Publikationen von M. Zweckstetter

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), S. 16059 - 16067 (2016)

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), S. 8685 - 8693 (2016)

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), S. 1010 - 1020 (2016)

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 4, 39 (2016)

Rezaei-Ghaleh, N.; Amininasab, M.; Kumar, S.; Walter , J.; Zweckstetter, M.: Phosphorylation modifies the molecular stability of beta-amyloid deposits. Nature Communications 7, 11359 (2016)

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), S. 585 - 594 (2016)

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), S. 79 - 83 (2016)

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), S. 525 - 537 (2016)

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), S. 275 - 290 (2016)

Ambadipudi, S.; Zweckstetter, M.: Targeting intrinsically disordered proteins in rational drug discovery. Expert Opinion on Drug Discocery 11 (1), S. 65 - 77 (2016)

Wysoczanski, P.; Zweckstetter, M.: Retention and splicing complex (RES) - the importance of cooperativity. RNA Biology 13 (2), S. 128 - 133 (2016)

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 290 (46), S. 27582 - 27593 (2015)

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), S. 5513 - 5524 (2015)

Jaremko, L.; Jaremko, M.; Giller, K.; Becker, S.; Zweckstetter, M.: Conformational flexibility in the transmembrane protein TSPO. Chemistry-A European Journal 21 (46), S. 16555 - 16563 (2015)

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), S. 299 - 307 (2015)

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), S. 10347 - 10351 (2015)

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), S. 1448 - 1458 (2015)

Jaremko, M.; Jaremko, L.; Jaipuria, G.; Becker, S.; Zweckstetter, M.: Structure of the mammalian TSPO/PBR protein. Biochemical Society Transactions 43 (4), S. 566 - 571 (2015)

Wysoczanski, P.; Becker, S.; Zweckstetter, M.: Structures of intermediates during RES complex assembly. Scientific Reports 5, 12545 (2015)

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), S. 3971 - 3981 (2015)