UniSysCat Publications

  • Path probability ratios for Langevin dynamics—Exact and approximate, S. Kieninger, B. G. Keller, The Journal of Chemical Physics 2021, 154, 94102–0, 10.1063/5.0038408
  • In-cell architecture of an actively transcribing-translating expressome, F. J. O’Reilly, L. Xue, A. Graziadei, L. Sinn, S. Lenz, D. Tegunov, C. Blötz, N. Singh, W. J. H. Hagen, P. Cramer, J. Stülke, J. Mahamid, J. Rappsilber, Science 2020, 369, 554–557, 10.1126/science.abb3758
  • Stereochemical Elucidation of Natural Products from Residual Chemical Shift Anisotropies in a Liquid Crystalline Phase, X. L. Li, L. P. Chi, A. Navarro-Vázquez, S. Hwang, P. Schmieder, X. M. Li, X. Li, S. Q. Yang, X. Lei, B. G. Wang, H. Sun, Journal of the American Chemical Society 2019, 142, 2301–2309, 10.1021/jacs.9b10961
  • Molecular Mechanism of the pH-Dependent, J. O. Joswig, J. Anders, H. Zhang, C. Rademann, B. G. Keller, MPG.PuRe 2020, 10.1101/2020.03.11.986851
  • Absorption and Emission Spectroscopic Investigation of the Thermal Dynamics of the Archaerhodopsin 3 Based Fluorescent Voltage Sensor Archon2, A. Penzkofer, A. Silapetere, P. Hegemann, International Journal of Molecular Sciences 2020, 21, 6576–0, 10.3390/ijms21186576
  • Dual Photoisomerization on Distinct Potential Energy Surfaces in a UV-Absorbing Rhodopsin, Y. Hontani, M. Broser, M. Luck, J. Weißenborn, M. Kloz, P. Hegemann, J. T. M. Kennis, Journal of the American Chemical Society 2020, 142, 11464–11473, 10.1021/jacs.0c03229
  • Photocycle Dynamics of the Archaerhodopsin 3 Based Fluorescent Voltage Sensor QuasAr1, A. Penzkofer, A. Silapetere, P. Hegemann, International Journal of Molecular Sciences 2019, 21, 160–0, 10.3390/ijms21010160
  • Absorption and Emission Spectroscopic Investigation of the Thermal Dynamics of the Archaerhodopsin 3 Based Fluorescent Voltage Sensor QuasAr1, Penzkofer, Silapetere, Hegemann, International Journal of Molecular Sciences 2019, 20, 4086–0, 10.3390/ijms20174086
  • Unifying photocycle model for light adaptation and temporal evolution of cation conductance in channelrhodopsin-2, J. Kuhne, J. Vierock, S. A. Tennigkeit, M. A. Dreier, J. Wietek, D. Petersen, K. Gavriljuk, S. F. El-Mashtoly, P. Hegemann, K. Gerwert, Proceedings of the National Academy of Sciences 2019, 116, 9380–9389, 10.1073/pnas.1818707116
  • Tracking Pore Hydration in Channelrhodopsin by Site-Directed Infrared-Active Azido Probes, B. S. Krause, J. C. D. Kaufmann, J. Kuhne, J. Vierock, T. Huber, T. P. Sakmar, K. Gerwert, F. J. Bartl, P. Hegemann, Biochemistry 2019, 58, 1275–1286, 10.1021/acs.biochem.8b01211
  • Engineered Passive Potassium Conductance in the KR2 Sodium Pump, A. Vogt, A. Silapetere, C. Grimm, F. Heiser, M. Ancina Möller, P. Hegemann, Biophysical Journal 2019, 116, 1941–1951, 10.1016/j.bpj.2019.04.001
  • MerMAIDs: a family of metagenomically discovered marine anion-conducting and intensely desensitizing channelrhodopsins, J. Oppermann, P. Fischer, A. Silapetere, B. Liepe, S. Rodriguez-Rozada, J. Flores-Uribe, E. Peter, A. Keidel, J. Vierock, J. Kaufmann, M. Broser, M. Luck, F. Bartl, P. Hildebrandt, J. S. Wiegert, O. Béjà, P. Hegemann, J. Wietek, Nature Communications 2019, 10, 10.1038/s41467-019-11322-6
  • Red, Orange, Green: Light- and Temperature-Dependent Color Tuning in a Cyanobacteriochrome, D. Buhrke, G. Battocchio, S. Wilkening, M. Blain-Hartung, T. Baumann, F. J. Schmitt, T. Friedrich, M. A. Mroginski, P. Hildebrandt, Biochemistry 2019, 59, 509–519, 10.1021/acs.biochem.9b00931
  • Probing Structure and Reaction Dynamics of Proteins Using Time-Resolved Resonance Raman Spectroscopy, D. Buhrke, P. Hildebrandt, Chemical Reviews 2019, 120, 3577–3630, 10.1021/acs.chemrev.9b00429
  • Picometer Resolution Structure of the Coordination Sphere in the Metal-Binding Site in a Metalloprotein by NMR, A. Bertarello, L. Benda, K. J. Sanders, A. J. Pell, M. J. Knight, V. Pelmenschikov, L. Gonnelli, I. C. Felli, M. Kaupp, L. Emsley, R. Pierattelli, G. Pintacuda, Journal of the American Chemical Society 2020, 10.1021/jacs.0c07339
  • Relativistic Heavy-Neighbor-Atom Effects on NMR Shifts: Concepts and Trends Across the Periodic Table, J. Vı́cha, J. Novotný, S. Komorovsky, M. Straka, M. Kaupp, R. Marek, Chemical Reviews 2020, 120, 7065–7103, 10.1021/acs.chemrev.9b00785
  • Oxidative and reductive cyclization in stiff dithienylethenes, M. Kleinwächter, E. Teichmann, L. Grubert, M. Herder, S. Hecht, Beilstein Journal of Organic Chemistry 2018, 14, 2812–2821, 10.3762/bjoc.14.259
  • Effiziente lichtinduzierte p -Modulation, gekoppelt mit basenkatalysierter Photochromie, J. Gurke, Š. Budzák, B. M. Schmidt, D. Jacquemin, S. Hecht, Angewandte Chemie 2018, 130, 4888–4893, 10.1002/ange.201801270
  • Shining a Light on Proteolysis Targeting Chimeras, E. Teichmann, S. Hecht, ACS Central Science 2019, 5, 1645–1647, 10.1021/acscentsci.9b00955
  • Life as we don\\\\\\\'t (yet) know it, N. Budisa in Art as we don’t know it (Hrsg.: Berger, E.; Kasperi Mäki-Reinikka; Kira O’Reilly; Sederholm, H., ), Aalto University Publication Series, 2020, 0–0, ISBN: 9789526088228
  • Expanding the DOPA Universe with Genetically Encoded, Mussel‐Inspired Bioadhesives for Material Sciences and Medicine, N. Budisa, T. Schneider, ChemBioChem 2019, 20, 2163–2190, 10.1002/cbic.201900030
  • Anticipating alien cells with alternative genetic codes: away from the alanine world!, V. Kubyshkin, N. Budisa, Current Opinion in Biotechnology 2019, 60, 242–249, 10.1016/j.copbio.2019.05.006
  • Bilayer thickness determines the alignment of model polyproline helices in lipid membranes, V. Kubyshkin, S. L. Grage, A. S. Ulrich, N. Budisa, Physical Chemistry Chemical Physics 2019, 21, 22396–22408, 10.1039/c9cp02996f
  • Promotion of the collagen triple helix in a hydrophobic environment, V. Kubyshkin, N. Budisa, Organic & Biomolecular Chemistry 2019, 17, 2502–2507, 10.1039/c9ob00070d
  • The Alanine World Model for the Development of the Amino Acid Repertoire in Protein Biosynthesis, V. Kubyshkin, N. Budisa, International Journal of Molecular Sciences 2019, 20, 5507–0, 10.3390/ijms20215507
  • Computational Aminoacyl-tRNA Synthetase Library Design for Photocaged Tyrosine, T. Baumann, M. Hauf, F. Richter, S. Albers, A. Möglich, Z. Ignatova, N. Budisa, International Journal of Molecular Sciences 2019, 20, 2343–0, 10.3390/ijms20092343
  • In-Cell Synthesis of Bioorthogonal Alkene Tag S-Allyl-Homocysteine and Its Coupling with Reprogrammed Translation, S. Nojoumi, Y. Ma, S. Schwagerus, C. P. R. Hackenberger, N. Budisa, International Journal of Molecular Sciences 2019, 20, 2299–0, 10.3390/ijms20092299
  • Synthesis of New Aza‐ and Thia‐Crown Ether Based Amino Acids, T. Schneider, N. Brüssow, A. Yuvanc, N. Budisa, ChemistrySelect 2020, 5, 2854–2857, 10.1002/slct.202000122
  • Xenobiology: A Journey towards Parallel Life Forms, N. Budisa, V. Kubyshkin, M. Schmidt, ChemBioChem 2020, 21, 2228–2231, 10.1002/cbic.202000141
  • Phage capsid nanoparticles with defined ligand arrangement block influenza virus entry, D. Lauster, S. Klenk, K. Ludwig, S. Nojoumi, S. Behren, L. Adam, M. Stadtmüller, S. Saenger, S. Zimmler, K. Hönzke, L. Yao, U. Hoffmann, M. Bardua, A. Hamann, M. Witzenrath, L. E. Sander, T. Wolff, A. C. Hocke, S. Hippenstiel, S. De Carlo, J. Neudecker, K. Osterrieder, N. Budisa, R. R. Netz, C. Böttcher, S. Liese, A. Herrmann, C. P. R. Hackenberger, Nature Nanotechnology 2020, 15, 373–379, 10.1038/s41565-020-0660-2
  • Discovery and Characterization of a New Cold-Active Protease From an Extremophilic Bacterium via Comparative Genome Analysis and in vitro Expression, A. Perfumo, G. J. Freiherr von Sass, E. L. Nordmann, N. Budisa, D. Wagner, Frontiers in Microbiology 2020, 11, 10.3389/fmicb.2020.00881
  • An Engineered Escherichia coli Strain with Synthetic Metabolism for In‐cell Production of Translationally Active Methionine Derivatives, C. J. Schipp, Y. Ma, A. Al-Shameri, F. D'Alessio, P. Neubauer, R. Contestabile, N. Budisa, M. L. di Salvo, ChemBioChem 2020, 10.1002/cbic.202000257
  • Cryo-EM structures of holo condensin reveal a subunit flip-flop mechanism, B. G. Lee, F. Merkel, M. Allegretti, M. Hassler, C. Cawood, L. Lecomte, F. J. O’Reilly, L. R. Sinn, P. Gutierrez-Escribano, M. Kschonsak, S. Bravo, T. Nakane, J. Rappsilber, L. Aragon, M. Beck, J. Löwe, C. H. Haering, Nature 2020, 27, 743–751, 10.1038/s41594-020-0457-x
  • Spectroscopic investigations under whole-cell conditions provide new insight into the metal hydride chemistry of [FeFe]-hydrogenase, L. S. Mészáros, P. Ceccaldi, M. Lorenzi, H. J. Redman, E. Pfitzner, J. Heberle, M. Senger, S. T. Stripp, G. Berggren, Chemical Science 2020, 11, 4608–4617, 10.1039/D0SC00512F
  • The structure of human thyroglobulin, F. Coscia, A. Taler-Verčič, V. T. Chang, L. Sinn, F. J. O’Reilly, T. Izoré, M. Renko, I. Berger, J. Rappsilber, D. Turk, J. Löwe, Nature 2020, 578, 627–630, 10.1038/s41586-020-1995-4
  • How [FeFe]-Hydrogenase Facilitates Bidirectional Proton Transfer, M. Senger, V. Eichmann, K. Laun, J. Duan, F. Wittkamp, G. Knör, U. P. Apfel, T. Happe, M. Winkler, J. Heberle, S. T. Stripp, Journal of the American Chemical Society 2019, 141, 17394–17403, 10.1021/jacs.9b09225
  • Asymmetry in the Ligand Coordination Sphere of the [FeFe] Hydrogenase Active Site Is Reflected in the Magnetic Spin Interactions of the Aza-propanedithiolate Ligand, E. J. Reijerse, V. Pelmenschikov, J. A. Birrell, C. P. Richers, M. Kaupp, T. B. Rauchfuss, S. P. Cramer, W. Lubitz, The Journal of Physical Chemistry Letters 2019, 10, 6794–6799, 10.1021/acs.jpclett.9b02354
  • Insights from Te and Fe nuclear resonance vibrational spectroscopy: a [4Fe–4Te] cluster from two points of view, F. Wittkamp, N. Mishra, H. Wang, H. C. Wille, R. Steinbrügge, M. Kaupp, S. P. Cramer, U. P. Apfel, V. Pelmenschikov, Chemical Science 2019, 10, 7535–7541, 10.1039/c9sc02025j
  • Site‐Resolved Observation of Vibrational Energy Transfer Using a Genetically Encoded Ultrafast Heater, T. Baumann, M. Hauf, F. Schildhauer, K. B. Eberl, P. M. Durkin, E. Deniz, J. G. Löffler, C. G. Acevedo‐Rocha, J. Jaric, B. M. Martins, H. Dobbek, J. Bredenbeck, N. Budisa, Angewandte Chemie International Edition 2019, 58, 2899–2903, 10.1002/anie.201812995
  • 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
  • Efficient Light-Induced p  Modulation Coupled to Base-Catalyzed Photochromism, J. Gurke, Š. Budzák, B. M. Schmidt, D. Jacquemin, S. Hecht, Angewandte Chemie International Edition 2018, 57, 4797–4801, 10.1002/anie.201801270