Grund, T. N.; Kabashima, Y.; Kusumoto, T.; Wu, D.; Welsch, S.; Sakamoto, J.; Michel, H.; Safarian, S.: The cryoEM structure of cytochrome bd from C. glutamicum provides novel insights into structural properties of actinobacterial terminal oxidases. Frontiers in Chemistry (2023)
Zhao, J.; Xie, H.; Mehdipour, A. R.; Safarian, S.; Ermler, U.; Münke, C.; Thielmann, Y.; Hummer, G.; Ebersberger, I.; Wang, J.et al.; Michel, H.: The structure of the Aquifex aeolicus MATE family multidrug resistance transporter and sequence comparisons suggest the existence of a new subfamily. Proceedings of the National Academy of Sciences of the United States of America 118 (46), e2107335118 (2021)
Safarian, S.; Opel-Reading, H. K.; Wu, D.; Mehdipour, A. R.; Hards, K.; Harold, L. H.; Radloff, M.; Stewart, I.; Welsch, S.; Hummer, G.et al.; Cook, G. M.; Krause, K. L.; Michel, H.: The cryo-EM structure of the bd oxidase from M. tuberculosis reveals a unique structural framework and enables rational drug design to combat TB. Nature Communications 12 (1), 5236 (2021)
Wu, D.; Grund, T. N.; Welsch, S.; Mills, D.; Michel, M.; Safarian, S.; Michel, H.: Structural basis for amino acid exchange by a human heteromeric amino acid transporter. Proceedings of the National Academy of Sciences of the United States of America 117 (35), 202008111, pp. 21281 - 21287 (2020)
Elamri, I.; Radloff, M.; Hohmann, K. F.; Nimbarte, V. D.; Nasiri, H. R.; Bolte, M.; Safarian, S.; Michel, H.; Schwalbe, H.: Synthesis and Biological Screening of new Lawson Derivatives as selective substrate‐based Inhibitors of Cytochrome bo3 Ubiquinol Oxidase from Escherichia coli. ChemMedChem 15 (14), pp. 1262 - 1271 (2020)
Safarian, S.: Structural insights into cytochrome bd-type oxygen reductases. Dissertation, 176 pp., Fachbereich Biochemie, Chemie, Pharmazie, Johann Wolfgang Goethe-Universität Frankfurt, Frankfurt am Main (2017)
Safarian, S.: Lipid based techniques for reconstitution and biophysical investigations of membrane proteins. Master, 89 pp., Goethe University, Frankfurt am Main, Germany (2012)
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.