Ficner, Ralf

[["dc.bibliographiccitation.firstpage","s30"],["dc.bibliographiccitation.issue","a1"],["dc.bibliographiccitation.journal","Acta Crystallographica Section A Foundations and Advances"],["dc.bibliographiccitation.lastpage","s30"],["dc.bibliographiccitation.volume","72"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Monecke, Thomas"],["dc.contributor.author","Port, Sarah A."],["dc.contributor.author","Weiß, Manfred S."],["dc.contributor.author","Kehlenbach, Ralph H."],["dc.contributor.author","Dickmanns, Achim"],["dc.date.accessioned","2020-12-10T18:26:02Z"],["dc.date.available","2020-12-10T18:26:02Z"],["dc.date.issued","2016"],["dc.identifier.doi","10.1107/S2053273316099526"],["dc.identifier.issn","2053-2733"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/75925"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.status","final"],["dc.title","Crystal structure of the 239 kDa nuclear export complex CRM1 - RanGTP - Snurportin1 - Nup214 - MBP"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["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.firstpage","847"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","ChemMedChem"],["dc.bibliographiccitation.lastpage","854"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Mahal, Katharina"],["dc.contributor.author","Resch, Marcus"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Schobert, Rainer"],["dc.contributor.author","Biersack, Bernhard"],["dc.contributor.author","Mueller, Thomas"],["dc.date.accessioned","2017-09-07T11:46:19Z"],["dc.date.available","2017-09-07T11:46:19Z"],["dc.date.issued","2014"],["dc.description.abstract","Two analogues of the discontinued tumor vascular-disrupting agent verubulin (Azixa (R), MPC-6827, 1) featuring benzo-1,4-dioxan-6-yl (compound 5a) and N-methylindol-5-yl (compound 10) residues instead of the para-anisyl group on the 4-(methylamino)-2-methylquinazoline pharmacophore, were prepared and found to exceed the antitumor efficacy of the lead compound. They were antiproliferative with single-digit nanomolar IC50 values against a panel of nine tumor cell lines, while not affecting nonmalignant fibroblasts. Indole 10 surpassed verubulin in seven tumor cell lines including colon, breast, ovarian, and germ cell cancer cell lines. In line with docking studies indicating that compound 10 may bind the colchicine binding site of tubulin more tightly (E-bind=-9.8kcalmol(-1)) than verubulin (E-bind=-8.3kcalmol(-1)), 10 suppressed the formation of vessel-like tubes in endothelial cells and destroyed the blood vessels in the chorioallantoic membrane of fertilized chicken eggs at nanomolar concentrations. When applied to nude mice bearing a highly vascularized 1411HP germ cell xenograft tumor, compound 10 displayed pronounced vascular-disrupting effects that led to hemorrhages and extensive central necrosis in the tumor."],["dc.identifier.doi","10.1002/cmdc.201300531"],["dc.identifier.gro","3142148"],["dc.identifier.isi","000333749200020"],["dc.identifier.pmid","24678059"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/5066"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Wiley-v C H Verlag Gmbh"],["dc.relation.eissn","1860-7187"],["dc.relation.issn","1860-7179"],["dc.title","Effects of the Tumor-Vasculature-Disrupting Agent Verubulin and Two Heteroaryl Analogues on Cancer Cells, Endothelial Cells, and Blood Vessels"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["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","1"],["dc.bibliographiccitation.journal","RNA Biology"],["dc.bibliographiccitation.lastpage","15"],["dc.contributor.author","Sievers, Katharina"],["dc.contributor.author","Welp, Luisa"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2021-09-01T06:42:13Z"],["dc.date.available","2021-09-01T06:42:13Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1080/15476286.2021.1950980"],["dc.identifier.pmid","34241577"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/89006"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/320"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-455"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.eissn","1555-8584"],["dc.relation.issn","1547-6286"],["dc.relation.workinggroup","RG Ficner (Molecular Structural Biology)"],["dc.title","Structural and functional insights into human tRNA guanine transgylcosylase"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","6823"],["dc.bibliographiccitation.issue","23"],["dc.bibliographiccitation.journal","EMBO Journal"],["dc.bibliographiccitation.lastpage","6831"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","Reuter, K."],["dc.contributor.author","Mofid, M."],["dc.contributor.author","Marahiel, M."],["dc.contributor.author","Ficner, R."],["dc.date.accessioned","2017-09-07T11:47:26Z"],["dc.date.available","2017-09-07T11:47:26Z"],["dc.date.issued","1999"],["dc.description.abstract","The Bacillus subtilis Sfp protein activates the peptidyl carrier protein (PCP) domains of surfactin synthetase by transferring the 4'-phosphopantetheinyl moiety of coenzyme A (CoA) to a serine residue conserved in all PCPs. Its wide PCP substrate spectrum renders Sfp a biotechnologically valuable enzyme for use in combinatorial non-ribosomal peptide synthesis. The structure of the SfpCoA complex determined at 1.8 Angstrom resolution reveals a novel alpha/beta-fold exhibiting an unexpected intramolecular 2-fold pseudosymmetry, This suggests a similar fold and dimerization mode for the homodimeric phosphopantetheinyl transferases such as acyl carrier protein synthase, The active site of Sfp accommodates a magnesium ion, which is complexed by the CoA pyrophosphate, the side chains of three acidic amino acids and one water molecule. CoA is bound in a fashion that differs in many aspects from all known CoA-protein complex structures. The structure reveals regions likely to be involved in the interaction with the PCP substrate."],["dc.identifier.doi","10.1093/emboj/18.23.6823"],["dc.identifier.gro","3144430"],["dc.identifier.isi","000084177700024"],["dc.identifier.pmid","10581256"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2053"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0261-4189"],["dc.title","Crystal structure of the surfactin synthetase-activating enzyme Sfp: a prototype of the 4 '-phosphopantetheinyl transferase superfamily"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","c59"],["dc.bibliographiccitation.issue","a1"],["dc.bibliographiccitation.journal","Acta Crystallographica Section A Foundations of Crystallography"],["dc.bibliographiccitation.lastpage","c60"],["dc.bibliographiccitation.volume","61"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Strasser, A."],["dc.contributor.author","Dickmanns, A."],["dc.contributor.author","Lührmann, R."],["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/S0108767305097473"],["dc.identifier.pii","S0108767305097473"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103890"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0108-7673"],["dc.title","Structural basis for specific recognition of the UsnRNP m 3 G-cap by snurportin1"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1481"],["dc.bibliographiccitation.journal","Acta Crystallographica Section F Structural Biology Communications"],["dc.bibliographiccitation.lastpage","1487"],["dc.bibliographiccitation.volume","71"],["dc.contributor.author","Monecke, Thomas"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Weiss, Manfred S."],["dc.contributor.author","Port, Sarah A."],["dc.contributor.author","Kehlenbach, Ralph H."],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2017-09-07T11:54:49Z"],["dc.date.available","2017-09-07T11:54:49Z"],["dc.date.issued","2015"],["dc.description.abstract","High conformational flexibility is an intrinsic and indispensable property of nuclear transport receptors, which makes crystallization and structure determination of macromolecular complexes containing exportins or importins particularly challenging. Here, the crystallization and structure determination of a quaternary nuclear export complex consisting of the exportin CRM1, the small GTPase Ran in its GTP-bound form, the export cargo SPN1 and an FG repeat-containing fragment of the nuclear pore complex component nucleoporin Nup214 fused to maltose-binding protein is reported. Optimization of constructs, seeding and the development of a sophisticated protocol including successive PEG-mediated crystal dehydration as well as additional post-mounting steps were essential to obtain well diffracting crystals."],["dc.identifier.doi","10.1107/S2053230X15021524"],["dc.identifier.gro","3141769"],["dc.identifier.isi","000369376500007"],["dc.identifier.pmid","26625290"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/868"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft [Sonderforschungsbereich SFB860]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Int Union Crystallography"],["dc.relation.issn","2053-230X"],["dc.title","Combining dehydration, construct optimization and improved data collection to solve the crystal structure of a CRM1-RanGTP-SPN1-Nup214 quaternary nuclear export complex"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","541"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Cell"],["dc.bibliographiccitation.lastpage","552"],["dc.bibliographiccitation.volume","121"],["dc.contributor.author","Dierks, T."],["dc.contributor.author","Dickmanns, A."],["dc.contributor.author","Preusser-Kunze, A."],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Mariappan, M."],["dc.contributor.author","Von Figura, K."],["dc.contributor.author","Ficner, R."],["dc.contributor.author","Rudolph, M."],["dc.date.accessioned","2017-09-07T11:54:25Z"],["dc.date.available","2017-09-07T11:54:25Z"],["dc.date.issued","2005"],["dc.description.abstract","Sulfatases are enzymes essential for degradation and remodeling of sulfate esters. Formylglycine (FGly), the key catalytic residue in the active site, is unique to sulfatases. In higher eukaryotes, FGly is generated from a cysteine precursor by the FGly-generating enzyme (FGE). Inactivity of FGE results in multiple sulfatase deficiency (MSD), a fatal autosomal recessive syndrome. Based on the crystal structure, we report that FGE is a single-domain monomer with a surprising paucity of secondary structure and adopts a unique fold. The effect of all 18 missense mutations found in MSD patients is explained by the FGE structure, providing a molecular basis of MSD. The catalytic mechanism of FGly generation was elucidated by six high-resolution structures of FGE in different redox environments. The structures allow formulation of a novel oxygenase mechanism whereby FGE utilizes molecular oxygen to generate FGly via a cysteine sulfenic acid intermediate."],["dc.identifier.doi","10.1016/j.cell.2005.03.001"],["dc.identifier.gro","3143846"],["dc.identifier.isi","000229331200011"],["dc.identifier.pmid","15907468"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3452"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1405"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0092-8674"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]