Research Group Structure Determination of Proteins Using NMR

Publications

Journal Article (193)

  1. 1.
    Kadavath, H.; Cabrales-Fontela, Y.; Jaremko, M.; Jaremko, L.; Overkamp, K.; Biernat, J.; Mandelkow, E.; Zweckstetter, M.: The binding mode of a repeat-like Tau sequence with tubulin. Angewandte Chemie International Edition 57 (12), pp. 3246 - 3250 (2018)
  2. 2.
    Jaipuria, G.; Ukmar-Godec, T.; Zweckstetter, M.: Challenges and approaches to understand cholesterol-binding impact on membrane protein function: An NMR view. Cellular and Molecular Life Sciences (2018)
  3. 3.
    Tolö, J.; Taschenberger, G.; Leite, K.; Stahlberg, M. A.; Spehlbrink, G.; Kues, J.; Munari, F.; Capaldi, S.; Becker, S.; Zweckstetter, M. et al.; Dean, C.; Bähr, M.; Kügler, S.: Pathophysiological consequences of neuronal alpha-Synuclein overexpression: Impacts on ion homeostasis, stress signaling, mitochondrial integrity, and electrical activity. Frontiers in Molecular Neuroscience (2018)
  4. 4.
    Martinez Hernandez, A.; Urbanke, H.; Gillman, A. L.; Lee, J.; Ryazanov, S.; Agbemenyah, H. Y.; Benito, E.; Jain, G.; Kaurani, L.; Grigorian, G. et al.; Leonov, A.; Rezaei-Ghaleh, N.; Wilken, P.; Arce, F. T.; Wagner, J.; Fuhrman, M.; Caruana, M.; Camilleri, A.; Vassallo, N.; Zweckstetter, M.; Benz, R.; Giese, A.; Schneider, A.; Korte, M.; Lal, R.; Griesinger, C.; Eichele, G.; Fischer, A.: The diphenylpyrazole compound anle138b blocks Aβ channels and rescues disease phenotypes in a mouse model for amyloid pathology. EMBO Molecular Medicine 10 (1), pp. 32 - 47 (2018)
  5. 5.
    Cabrales-Fontela, Y.; Kadavath, H.; Biernat, J.; Riedel, D.; Mandelkow, E.; Zweckstetter, M.: Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau. Nature Communications (2017)
  6. 6.
    Bharat, V.; Siebrecht, M.; Burk, K.; Ahmed, S.; Reissner, C.; Kohansal-Nodehi, M.; Steubler, V.; Zweckstetter, M.; Ting, J. T.; Dean, C.: Capture of dense core vesicles at synapses by JNK-dependent phosphorylation of Synaptotagmin-4. Cell Reports (2017)
  7. 7.
    Fonseca-Ornelas, L.; Schmidt, C. D.; Camacho-Zarco, A. R.; Fernandez, C. O.; Becker, S.; Zweckstetter, M.: Small molecule-induced soluble oligomers of α-synuclein with helical structure. Chemistry. A European Journal 23 (53), pp. 13010 - 13014 (2017)
  8. 8.
    Ambadipudi, S.; Biernat, J.; Riedel, D.; Mandelkow, E.; Zweckstetter, M.: Liquid-liquid phase separation of the microtubule-binding repeats of the Alzheimer-related protein Tau. Nature Communications (2017)
  9. 9.
    Rezaei-Ghaleh, N.; Bakhtiari, D.; Rashidi, A.: Reverse allostasis in biological systems: Minimal conditions and implications. Journal of Theoretical Biology 426, pp. 134 - 139 (2017)
  10. 10.
    Baker, J. D.; Shelton, L. B.; Zheng, D. L.; Favretto, F.; Nordhues, B. A.; Darling, A.; Sullivan, L. E.; Sun, Z. Y.; Solanki, P. K.; Martin, M. D. et al.; Suntharalingam, A.; Sabbagh, J. J.; Becker, S.; Mandelkow, E.; Uversky, V. N.; Zweckstetter, M.; Dickey, C. A.; Koren, J.; Blair, L. J.: Human cyclophilin 40 unravels neurotoxic amyloids. PLoS Biology (2017)
  11. 11.
    Vincente Miranda, H.; Szego, E. M.; Oliveira, L. M.; Breda, C.; Darendelioglu, E.; de Oliveira, R. M.; Ferreira, D. G.; Gomes, M. A.; Rott, R.; Oliveira, M. et al.; Munari, F.; Enguita, F. J.; Simoes, T.; Rodrigues, E. F.; Heinrich, M.; Martins, I. C.; Zamolo, I.; Riess, O.; Cordeiro, C.; Ponces-Freire, A.; Lashuel, H. A.; Santos, N. C.; Lopes, L. V.; Xiang, W.; Jovin, T. M.; Penque, D.; Engelender, S.; Zweckstetter, M.; Klucken, J.; Giorgini, F.; Quintas, A.; Outeiro, T. F.: Glycation potentiates alpha-synuclein-associated neurodegeneration in synucleinopathies. Brain 140 (5), pp. 1399 - 1419 (2017)
  12. 12.
    Zweckstetter, M.; Requena, J. R.; Wille, H.: Elucidating the structure of an infectious protein. PLoS Pathogens (2017)
  13. 13.
    de Oliveira, R. M.; Miranda, H. V.; Francelle, L.; Pinho, R.; Szegö, E. M.; Martinho, R.; Munari, F.; Lázaro, D. F.; Moniot, S.; Guerreiro, P. et al.; Fonseca, L.; Marijanovic, Z.; Antas, P.; Gerhardt, E.; Enguita, F. J.; Fauvet, B.; Penque, D.; Pais, T. F.; Tong, Q.; Becker, S.; Kügler, S.; Lashuel, H. A.; Steegborn, C.; Zweckstetter, M.; Outeiro, T. F.: The mechanism of sirtuin 2–mediated exacerbation of alpha-synuclein toxicity in models of Parkinson disease. PLoS Biology (2017)
  14. 14.
    Miotto, M. C.; Pavese, M. D.; Quintanar, L.; Zweckstetter, M.; Griesinger, C.; Fernández, C. O.: Bioinorganic chemistry of Parkinson's disease: Affinity and structural features of Cu(I) binding to the full-length β-synuclein protein. Inorganic Chemistry 56 (17), pp. 10387 - 10395 (2017)
  15. 15.
    Oroz, J.; Kim, J. H.; Chang, B. J.; Zweckstetter, M.: Mechanistic basis for the recognition of a misfolded protein by the molecular chaperone Hsp90. Nature Structural and Molecular Biology 24, pp. 407 - 413 (2017)
  16. 16.
    Kim, J. H.; Oroz, J.; Zweckstetter, M.: Structure of monomeric transthyretin carrying the clinically important T119M mutation. Angewandte Chemie International Edition 55 (52), pp. 16168 - 16171 (2016)
  17. 17.
    Marsh, D.: Nuclear spin-lattice relaxation in nitroxide spin-label EPR. Journal of Magnetic Resonance 272, pp. 166 - 171 (2016)
  18. 18.
    Villar-Piqué, A.; da Fonseca, T. L.; Sant’Anna, R.; Szegö, E. M.; Fonseca-Ornelas, L.; Pinho, R.; Carija, A.; Gerhardt, E.; Masaracchia, C.; Gonzalezf, E. A. et al.; Rossetti, G.; Carloni, P.; Fernández, C. O.; Foguel, D.; Milosevic, I.; Zweckstetter, M.; Ventura, S.; Outeiro, T. F.: Environmental and genetic factors support the dissociation between α-synuclein aggregation and toxicity. Proceedings of the National Academy of Sciences of the United States of Amerca (2016)
  19. 19.
    Briones, R.; Weichbrodt, C.; Paltrinieri, L.; Mey, I.; Villinger, S.; Giller, K.; Lange, A.; Zweckstetter, M.; Griesinger, C.; Becker, S. et al.; Steinem, C.; de Groot, B. L.: Voltage dependence of conformational dynamics and subconducting states of VDAC-1. Biophysical Journal 111 (6), pp. 1223 - 1234 (2016)
  20. 20.
    Jaremko, M.; Jaremko, L.; Villinger, S.; Schmidt, C. D.; Griesinger, C.; Becker, S.; Zweckstetter, M.: High-resolution NMR determination of the dynamic structure of membrane proteins. Angewandte Chemie International Edition 55 (35), pp. 101518 - 10521 (2016)
  21. 21.
    Fonseca-Ornelas, L.; Zweckstetter, M.: The protonation state of histidine 111 regulates the aggregation of the evolutionary most conserved region of the human prion protein. Protein Science 25 (8), pp. 1563 - 1567 (2016)
  22. 22.
    Rezaei-Ghaleh, N.; Kumar, S.; Walter, J.; Zweckstetter, M.: Phosphorylation interferes with maturation of amyloid-β fibrillar structure in the N terminus. Journal of Biological Chemistry 291 (31), pp. 16059 - 16067 (2016)
  23. 23.
    Beyer, I.; Rezaei-Ghaleh, N.; Klafki, H. W.; Jahn, O.; Haussmann, U.; Wiltfang, J.; Zweckstetter, M.; Knölker, H. J.: Solid-phase synthesis and characterization of N-terminally elongated A beta(-3-x)-peptides. Chemistry-A European Journal 22 (25), pp. 8685 - 8693 (2016)
  24. 24.
    Akoury, E.; Mukrasch, M.; Biernat, J.; Tepper, K.; Ozenne, V.; Mandelkow, E.; Blackledge, M.; Zweckstetter, M.: Remodeling of the conformational ensemble of the repeat domain of tau by an aggregation enhancer. Protein Science 25 (5), pp. 1010 - 1020 (2016)
  25. 25.
    Tatenhorst, L.; Eckermann, K.; Dambeck, V.; Fonseca-Ornelas, L.; Walle, H.; da Fonseca, T. L.; Koch, J. C.; Becker, S.; Toenges, L.; Bahr, M. et al.; Outeiro, T. F.; Zweckstetter, M.; Lingor, P.: Fasudil attenuates aggregation of alpha-synuclein in models of Parkinson's disease. Acta Neuropathologica Communications (2016)
  26. 26.
    Rezaei-Ghaleh, N.; Amininasab, M.; Kumar, S.; Walter , J.; Zweckstetter, M.: Phosphorylation modifies the molecular stability of beta-amyloid deposits. Nature Communications (2016)
  27. 27.
    Ge, L.; Villinger, S.; Mari, S. A.; Giller, K.; Griesinger, C.; Becker, S.; Müller, D. J.; Zweckstetter, M.: Molecular plasticity of the human Voltage-Dependent Anion Channel embedded into a membrane. Structure 24 (4), pp. 585 - 594 (2016)
  28. 28.
    Jaremko, M.; Jaremko, L.; Giller, K.; Becker, S.; Zweckstetter, M.: Backbone and side-chain resonance assignment of the A147T polymorph of mouse TSPO in complex with a high-affinity radioligand. Biomolecular NMR Assignments 10 (1), pp. 79 - 83 (2016)
  29. 29.
    Kumar, S.; Wirths, O.; Stüber, K.; Wunderlich, P.; Koch, P.; Theil, S.; Rezaei-Ghaleh, N.; Zweckstetter, M.; Bayer, T. A.; Bruestle, O. et al.; Thal, D. R.; Walter, J.: Phosphorylation of the amyloid beta-peptide at Ser26 stabilizes oligomeric assembly and increases neurotoxicity. Acta Neuropathologica 131 (4), pp. 525 - 537 (2016)
  30. 30.
    Tenreiro, S.; Rosado-Ramos, R.; Gerhardt, E.; Favretto, F.; Magalhães, F.; Popova, B.; Becker, S.; Zweckstetter, M.; Braus, G. H.; Outeiro, T. F.: Yeast reveals similar molecular mechanisms underlying alpha- and beta-synuclein toxicity. Human Molecular Genetics 25 (2), pp. 275 - 290 (2016)
  31. 31.
    Ambadipudi, S.; Zweckstetter, M.: Targeting intrinsically disordered proteins in rational drug discovery. Expert Opinion on Drug Discocery 11 (1), pp. 65 - 77 (2016)
  32. 32.
    Wysoczanski, P.; Zweckstetter, M.: Retention and splicing complex (RES) - the importance of cooperativity. RNA Biology 13 (2), pp. 128 - 133 (2016)
  33. 33.
    Moree, B.; Yin, G.; Lazaro, D. F.; Munari, F.; Strohäker, T.; Giller, K.; Becker, S.; Outeiro, T. F.; Zweckstetter, M.; Salafsky, J.: Small molecules detected by second-harmonic generation modulate the conformation of monomeric α-synuclein and reduce its aggregation in cell. Journal of Biological Chemistry (2015)
  34. 34.
    Rauscher, S.; Gapsys, V.; Gajda, M. J.; Zweckstetter, M.; de Groot, B. L.; Grubmüller, H.: Structural ensembles of intrinsically disordered proteins depend strongly on force field: A comparison to experiment. Journal of Chemical Theory and Computation 11 (11), pp. 5513 - 5524 (2015)
  35. 35.
    Jaremko, L.; Jaremko, M.; Giller, K.; Becker, S.; Zweckstetter, M.: Conformational flexibility in the transmembrane protein TSPO. Chemistry-A European Journal 21 (46), pp. 16555 - 16563 (2015)
  36. 36.
    Gapsys, V.; Narayanan, R. L.; Xiang, S.; de Groot, B. L.; Zweckstetter, M.: Improved validation of IDP ensembles by one-bond Cα-Hα scalar couplings. Journal of Biomolecular NMR 63 (3), pp. 299 - 307 (2015)
  37. 37.
    Kadavath, H.; Jaremko, M.; Jaremko, L.; Biernat, J.; Mandelkow, E.; Zweckstetter, M.: Folding of the Tau protein on microtubules. Angewandte Chemie International Edition 54 (35), pp. 10347 - 10351 (2015)
  38. 38.
    Schwalbe, M.; Kadavath, H.; Biernat, J.; Ozenne, V.; Blackledge, M.; Mandelkow, E.; Zweckstetter, M.: Structural impact of Tau phosphorylation at threonine 231. Structure 23 (8), pp. 1448 - 1458 (2015)
  39. 39.
    Jaremko, M.; Jaremko, L.; Jaipuria, G.; Becker, S.; Zweckstetter, M.: Structure of the mammalian TSPO/PBR protein. Biochemical Society Transactions (2015)
  40. 40.
    Wysoczanski, P.; Becker, S.; Zweckstetter, M.: Structures of intermediates during RES complex assembly. Scientific Reports (2015)
  41. 41.
    Fontaine, S. N.; Martin, M. D.; Akoury, E.; Assimon, V. A.; Borysov, S.; Nordhues, B. A.; Sabbagh, J. J.; Cockman, M.; Gestwicki, J. E.; Zweckstetter, M. et al.; Dickey, C. A.: The active Hsc70/tau complex can be exploited to enhance tau turnover without damaging microtubule dynamics. Human Molecular Genetics 24 (14), pp. 3971 - 3981 (2015)
  42. 42.
    Jaremko, M.; Jaremko, L.; Giller, K.; Becker, S.; Zweckstetter, M.: Structural integrity of the A147T polymorph of mammalian TSPO. ChemBioChem 16 (10), pp. 1483 - 1489 (2015)
  43. 43.
    Gut, P.; Zweckstetter, M.; Banati, R. B.: Lost in translocation: The functions of the 18-kD translocator protein. Trends in Endocrinology and Metabolism (2015)
  44. 44.
    Kadavath, H.; Hofele, R. V.; Biernat, J.; Kumar, S.; Tepper, K.; Urlaub, H.; Mandelkow, E.; Zweckstetter, M.: Tau stabilizes microtubules by binding at the interface between tubulin heterodimers. Proceedings of the National Academy of Sciences of the United States of America (2015)
  45. 45.
    Kunadt, M.; Eckermann, K.; Stuendl, A.; Gong, J.; Russo, B.; Strauss, K.; Rai, S.; Kügler, S.; Falomir Lockhart, L. J.; Schwalbe, M. et al.; Krumova, P.; Oliveira, L. M. A.; Bähr, M.; Möbius, W.; Levin, J.; Giese, A.; Kruse, N.; Mollenhauer, B.; Geiss-Friedlander, R.; Ludolph, A. C.; Freischmidt, A.; Feiler, M. S.; Danzer, K. M.; Zweckstetter, M.; Jovin, T. M.; Simons, M.; Weishaupt, J. H.; Schneider, A.: Extracellular vesicle sorting of α-Synuclein is regulated by sumoylation. Acta Neuropathologica 129 (5), pp. 695 - 713 (2015)
  46. 46.
    Rezaei-Ghaleh, N.; Klama, F.; Munari, F.; Zweckstetter, M.: HYCUD: A computational tool for prediction of effective rotational correlation time in flexible proteins. Bioinformatics 31 (8), pp. 1319 - 1321 (2015)
  47. 47.
    Mbefo, M. K.; Fares, M. B.; Paleologou, K.; Oueslati, A.; Yin, G.; Tenreiro, S.; Pinto, M.; Outeiro, T.; Zweckstetter, M.; Masliah, E. et al.; Lashuel, H. A.: Parkinson disease mutant E46K enhances alpha-synuclein phosphorylation in mammalian cell lines, in yeast, and in vivo. Journal of Biological Chemistry (2015)
  48. 48.
    Gattin, Z.; Schneider, R.; Laukat, Y.; Giller, K.; Maier, E.; Zweckstetter, M.; Griesinger, C.; Benz, R.; Becker, S.; Lange, A.: Solid-state NMR, electrophysiology and molecular dynamics characterization of human VDAC2. Journal of Biomolecular NMR 61 (3-4), pp. 311 - 320 (2015)
  49. 49.
    Camacho-Zarco, A. R.; Munari, F.; Wegstroth, M.; Liu, W. M.; Ubbink, M.; Becker, S.; Zweckstetter, M.: Multiple paramagnetic effects through a tagged reporter protein. Angewandte Chemie International Edition 54 (1), pp. 336 - 339 (2015)
  50. 50.
    Miotto, M. C.; Valiente-Gabioud, A. A.; Rossetti, G.; Zweckstetter, M.; Carloni, P.; Selenko, P.; Griesinger, C.; Binolfi, A.; Fernández, C. O.: Copper binding to the N-terminally acetylated, naturally occurring form of alpha-synuclein induces local helical folding. Journal of the American Chemical Society 137 (20), pp. 6444 - 6447 (2015)
  51. 51.
    Fonseca-Ornelas, L.; Eisbach, S. E.; Paulat, M.; Giller, K.; Fernandez, C. O.; Outeiro, T. F.; Becker, S.; Zweckstetter, M.: Small molecule-mediated stabilization of vesicle-associated helical alpha-synuclein inhibits pathogenic misfolding and aggregation. Nature Communications (2014)
  52. 52.
    Bajaj, R.; Munari, F.; Becker, S.; Zweckstetter, M.: Interaction of the intermembrane space domain of Tim23 protein with mitochondrial membranes. Journal of Biological Chemistry 289 (50), pp. 34620 - 34626 (2014)
  53. 53.
    Miotto, M. C.; Binolfi, A.; Zweckstetter, M.; Griesinger, C.; Fernandez, C. O.: Bioinorganic chemistry of synucleinopathies: Deciphering the binding features of Met motifs and His-50 in AS-Cu(I) interactions. Journal of Inorganic Biochemistry 141, pp. 208 - 211 (2014)
  54. 54.
    Yao, X.; Becker, S.; Zweckstetter, M.: A six-dimensional alpha proton detection-based APSY experiment for backbone assignment of intrinsically disordered proteins. Journal of Biomolecular NMR 60 (4), pp. 231 - 240 (2014)
  55. 55.
    Parigi, G.; Rezaei-Ghaleh, N.; Giachetti, A.; Becker, S.; Fernandez, C.; Blackledge, M.; Griesinger, C.; Zweckstetter, M.; Luchinat, C.: Long-range correlated dynamics in intrinsically disordered proteins. Journal of the American Chemical Society 136 (46), pp. 16201 - 16209 (2014)
  56. 56.
    Yao, X.; Dürr, U. H. N.; Gattin, Z.; Laukat, Y.; Narayanan, R.L.; Brückner, A. K.; Meisinger, C.; Lange, A.; Becker, S.; Zweckstetter, M.: NMR-based detection of hydrogen/deuterium exchange in liposome-embedded membrane proteins. PLOS One (2014)
  57. 57.
    Bajaj, R.; Jaremko, L.; Jaremko, M.; Becker, S.; Zweckstetter, M.: Molecular basis of the dynamic structure of the TIM23 complex in the mitochondrial intermembrane space. Structure 22 (10), pp. 1501 - 1511 (2014)
  58. 58.
    Wysoczanski, P.; Schneider, C.; Xiang, S. Q.; Munari, F.; Trowitzsch, S.; Wahl, M. C.; Lührmann, R.; Becker, S.; Zweckstetter, M.: Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex. Nature Structural and Molecular Biology 21 (10), pp. 911 - 918 (2014)
  59. 59.
    Yin, G.; Lopes da Fonseca, T.; Eisbach, S. E.; Anduaga, A. M.; Breda, C.; Orcellet, M. L.; Szegő, E. M.; Guerreiro, P.; Lázaro, D. F.; Braus, G. H. et al.; Fernandez, C. O.; Griesinger, C.; Becker, S.; Goody, R. S.; Itzen, A.; Giorgini, F.; Outeiro, T. F.; Zweckstetter, M.: α-Synuclein interacts with the switch region of Rab8a in a Ser129 phosphorylation-dependent manner. Neurobiology of Disease 70, pp. 149 - 161 (2014)
  60. 60.
    Jaremko, L.; Jaremko, M.; Becker, S.; Zweckstetter, M.: Toward the functional oligomerization state of tryptophan-rich sensory proteins. Protein Science 23 (8), pp. 1154 - 1160 (2014)
  61. 61.
    Jensen, M. R.; Zweckstetter, M.; Huang, J.; Blackledge, M.: Exploring free-energy landscapes of intrinsically disordered proteins at atomic resolution using NMR spectroscopy. Chemical Reviews 114 (13), pp. 6632 - 6660 (2014)
  62. 62.
    Xiang, S. Q.; Zweckstetter, M.: Detection of a transient intramolecular hydrogen bond using (l)J(NH) scalar couplings. Journal of Magnetic Resonance 243, pp. 93 - 97 (2014)
  63. 63.
    Villinger, S.; Giller, K.; Bayrhuber, M.; Lange, A.; Griesinger, C.; Becker, S.; Zweckstetter, M.: Nucleotide interactions of the human voltage-dependent anion channel. Journal of Biological Chemistry 289 (19), pp. 13397 - 13406 (2014)
  64. 64.
    Miotto, M. C.; Rodriguez, E. E.; Valiente-Gabioud, A. A.; Torres-Monserrat, V.; Binolfi, A.; Quintanar, L.; Zweckstetter, M.; Griesinger, C.; Fernandez, C. O.: Site-specific copper-catalyzed oxidation of alpha-synuclein: Tightening the link between metal binding and protein oxidative damage in Parkinson's disease. Inorganic Chemistry 53 (9), pp. 4350 - 4358 (2014)
  65. 65.
    Munari, F.; Gajda, M. J.; Hiragami-Hamada, K.; Fischle, W.; Zweckstetter, M.: Characterization of the effects of phosphorylation by CK2 on the structure and binding properties of human HP1 beta. FEBS Letters 588 (7), pp. 1094 - 1099 (2014)
  66. 66.
    Rezaei-Ghaleh, N.; Amininasab, M.; Giller, K.; Kumar, S.; Stuendl, A.; Schneider, A.; Becker, S.; Walter, J.; Zweckstetter, M.: Turn plasticity distinguishes different modes of amyloid-beta aggregation. Journal of the American Chemical Society 136 (13), pp. 4913 - 4919 (2014)
  67. 67.
    Jaremko, L.; Jaremko, M.; Giller, K.; Becker, S.; Zweckstetter, M.: Structure of the mitochondrial translocator protein in complex with a diagnostic ligand. Science 343 (6177), pp. 1363 - 1366 (2014)
  68. 68.
    Karagoz, G. E.; Duarte, A. M. S.; Akoury, E.; Ippel, H.; Biernat, J.; Luengo, T. M.; Radli, M.; Didenko, T.; Nordhues, B. A.; Veprintsev, D. B. et al.; Dickey, C. A.; Mandelkow, E.; Zweckstetter, M.; Boelens, R.; Madl, T.; Rudiger, S. G. D.: Hsp90-Tau complex reveals molecular basis for specificity in chaperone action. Cell 156 (5), pp. 963 - 974 (2014)
  69. 69.
    Schwalbe, M.; Ozenne, V.; Bibow, S.; Jaremko, M.; Jaremko, L.; Gajda, M. J.; Jensen, M. R.; Biernat, J.; Becker, S.; Mandelkow, E. et al.; Zweckstetter, M.; Blackledge, M.: Predictive atomic resolution descriptions of intrinsically disordered hTau40 and alpha-synuclein in solution from NMR and small angle scattering. Structure 22 (2), pp. 238 - 249 (2014)
  70. 70.
    Buhl, T.; Braun, A.; Forkel, S.; Moebius, W.; van Werven, L.; Jahn, O.; Rezaei-Ghaleh, N.; Zweckstetter, M.; Mempel, M.; Schoen, M. P. et al.; Haennssle, H. A.: Internalization routes of cell-penetrating melanoma antigen peptides into human dendritic cells. Experimental Dermatology 23 (1), pp. 20 - 26 (2014)
  71. 71.
    Schwalbe, M.; Biernat, J.; Bibow, S.; Ozenne, V.; Jensen, M. R.; Kadavath, H.; Blackledge, M.; Mandelkow, E.; Zweckstetter, M.: Phosphorylation of human Tau protein by microtubule affinity-regulating kinase 2. Biochemistry 52 (50), pp. 9068 - 9079 (2013)
  72. 72.
    Xiang, S. Q.; Gapsys, V.; Kim, H. Y.; Bessonov, S.; Hsiao, H. H.; Möhlmann, S.; Klaukien, V.; Ficner, R.; Becker, S.; Urlaub, H. et al.; Lührmann, R.; de Groot, B.; Zweckstetter, M.: Phosphorylation drives a dynamic switch in serine/arginine-rich proteins. Structure 21 (12), pp. 2162 - 2174 (2013)
  73. 73.
    Rezaei-Ghaleh, N.; Klama, F.; Munari, F.; Zweckstetter, M.: Predicting the rotational tumbling of dynamic multidomain proteins and supramolecular complexes. Angewandte Chemie International Edition 52 (43), pp. 11410 - 11414 (2013)
  74. 74.
    Taschenberger, G.; Toloe, J.; Tereshchenko, J.; Akerboom, J.; Wales, P.; Benz, R.; Becker, S.; Outeiro, T. F.; Looger, L. L.; Bähr, M. et al.; Zweckstetter, M.; Kügler, S.: Beta-synuclein aggregates and induces neurodegeneration in dopaminergic neurons. Annals of Neurology (2013)
  75. 75.
    Bouter, I.; Dittrich, K.; Wittnam, J. L.; Rezaei-Ghaleh, N.; Pillot, T.; Papot-Coutourier, S.; Lefebvre, T.; Sprenger, F.; Wirths, O.; Zweckstetter, M. et al.; Bayer, T. A.: N-truncated amyloid beta (A beta) 4-42 forms stable aggregates and induces acute and long-lasting behavioral deficits. Acta Neuropathologica 126 (2), pp. 189 - 205 (2013)
  76. 76.
    Aggarwal, S.; Snaidero, N.; Pähler, G.; Frey, S.; Sanchez, P.; Zweckstetter, M.; Janshoff, A.; Schneider, A.; Weil, M. T.; Schaap, I. A. T. et al.; Görlich, D.; Simons, M.: Myelin membrane assembly is driven by a phase transition of myelin basic proteinsiInto a cohesive protein meshwork. PLoS Biology (2013)
  77. 77.
    Wagner, J.; Ryazanov, S.; Leonov, A.; Levin, J.; Shi, S.; Schmidt, F.; Prix, C.; Pan-Montojo, F.; Bertsch, U.; Mitteregger-Kretzschmar, G. et al.; Geissen, M.; Eiden, M.; Leidel, F.; Hirschberger, T.; Deeg, A. A.; Krauth, J.; Zinth, W.; Tavan, P.; Pilger, J.; Zweckstetter, M.; Frank, T.; Baehr, M.; Weishaupt, J. H.; Uhr, M.; Urlaub, H.; Teichmann, U.; Samwer, M.; Bötzel, K.; Groschup, M.; Kretzschmar, H.; Griesinger, C.; Giese, A.: Anle138b: a novel oligomer modulator for disease-modifying therapy of neurodegenerative diseases such as prion and Parkinson's disease. Acta Neuropathologica 125 (6), pp. 795 - 813 (2013)
  78. 78.
    Zweckstetter, M.: Conserved amyloid core structure of stop mutants of the human prion protein. Prion 7 (3), pp. 193 - 197 (2013)
  79. 79.
    Munari, F.; Rezaei-Ghaleh, N.; Xiang, S. Q.; Fischle, W.; Zweckstetter, M.: Structural plasticity in human heterochromatin protein 1 beta. PLoS One (2013)
  80. 80.
    Jaremko, M.; Jaremko, L.; Kim, H. Y.; Cho, M. K.; Schwieters, C. D.; Giller, K.; Becker, S.; Zweckstetter, M.: Cold denaturation of a protein dimer monitored at atomic resolution. Nature Chemical Biology 9 (4), pp. 264 - 270 (2013)
  81. 81.
    Jinwal, U. K.; Akoury, E.; Abisambra, J. F.; O'Leary, J. C.; Thompson, A. D.; Blair, L. J.; Jin, Y.; Bacon, J.; Nordhues, B. A.; Cockman, M. et al.; Zhang, J.; Li, P.; Zhang, B.; Borysov, S.; Uversky, V. N.; Biernat, J.; Mandelkow, E.; Gestwicki, J. E.; Zweckstetter, M.; Dickey, C. A.: Imbalance of Hsp70 family variants fosters tau accumulation. FASEB Journal 27 (4), pp. 1450 - 1459 (2013)
  82. 82.
    Akoury, E.; Pickardt, M.; Gajda, M. J.; Biernat, J.; Mandelkow, E.; Zweckstetter, M.: Mechanistic basis of phenothiazine-driven inhibition of Tau aggregation. Angewandte Chemie-International Edition 52 (12), pp. 3511 - 3515 (2013)
  83. 83.
    Xiang, S. Q.; Narayanan, R. L.; Becker, S.; Zweckstetter, M.: N-H spin-spin couplings: Probing hydrogen bonds in proteins. Angewandte Chemie-International Edition 52 (12), pp. 3525 - 3528 (2013)
  84. 84.
    Skora, L.; Fonseca, L.; Hofele, R. V.; Riedel, D.; Giller, K.; Watzlawik, J.; Schulz-Schaeffer, W. J.; Urlaub, H.; Becker, S.; Zweckstetter, M.: Burial of the polymorphic residue 129 in amyloid fibrils of prion stop mutants. Journal of Biological Chemistry (2013)
  85. 85.
    Akoury, E.; Gajda, M.; Pickhardt, M.; Biernat, J.; Pornsuwan, S.; Griesinger, C.; Mandelkow, E.; Zweckstetter, M.: Inhibition of tau filament formation by conformational modulation. Journal of the American Chemical Society 135 (7), pp. 2853 - 2862 (2013)
  86. 86.
    Skora, L.; Zweckstetter, M.: Determination of amyloid core structure using chemical shifts. Protein Science 21 (12), pp. 1948 - 1953 (2012)
  87. 87.
    Kroth, H.; Ansaloni, A.; Varisco, Y.; Jan, A.; Sreenivasachary, N.; Rezaei-Ghaleh, N.; Giriens, V.; Lohmann, S.; López-Deber, M. P.; Adolfsson, O. et al.; Pihlgren, M.; Paganetti, P.; Froestl, W.; Nagel-Steger, L.; Willbold, D.; Schrader, T.; Zweckstetter, M.; Pfeifer, A.; Lashuel, H. A.; Muhs, A.: Discovery and structure activity relationship of small molecule inhibitors of toxic β-amyloid-42 fibril formation. Journal of Biological Chemistry 287 (41), pp. 34786 - 34800 (2012)
  88. 88.
    Munari, F.; Soeroes, S.; Zenn, H. M.; Schomburg, A.; Kost, N.; Schröder, S.; Klingberg, R.; Rezaei-Ghaleh, N.; Stützer, A.; Gelato, K. A. et al.; Walla, P. J.; Becker, S.; Schwarzer, D.; Zimmermann, B.; Fischle, W.; Zweckstetter, M.: Methylation of K9 in histone H3 directs alternative modes of highly dynamic interaction of heterochromatin protein hHP1β with the nucleosome. Journal of Biological Chemistry 287 (40), pp. 33756 - 33765 (2012)
  89. 89.
    El-Turk, F.; Fauvet, B.; Ashrafi, A.; Ouertatani-Sakouhi, H.; Cho, M. K.; Neri, M.; Cascella, M.; Rothlisberger, U.; Pojer, F.; Zweckstetter, M. et al.; Lashuel, H.: Characterization of molecular determinants of the conformational stability of macrophage migration inhibitory factor: Leucine 46 hydrophobic pocket. PLoS One (2012)
  90. 90.
    Zachariae, U.; Schneider, R.; Briones, R.; Gattin, Z.; Demers, J. P.; Giller, K.; Maier, E.; Zweckstetter, M.; Griesinger, C.; Becker, S. et al.; Benz, R.; de Groot, B. L.; Lange, A.: Beta-barrel mobility underlies closure of the voltage-dependent anion channel. Structure 20 (9), pp. 1540 - 1549 (2012)
  91. 91.
    Cho, M. K.; Xiang , S.; Kim, H. Y.; Becker, S.; Zweckstetter, M.: Cold-induced changes in the protein ubiquitin. PLoS One (2012)
  92. 92.
    Petroi, D.; Popova, B.; Taheri-Talesh, N.; Irniger, S.; Shapasandzadeh, H.; Zweckstetter, M.; Outeiro, T. F.; Braus, G. H.: Aggregate clearance of α-synuclein in Saccharomyces cerevisiae depends more on autophagosome and vacuole function than on the proteasome. Journal of Biological Chemistry (2012)
  93. 93.
    Rezaei-Ghaleh, N.; Blackledge, M.; Zweckstetter, M.: Intrinsically disordered proteins: from sequence and conformational properties toward drug discovery. ChemBioChem 13 (7), pp. 930 - 950 (2012)
  94. 94.
    Taschenberger, G.; Garrido, M.; Tereshchenko, Y.; Baehr, M.; Zweckstetter, M.; Kuegler, S.: Aggregation of alpha Synuclein promotes progressive in vivo neurotoxicity in adult rat dopaminergic neurons. Acta Neuropathologica 123 (5), pp. 671 - 683 (2012)
  95. 95.
    Berger, R.; Courtieu, J.; Gil, R. R.; Griesinger, C.; Köck, M.; Lesot, P.; Luy, B.; Merlet, D.; Navarro-Vazquez, A.; Reggelin, M. et al.; Reinscheid, U. M.; Thiele, C. M.; Zweckstetter, M.: Is enantiomer assignment possible by NMR spectroscopy using residual dipolar couplings from chiral nonracemic alignment media?—A critical assessment. Angewandte Chemie International Edition 51 (33), pp. 8388 - 8391 (2012)
  96. 96.
    Daebel, V.; Chinnathambi, S.; Biernat, J.; Schwalbe, M.; Habenstein, B.; Loquet, A.; Akoury, E.; Tepper, K.; Mueller, H.; Baldus, M. et al.; Griesinger, C.; Zweckstetter, M.; Mandelkow, E.; Vijayan, V.; Lange, A.: β-sheet core of Tau paired helical filaments revealed by solid-state NMR. Journal of the American Chemical Society 134 (34), pp. 13982 - 13989 (2012)
  97. 97.
    Ozenne, V.; Schneider, R.; Yao, M.; Huang, J.-R.; Salmon, L.; Zweckstetter, M.; Jensen, M. R.; Blackledge, M.: Mapping the potential energy landscape of intrinsically disordered proteins at amino acid resolution. Journal of the American Chemical Society 134 (36), pp. 15138 - 15148 (2012)
  98. 98.
    Bibow, S.; Ozenne, V.; Biernat, J.; Blackledge, M.; Mandelkow, E.; Zweckstetter, M.: Structural impact of proline-directed pseudophosphorylation at AT8, AT100, and PHF1 epitopes on 441-residue tau. Journal of the American Chemical Society 133 (40), pp. 15842 - 15845 (2011)
  99. 99.
    Lamberto, C. R.; Torres-Monserrat, V.; Bertoncini, C. W.; Salvatella, X.; Zweckstetter, M.; Griesinger, C.; Fernandez, C. O.: Toward the discovery of effective polycyclic inhibitors of alpha-Synuclein amyloid assembly. Journal of Biological Chemistry 286 (37), pp. 32036 - 32044 (2011)
 
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