UniSysCat Publications

• Electrochemically assisted SERS sensing of adenosine triphosphate using a carbon microelectrode with composite plasmonic nanostructures, H. Zhou, J. Kneipp, Vibrational Spectroscopy 2024, 131, 103661–0, 10.1016/j.vibspec.2024.103661
• 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
• Accurate Determination of Motional Amplitudes in Biomolecules by Solid-State NMR, V. Chevelkov, S. Lange, H. Sawczyc, A. Lange, ACS Physical Chemistry Au 2023, 3, 199–206, 10.1021/acsphyschemau.2c00053
• 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
• The opening dynamics of the lateral gate regulates the activity of rhomboid proteases, C. Bohg, C. Öster, B. Türkaydin, M. Lisurek, P. Sanchez-Carranza, S. Lange, T. Utesch, H. Sun, A. Lange, Science Advances 2023, 9, 10.1126/sciadv.adh3858
• Surface-enhanced infrared absorption spectroscopy, J. Kozuch, K. Ataka, J. Heberle, Nature Reviews Methods Primers 2023, 3, 1–19, 10.1038/s43586-023-00253-8
• Photoswitchable Inhibitors to Optically Control Specific Kinase Activity, T. Aguirre, E. Teichmann, F. Q. Römpp, R. Vivier, C. Bryant, M. A. Hulverson, W. C. Van Voorhis, K. K. Ojo, J. S. Doggett, D. Fiedler, S. Hecht, ACS Chemical Biology 2023, 18, 1378–1387, 10.1021/acschembio.3c00119
• CommonNNClustering─A Python Package for Generic Common-Nearest-Neighbor Clustering, J. O. Kapp-Joswig, B. G. Keller, Journal of Chemical Information and Modeling 2023, 63, 1093–1098, 10.1021/acs.jcim.2c01493
• Vibrational Spectroscopy of Phytochromes, P. Hildebrandt, Biomolecules 2023, 13, 1007–0, 10.3390/biom13061007
• Experimental Assessment of the Electronic and Geometrical Structure of a Near-Infrared Absorbing and Highly Fluorescent Microbial Rhodopsin, M. Broser, T. Andruniów, A. Kraskov, R. Palombo, S. Katz, M. Kloz, J. Dostál, C. Bernardo, J. T. M. Kennis, P. Hegemann, M. Olivucci, P. Hildebrandt, The Journal of Physical Chemistry Letters 2023, 14, 9291–9295, 10.1021/acs.jpclett.3c02167
• On the Role of a Conserved Tryptophan in the Chromophore Pocket of Cyanobacteriochrome, M. Blain-Hartung, G. Johannes von Sass, J. Plaickner, S. Katz, O. Tu Hoang, M. Andrea Mroginski, N. Esser, N. Budisa, K. T. Forest, P. Hildebrandt, Journal of Molecular Biology 2023, 168227–0, 10.1016/j.jmb.2023.168227
• Orthogonal translation with 5‐cyanotryptophan as an infrared probe for local structural information, electrostatics, and hydrogen bonding, G. J. von Freiherr Sass, M. Blain‐Hartung, T. Baumann, K. T. Forest, P. Hildebrandt, N. Budisa, Protein Science 2023, 32, 10.1002/pro.4705
• Protein structure prediction with in-cell photo-crosslinking mass spectrometry and deep learning, K. Stahl, A. Graziadei, T. Dau, O. Brock, J. Rappsilber, Nature Biotechnology 2023, 10.1038/s41587-023-01704-z
• Light-Induced Orthogonal Fragmentation of Crosslinked Peptides, L. Kolbowski, A. Belsom, A. M. Pérez-López, T. Ly, J. Rappsilber, JACS Au 2023, 3, 2123–2130, 10.1021/jacsau.3c00199
• Establishment of dsDNA-dsDNA interactions by the condensin complex, M. Tang, G. Pobegalov, H. Tanizawa, Z. A. Chen, J. Rappsilber, M. Molodtsov, K. i. Noma, F. Uhlmann, Molecular Cell 2023, 83, 3787–3800000000000, 10.1016/j.molcel.2023.09.019
• Protein complexes in cells by ‐assisted structural proteomics, F. J. O'Reilly, A. Graziadei, C. Forbrig, R. Bremenkamp, K. Charles, S. Lenz, C. Elfmann, L. Fischer, J. Stülke, J. Rappsilber, Molecular Systems Biology 2023, 19, 10.15252/msb.202311544
• Cleavable Cross-Linkers Redefined by a Novel MS -Trigger Algorithm, L. Kolbowski, L. Fischer, J. Rappsilber, Analytical Chemistry 2023, 95, 15461–15464, 10.1021/acs.analchem.3c01673
• 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
• Photomanipulation of Minimal Synthetic Cells: Area Increase, Softening, and Interleaflet Coupling of Membrane Models Doped with Azobenzene‐Lipid Photoswitches, M. Aleksanyan, A. Grafmüller, F. Crea, V. N. Georgiev, N. Yandrapalli, S. Block, J. Heberle, R. Dimova, Advanced Science 2023, 10, 2304336–0, 10.1002/advs.202304336
• Diversity of rhodopsin cyclases in zoospore-forming fungi, M. Broser, W. Busse, A. Spreen, M. Reh, Y. A. Bernal Sierra, S. Hwang, T. Utesch, H. Sun, P. Hegemann, Proceedings of the National Academy of Sciences 2023, 120, 10.1073/pnas.2310600120
• Mechanistic Studies of Membrane Proteins Using Integrated Solid-state NMR and Computational Approaches, S. Mohr, Y. K. Aldakul, H. Sun, H. Sawczyc, A. Lange in New Developments in NMR Integrated Structural Biology (Hrsg.: Tatyana Polenova, Caitlin M. Quinn, Angela M. Gronenborn), Royal Society of Chemistry, 2023, 268–300, ISBN: 978-1-83916-183-4
• 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
• Direct Detection of Bound Ammonium Ions in the Selectivity Filter of Ion Channels by Solid-State NMR, C. Öster, K. Tekwani Movellan, B. Goold, K. Hendriks, S. Lange, S. Becker, B. L. de Groot, W. Kopec, L. B. Andreas, A. Lange, Journal of the American Chemical Society 2022, 144, 4147–4157, 10.1021/jacs.1c13247
• Photoactivation of a Mechanosensitive Channel, F. Crea, A. Vorkas, A. Redlich, R. Cruz, C. Shi, D. Trauner, A. Lange, R. Schlesinger, J. Heberle, Frontiers in Molecular Biosciences 2022, 9, 10.3389/fmolb.2022.905306
• QuasAr Odyssey: the origin of fluorescence and its voltage sensitivity in microbial rhodopsins, A. Silapetere, S. Hwang, Y. Hontani, R. G. Fernandez Lahore, J. Balke, F. V. Escobar, M. Tros, P. E. Konold, R. Matis, R. Croce, P. J. Walla, P. Hildebrandt, U. Alexiev, J. T. M. Kennis, H. Sun, T. Utesch, P. Hegemann, Nature Communications 2022, 13, 10.1038/s41467-022-33084-4
• Potential Distribution across Model Membranes, T. Utesch, J. Staffa, S. Katz, G. Yao, J. Kozuch, P. Hildebrandt, The Journal of Physical Chemistry B 2022, 126, 7664–7675, 10.1021/acs.jpcb.2c05372
• Monitoring the Progression of Cell-Free Expression of Microbial Rhodopsins by Surface Enhanced IR Spectroscopy: Resolving a Branch Point for Successful/Unsuccessful Folding, K. Ataka, A. Baumann, J. L. Chen, A. Redlich, J. Heberle, R. Schlesinger, Frontiers in Molecular Biosciences 2022, 9, 1–9, 10.3389/fmolb.2022.929285
• Membrane Protein Activity Induces Specific Molecular Changes in Nanodiscs Monitored by FTIR Difference Spectroscopy, F. Baserga, A. Vorkas, F. Crea, L. Schubert, J. L. Chen, A. Redlich, M. La Greca, J. Storm, S. Oldemeyer, K. Hoffmann, R. Schlesinger, J. Heberle, Frontiers in Molecular Biosciences 2022, 9, 1–12, 10.3389/fmolb.2022.915328
• Trapping an Oxidized and Protonated Intermediate of the [FeFe]-Hydrogenase Cofactor under Mildly Reducing Conditions, M. Senger, J. Duan, M. V. Pavliuk, U. P. Apfel, M. Haumann, S. T. Stripp, Inorganic Chemistry 2022, 61, 10036–10042, 10.1021/acs.inorgchem.2c00954
• Antimicrobial Polymers of Linear and Bottlebrush Architecture: Probing the Membrane Interaction and Physicochemical Properties, A. M. Bapolisi, P. Kielb, M. Bekir, A. Lehnen, C. Radon, S. Laroque, P. Wendler, H. M. Müller‐Werkmeister, M. Hartlieb, Macromolecular Rapid Communications 2022, 43, 2200288–0, 10.1002/marc.202200288
• Surface enhanced Raman scattering for probing cellular biochemistry, C. Spedalieri, J. Kneipp, Nanoscale 2022, 14, 5314–5328, 10.1039/D2NR00449F
• Arabidopsis PFA-DSP-Type Phosphohydrolases Target Specific Inositol Pyrophosphate Messengers, P. Gaugler, R. Schneider, G. Liu, D. Qiu, J. Weber, J. Schmid, N. Jork, M. Häner, K. Ritter, N. Fernández-Rebollo, R. F. H. Giehl, M. N. Trung, R. Yadav, D. Fiedler, V. Gaugler, H. J. Jessen, G. Schaaf, D. Laha, Biochemistry 2022, 61, 1213–1227, 10.1021/acs.biochem.2c00145
• Probing Factor Xa Protein–Ligand Interactions: Accurate Free Energy Calculations and Experimental Validations of Two Series of High-Affinity Ligands, M. I. Fernández-Bachiller, S. Hwang, M. E. Schembri, P. Lindemann, M. Guberman, S. Herziger, E. Specker, H. Matter, D. W. Will, J. Czech, M. Wagner, A. Bauer, H. Schreuder, K. Ritter, M. Urmann, V. Wehner, H. Sun, M. Nazaré, Journal of Medicinal Chemistry 2022, 65, 13013–13028, 10.1021/acs.jmedchem.2c00865
• Solving the Azobenzene Entropy Puzzle: Direct Evidence for Multi-State Reactivity, M. Reimann, E. Teichmann, S. Hecht, M. Kaupp, The Journal of Physical Chemistry Letters 2022, 13, 10882–10888, 10.1021/acs.jpclett.2c02838
• Solving the Azobenzene Entropy Puzzle: Direct Evidence for Multi-State Reactivity, M. Reimann, E. Teichmann, S. Hecht, M. Kaupp, The Journal of Physical Chemistry Letters 2022, 13, 10882–10888, 10.1021/acs.jpclett.2c02838
• GROMACS Stochastic Dynamics and BAOAB Are Equivalent Configurational Sampling Algorithms, S. Kieninger, B. G. Keller, Journal of Chemical Theory and Computation 2022, 18, 5792–5798, 10.1021/acs.jctc.2c00585
• Structure and Interaction of Ceramide-Containing Liposomes with Gold Nanoparticles as Characterized by SERS and Cryo-EM, Y. Feng, Z. Kochovski, C. Arenz, Y. Lu, J. Kneipp, The Journal of Physical Chemistry C 2022, 126, 13237–13246, 10.1021/acs.jpcc.2c01930
• 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
• 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
• Protein Nanopore Membranes Prepared by a Simple Langmuir–Schaefer Approach, M. S. Schwieters, M. Mathieu‐Gaedke, M. Westphal, R. Dalpke, M. Dirksen, D. Qi, M. Grull, T. Bick, S. Taßler, D. F. Sauer, M. Bonn, P. Wendler, T. Hellweg, A. Beyer, A. Gölzhäuser, U. Schwaneberg, U. Glebe, A. Böker, Small 2021, 17, 2102975–0, 10.1002/smll.202102975
• Construction of Highly Ordered Glyco‐Inside Nano‐Assemblies through RAFT Dispersion Polymerization of Galactose‐Decorated Monomer, L. Qiu, H. Zhang, T. Bick, J. Martin, P. Wendler, A. Böker, U. Glebe, C. Xing, Angewandte Chemie International Edition 2021, 60, 11098–11103, 10.1002/anie.202015692
• Probing the Intracellular Bio-Nano Interface in Different Cell Lines with Gold Nanostars, C. Spedalieri, G. P. Szekeres, S. Werner, P. Guttmann, J. Kneipp, Nanomaterials 2021, 11, 1183–0, 10.3390/nano11051183
• Intracellular optical probing with gold nanostars, C. Spedalieri, G. P. Szekeres, S. Werner, P. Guttmann, J. Kneipp, Nanoscale 2021, 13, 968–979, 10.1039/D0NR07031A
• Reliable identification of protein-protein interactions by crosslinking mass spectrometry, S. Lenz, L. R. Sinn, F. J. O’Reilly, L. Fischer, F. Wegner, J. Rappsilber, Nature Communications 2021, 12, 10.1038/s41467-021-23666-z
• Retention time prediction using neural networks increases identifications in crosslinking mass spectrometry, S. H. Giese, L. R. Sinn, F. Wegner, J. Rappsilber, Nature Communications 2021, 12, 10.1038/s41467-021-23441-0
• Dissecting the activation of insulin degrading enzyme by inositol pyrophosphates and their bisphosphonate analogs, S. Hostachy, T. Utesch, K. Franke, G. L. Dornan, D. Furkert, B. Türkaydin, V. Haucke, H. Sun, D. Fiedler, Chemical Science 2021, 12, 10696–10702, 10.1039/D1SC02975D
• The mechanism behind enhanced reactivity of unsaturated phosphorus(v) electrophiles towards thiols, Y. Park, A. L. Baumann, H. Moon, S. Byrne, M. A. Kasper, S. Hwang, H. Sun, M. H. Baik, C. P. R. Hackenberger, Chemical Science 2021, 12, 8141–8148, 10.1039/D1SC01730F
• A combination of solid-state NMR and MD simulations reveals the binding mode of a rhomboid protease inhibitor, C. Bohg, C. Öster, T. Utesch, S. Bischoff, S. Lange, C. Shi, H. Sun, A. Lange, Chemical Science 2021, 12, 12754–12762, 10.1039/D1SC02146J
• Proteinanalytik mittels Crosslinking-Massenspektrometrie Synergistische Kombination von kovalenter Bindungsknüpfung und LC-MS, L. Sinn, J. Rappsilber, GIT Labor-Fachzeitschrift 2021, 59, 17–20,
• 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
• Markov models from the square root approximation of the Fokker–Planck equation: calculating the grid-dependent flux, L. Donati, M. Weber, B. G. Keller, Journal of Physics: Condensed Matter 2021, 33, 115902–0, 10.1088/1361-648X/abd5f7
• The molecular basis for the pH-dependent calcium affinity of the pattern recognition receptor langerin, J. O. Joswig, J. Anders, H. Zhang, C. Rademacher, B. G. Keller, Journal of Biological Chemistry 2021, 296, 100718–0, 10.1016/j.jbc.2021.100718
• Structural insights into Cullin4-RING ubiquitin ligase remodelling by Vpr from simian immunodeficiency viruses, S. Banchenko, F. Krupp, C. Gotthold, J. Bürger, A. Graziadei, F. J. O’Reilly, L. Sinn, O. Ruda, J. Rappsilber, C. M. T. Spahn, T. Mielke, I. A. Taylor, D. Schwefel, PLOS Pathogens 2021, 17, 10.1371/journal.ppat.1009775
• Structural plasticity of the selectivity filter in a nonselective ion channel, R. N. Roy, K. Hendriks, W. Kopec, S. Abdolvand, K. L. Weiss, B. L. de Groot, A. Lange, H. Sun, L. Coates, IUCrJ 2021, 8, 421–430, 10.1107/S205225252100213X
• Sodium Ions Do Not Stabilize the Selectivity Filter of a Potassium Channel, K. Hendriks, C. Öster, C. Shi, H. Sun, A. Lange, Journal of Molecular Biology 2021, 433, 167091–0, 10.1016/j.jmb.2021.167091
• Structural Plasticity of the Selectivity Filter in Cation Channels, K. Hendriks, C. Öster, A. Lange, Frontiers in Physiology 2021, 12, 10.3389/fphys.2021.792958
• Investigation of a potential electrogenic transport-system for -inositol in the small intestine of laying hens, K. Röhm, F. Gonzalez-Uarquin, R. K. Harmel, M. Nguyen Trung, M. Diener, D. Fiedler, K. Huber, J. Seifert, British Poultry Science 2021, 63, 91–97, 10.1080/00071668.2021.1958301
• Shulin packages axonemal outer dynein arms for ciliary targeting, G. R. Mali, F. A. Ali, C. K. Lau, F. Begum, J. Boulanger, J. D. Howe, Z. A. Chen, J. Rappsilber, M. Skehel, A. P. Carter, Science 2021, 371, 910–916, 10.1126/science.abe0526
• 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
• 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
• 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
• 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
• 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
• Multiomics Analysis Provides Insight into the Laboratory Evolution of toward the Metabolic Usage of Fluorinated Indoles, F. Agostini, L. Sinn, D. Petras, C. J. Schipp, V. Kubyshkin, A. A. Berger, P. C. Dorrestein, J. Rappsilber, N. Budisa, B. Koksch, ACS Central Science 2020, 7, 81–92, 10.1021/acscentsci.0c00679
• 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 structural & molecular biology 2020, 27, 743–751, 10.1038/s41594-020-0457-x
• 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
• Combining free energy calculations with tailored enzyme activity assays to elucidate substrate binding of a phospho-lysine phosphatase, A. Hauser, S. Hwang, H. Sun, C. P. R. Hackenberger, Chemical Science 2020, 11, 12655–12661, 10.1039/D0SC03930F
• 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
• Electrolysis of low-grade and saline surface water, W. Tong, M. Forster, F. Dionigi, S. Dresp, R. Sadeghi Erami, P. Strasser, A. J. Cowan, P. Farràs, Nature Energy 2020, 5, 367–377, 10.1038/s41560-020-0550-8
• Electrocatalytic CO Reduction on CuO Nanocubes: Tracking the Evolution of Chemical State, Geometric Structure, and Catalytic Selectivity using Operando Spectroscopy, T. Möller, F. Scholten, T. N. Thanh, I. Sinev, J. Timoshenko, X. Wang, Z. Jovanov, M. Gliech, B. Roldan Cuenya, A. S. Varela, P. Strasser, Angewandte Chemie International Edition 2020, 59, 17974–17983, 10.1002/anie.202007136
• Electrochemical Approaches toward CO Capture and Concentration, S. E. Renfrew, D. E. Starr, P. Strasser, ACS Catalysis 2020, 10, 13058–13074, 10.1021/acscatal.0c03639
• Temperature Dependence of Structural Dynamics at the Catalytic Cofactor of [FeFe]-hydrogenase, S. T. Stripp, S. Mebs, M. Haumann, Inorganic Chemistry 2020, 59, 16474–16488, 10.1021/acs.inorgchem.0c02316
• 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
• 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
• Shining a Light on Proteolysis Targeting Chimeras, E. Teichmann, S. Hecht, ACS Central Science 2019, 5, 1645–1647, 10.1021/acscentsci.9b00955
• 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
• 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
• In Situ Structural Restraints from Cross-Linking Mass Spectrometry in Human Mitochondria, P. S. J. Ryl, M. Bohlke-Schneider, S. Lenz, L. Fischer, L. Budzinski, M. Stuiver, M. M. L. Mendes, L. Sinn, F. J. O’Reilly, J. Rappsilber, Journal of Proteome Research 2019, 19, 327–336, 10.1021/acs.jproteome.9b00541
• 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
• Structure and Dynamics of the Rhomboid Protease GlpG in Liposomes Studied by Solid-State NMR, C. Shi, C. Öster, C. Bohg, L. Li, S. Lange, V. Chevelkov, A. Lange, Journal of the American Chemical Society 2019, 141, 17314–17321, 10.1021/jacs.9b08952
• 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
• 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