PUBLIKATIONEN VON PROF. DR. TERESA CARLOMAGNO

Journale

  • Marchanka, A.; Carlomagno T. (2019): Solid-State NMR Spectroscopy of RNA.Methods Enzymol. 2019, 615, 333-371
    DOI: 10.1016/bs.mie.2018.08.029
  • Lercher, L.; Danilenko, N.; Kirkpatrick, J.; Carlomagno, T. (2018): Structural characterization of the Asf1-Rtt109 interaction and its role in histone acetylation.Nucleic Acids Res 2018, 46(5), 2279-2289
    DOI: 10.1093/nar/gkx1283
  • Marchanka, A.; Kreutz, C.; Carlomagno, T. (2018): Isotope labeling for studying RNA ba solid-state NMR spectroscopy.Journal of Biomolecular NMR 2018, 71(3,SI), 151-164
    DOI: 10.1007/s10858-018-0180-7
  • Marchanka, A.; Stanec, J.; Pintacuda, G.; Carlomagno, T. (2018): Rapid access to RNA resonances by proton-detected solid-state NMR at > 100 kHz MAS.Chemical Communications 2018, 54(65), 8972-8975
    DOI: 10.1039/c8cc04437f
  • Codutti, L.; Grimaldi, M.; Carlomagno, T. (2017): Structure-Based Design of Scaffolds Targeting PDE10A by INPHARMA-NMR.J. Chem. Inf. Model. 2017, 57 (6), 1488-1498
    DOI: 10.1021/acs.jcim.7b00246
  • Karaca, E.; Rodrigues, J. P. G. L. M.; Graziadei, A.; Bonvin, A. M. J. J.; Carlomagno, C. (2017): M3: an integrative framework for structure determination of molecular machinesNature Methods 2017, 14 897-902
    DOI: 10.1038/nmeth.4392
  • Scherer, S.; Wollrab, E.; Codutti, L.; Carlomagno, T.; Gomes da Costa, S.; Volkmer, A.; Bronja, A.; Schmtz, O. J.; Ott, A. (2017): Chemical Analysis of a “Miller-Type” Complex Prebiotic BrothOrig. Life Evol. Biosph. 2017, 47 381-403
    DOI: /10.1007/s11084-016-9528-8
  • Bowman, A.; Lercher, L.; Singh, H. R.; Zinne, D.; Timinszky, G.; Carlomagno, T.; Ladurner, A. G. (2016): The histone chaperone sNASP binds a conserved peptide motif within the globular core of histone H3 through its TPR repeats.Nucleic Acids Res. 2016, 44(7), 3105-3117
    DOI: 10.1093/nar/gkv1372
  • Graziadei, A.; Masiewicz, P.; Lapinaite, A.; Carlomagno, T. (2016): Archaea box C/D enzymes methylate two distinct substrate rRNA sequences with different efficiencyRNA. 2016, 22, 764-772
    DOI: 10.1261/rna.054320.115
  • Kozak, S.; Lercher, L.; Karanth, M. N.; Meijers, R.; Carlomagno, T.; Boivin, S. (2016): Optimization of protein samples for NMR using thermal shift assays.Journal of Biomolecular NMR 2016, 64(4), 281-289
    DOI: 10.1007/s10858-016-0027-z
  • Kuehne, C.; Singer, H. M.; Grabisch, E.; Codutti, L.; Carlomagno, T.; Scrima, A.; Erhardt, M. (2016): RflM mediates target specificity of the RcsCDB phosphorelay system for transcriptional repression of flagellar synthesis in Salmonella enterica.Mol. Microbiol. 2016, 101(5), 841-855
    DOI: 10.1111/mmi.13427
  • Miller, T. C. R.; Simon, B.; Rybin V.; Grötsch, H.; Curtet, S.; Khochbin, S.; Carlomagno, T.; Müller C. W. (2016): A bromodomain–DNA interaction facilitates acetylation-dependent bivalent nucleosome recognition by the BET protein BRDTNat. Commun. 2016, 7
    DOI: 10.1038/ncomms13855
  • Wollrab, E.; Scherer, S.; Abriet, F.; Carré, V.; Carlomagno, T.; Codutti, L.; Ott, A. (2016): Chemical Analysis of a "Miller-Type" Complex Prebiotic Broth: Part I: Chemical Diversity, Oxygen and Nitrogen Based Polymers.Orig. Life Evol. Biosph. 2016, 46 (2-3), 149-169
    DOI: 10.1007/s11084-015-9468-8
  • Marchanka A., Simon B., Althoff-Ospelt G., Carlomagno T. (2015): RNA structure determination by solid-state NMR spectroscopyNature Communications, 2015, 6, 7024
    DOI: 10.1038/ncomms8024
  • Simon B., Masiewicz P., Ephrussi A., Carlomagno T. (2015): The structure of the SOLE element of oskar mRNARNA Society, 2015, 21(8), 1444-1453
    DOI: 10.1261/rna.049601.115
  • Bock T, Chen WH, Ori A, Malik N, Silva-Martin N, Huerta-Cepas J, Powell ST, Kastritis PL, Smyshlyaev G, Vonkova I, Kirkpatrick J, Doerks T, Nesme L, Baßler J, Kos M, Hurt E, Carlomagno T, Gavin AC, Barabas O, Müller CW, van Noort V, Beck M, Bork P. (2014): An integrated approach for genome annotation of the eukaryotic thermophile Chaetomium thermophilum.Nucleic Acids Research
    DOI: 10.1093/nar/gku1147
  • Canales A, Nieto L, Rodríguez-Salarichs J, Sánchez-Murcia PA, Coderch C, Cortés-Cabrera A, Paterson I, Carlomagno T, Gago F, Andreu JM, Altmann KH, Jiménez-Barbero J, Díaz JF. (2014): Molecular recognition of epothilones by microtubules and tubulin dimers revealed by biochemical and NMR approaches.ACS Chemical Biology
  • Carlomagno T. (2014): Present and future of NMR for RNA-protein complexes: a perspective of integrated structural biologyJournal of Magnetic Resonance
    DOI: 10.1016/j.jmr.2013.10.007
  • Findeisen P, Mühlhausen S, Dempewolf S, Hertzog J, Zietlow A, Carlomagno T, Kollmar M. (2014): Six subgroups and extensive recent duplications characterize the evolution of the eukaryotic tubulin protein familyEnviromental Epigenetics
    DOI: 10.1093/gbe/evu187
  • Asami S, Rakwalska-Bange M, Carlomagno T, Reif B. (2013): Protein-RNA interfaces probed by 1H-detected MAS solid-state NMR spectroscopy, Angew. Chem. Int. Ed. Engl. 52(8):2345-2349
    DOI: 10.1002/anie.201208024
  • Carlomagno T, Amata I, Codutti L, Falb M, Fohrer J, Masiewicz P, Simon B. (2013): Structural principles of RNA catalysis in a 2'-5' lariat-forming ribozyme, J. Am. Chem. Soc. 135(11):4403-4411 JACS
    DOI: 10.1021/ja311868t
  • Lapinaite A, Simon B, Skjaerven L, Rakwalska-Bange M, Gabel F, Carlomagno T. (2013): The structure of the box C/D enzyme reveals regulation of RNA methylation, Nature 502(7472):519-523
    DOI: 10.1038/nature12581
  • Latek D, Pasznik P, Carlomagno T, Filipek S. (2013): Towards improved quality of GPCR models by usage of multiple templates and profile-profile comparison, PLoS ONE 8(2):e56742
    DOI: 0.1371/journal.pone.0056742
  • Marchanka A, Simon B, Carlomagno T. (2013): A suite of solid-state NMR experiments for RNA intranucleotide resonance assignment in a 21 kDa protein-RNA complex, Angew. Chem. Int. Ed. Engl. 52(38):9996-10001
    DOI: 10.1002/anie.201304779
  • Riplinger S, Carlomagno T, Wabnitz GH, Samstag Y. (2013): A reducing milieu renders cofilin insensitive to phosphatidylinositol 4,5-bisphosphate (PIP2) inhibition, J. Biol. Chem. 288(41):29430-29439
    DOI: 10.1074/jbc.m113.479766
  • Skjærven L, Codutti L, Angelini A, Grimaldi M, Latek D, Monecke P, Dreyer MK, Carlomagno T. (2013): Accounting for conformational variability in protein-ligand docking with NMR-guided rescoring JACS
    DOI: 10.1021/ja4007468
  • Ballaré C, Lange M, Lapinaite A, Martin GM, Morey L, Pascual G, Liefke R, Simon B, Shi Y, Gozani O, Carlomagno T, Benitah SA, Di Croce L. (2012): Phf19 links methylated Lys36 of histone H3 to regulation of Polycomb activity, Nat. Struct. Mol. Biol. 19(12):1257-1265 Nature Structural and Molecular Biology
    DOI: 10.1038/nsmb.2434
  • Carlomagno T. (2012): NMR in natural products: understanding conformation, configuration and receptor interactions, Nat. Prod. Rep., 2012,29, 536-554
    DOI: 10.1039/c2np00098a
  • Dreisigacker S, Latek D, Bockelmann S, Huss M, Wieczorek H, Filipek S, Gohlke H, Menche D, Carlomagno T. (2012): Understanding the inhibitory effect of highly potent and selective archazolides binding to the vacuolar ATPase, J Chem Inf Model 52(8):2265-2272 Journal of Chemical Information and Modeling
    DOI: doi:10.1021/ci300242d
  • Persch E, Basile T, Bockelmann S, Huss M, Wieczorek H, Carlomagno T, Menche D. (2012): Synthesis and biological evaluation of a water-soluble derivative of the potent V-ATPase inhibitor archazolid, Bioorg. Med. Chem. Lett. 22(24):7735-7738 Bioorganic and Medicinal Chemistry Letters
    DOI: 10.1016/j.bmcl.2012.09.081
  • Stauch B, Orts J, Carlomagno T. (2012): The description of protein internal motions aids selection of ligand binding poses by the INPHARMA method, J. Biomol. NMR 54(3):245-256 Journal of Biomolecular MNR
    DOI: 10.1007/s10858-012-9662-1
  • B. Stauch, B. Simon, T. Basile, G. Schneider, N. P. Malek, M. Kalesse, T. Carlomagno (2010): Elucidation of the Structure and Intermolecular Interactions of a Reversible Cyclic-Peptide Inhibitor of the Proteasome by NMR Spectroscopy and Molecular ModelingAngew. Chem. Int. Ed. 2010, 23, 3934
    DOI: 10.1002/anie.201000140
  • L. Bülow, I. Nickeleit, A.-K. Girbig, T. Brodmann, A. Rentsch, U. Eggert, F. Sasse, H. Steinmetz, R. Frank, T. Carlomagno, N. P. Malek, M. Kalesse (2010): Synthesis and Biological Characterization of Argyrin FChemMedChem. 2010, 5, 832
    DOI: 10.1002/cmdc.201000080
  • I. Nickeleit, S. Zender, F. Sasse, R. Geffers, G. Brandes, I. Sörensen, H. Steinmetz, S. Kubicka, T. Carlomagno, D. Menche, J. Buer, A. Gossler, M. P. Manns, M. Kalesse, R. Frank, N. P. Malek (2008): A myxobacterial cyclic peptide metabolite is a highly selective proteasome inhibitor and potent antitumor leadJournal of Peptide Science 2008, 14, 43
    DOI: 10.1002/psc.1089
  • D. Ragunathan, V. M. Sanchez-Pedregal, J. Junker, M. Kalesse, A. Kirschning, T. Carlomagno (2006): TAR-RNA recognition by a novel aminoglycoside analogueNucl. Acid. Res. 2006, 34, 3599
    DOI: 10.1093/nar/gkl494

[nicht kategorisiert]

  • Lercher L., Danilenko N., Kirkpatrick J., Carlomango T. (2018): Structural characterization of the Asf1-Rtt109 interaction and its role in histone acetylationNucleic Acids Res., 2018, 46(5), 2279-2289
    DOI: 10.1093/nar/gkx1283
  • Marchanka A., Kreutz C., Carlomagno T. (2018): Isotope labeling for studying RNA by solid - state NMR spectroscopyJ. Biomol NMR, 71, Issue 3, 151-164
    DOI: 10.1007/s10858-018-0180-7
  • Marchanka A., Stanek J., Pintacuda G. and Carlomagno T. (2018): Rapid access to RNA resonances by proton-detected solid-state NMR at >100 kHz MASChem. Comm. June 28 2018
    DOI: 10.1039/C8CC04437F
  • Codutti L., Grimaldi M., Carlomagno T. (2017): Structure-Based Design of Scaffolds Targeting PDE10A by Inpharma-NMRJ. Chem Inf. Model, 2017, 57(6), 1488-1498
    DOI: 10.1021/acs.jcim.7b00246
  • Karaca E., Rodrigues J.P.G.L.M., Graziadei A., Bonvin A.M.J.J., Carlomagno T. (2017): M3: An integrative framework for structure determination of molecular machinesNat. Methods, 2017, 14, 867-902
    DOI: 10.1038/nmeth.4392
  • Scherer S., Wolrab E., Codutti L., Carlomagno T., da Costa S.G., Volkmer A., Bronja A., Schmitz O.J., Ott A. (2017): Chemical Analysis of a "Miller-Type" Complex Prebiotic Broth: Part II: Gas, Oil, Water and the Oil/Water-InterfaceOrigins of Life and Evolution of Biospheres, 2017, 47(4), 381-403
    DOI: 10.1007/s11084-016-9528-8
  • Bowman A., Lercher L., Singh H.R., Zinne D., Timinszky G., Carlomagno T., Ladurner A.G. (2016): The histone chaperone sNASP binds a conserved peptide motif within the globular core of histone H3 through its TPR repeatsNucleic Acids Res., 2016, 44(7), 3105-3117
    DOI: 10.1093/nar/gkv1372
  • Graziadei A., Masiewicz P., Lapinaite A., Carlomagno T. (2016): Archaea box C/D enzymes methylate two distinct substrate rRNA sequences with different efficiencyRNA, 2016, 22(5), 764-772
    DOI: 10.1261/rna.054320.115
  • Kozak S., Lercher L., Karanth M.N., Meijers R., Carlomagno T. Boivin S. (2016): Optimization of protein samples for NMR using thermal shift assaysJ. Biomol. NMR, 2016, 64(4), 281-289
    DOI: 10.1007/s10858-016-0027-z
  • Kühne C., Singer H.M., Grabisch E., Codutti L., Carlomagno T., Scrima A., Erhardt M. (2016): RfIM mediates target specificity of the RcsCDB phosphorelay system for transcriptional repression of flagellar synthesis in Salmonella entericaMol. Microbiol., 2016, 101(5), 841-855
    DOI: 10.1111/mmi.13427
  • Miller T.C., Simon B., Rybin V., Grotsch H., Curtet S., Khochbin S., Carlomagno T., Müller C.W. (2016): A bromodomain-DNA interaction facilitates acetylation-dependent bivalent nucleosome recognition by the BET protein BRDTNat. Commun., 2016, 7, 13855
    DOI: 10.1038/ncomms13855
  • Wollrab E., Scherer S., Aubriet F., Carre V., Carlomagno T. Codutti L., Ott A. (2016): Chemical Analysis of a "Miller-Type" Complex Prebiotic Broth: Part I: Chemical Diversity, Oxygen and Nitrogen Based PolymersOrig. Live Evo.l Biosph., 2016, 46(2-3), 149-169
    DOI: 10.1007/s11084-015-9468-8
  • Codutti L., Leppek K., Zalesak J., Windeisen V., Masiewicz P., Stoecklin G., Carlomagno T. (2015): A Distinct, Sequence-Induced Conformation Is Required for Recognition of the Constitutive Decay Element RNA by RoquinStructure., 2015, 23(8), 1437-1447
    DOI: 10.1016/j.str.2015.06.001
  • Onila I., ten Brink T., Fredriksson K., Codutti L., Mazur A., Griesinger C., Carlomagno T. Exner T.E. (2015): On-the-Fly Integration of Data from a Spin-Diffusion-Based NMR Experiment into Protein-Ligand DockingJ. Chem. Inf. Model., 2015, 55(9), 1962-1972
    DOI: 10.1021/acs.jcim.5b00235
  • Sikorska J., Codutti L., Skaerven L., Elshorst B., Saez-Ameneiro R., Angelini A., Monecke P., Carlomagno T. (2015): Identification of new scaffolds with INPHARMA-based virtual screeningMed. Chem. Com., 2015, 6, 1501-1507
    DOI: 10.1039/C5MD00116A