Adolph, C.; Cheung, C.-Y.; McNeil, M. B.; Jowsey, W. J.; Williams, Z. C.; Hards, K.; Harold, L. K.; Aboelela, A.; Bujaroski, R. S.; Buckley, B. J.et al.; Tyndall, J. D. A.; Li, Z.; Langer, J. D.; Preiss, L.; Meier, T.; Steyn, A. J. C.; Rhee, K. Y.; Berney, M.; Kelso, M. J.; Cook, G. M.: A dual-targeting succinate dehydrogenase and F1Fo-ATP synthase inhibitor rapidly sterilizes replicating and non-replicating Mycobacterium tuberculosis. Cell Chemical Biology 31, pp. 683 - 698.e7 (2024)
Meier-Credo, J.; Preiss, L.; Wüllenweber, I.; Resemann, A.; Nordmann, C.; Zabret, J.; Suckau, D.; Michel, H.; Nowacyk, M. M.; Meier, T.et al.; Langer, J. D.: Top-Down Identification and Sequence Analysis of Small Membrane Proteins Using MALDI-MS/MS. Journal of the American Society for Mass Spectrometry 33 (7), pp. 1293 - 1302 (2022)
Hards, K.; Cheung, C.-Y.; Waller, N.; Adolph, C.; Keighley, L.; Tee, Z. S.; Harold, L. K.; Menorca, A.; Bujaroski, R. S.; Buckley, B. J.et al.; Tyndall, J. D.A.; McNeil, M. B.; Rhee, K. Y.; Opel-Reading, H. K.; Krause, K.; Preiss, L.; Langer, J. D.; Meier, T.; Hasenoehrl, E. J.; Berney, M.; Kelso, M. J.; Cook, G. M.: An amiloride derivative is active against the F1Fo-ATP synthase and cytochrome bd oxidase of Mycobacterium tuberculosis. Communications Biology 5 (1), 166 (2022)
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), pp. 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 Fo rotor ring in complex with the anti-TB drug bedaquiline. Science Advances 1 (4), pp. 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), pp. 973 - 984 (2014)
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), pp. 7874 - 7879 (2013)
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), pp. 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), pp. 5497 - 5506 (2011)
Preiss, L.; Yildiz, Ö.; Hicks, D. B.; Krulwich, T. A.; Meier, T.: A New Type of Proton Coordination in an F1Fo-ATP Synthase Rotor Ring. PLoS Biology 8 (8), e1000443 (2010)
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), pp. 611 - 618 (2009)
Preiß, L.: Structural and functional characterization of the rotor rings from a Bacillus and a Mycobacterium F1F0 ATP synthase. Dissertation, 219 pp., Goethe-Universität, Frankfurt am Main (2014)
Preiß, L.: Strukturuntersuchungen an c - Ringen der ATP-Synthase aus alkaliphilen Bakterien. Diploma, Johann Wolfgang Goethe-Universität, Frankfurt am Main (2009)
Researchers at the Max Planck Institute of Biophysics and the University of Cologne developed a new optical tool to study ferroptosis, a form of iron-driven cell death. Better understanding of how it spreads could open doors to new therapies.
On February 5, 2024, we participated in the “Frankfurt Stands Up for Democracy” demonstration, standing alongside nearly 20,000 participants representing over 100 institutions, organizations, and companies across the Frankfurt region.
The Max Planck Institute of Biophysics is part of the new science network Frankfurt Alliance together with 15 other research institutions in the Rhine-Main metropolitan area
The fellow program promotes cooperation between Max Planck Institutes and outstanding professors at universities. From March 2024, Müller-McNicoll will lead a small research group at the MPI in Frankfurt for five years to investigate RNA, the carrier of genetic information in the cell, and its regulation.