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Dr. Patrick Scheerer

Research interests

  • elucidating molecular details and mechanisms of signal transduction processes in membrane proteins (G protein-coupled receptors, ion channels), signal transduction-related proteins (G proteins, arrestins, phosphodiesterases), photoreceptors (phytochromes, opsins, photolyases) and metalloenzymes ([NiFe]-hydrogenases)
     
  • molecular biology/protein large-scale production methods, biophysical assays (e.g. MST/nanoDSF/Nanodiscs/SMALPs), conventional and LCP crystallization, Nanobodies screening and production, cell-based signaling assays
     
  • protein X-ray crystallography, cryo-electron microscopy, free-electron laser techniques, time-resolved structural biology

Research Units in UniSysCat

Research Unit B
Research Unit C
Research Unit E

Dr. Patrick Scheerer
Charité – Universitätsmedizin
Institute of Medical Physics and Biophysics
Group Structural Biology of Cellular Signaling
Protein X-ray Crystallography - Cryo-Electron Microscopy - Signal Transduction
Charitéplatz 1
10117 Berlin
+49 (0)30 450 524 178
+49 (0)30 450 524 952
patrick.scheerer(at)charite.de
https://biophysik.charite.de/scheerer

 

List of UniSysCat Publications

UniSysCat Publications

  • Expanding the scope of resonance Raman spectroscopy in hydrogenase research: New observable states and reporter vibrations, C. C. M. Bernitzky, G. Caserta, S. Frielingsdorf, J. Schoknecht, A. Schmidt, P. Scheerer, O. Lenz, P. Hildebrandt, C. Lorent, I. Zebger, M. Horch, Journal of Inorganic Biochemistry 2025, 262, 112741–0, 10.1016/j.jinorgbio.2024.112741
  • ISG15 blocks cardiac glycolysis and ensures sufficient mitochondrial energy production during Coxsackievirus B3 infection, C. Bredow, F. Thery, E. K. Wirth, S. Ochs, M. Kespohl, G. Kleinau, N. Kelm, N. Gimber, J. Schmoranzer, M. Voss, K. Klingel, J. Spranger, K. Renko, M. Ralser, M. Mülleder, A. Heuser, K. P. Knobeloch, P. Scheerer, J. Kirwan, U. Brüning, N. Berndt, F. Impens, A. Beling, Cardiovascular Research 2024, 1–14, 10.1093/cvr/cvae026
  • Mechanisms of thyrotropin receptor–mediated phenotype variability deciphered by gene mutations and M453T-knockin model, K. Makkonen, M. Jännäri, L. Crisóstomo, M. Kuusi, K. Patyra, V. Melnyk, V. Linnossuo, J. Ojala, R. Ravi, C. Löf, J. A. Mäkelä, P. Miettinen, S. Laakso, M. Ojaniemi, J. Jääskeläinen, M. Laakso, F. Bossowski, B. Sawicka, K. Stożek, A. Bossowski, G. Kleinau, P. Scheerer, FinnGen, M. P. Reeve, J. Kero, JCI Insight 2024, 9, 22–0, 10.1172/jci.insight.167092
  • Mechanistic insights into G-protein coupling with an agonist-bound G-protein-coupled receptor, H. Batebi, G. Pérez-Hernández, S. N. Rahman, B. Lan, A. Kamprad, M. Shi, D. Speck, J. K. S. Tiemann, R. Guixà-González, F. Reinhardt, P. F. Stadler, M. M. Papasergi-Scott, G. Skiniotis, P. Scheerer, B. K. Kobilka, J. M. Mathiesen, X. Liu, P. W. Hildebrand, Nature structural & molecular biology 2024, 10.1038/s41594-024-01334-2
  • Are Melanocortin Receptors Present in Extant Protochordates?, R. L. Ji, S. S. Jiang, G. Kleinau, P. Scheerer, Y. X. Tao, Biomolecules 2024, 14, 1120–0, 10.3390/biom14091120
  • Simultaneous spectral illumination of microplates for high-throughput optogenetics and photobiology, A. Vogt, R. Paulat, D. Parthier, V. Just, M. Szczepek, P. Scheerer, Q. Xu, A. Möglich, D. Schmitz, B. R. Rost, N. Wenger, Biological Chemistry 2024, 10.1515/hsz-2023-0205
  • Cryo-EM captures early ribosome assembly in action, B. Qin, S. M. Lauer, A. Balke, C. H. Vieira-Vieira, J. Bürger, T. Mielke, M. Selbach, P. Scheerer, C. M. T. Spahn, R. Nikolay, Nature Communications 2023, 14, 1–10, 10.1038/s41467-023-36607-9
  • Structure of the actively translating plant 80S ribosome at 2.2 Å resolution, J. Smirnova, J. Loerke, G. Kleinau, A. Schmidt, J. Bürger, E. H. Meyer, T. Mielke, P. Scheerer, R. Bock, C. M. T. Spahn, R. Zoschke, Nature Plants 2023, 9, 987–1000, 10.1038/s41477-023-01407-y
  • Time‐resolved fluorescence anisotropy with Atto 488‐labeled phytochrome Agp1 from, A. Elkurdi, G. Guigas, L. Hourani‐Alsharafat, P. Scheerer, G. U. Nienhaus, N. Krauß, T. Lamparter, Photochemistry and Photobiology 2023, 1–12, 10.1111/php.13851
  • Stepwise conversion of the Cys [4Fe-3S] to a Cys [4Fe-4S] cluster and its impact on oxygen tolerance of [NiFe]-hydrogenase, A. Schmidt, J. Kalms, C. Lorent, S. Katz, S. Frielingsdorf, R. M. Evans, J. Fritsch, E. Siebert, C. Teutloff, F. A. Armstrong, I. Zebger, O. Lenz, P. Scheerer, Chemical Science 2023, 10.1039/D3SC03739H
  • Intramolecular activity regulation of adhesion GPCRs in light of recent structural and evolutionary information, G. Kleinau, A. H. Ali, F. Wiechert, M. Szczepek, A. Schmidt, C. M. T. Spahn, I. Liebscher, T. Schöneberg, P. Scheerer, Pharmacological Research 2023, 197, 106971–0, 10.1016/j.phrs.2023.106971
  • Is the Neuropeptide PEN a Ligand of GPR83?, Y. Giesecke, V. Asimi, V. Stulberg, G. Kleinau, P. Scheerer, B. Koksch, C. Grötzinger, International Journal of Molecular Sciences 2023, 24, 15117–0, 10.3390/ijms242015117
  • Phytochrome-Interacting Proteins, G. Kaeser, N. Krauß, C. Roughan, L. Sauthof, P. Scheerer, T. Lamparter, Biomolecules 2023, 14, 9–0, 10.3390/biom14010009
  • Ultrafast proton-coupled isomerization in the phototransformation of phytochrome, Y. Yang, T. Stensitzki, L. Sauthof, A. Schmidt, P. Piwowarski, F. Velazquez Escobar, N. Michael, A. D. Nguyen, M. Szczepek, F. N. Brünig, R. R. Netz, M. A. Mroginski, S. Adam, F. Bartl, I. Schapiro, P. Hildebrandt, P. Scheerer, K. Heyne, Nature Chemistry 2022, 14, 823–830, 10.1038/s41557-022-00944-x
  • Expression and Characterization of Relaxin Family Peptide Receptor 1 Variants, D. Speck, G. Kleinau, M. Meininghaus, A. Erbe, A. Einfeldt, M. Szczepek, P. Scheerer, V. Pütter, Frontiers in Pharmacology 2022, 12, 10.3389/fphar.2021.826112
  • A cytosolic disulfide bridge‐supported dimerization is crucial for stability and cellular distribution of Coxsackievirus B3 protein 3A, M. Voss, G. Kleinau, N. Gimber, K. Janek, C. Bredow, F. Thery, F. Impens, J. Schmoranzer, P. Scheerer, P. Kloetzel, A. Beling, The FEBS Journal 2022, 289, 3826–3838, 10.1111/febs.16368
  • Functional modulation of PTH1R activation and signaling by RAMP2, K. Nemec, H. Schihada, G. Kleinau, U. Zabel, E. O. Grushevskyi, P. Scheerer, M. J. Lohse, I. Maiellaro, Proceedings of the National Academy of Sciences 2022, 119, 1–12, 10.1073/pnas.2122037119
  • Resonance Raman spectroscopic analysis of the iron–sulfur cluster redox chain of the membrane‐bound [NiFe]‐hydrogenase, E. Siebert, A. Schmidt, S. Frielingsdorf, J. Kalms, U. Kuhlmann, O. Lenz, P. Scheerer, I. Zebger, P. Hildebrandt, Journal of Raman Spectroscopy 2021, 10.1002/jrs.6163
  • Local Electric Field Changes during the Photoconversion of the Bathy Phytochrome Agp2, A. Kraskov, J. von Sass, A. D. Nguyen, T. O. Hoang, D. Buhrke, S. Katz, N. Michael, J. Kozuch, I. Zebger, F. Siebert, P. Scheerer, M. A. Mroginski, N. Budisa, P. Hildebrandt, Biochemistry 2021, 60, 2967–2977, 10.1021/acs.biochem.1c00426
  • Structures of active melanocortin-4 receptor–Gs-protein complexes with NDP-α-MSH and setmelanotide, N. A. Heyder, G. Kleinau, D. Speck, A. Schmidt, S. Paisdzior, M. Szczepek, B. Bauer, A. Koch, M. Gallandi, D. Kwiatkowski, J. Bürger, T. Mielke, A. G. Beck-Sickinger, P. W. Hildebrand, C. M. T. Spahn, D. Hilger, M. Schacherl, H. Biebermann, T. Hilal, P. Kühnen, B. K. Kobilka, P. Scheerer, Cell Research 2021, 31, 1176–1189, 10.1038/s41422-021-00569-8
  • Phytochromes in Agrobacterium fabrum, T. Lamparter, P. Xue, A. Elkurdi, G. Kaeser, L. Sauthof, P. Scheerer, N. Krauß, Frontiers in Plant Science 2021, 12, 1–14, 10.3389/fpls.2021.642801
  • MicroRNA-100-5p and microRNA-298-5p released from apoptotic cortical neurons are endogenous Toll-like receptor 7/8 ligands that contribute to neurodegeneration, T. Wallach, Z. J. Mossmann, M. Szczepek, M. Wetzel, R. Machado, M. Raden, M. Miladi, G. Kleinau, C. Krüger, P. Dembny, D. Adler, Y. Zhai, V. Kumbol, O. Dzaye, J. Schüler, M. Futschik, R. Backofen, P. Scheerer, S. Lehnardt, Molecular Neurodegeneration 2021, 16, 1–24, 10.1186/s13024-021-00498-5
  • Functional differences between TSHR alleles associate with variation in spawning season in Atlantic herring, J. Chen, H. Bi, M. E. Pettersson, D. X. Sato, A. P. Fuentes-Pardo, C. Mo, S. Younis, O. Wallerman, P. Jern, G. Molés, A. Gómez, G. Kleinau, P. Scheerer, L. Andersson, Communications Biology 2021, 4, 1–13, 10.1038/s42003-021-02307-7
  • Phytochrome Mediated Responses in Agrobacterium fabrum: Growth, Motility and Plant Infection, P. Xue, Y. Bai, G. Rottwinkel, E. Averbukh, Y. Ma, T. Roeder, P. Scheerer, N. Krauß, T. Lamparter, Current Microbiology 2021, 78, 2708–2719, 10.1007/s00284-021-02526-5
  • Structural Complexity and Plasticity of Signaling Regulation at the Melanocortin-4 Receptor, G. Kleinau, N. A. Heyder, Y. X. Tao, P. Scheerer, International Journal of Molecular Sciences 2020, 21, 5728–0, 10.3390/ijms21165728
  • Design of a light-gated proton channel based on the crystal structure of rhodopsin, R. Fudim, M. Szczepek, J. Vierock, A. Vogt, A. Schmidt, G. Kleinau, P. Fischer, F. Bartl, P. Scheerer, P. Hegemann, Science Signaling 2019, 12, 10.1126/scisignal.aav4203
  • The Pathogenic TSH β-subunit Variant C105Vfs114X Causes a Modified Signaling Profile at TSHR, L. Kalveram, G. Kleinau, K. Szymańska, P. Scheerer, A. Rivero-Müller, A. Grüters-Kieslich, H. Biebermann, International Journal of Molecular Sciences 2019, 20, 5564–0, 10.3390/ijms20225564
  • Recurrent convergent evolution at amino acid residue 261 in fish rhodopsin, J. Hill, E. D. Enbody, M. E. Pettersson, C. G. Sprehn, D. Bekkevold, A. Folkvord, L. Laikre, G. Kleinau, P. Scheerer, L. Andersson, Proceedings of the National Academy of Sciences 2019, 116, 18473–18478, 10.1073/pnas.1908332116
  • Signal Transduction and Pathogenic Modifications at the Melanocortin-4 Receptor: A Structural Perspective, N. Heyder, G. Kleinau, M. Szczepek, D. Kwiatkowski, D. Speck, L. Soletto, J. M. Cerdá-Reverter, H. Krude, P. Kühnen, H. Biebermann, P. Scheerer, Frontiers in Endocrinology 2019, 10, 1–18, 10.3389/fendo.2019.00515
  • The Axonal Membrane Protein PRG2 Inhibits PTEN and Directs Growth to Branches, A. Brosig, J. Fuchs, F. Ipek, C. Kroon, S. Schrötter, M. Vadhvani, A. Polyzou, J. Ledderose, M. van Diepen, H. G. Holzhütter, T. Trimbuch, N. Gimber, J. Schmoranzer, I. Lieberam, C. Rosenmund, C. Spahn, P. Scheerer, M. Szczepek, G. Leondaritis, B. J. Eickholt, Cell Reports 2019, 29, 2028–2040, 10.1016/j.celrep.2019.10.039
  • Evaluation of a rare glucose‐dependent insulinotropic polypeptide receptor variant in a patient with diabetes, S. F. Jacobi, N. Khajavi, G. Kleinau, A. Teumer, P. Scheerer, G. Homuth, H. Völzke, S. Wiegand, P. Kühnen, H. Krude, M. Gong, K. Raile, H. Biebermann, Diabetes, Obesity and Metabolism 2019, 21, 1168–1176, 10.1111/dom.13634

Publications (selection)

A. Schmidt, L. Sauthof, M. Szczepek, M. F. Lopez, F. V. Escobar, B. M. Qureshi, N. Michael, D. Buhrke, T. Stevens, D. Kwiatkowski, D. von Stetten, M. A. Mroginski, N. Krauß, T. Lamparter, P. Hildebrandt, P. Scheerer, Structural snapshot of a bacterial phytochrome in its functional intermediate state. Nature Communications  2018, 9(1), 4912.

J. Kalms, A. Schmidt, S. Frielingsdorf, T. Utesch, G. Gotthard, D. von Stetten, P. van der Linden, A. Royant, M. A. Mroginski, P. Carpentier, O. Lenz, P. Scheerer, Tracking the route of molecular oxygen in O2-tolerant membrane-bound [NiFe] hydrogenase. Proc Natl Acad Sci U S A.  2018, 115(10), E2229-E2237.

B. M. Qureshi, A. Schmidt, E. Behrmann, J. Bürger, T. Mielke, C. M. T. Spahn, M. Heck, P. Scheerer, Mechanistic insights into the role of prenyl-binding protein PrBP/δ in membrane dissociation of phosphodiesterase 6, Nature Communications  2018, 9(1), 90.

M. Szczepek, F. Beyrière, K. P. Hofmann, M. Elgeti, R. Kazmin, A. Rose, F. J. Bartl, D. von Stetten, M. Heck, M. E. Sommer, P. W. Hildebrand, P. Scheerer, Crystal structure of a common GPCR binding interface for G protein and arrestin, Nature Communications 2014, 5, 4801.

S. Frielingsdorf, J. Fritsch, A. Schmidt, M. Hammer, J. Löwenstein, E. Siebert, V. Pelmenschikov, T. Jaenicke, J. Kalms, Y. Rippers, F. Lendzian, I. Zebger, C. Teutloff, M. Kaupp, R. Bittl, P. Hildebrandt, B. Friedrich, O. Lenz, P. Scheerer, Reversible [4Fe-3S] cluster morphing in an O2-tolerant [NiFe] hydrogenase, Nature Chemical Biology 2014, 10, 378–385.

Y. J. Kim, K. P. Hofmann, O. P. Ernst, P. Scheerer, H. W. Choe, M. E. Sommer, Crystal structure of pre-activated arrestin p44, Nature 2013, 497, 142–146.

H.-W. Choe, Y. J. Kim, J. H. Park, T. Morizumi, E. F. Pai, N. Krauss, K. P. Hofmann, P. Scheerer, O. P. Ernst, Crystal structure of metarhodopsin II, Nature 2011, 471, 651–55.

J. Fritsch, P. Scheerer, S. Frielingsdorf, S. Kroschinsky, B. Friedrich, O. Lenz, C. M. Spahn, The crystal structure of an oxygen-tolerant hydrogenase uncovers a novel iron-sulphur centre, Nature 2011, 479, 249–252.

J. H. Park, P. Scheerer, K. P. Hofmann, H. W. Choe, O. P. Ernst, Crystal structure of the ligand-free G-protein-coupled receptor opsin, Nature 2008, 454, 183–187.

P. Scheerer, J. H. Park, P. W. Hildebrand, Y. J. Kim, N. Krauss, H. W. Choe, K. P. Hofmann, O. P. Ernst, Crystal structure of opsin in its G-protein-interacting conformation, Nature 2008, 455, 497–502.