Arturo Juárez Carrillo: S. Eschenburg, N. Genov, K. Peters, S. Fittkau, S. Stoeva, K.S. Wilson, C. Betzel. (1998). Crystal structure of subtilisin DY, a random mutant of subtilisin Carlsberg. Eur. J. Biochem., 257, 309-318.
Lucie Dobiášová: K.P. Bzymek, K.A. Avery, Y. Ma, D.A. Horne, J.C. Williams. (2016). Natural and non-natural amino-acid side-chain substitutions: affinity and diffraction studies of meditope-Fab complexes. Acta Cryst. F72, 820-830.
Petr Slavíček: J. Kottur, D.T. Nair. (2018). Pyrophosphate hydrolysis is an intrinsic and critical step of the DNA synthesis reaction. Nucleic Acids Research, 46, 5875-5885.
Jakub Hrubý: D. Shin et al.. (2020). Papain-like protease regulates SARS-CoV-2 viral spread and innate immunity. Nature, ... detail.
Milan Kočí: C. Chung, A. W. Dean, J. M. Woolven, P. Bamborough. (2012). Fragment-Based Discovery of Bromodomain Inhibitors Part 1: Inhibitor Binding Modes and Implications for Lead Discovery. J. Med. Chem., 55, 576-586.
Karolína Špeldová: G.J. Davis, W.F. Bosron, C.L. Stone, K. Owusu-Dekyi, T.D. Hurley. (1996). X-ray structure of human beta3beta3 alcohol dehydrogenase. The contribution of ionic interactions to coenzyme binding. J. Biol. Chem., 271, 17057-17061.
Matthieu Guerin: R.K. Deka, C.A. Btrautigam, W.Z. Liu, D.R. Tomchick, M.V. Norgard. (2015). Evidence for Posttranslational Protein Flavinylation in the Syphilis Spirochete Treponema pallidum: Structural and Biochemical Insights from the Catalytic Core of a Periplasmic Flavin-Trafficking Protein. Mbio, 6, e00519-e00515.
Chloé Monique Macquigneau: J.R. Tame, B. Vallone. (2000). The structures of deoxy human haemoglobin and the mutant Hb Tyralpha42His at 120 K. Acta Cryst. D, 56, 805-811.
Lisa Terzo-Meurillon: A. Sharma, J. Kottur, N. Narayanan, D.T. Nair. (2013). A strategically located serine residue is critical for the mutator activity of DNA polymerase IV from Escherichia coli. Nucleic Acids Research, 41, 5104-5114.
Kseniia Tailasheva: M.B. Young et al.. (2004). Discovery and evaluation of potent P1 aryl heterocycle-based thrombin inhibitors. J. Med. Chem., 47, 2995-3008.
Pavla Bérešová: P. Kumar, V. Reithofer, M. Reisinger, S. Wallner, T. Pavkov-Keller, P. Macheroux, K. Gruber. (2016). Substrate complexes of human dipeptidyl peptidase III reveal the mechanism of enzyme inhibition. Sci Rep, 6, 23787-23787.
Fredrika Landmark: B. Calamini, B.D. Santarsiero, J.A. Boutin, A.D. Mesecar. (2008). Kinetic, thermodynamic and X-ray structural insights into the interaction of melatonin and analogues with quinone reductase 2. Biochem. J., 413,81-91.
Celien Mertens: (6BMG)
Iveta Terezie Pelikánová: M.P. Clark et al. (2014). Discovery of a Novel, Fist-in-Class, Orally Bioavailable Azaindole Inhibitor (VX-787) of Influenza PB2. J. Med. Chem., 57, 6668-6678.
Dalibor Řepček: M. Fan, Y. Xiao, M. Li, W. Chang. (2016). Crystal Structures of Arabidopsis thaliana Oxalyl-CoA Synthetase Essential for Oxalate Degradation. Mol. Plant, 9, 1349-1352.
Viktorie Navarová: N. Ramasubbu, V. Paloth, Y. Luo, G.D. Brayer, M.J. Levine (1996). Structure of Human Salivary alpha-Amylase at 1.6 Å Resolution: Implications for its Role in the Oral Cavity. Acta Cryst., D52, 435-446.
Petr Veřtát: R.J.C. Hilf, C. Bertozzi, I. Zimmermann, A. Reiter, D. Trauner, R. Dutzler. (2010). Structural basis of open channel block in a prokaryotic pentameric ligand-gated ion channel. Nat. Struct. Mol. Biol., 17, 1330-1336.
Miroslav Lebeda: P. Neumann, D. Lieber, S. Meyer, P. Dautel, A. Kerth, I. Kraus, W. Garten, M.T. Stubbs. (2009). Crystal structure of the Borna disease virus matrix protein (BDV-M) reveals ssRNA binding properties. Proc. Natl. Acad. Sci. USA, 106, 3710-3715.
Martin Malý: T. Schulte, F.P. Sharples, R.G. Hiller, E. Hofmann. (2009). X-Ray Structure of the High-Salt Form of the Peridinin-Chlorophyll A-Protein from the Dinoflagellate Amphidinium Carterae: Modulation of the Spectral Properties of Pigments by the Protein Environment. Biochemistry, 48, 4466-4475.