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)

Pogoryelov, D.; Krah, A.; Langer, J. D.; Yildiz, Ö.; Faraldo-Gómez, J. D.; Meier, T.: Microscopic rotary mechanism of ion translocation in the F_o complex of ATP synthases. Nature Chemical Biology 6, S. 891 - 899 (2010)

Hoffmann, J.; Sokolova, L.; Preiss, L.; Hicks, D. B.; Krulwich, T. A.; Morgner, N.; Wittig, I.; Schägger, H.; Meier, T.; Brutschy, B.: ATP synthases: cellular nanomotors characterized by LILBID mass spectrometry. Physical Chemistry Chemical Physics 12 (41), S. 13375 - 13382 (2010)

Preiss, L.; Yildiz, Ö.; Hicks, D. B.; Krulwich, T. A.; Meier, T.: A New Type of Proton Coordination in an F₁F_o-ATP Synthase Rotor Ring. PLoS Biology 8 (8), e1000443 (2010)

Krah, A.; Pogoryelov, D.; Langer, J. D.; Bond, P. J.; Meier, T.; Faraldo-Gómez, J. D.: Structural and energetic basis for H⁺ versus Na⁺ binding selectivity in ATP synthase F_o rotors. Biochimica et Biophysica Acta: BBA 1797, S. 763 - 772 (2010)

Krah, A.; Pogoryelov, D.; Meier, T.; Faraldo-Gómez, J. D.: On the Structure of the Proton-Binding Site in the F_o Rotor of Chloroplast ATP Synthases. Journal of Molecular Biology 395, S. 20 - 27 (2010)

Pogoryelov, D.; Yildiz, Ö.; Faraldo-Gómez, J. D.; Meier, T.: High-resolution structure of the rotor ring of a proton-dependent ATP synthase. Nature Structural and Molecular Biology 16 (10), S. 1068 - 1073 (2009)

Meier, T.; Krah, A.; Bond, P. J.; Pogoryelov, D.; Diederichs, K.; Faraldo-Gómez, J. D.: Complete Ion-Coordination Structure in the Rotor Ring of Na⁺-Dependent F-ATP Synthases. Journal of Molecular Biology 391 (2), S. 498 - 507 (2009)

Matthies, D.; Preiss, L.; Klyszejko, A. L.; Muller, D. J.; Cook, G. M.; Vonck, J.; Meier, T.: The c₁₃ Ring from a Thermoalkaliphilic ATP Synthase Reveals an Extended Diameter Due to a Special Structural Region. Journal of Molecular Biology 388 (3), S. 611 - 618 (2009)

Morgner, N.; Hoffmann, J.; Barth, H.-D.; Meier, T.; Brutschy, B.: LILBID-mass spectrometry applied to the mass analysis of RNA polymerase II and an F₁F_o-ATP synthase. International Journal of Mass Spectrometry 277 (1-3), S. 309 - 313 (2008)

Pogoryelov, D.; Nikolaev, Y.; Schlattner, U.; Pervushin, K.; Dimroth, P.; Meier, T.: Probing the rotor subunit interface of the ATP synthase from Ilyobacter tartaricus. The FEBS Journal 275 (19), S. 4850 - 4862 (2008)

Fritz, M.; Klyszeijko, A. L.; Morgner, N.; Vonck, J.; Brutschy, B.; Muller, D. J.; Meier, T.; Müller, V.: An intermediate step in the evolution of ATPases - a hybrid F₀–V₀ rotor in a bacterial Na⁺ F₁F₀ ATP synthase. The FEBS Journal 275 (9), S. 1999 - 2007 (2008)

Meier, T.; Morgner, N.; Matthies, D.; Pogoryelov, D.; Keis, S.; Cook, G. M.; Dimroth, P.; Brutschy, B.: A tridecameric c ring of the adenosine triphosphate (ATP) synthase from the thermoalkaliphilic Bacillus sp. strain TA2.A1 facilitates ATP synthesis at low electrochemical proton potential. Molecular Microbiology 65 (5), S. 1181 - 1192 (2007)

Pogoryelov, D.; Reichen, C.; Klyszejko, A. L.; Brunisholz, R.; Muller, D. J.; Dimroth, P.; Meier, T.: The oligomeric state of c rings from cyanobacterial F-ATP synthases varies from 13 to 15. Journal of Bacteriology 189 (16), S. 5895 - 5902 (2007)

Pogoryelov, D.; Yu, J.; Meier, T.; Vonck, J.; Dimroth, P.; Muller, D. J.: The c₁₅ ring of the Spirulina platensis F-ATP synthase: F₁/F₀ symmetry mismatch is not obligatory. EMBO Reports 6 (11), S. 1040 - 1044 (2005)

Vonck, J.; von Nidda, T. K.; Meier, T.; Matthey, U.; Mills, D. J.; Kühlbrandt, W.; Dimroth, P.: Molecular architecture of the undecameric rotor of a bacterial Na⁺-ATP synthase. Journal of Molecular Biology 321 (2), S. 307 - 316 (2002)

Krasnoselska, G. O.; Meier, T.: Purification and Reconstitution of Ilyobacter tartaricus ATP Synthase. In: Springer Protocols: Methods in Molecular Biology: Molecular Motors, Bd. 2881, S. 65 - 86 (Hg. Lavelle, C.; Le Gall , A.) (2025)

Krasnoselska, G. O.; Meier, T.: Purification and Reconstitution of Ilyobacter tartaricus ATP Synthase. In: Methods in Molecular Biology (MIMB), Bd. 1805, S. 51 - 71 (Hg. Lavelle, C.). Humana Press, New York (2018)

Meier, T.; Pogoryelov, D.: ATP Synthase Structure. In: Encyclopedia of Biophysics, S. 129 - 134 (Hg. Roberts, G.). Springer, Berlin, Heidelberg/Germany [et al.] (2013)

Meier, T.; Faraldo-Gómez, J. D.; Börsch, M.: ATP-Synthase - A Paradigmatic Molecular Machine. In: Molecular Machines in Biology, Chapter 11, S. 208 - 238 (Hg. Frank, J.). Cambridge University Press, New York (2011)

Hammann, E.; Zappe, A.; Keis, S.; Ernst, S.; Matthies, D.; Meier, T.; Cook, G. M.; Börsch, M.: Step size of the rotary proton motor in single F_oF₁-ATP synthase from a thermoalkaliphilic bacterium by DCO-ALEX FRET. In: Proceedings of the SPIE, Bd. 8228. Proceedings of SPIE; 8228 : Single Molecule Spectroscopy and Superresolution Imaging V, 13 February 2012. (2012)