Publikationen von Thomas Meier

Blum, T.; Hahn, A.; Meier, T.; Davies, K. M.; Kühlbrandt, W.: Dimers of mitochondrial ATP synthase induce membrane curvature and self-assemble into rows. Proceedings of the National Academy of Sciences of the United States of America 116 (10), S. 4250 - 4255 (2019)

Eisel, B.; Hartrampf, F. W. W.; Meier, T.; Trauner, D.: Reversible Optical Control of F₁F₀-ATP Synthase Using Photoswitchable Inhibitors. FEBS Letters 592 (3), S. 343 - 355 (2018)

Hahn, A.; Vonck, J.; Mills, D. J.; Meier, T.; Kühlbrandt, W.: Structure, mechanism, and regulation of the chloroplast ATP synthase. Science 360 (6389), S. 1 - 10 (2018)

He, C.; Preiss, L.; Wang, B.; Fu, L.; Wen, H.; Zhang, X.; Cui, H.; Meier, T.; Yin, D.: Structural Simplification of Bedaquiline: the Discovery of 3-(4-(N,N-Dimethylaminomethyl)phenyl)quinoline-Derived Antitubercular Lead Compounds. ChemMedChem 12, S. 106 - 119 (2017)

Schulz, S.; Wilkes, M.; Mills, D. J.; Kühlbrandt, W.; Meier, T.: Molecular architecture of the N‐type ATPase rotor ring from Burkholderia pseudomallei. EMBO Reports 18 (6), S. 1 - 10 (2017)

Leone, V.; Pogoryelov, D.; Meier, T.; Faraldo-Gómez, J. D.: On the principle of ion selectivity in Na⁺/H⁺-coupled membrane proteins: Experimental and theoretical studies of an ATP synthase rotor. Proceedings of the National Academy of Sciences of the United States of America 112 (10), S. E1057 - E1066 (2015)

Preiss, L.; Hicks, D. B.; Suzuki, S.; Meier, T.; Krulwich, T. A.: Alkaliphilic bacteria with impact on industrial applications, concepts of early life forms, and bioenergetics of ATP synthesis. Frontiers in Bioengineering and Biotechnology 3 (75), S. 1 - 16 (2015)

Preiss, L.; Langer, J. D.; Yildiz, Ö.; Eckhardt-Strelau, L.; Guillemont, J. E. G.; Koul, A.; Meier, T.: Structure of the mycobacterial ATP synthase F_o rotor ring in complex with the anti-TB drug bedaquiline. Science Advances 1 (4), S. 1 - 8 (2015)

Preiss, L.; Langer, J. D.; Hicks, D. B.; Liu, J.; Yildiz, Ö.; Krulwich, T. A.; Meier, T.: The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic lifestyle. Molecular Microbiology 92 (5), S. 973 - 984 (2014)

Matthies, D.; Zhou, W.; Klyszejko, A. L.; Anselmi, C.; Yildiz, Ö.; Brandt, K.; Müller, V.; Faraldo-Gómez, J. D.; Faraldo-Gómez, J. D.; Meier, T.: High-resolution structure and mechanism of an F/V-hybrid rotor ring in a Na⁺-coupled ATP synthase. Nature Communications 5, 5286 (2014)

Halang, P.; Leptihn, S.; Meier, T.; Vorburger, T.; Steuber, J.: The function of the Na⁺-driven flagellum of Vibrio cholerae is determined by osmolality and pH. Journal of Bacteriology 195 (21), S. 4888 - 4899 (2013)

Schulz, S.; Iglesias-Cans, M.; Krah, A.; Yildiz, Ö.; Leone, V.; Matthies, D.; Cook, G. M.; Faraldo-Gómez, J. D.; Meier, T.: A New Type of Na⁺-Driven ATP Synthase Membrane Rotor with a Two-Carboxylate Ion-Coupling Motif. PLoS Biology 11 (6), e1001596, S. 1 - 12 (2013)

Preiss, L.; Klyszejko, A. L.; Hicks, D. B.; Liu, J.; Fackelmayer, O. J.; Yildiz, Ö.; Krulwich, T. A.; Meier, T.: The c-ring stoichiometry of ATP synthase is adapted to cell physiological requirements of alkaliphilic Bacillus pseudofirmus OF4. Proceedings of the National Academy of Sciences of the United States of America 110 (19), S. 7874 - 7879 (2013)

Hakulinen, J. K.; Klyszejko, A. L.; Hoffmann, J.; Eckardt-Strelau, L.; Brutschy, B.; Vonck, J.; Meier, T.: Structural study on the architecture of the bacterial ATP synthase F₀ motor. Proceedings of the National Academy of Sciences of the United States of America 109 (30), S. E2050 - E2056 (2012)

Pogoryelov, D.; Klyszejko, A.; Krasnoselska, G. O.; Heller, E.-M.; Leone, V.; Langer, J. D.; Vonck, J.; Müller, D. J.; Faraldo-Gómez, J. D.; Meier, T.: Engineering rotor ring stoichiometries in the ATP synthase. Proceedings of the National Academy of Sciences of the United States of America 109 (25), S. E1599 - E1608 (2012)

Symersky, J.; Pagadala, V.; Osowski, D.; Krah, A.; Meier, T.; Faraldo-Gómez, J. D.; Mueller, D. M.: Structure of the c₁₀ ring of the yeast mitochondrial ATP synthase in the open conformation. Nature Structural and Molecular Biology 19, S. 485 - 491 (2012)

McMillan, D. G. G.; Ferguson, S. A.; Dey, D.; Schröder, K.; Aung, H. L.; Carbone, V.; Attwood, G. T.; Ronimus, R. S.; Meier, T.; Janssen, P. H. et al.; Cook, G. M.: A₁A_o-ATP Synthase of Methanobrevibacter ruminantium Couples Sodium Ions for ATP Synthesis under Physiological Conditions. The Journal of Biological Chemistry 286 (46), S. 39882 - 39892 (2011)

Matthies, D.; Haberstock, S.; Joos, F.; Dötsch, V.; Vonck, J.; Bernhard, F.; Meier, T.: Cell-Free Expression and Assembly of ATP Synthase. Journal of Molecular Biology 413, S. 593 - 603 (2011)

Kalamorz, F.; Keis, S.; McMillan, D. G. G.; Olsson, K.; Stanton, J.-A.; Stockwell, P.; Black, M. A.; Klingeman, D. M.; Land, M. L.; Han, C. S. et al.; Martin, S. L.; Becher, S. A.; Peddie, C. J.; Morgan, H. W.; Matthies, D.; Preiß, L.; Meier, T.; Brown, S. D.; Cook, G. M.: Draft Genome Sequence of the Thermoalkaliphilic Caldalkalibacillus thermarum Strain TA2.A1. Journal of Bacteriology 193 (16), S. 4290 - 4291 (2011)

Liu, J.; Fackelmayer, O. J.; Hicks, D. B.; Preiß, L.; Meier, T.; Sobie, E. A.; Krulwich, T. A.: Mutations in a Helix-1 Motif of the ATP Synthase c-Subunit of Bacillus pseudofirmus OF4 Cause Functional Deficits and Changes in the c-Ring Stability and Mobility on Sodium Dodecyl Sulfate–Polyacrylamide Gel Electrophoresis. Biochemistry 50 (24), S. 5497 - 5506 (2011)