crystal structure of the Rab33B/Atg16L1 effector complex"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","102144"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.contributor.author","Heidemann, Jana L."],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Krüger, Larissa"],["dc.contributor.author","Wicke, Dennis"],["dc.contributor.author","Vinhoven, Liza"],["dc.contributor.author","Linden, Andreas"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Stülke, Jörg"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2022-07-01T07:35:47Z"],["dc.date.available","2022-07-01T07:35:47Z"],["dc.date.issued","2022"],["dc.identifier.doi","10.1016/j.jbc.2022.102144"],["dc.identifier.pii","S0021925822005865"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/112267"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-581"],["dc.relation.issn","0021-9258"],["dc.title","Structural basis for c-di-AMP-dependent regulation of the bacterial stringent response by receptor protein DarB"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","785"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Structure"],["dc.bibliographiccitation.lastpage","795.e4"],["dc.bibliographiccitation.volume","26"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2020-12-10T15:21:31Z"],["dc.date.available","2020-12-10T15:21:31Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1016/j.str.2018.03.004"],["dc.identifier.issn","0969-2126"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/73053"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Validating Resolution Revolution"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["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"]]

[["dc.bibliographiccitation.firstpage","705"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Acta crystallographica. Section D, Structural biology"],["dc.bibliographiccitation.lastpage","717"],["dc.bibliographiccitation.volume","72"],["dc.contributor.author","Tauchert, Marcel J."],["dc.contributor.author","Hémonnot, Clément"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Köster, Sarah"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Dickmanns, Achim"],["dc.date.accessioned","2020-12-10T18:26:04Z"],["dc.date.available","2020-12-10T18:26:04Z"],["dc.date.issued","2016"],["dc.description.abstract","In eukaryotic cells, the exchange of macromolecules between the nucleus and cytoplasm is highly selective and requires specialized soluble transport factors. Many of them belong to the importin-beta superfamily, the members of which share an overall superhelical structure owing to the tandem arrangement of a specific motif, the HEAT repeat. This structural organization leads to great intrinsic flexibility, which in turn is a prerequisite for the interaction with a variety of proteins and for its transport function. During the passage from the aqueous cytosol into the nucleus, the receptor passes the gated channel of the nuclear pore complex filled with a protein meshwork of unknown organization, which seems to be highly selective owing to the presence of FG-repeats, which are peptides with hydrophobic patches. Here, the structural changes of free importin-beta from a single organism, crystallized in polar (salt) or apolar (PEG) buffer conditions, are reported. This allowed analysis of the structural changes, which are attributable to the surrounding milieu and are not affected by bound interaction partners. The importin-beta structures obtained exhibit significant conformational changes and suggest an influence of the polarity of the environment, resulting in an extended conformation in the PEG condition. The significance of this observation is supported by SAXS experiments and the analysis of other crystal structures of importin-beta deposited in the Protein Data Bank."],["dc.identifier.doi","10.1107/S2059798316004940"],["dc.identifier.fs","622294"],["dc.identifier.gro","3141673"],["dc.identifier.isi","000379911500002"],["dc.identifier.issn","2059-7983"],["dc.identifier.pmid","27303791"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/75940"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","2059-7983"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.subject.gro","x-ray scattering"],["dc.subject.gro","molecular biophysics"],["dc.title","Impact of the crystallization condition on importin-β conformation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["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"]]

[["dc.bibliographiccitation.firstpage","1678"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Structure"],["dc.bibliographiccitation.volume","26"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2022-03-01T11:45:23Z"],["dc.date.available","2022-03-01T11:45:23Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1016/j.str.2018.10.028"],["dc.identifier.pii","S0969212618303897"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103311"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0969-2126"],["dc.rights.uri","https://www.elsevier.com/tdm/userlicense/1.0/"],["dc.title","Validating Resolution Revolution"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","88"],["dc.bibliographiccitation.issue","1-2"],["dc.bibliographiccitation.journal","Journal of Molecular Catalysis B Enzymatic"],["dc.bibliographiccitation.lastpage","92"],["dc.bibliographiccitation.volume","61"],["dc.contributor.author","Weidner, Annett"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Pech, Andreas"],["dc.contributor.author","Stubbs, Milton T."],["dc.contributor.author","Tittmann, Kai"],["dc.date.accessioned","2018-11-07T11:22:52Z"],["dc.date.available","2018-11-07T11:22:52Z"],["dc.date.issued","2009"],["dc.description.abstract","Pyruvate oxidase from Escherichia coli (EcPOX) is a thiamin diphosphate- (ThDP) and FAD-dependent peripheral membrane protein that carries out the irreversible oxidative decarboxylation of pyruvate to acetate and carbon dioxide. Concomitant two-electron reduction of the flavin cofactor was suggested to induce a Structural rearrangement of the C-terminus triggering recruitment of the protein from the cytosol to the cell membrane, where the electrons are eventually transferred to final electron acceptor ubiquinone 8. Binding to the membrane, or alternatively, mild proteolytic digestion leads to a multifold enhancement of both the catalytic activity and substrate affinity. Recent X-ray crystallographic studies on EcPOX in the resting state and on a C-terminal truncation variant mimicking the membrane-bound activated form have fueled our understanding of the membrane-binding mechanism and concomitant catalytic activation. In the resting state, the auto-inhibitory C-terminal membrane anchor adopts a half-barrel/helix fold that occludes the active site. Upon activation, the C-terminus is expelled and becomes structurally flexible thereby freeing the active site. Circular dichroism spectroscopic analysis revealed the isolated C-terminus to be disordered, however, formation of a helical structure was observed in the presence of micelles. Limited proteolysis experiments indicate that activation of EcPOX involves at least two sequential structural transitions: the first occurring after binding of pyruvate to ThDP and the second after two-electron reduction of the flavin. (C) 2009 Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.molcatb.2009.02.020"],["dc.identifier.isi","000271169600015"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/56068"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.publisher.place","Amsterdam"],["dc.relation.conference","International Conference on Mechanisms and Physiology of Thiamine"],["dc.relation.eventlocation","Wittenberg, GERMANY"],["dc.relation.issn","1381-1177"],["dc.title","New insights into the membrane-binding and activation mechanism of pyruvate oxidase from Escherichia coli"],["dc.type","conference_paper"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Critical Care Medicine"],["dc.bibliographiccitation.volume","29"],["dc.contributor.author","Hinz, Jose Maria"],["dc.contributor.author","Neumann, P."],["dc.contributor.author","Hahn, G."],["dc.contributor.author","Dudykevych, T."],["dc.contributor.author","Hellige, Gerhard"],["dc.contributor.author","Burchardi, Hilmar"],["dc.date.accessioned","2018-11-07T11:20:41Z"],["dc.date.available","2018-11-07T11:20:41Z"],["dc.date.issued","2001"],["dc.format.extent","A84"],["dc.identifier.isi","000172920900273"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/55599"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Lippincott Williams & Wilkins"],["dc.publisher.place","Philadelphia"],["dc.relation.issn","0090-3493"],["dc.title","Regional pulmonary pressure volume curves by electrical impedance tomography"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]