sav_logo
Departments
Organization Structure
Executive Body
Management Board
Supervisory Board
Scientific Board
Departments
Labour Union
Seminars
PhD Study
Documents
GDPR
Public Information
Links
Journal Biologia[IF: 1.350]
Biologia
Department of Biochemistry and Protein StructureKutejova.jpg

Dr. Eva Kutejova

head of department

Laboratory of Biochemistry and Protein Structure

Dr. Eva Kutejova (group leader)

ATP-dependent proteases in mitochondria

Mitochondrial proteases control key steps during mitochondrial biogenesis by proteolytic processing of regulatory proteins. A prevailing role can be assigned to ATP-dependent AAA proteases. Processes in focus of our research are mitochondrial posttranslational regulations, the control of the assembly of nucleoid complex, as well as proteolytic processes regulating mitochondrial dynamics. Mitochondria play an important role in cellular function, cell differentiation, and cell death processes. Mitochondrial dysfunction contributes to ageing, pathogenesis of many neurodegenerative disorders and cancer. We are analyzing the processing and degradation of various key players regulating mitochondrial dynamics in S. cerevisiae and human cells.

Structural and functional studies on human ryanodine receptor 2

Regular hearth function is one of the fundamental physiological functions fundamental for human life. The protein which plays a key role in this process is ryanodine receptor 2 (RyR2), which is expressed predominantly in heart muscle. RyR2, a calcium channel, mediates calcium release from sarcoplasmic reticulum into the cytoplasm causing regular heart contraction. Improper RyR2 function is a cause of severe heart diseases (CPVT1, ARVD2, SIDS, SUO). We study structure and function of RyR2 using bioinformatics, proteomics, molecular and structural biology. An important milestone on this way was determination of the structure of the RyR2 N-terminal part by X-ray and SAXS analysis. We have also succeeded to prepare and characterize several RyR2 mutants associated with above mentioned diseases.

Septin - cell division

Group of dr. Farkašovský is focusing on mechanisms of regulation of cell cycle in yeast S. cerevisiae. Septins are conserved guanine nucleotide binding proteins present in most eukaryotic organisms, involved in the cytokinesis and membrane remodelling functions. Major aim of the project is to explain how the specific protein-protein interactions and posttranslational modifications induce changes in the polymerization of septin filaments or assembly of higher-order structures in vivo.

Projects in cooperation with other institutes of SAS

Using yeast S. cerevisiae as a model eukaryotic organism our research is aimed at answering the question how interactions between intracellular organelles contribute to maintenance of lipid homeostasis. We focus on involvement of phosphatidylinositol transfer proteins in maintaining membrane phospholipid composition and resistance to azole antifungals.

Laboratory of Neurobiology

Dr. Frantisek Jursky (group leader)

Neurotransmitter transporters are membrane proteins, grouped into family of sodium/chloride dependent transporters solute carrier 6 (SLC6). They regulate pools of several important neurotransmitters and their impairment leads to serious illnesses. While the structurally highly conserved core of transporters has adopted only small changes during the evolution, little is  known about the structure of the large extracellular glycosylated loop and cytoplasmatically protruding N- and C-terminal regions. These regions are not directly involved in transport, they however contain several important regulatory signals affecting final transporter performance. Our laboratory reported previously that some of the transporters are substrates of calcium dependent protease calpain. If this represents a new mode of transporters regulation is under ongoing investigation. We additionally recently found that the N-terminal regions of glycine transporters exhibit an atypical dynamic interaction with Coomassie dye, suggesting their high flexibility and unstructured character, confirmed by independent circular dichroism studies.

The glycine transporter GlyT1 colocalizes with NMDA receptor and because the glycine serves as the NMDA coagonist, GlyT1 plays important role in its regulation. We have recently found that benzophenanthridine alkaloids inhibit GlyT1 in micromolar range and we identified their putative binding pocket. Even though these alkaloids exhibits wide spectrum of interactions and these results might be mainly important for the toxicology of benzophenanthridines, optimization of the pharmacophore might lead to more specific GlyT1 inhibitors. NMDA receptor is involved in higher neuronal function, memory and pain transmission; therefore inhibitors of GlyT1 may provide important means to influence these processes and to treat the potential illnesses.

Neurotransmitter transporters contain PDZ binding motif in their very C-terminal region. We recently found that many of them interact in vitro with PDZ domains of MUPP1, a largest multiple PDZ signaling protein. These interaction studies revealed some 3D similarities of PDZ binding motifs not apparent from their primary amino acid sequences. 

Molecular Immunology Unit

Dr. Vladimir Leksa (group leader)

For properly working physiological processes well-balanced cellular responses are required. This includes mutual interactions of soluble factors, cell surface receptors and intracellular signalling molecules. The loss of control over these interactions leads to various impairments and pathological circumstances, e.g. tumorigenesis or inflammat ory disorders.

In particular, immune cells of both adaptive and innate branches of immune system, such as T cells, B cells, macrophages or dendritic cells, are constantly exposed to an array of stimuli; they must distinguish between self and non-self, danger and normal, what has to be tolerated and what attacked. Many molecular pathways are involved in this labor.

We in our laboratory study the spatial and temporal organization of cellular receptors, their ligands, and associated signalling molecules in controlling immunity. Our research interest is focused on molecules underlying control devices in protein transpo t. Our up-to-now data strongly indicate a regulatory function of the mannose 6-phosphate/insulin-like growth factor 2 receptor (CD222) in various cellular functions including proteolysis, cell migration, signal transduction, or endocytosis. Our goal is to decipher the role of this specific endosomal transporter, and protein trafficking in general, in immune responses in health and disease. Our major objective is to provide pharmacological tools to modulate these responses. Our laboratory closely collaborates with Molecular Immunology Unit in the Institute for Hygiene and Applied Immunology at the Medical University of Vienna Medical University. More information about the various research projects can be found also here.

Protein Evolution

Prof. Stefan Janecek (group leader)

Laboratory of Protein Evolution is engaged in basic research in the field of protein bioinformatics. It is focused on the in silico study of proteins at the molecular level, i.e. to compare the primary and tertiary protein structures and to draw the relationships between the sequence, structure and evolution on one side and function, specificity and stability of the other side. The main aim is - within a collaboration with experimental approaches - protein engineering and design. In the centre of attention, there are enzymes hydrolyzing starch and related oligo- and polysaccharides, mainly from the alpha-amylase families (~30 different enzyme specificities), currently classified in the CAZy system (Carbohydrate-Active Enzymes) into families of glycoside hydrolases GH13, GH57, GH119 and eventually also GH126. The interest is also in functionally and evolutionarily related enzymes from families GH70, GH77 and GH31, as well as in starch binding domains from the so-called CAZy CBM families.

Stefan Janecek represents a pioneer in the bioinformatics, i.e. in silico, approach to studying of proteins in Slovakia. He has been devoted to this scientific field for 25 years continuously, 15 last years being giving his experiences to students as a university teacher. He has published 80 CC articles reaching more than 2,000 WOS-SCI citations. Under his supervising, 5 PhD-students have already finished their studies successfully. He has been the founder and main organizer of a series of international symposia about the enzymes from the alpha-amylase family - ALAMYs, held from 2001 traditionally in the Smolenice Castle in Slovakia. In 2016, he established international open-access scientific journal Amylase. He is also one of curators and co-authors of the web-based encyclopedia for carbohydrate-active enzymes CAZypedia.

Staff

Research fellows:
     Prof. Stefan Janecek
     Dr. Eva Kutejova
     Dr. Vladimir Pevala
     Dr. Vladena Bauerova
     Dr. Marian Farkasovsky
     Dr. Jacob Bauer
     Dr. Martina Baliova
     Dr. Vladimir Leksa
     Dr. Lubica Urbanikova
     Dr. Frantisek Jursky
     Dr. Gabriela Ondrovicova
     Dr. Nina Kunova
     Dr. Marek Gabrisko
     Eszter Zsemlye
     Lucia Martinakova
     Filip Marecek
PhD students:
     Dr. Barbora Stojkovicova
     Veronika Kotrasova
     Iveta Jahodova
     Henrieta Havalova
     Monika Zamocka
     Adam Polacek
     Romana Prazenicova
Undergraduate students:
     Natalia Usakova
     Maria Malgotova

International scientific co-operation

  1. BioChemoInformatics Unit, Institute of Organic Synthesis and Photoreactivity, National Research Council , Bologna, Italy
  2. Biofyzikální chemie a molekulární onkologie Biofyzikální ústav Akademie věd České republiky, v.v.i. , Brno, Czech Republic
  3. Cardiff University School of Dentistry, Cardiff, United Kingdom
  4. Chemistry & Biochemistry Department at University of California, Los Angeles, Los Angeles, USA
  5. Department for Structural and Computational Biology, Max Perutz Labs, Vienna, Austria
  6. Department of Chemistry, University of York, York, United Kingdom
  7. Department of Dermatology, Medical University of Vienna, Vienna, Austria
  8. Dr. Dessy Natalia, Biochemistry Research Division, Faculty of Mathematics and Natural Sciences, Institut Teknologi Bandung, Bandung, Indonesia
  9. Dr. Jean-Luc Da Lage, Laboratoire Evolution, Génomes Comportement, Ecologie, CNRS, Université Paris Sud, Gif sur Yvette, France
  10. Dr. Kian Mau Goh, Department of Biosciences and Health Sciences, Universiti Teknologi Malaysia, Johor Bahru, Malaysia
  11. Dr. Natasa Bozic, Institute of Chemistry, Technology and Metallurgy, University of Belgrade, Belgrade, Serbia
  12. Dr. Paweł Filipkowski, Department of Food Chemistry, Technology and Biotechnology, Faculty of Chemistry, Gdansk University of Technology, Gdansk, Poland
  13. Institute of Cellular Biology and Pathology, 1st Faculty of Medicine, Charles University in Prague, Prague, Czech Republic
  14. Laboratory of Molecular Immunology, Institute of Molecular Genetics, AS CR, Praha, Czech Republic
  15. Microbiological Institute, Academy of Sciences of Czech Republic, Prague, Czech Republic
  16. Molecular Immunology Unit, Institute for Hygiene and Applied Immunology, Center for Pathophysiology, Infectiology and Immunology, Medical University of Vienna, Vienna, Austria
  17. National Centre for Biomolecular Research, Masaryk University, Brno, Czech Republic
  18. Prof. Birte Svensson, Enzyme and Protein Chemistry, Department of Systems Biology, Technical University of Denmark, Kgs. Lyngby - Copenhagen, Denmark
  19. Prof. Marc J.E.C. van der Maarel, Department Aquatic Biotechnology and Bioproduct Engineering, University of Groningen, Groningen, The Netherlands

Scientific projects

  • Building learning and research capacities in the structure and functional analysis of biomolecules for the needs of biomedicine and biotechnology.
    (Interreg V-A Slovak - Austria, ITMS 305011X666, May 2019 - Nov 2022)
    http://www.imb.savba.sk/strubiomol/
    Principal investigator: Eva Kutejová
  • Study of the effect of cardiac arrhythmia-associated mutations on the structure and function of the human ryanodine receptor 2.
    (VEGA 2/0131/2020, Jan 2020 - Dec 2023)
    Principal investigator: Vladena Bauerová

Selected Publications

  1. Janecek, S., Svensson, B.
    How many alpha-amylase GH families are there in the CAZy database?.
    (2022) Amylase 6: 1-10.
  2. Kunova, N., Havalova, H., Ondrovicova, G., Stojkovicova, B., Bauer, J., Bauerova-Hlinkova, V., Pevala, V., Kutejova, E.
    Mitochondrial processing peptidases - structure, function and the role in human diseases.
    (2022) Int J Mol Sci 23(3): 1-24.
  3. Bauer, J., Žoldák, G.
    Interpretation of Single-Molecule Force Experiments on Proteins Using Normal Mode Analysis.
    (2021) Nanomaterials 11: 2795-.
  4. Frankovsky, J., Keresztesova, B., Bellova, J., Kunova, N., Canigova, N., Hanakova, K., Bauer, J., Ondrovicova, G., Lukacova, V., Sivakova, B., Zdrahal, Z., Pevala, V., Prochazkova, K., Nosek, J., Kutejova, E.
    The yeast mitochondrial succinylome: Implications for regulation of mitochondrial nucleoids.
    (2021) J. Biol. Chem. 297 (4): 1-16.
  5. Havalova, H., Ondrovicova, G., Keresztesova, B., Bauer, J., Pevala, V., Kutejova, E., Kunova, N.
    Mitochondrial HSP70 Chaperone System - The Influence of Post-Translational Modifications and Involvement in Human Diseases.
    (2021) Int J Mol Sci 22(15): 8077-.
  6. Janickova, Z., Janecek, S.
    In silico analysis of fungal and chloride-dependent alpha-amylases within the family GH13 with identification of possible secondary surface-binding sites.
    (2021) Molecules 26: 5704-.
  7. Kotrasova, V., Keresztesova, B., Ondrovicova, G., Bauer, J., Havalova, H., Pevala, V., Kutejova, E., Kunova, N.
    Mitochondrial Kinases and the Role of Mitochondrial Protein Phosphorylation in Health and Disease.
    (2021) LIFE-BASEL 11: 82-.
  8. Leitner, J., Mahasongkram, K., Schatzlmaier, P., Pfisterer, K., Leksa, V., Pata, S., Kasinrerk, W., Stockinger, H., Steinberger, P.
    Differentiation and activation of human CD4 T cells is associated with a gradual loss of myelin and lymphocyte protein.
    (2021) Eur. J. Immunol. 51 (4): 848-863.
  9. Marecek, F., Moeller, M.S., Svensson, B., Janecek, S.
    A putative novel starch-binding domain revealed by in silico analysis of the N-terminal domain in bacterial amylomaltases from the family GH77.
    (2021) 3 Biotech 11: 229-.
  10. Urban, J., Suchankova, M., Ganovska, M., Leksa, V., Sandor, F., Tedlova, E., Konig, B., Bucova, M.
    The Role of CX3CL1 and ADAM17 in Pathogenesis of Diffuse Parenchymal Lung Diseases.
    (2021) Diagnostics 11(6): 1074-.
  11. Urbanikova, L.
    CE16 acetylesterases: in silico analysis, catalytic machinery prediction and comparison with related SGNH hydrolases.
    (2021) 3 Biotech 11: 84-.
  12. Baliova, M., Jursky, F.
    Comparison of SynCAM1/CADM1 PDZ interactions with MUPP1 using mammalian and bacterial pull-down systems.
    (2020) Brain Behav. 10: e01587-.
  13. Baliova, M., Jursky, F.
    Phosphomimetic Mutation of Glycine Transporter GlyT1 C-Terminal PDZ Binding Motif Inhibits its Interactions with PSD95.
    (2020) J. Mol. Neurosci. 70: 488-493.
  14. Baliova, M., Jursky, F.
    Phosphorylation of Serine 157 Protects the Rat Glycine Transporter GlyT2 from Calpain Cleavage.
    (2020) J. Mol. Neurosci. 70: 1216-1224.
  15. Bauer, J., Borko, L., Pavlovič, J., Kutejova, E., Bauerova-Hlinkova, V.
    Disease-Associated Mutations Alter the Dynamic Motion of the N-terminal Domain of the Human Cardiac Ryanodine Receptor.
    (2020) J. Biomol. Struct. Dyn. 38: 1054-1070.
  16. Bauerova-Hlinkova, V., Hajdúchová, D., Bauer, J.
    Structure and Function of the Human RyanodineReceptors and Their Association withMyopathies?Present State, Challenges,and Perspectives.
    (2020) Molecules 25: 4040-.
  17. Farkasovsky, M.
    Septin architecture and function in budding yeast.
    (2020) Biol. Chem. 401: 903-919.
  18. Gabrisko, M.
    The in silico characterization of neutral alpha-glucosidase C (GANC) and its evolution from GANAB.
    (2020) Gene 726: 144192-.
  19. Gulshan Ara, K.Z., Manberger, A., Gabrisko, M., Linares-Pasten, J.A., Jasilionis, A., Fridjonsson, O.H., Hreggvidsson, G.O., Janecek, S., Nordberg Karlsson, E.
    Characterization and diversity of the complete set of GH family 3 enzymes from Rhodothermus marinus DSM 4253.
    (2020) Sci Rep 10: 1329-.
  20. Janecek, S., Zamocka, B.
    A new GH13 subfamily represented by the alpha-amylase from the halophilic archaeon Haloarcula hispanica.
    (2020) Extremophiles 24: 207-217.
  21. Janecek, S., Martinovicova, M.
    New groups of protein homologues in the alpha-amylase family GH57 closely related to alpha-glucan branching enzymes and 4-alpha-glucanotransferases.
    (2020) Genetica 148: 77-86.
  22. Janickova, Z., Janecek, S.
    Fungal alpha-amylases from three GH13 subfamilies: their sequence-structural features and evolutionary relationships.
    (2020) Int. J. Biol. Macromol. 159: 763-772.
  23. Kerenyiova, L., Janecek, S.
    A detailed in silico analysis of the amylolytic family GH126 and its possible relatedness to family GH76.
    (2020) Carbohydr. Res. 494: 108082-.
  24. Kerenyiova, L., Janecek, S.
    Extension of the taxonomic coverage of the family GH126 outside Firmicutes and in silico characterization of its non-catalytic terminal domains.
    (2020) 3 Biotech 10: 420-.
  25. Vozarikova, V., Kunova, N., Bauer, J., Frankovsky, J., Kotrasova, V., Prochazkova, K., Dzugasova, V., Kutejova, E., Pevala, V., Nosek, J., Tomaska, L.
    Mitochondrial HMG-Box Containing Proteins: From Biochemical Properties to the Roles in Human Diseases.
    (2020) Biomolecules 10: 1193-.
  26. Baliova, M., Jursky, F.
    Similarity of Coomassie Dye Spectral Absorbance Dynamic of Sequentially Distant Polymeric N-Terminal Segments of Glycine and GABA Transporters.
    (2019) ChemistrySelect 4: 6304 -6308.
  27. Bauer, J., Pavlovič, J., Bauerova-Hlinkova, V.
    Normal Mode Analysis as a Routine Part of a Structural Investigation.
    (2019) Molecules 24: 1-20.
  28. Janecek, S., Marecek, F., MacGregor, E.A., Svensson, B.
    Starch-binding domains as CBM families - history, occurrence, structure, function and evolution.
    (2019) Biotechnol. Adv. 37: 107451-.
  29. Jeszeova, L., Benzova, R., Glustíkova, M., Siskova, A., Kisova, Z., Plany, M., Krakova, L., Bauerova-Hlinkova, V., Pangallo, D.
    Biocleaning of historical documents: The use and characterization of bacterial enzymatic resources.
    (2019) Int. Biodeterior. Biodegrad. 140: 416-112.
  30. Ohradanova-Repic, A., Machacek, C., Donner, C., Muhlgrabner, V., Petrovcikova, E., Zahradnikova, Jr., A., Vicikova, K., Horejsi, V., Stockinger, H., Leksa, V.
    The mannose 6-phosphate/insulin-like growth factor 2 receptor mediates plasminogen-induced efferocytosis .
    (2019) J. Leukoc. Biol. 105(3): 519-530.
  31. Pevalova, Z., Pevala, V., Blunsom, N.J., Tahotna, D., Kotrasova, V., Holic, R., Pokorna, L., Bauer, J., Kutejova, E., Cockroft, S., Griac, P.
    Yeast phosphatidylinositol transfer protein Pdr17 does not require high affinity phosphatidylinositol binding for its cellular function.
    (2019) Biochim. Biophys. Acta Mol. Cell Biol. Lipids 1864: 1412-1421.
  32. Šebová, R., Bauerova-Hlinkova, V., Beck, K., Nemčovičová, I., Bauer, J., Kúdelová, M.
    Residue Mutations in Murine Herpesvirus 68 Immunomodulatory Protein M3 Reveal Specific Modulation of Chemokine Binding.
    (2019) Front. Cell. Infect. Microbiol. 9:210: 1-14.
  33. Zhang, X., Leemhuis, H., Janecek, S., Martinovicova, M., Pijning, T., van der Maarel, M.J.
    Identification of Thermotoga maritima MSB8 GH57 alpha-amylase AmyC as a glycogen-branching enzyme with high hydrolytic activity.
    (2019) Appl. Microbiol. Biotechnol. 103: 6141-6151.
  34. Abbott, W., Alber, O., Bayer, E., Berrin, J.G., Boraston, A., Brumer, H., Brzezinski, R., Clarke, A., Cobucci-Ponzano, B., Cockburn, D., Coutinho, P., Czjzek, M., Dassa, B., Davies, G.J., Janecek, S.
    Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes.
    (2018) Glycobiology 28: 3-8.
  35. Baliova, M., Jursky, F.
    Specific glycine to alanine mutation eliminates dynamic interaction of polymeric GlyT1a N-terminus with Coomassie Brilliant Blue G-250.
    (2018) Electrophoresis 39: 1357-1360.
  36. Jeszeova, L., Bauerova-Hlinkova, V., Barath, P., Puskarova, A., Buckova, M., Krakova, L., Pangallo, D.
    Biochemical and proteomic characterization of the extracellular enzymatic preparate of Exiguobacterium undae, suitable for efficient animal glue removal.
    (2018) Appl. Microbiol. Biotechnol. 102: 6525-6536.
  37. Kacerikova, R., Godocikova, J., Wang, Z., Kutejova, E., Raunser, S., Farkasovsky, M.
    Modulation of septin higher-order structure by the Cdc28 protein kinase.
    (2018) Biologia 73: 1025-1033.
  38. Kuchtova, A., Gentry, M.S., Janecek, S.
    The unique evolution of the carbohydrate-binding module CBM20 in laforin.
    (2018) FEBS Lett. 592: 586-598.
  39. Kutejova, E.
    Mitochondrial Lon protease-unique structure and essential function in mammalian cells.
    (2018) Integr Cancer Sci Therap 5: 1-2.
  40. Leksa, V., Schiller, H.B., Stockinger, H.
    Biotin-Chasing Assay to Evaluate uPAR Stability and Cleavage on the Surface of Cells.
    (2018) Methods Mol Biol. 1731: 39-47.
  41. Martinovicova, M., Janecek, S.
    In silico analysis of the alpha-amylase family GH57: eventual subfamilies reflecting enzyme specificities.
    (2018) 3 Biotech 8: 307-.
  42. Ohradanova-Repic, A., Machacek, C., Charvet, C., Lager, F., Le Roux, D., Platzer, R., Leksa, V., Mitulovic, G., Burkard, T.R., Zlabinger, G.J., Fischer, M.B., Feuillet, V., Renault, G., Blüml, S., Benko, M.
    Extracellular Purine Metabolism Is the Switchboard of Immunosuppressive Macrophages and a Novel Target to Treat Diseases With Macrophage Imbalances.
    (2018) Front Immunol 9: 852-.
  43. Petrovcikova, E., Vicikova, K., Leksa, V.
    Extracellular vesicles ? biogenesis, composition, function, uptake and therapeutic applications.
    (2018) Biologia 73: 437-448.
  44. Vicikova, K., Petrovcikova, E., Manka, P., Drach, J., Stockinger, H., Leksa, V.
    Serum and urinary levels of CD222 in cancer: origin and diagnostic value..
    (2018) Neoplasma 19: 762-768.
  45. Zwirzitz, A., Reiter, M., Skrabana, R., Ohradanova-Repic, A., Majdic, O., Gutekova, M., Cehlar, O., Petrovcikova, E., Kutejova, E., Stanek, G., Stockinger, H., Leksa, V.
    Lactoferrin is a natural inhibitor of plasminogen activation.
    (2018) J. Biol. Chem. 293: 8600-8613.
  46. Faltinova, A., Tomaskova, N., Antalik, M., Sevcik, J., Zahradnikova, A.
    The N-Terminal Region of the Ryanodine Receptor Affects Channel Activation..
    (2017) Front. Physiol. 8:443: 1-15.
  47. Janecek, S., Majzlova, K., Svensson, B., MacGregor, E.A.
    The starch-binding domain family CBM41 - an in silico analysis of evolutionary relationships.
    (2017) Proteins 85: 1480-1492.
  48. Kunova, N., Ondrovicova, G., Bauer, J., Bellova, J., Ambro, L., Martinakova, L., Kotrasova, V., Kutejova, E., Pevala, V.
    The role of Lon-mediated proteolysis in the dynamics of mitochondrial nucleic acid-protein complexes.
    (2017) Sci Rep 7(631): 1-13.
  49. Leksa, V., Ilkova, A., Vicikova, K., Stockinger, H.
    Unravelling novel functions of the endosomal transporter mannose 6-phosphate/insulin-like growth factor receptor (CD222) in health and disease: An emerging regulator of the immune system..
    (2017) Immunol. Lett. 190: 194-200.
  50. Mieog, J.C., Janecek, S., Ral, J.P.
    New insight in cereal starch degradation: identification and structural characterization of four alpha-amylases in bread wheat.
    (2017) Amylase 1: 35-49.
  51. Sarian, F.D., Janecek, S., Pijning, T., Ihsanawati, -., Nurachman, Z., Radjasa, O.K., Dijkhuizen, L., Natalia, D., van der Maarel, M.J.
    A new group of glycoside hydrolase family 13 alpha-amylases with an aberrant catalytic triad.
    (2017) Sci Rep 7: 44230-.
  52. Zamocky, M., Janecek, S., Obinger, C.
    Fungal Hybrid B heme peroxidases - unique fusions of a heme peroxidase domain with a carbohydrate-binding domain .
    (2017) Sci Rep 7 (9393): 1-12-.
  53. Janecek, S., Gabrisko, M.
    Remarkable evolutionary relatedness among the enzymes and proteins from the alpha-amylase family.
    (2016) Cell. Mol. Life Sci. 73(14): 2707-2725.
  54. Janecek, S., Svensson, B.
    Amylolytic glycoside hydrolases.
    (2016) Cell. Mol. Life Sci. 73: 2601-2602.
  55. Juhasova, A., Baliova, M., Jursky, F.
    A Dynamic Interaction of Coomassie Dye with the Glycine Transporters N-termini.
    (2016) Protein J. 35: 371-378.
  56. Kereiche, S., Kovacik, L., Bednar, J., Pevala, V., Kunova, N., Ondrovicova, G., Bauer, J., Ambro, L., Bellova, J., Kutejova, E., Raska, I.
    The N-terminal domain plays a crucial role in the structure of a full-length human mitochondrial Lon protease..
    (2016) Sci Rep 6(33631): 1-10.
  57. Kuchtova, A., Janecek, S.
    Domain evolution in enzymes of the neopullulanase subfamily.
    (2016) Microbiology-(UK) 162(12): 2099-2115.
  58. Machacek, C., Supper, V., Leksa, V., Mitulovic, G., Spittler, A., Drbal, K., Suchanek, M., Ohradanova-Repic, A., Stockinger, H.
    Folate Receptor ? Regulates Integrin CD11b/CD18 Adhesion of a Macrophage Subset to Collagen.
    (2016) J. Immunol. 197(&): 2229-2238.
  59. Pevala, V., Truban, D., Bauer, J., Kostan, J., Kunova, N., Bellova, J., Brandstetter, M., Marini, V., Krejci, L., Tomaska, L., Nosek, J., Kutejova, E.
    The structure and DNA-binding properties of Mgm101 from a yeast with a linear mitochondrial genome.
    (2016) Nucleic Acids Res. 44(5): 2227-2239.
  60. Supper, V., Schiller, H.B., Paster, W., Forster, F., Boulegue, C., Mitulovic, G., Leksa, V., Ohradanova-Repic, A., Machacek, C., Schatzlmaier, P., Zlabinger, G.J., Stockinger, H.
    Association of CD147 and Calcium Exporter PMCA4 Uncouples IL-2 Expression from Early TCR Signaling.
    (2016) J. Immunol. 196(3): 1387-1399.
  61. Baliova, M., Juhasova, A., Jursky, F.
    The elution of certain protein affinity tags with millimolar concentrations of diclofenac.
    (2015) J. Chromatogr. B 1006: 187-193.
  62. Halgasova, N., Solteszova, B., Pevala, V., Kostan, J., Kutejova, E., Bukovska, G.
    A RepA-like protein from bacteriophage BFK20 is a multifunctional protein with primase, polymerase, NTPase and helicase activities.
    (2015) Virus Res. 210: 178-187.
  63. Janecek, S., Kuchtova, A., Petrovicova, S.
    A novel GH13 subfamily of alpha-amylases with a pair of tryptophans in the helix alpha3 of the catalytic TIM-barrel, the LPDlx signature in the conserved sequence region V and a conserved aromatic motif at the C-terminus.
    (2015) Biologia 70(10): 1284-1294.
  64. Jursky, F., Baliova, M., Juhasova, A.
    Structural insights into the benzophenanthridines binding to human glycine transporter GlyT1.
    (2015) Eur. J. Pharmacol. 765: 1-6.
  65. Kuchtova, A., Janecek, S.
    In silico analysis of family GH77 with focus on amylomaltases from borreliae and disproportionating enzymes DPE2 from plants and bacteria.
    (2015) BBA-Proteins Proteomics 1854: 1260-1268.
  66. Schilter, H., Cantemir-Stone, C.Z., Leksa, V., Ohradanova-Repic, A., Findlay, A.D., Deodhar, M., Stockinger, H., Song, X., Molloy, M., Marsh, C.B., Jarolimek, W.
    The mannose-6-phosphate analogue, PXS64, inhibits fibrosis via TGF-β1 pathway in human lung fibroblasts.
    (2015) Immunol. Lett. 2(165): 90-101.
  67. Ambro, L., Pevala, V., Ondrovicova, G., Bellova, J., Kunova, N., Kutejova, E., Bauer, J.
    Mutations to a glycine loop in the catalytic site of human Lon changes its protease, peptidase and ATPase activities.
    (2014) FEBS J. 281: 1784-1797.
  68. Baliova, M., Juhasova, A., Jursky, F.
    Using a collection of MUPP1 domains to investigate similarities of neurotransmitter transporters C-terminal PDZ motifs.
    (2014) Biochem. Biophys. Res. Commun. 454(1): 25-29.
  69. Bauer, J., Ondrovicova, G., Najmanova, L., Pevala, V., Kamenik, Z., Kostan, J., Janata, J., Kutejova, E.
    Structure and possible mechanism of the CcbJ methyltransferase from Streptomyces caelestis.
    (2014) Acta Crystallogr. D 70(4): 943-957.
  70. Borko, L., Bauerova-Hlinkova, V., Hostinova, E., Gasperik, J., Beck, K.F., Lai, A.F., Zahradnikova, A., Sevcik, J.
    Structural insights into the human RyR2 N-terminal region involved in cardiac arrhythmias.
    (2014) Acta Crystallogr. D D70(11): 2897-2912.
  71. Holic, R., Simova, Z., Ashlin, T., Pevala, V., Poloncova, K., Tahotna, D., Kutejova, E., Cockroft, S., Griac, P.
    Phosphatidylinositol binding of Saccharomyces cerevisiae Pdr16p represents an essential feature of this lipid transfer protein to provide protection against azole antifungals.
    (2014) Biochim. Biophys. Acta Mol. Cell Biol. Lipids 1841(10): 1483-1490.
  72. Janecek, S., Svensson, B., MacGregor, E.A.
    Alpha-amylase: an enzyme specificity found in various families of glycoside hydrolases.
    (2014) Cell. Mol. Life Sci. 71: 1149-1170.
  73. Kereiche, S., Kovacik, L., Pevala, V., Ambro, L., Bellova, J., Kutejova, E., Raska, I.
    Three-Dimensional Reconstruction of the S885A Mutant of Human Mitochondrial Lon Protease.
    (2014) Folia Biol.-Prague 60(Suppl 1): 62-65.
  74. Majzlova, K., Janecek, S.
    Two structurally related starch-binding domain families CBM25 and CBM26.
    (2014) Biologia 69(9): 1087-1096.
  75. Mihalikova, A., Baliova, M., Jursky, F.
    Effect of phosphomimetic mutations on the C-terminal sensitivity of glycine transporter GlyT1 to calpain.
    (2014) Neurosci. Res. 81-82: 85-91.
  76. Mihalikova, A., Baliova, M., Jursky, F.
    Calcium Dependent Interaction of Calmodulin with the GlyT1 C-terminus.
    (2014) Neurochem. Res. 39(11): 2225-2233.
  77. Pace, C.N., Fu, H., Lee, F.K., Landua, J., Trevino, S.R., Schell, D., Thurlkill, R.L., Imura, S., Scholtz, J.M., Gajiwala, K., Sevcik, J., Urbanikova, L., Myers, J.K., Takano, K., Hebert, E.J.
    Contribution of hydrogen bonds to protein stability.
    (2014) Protein Sci. 23(5): 652-661.
  78. Pfisterer, K., Forster, F., Paster, W., Supper, V., Ohradanova-Repic, A., Eckerstorfer, P., Zwirzitz, A., Donner, C., Boulegue, C., Schiller, H.B., Ondrovicova, G., Acuto, O., Stockinger, H., Leksa, V.
    The Late Endosomal Transporter CD222 Directs the Spatial Distribution and Activity of Lck..
    (2014) J. Immunol. 193(6): 2718-2732.
  79. Ranjani, V., Janecek, S., Chai, K.P., Shahir, S., Raja Abd Rahman, R.N., Chan, K.G., Goh, K.M.
    Protein engineering of selected residues from conserved sequence regions of a novel Anoxybacillus alpha-amylase.
    (2014) Sci Rep 4: 5850-.
  80. Blesak, K., Janecek, S.
    Two potentially novel amylolytic enzyme specificities in the prokaryotic glycoside hydrolase alpha-amylase family GH57.
    (2013) Microbiology-(UK) 159: 2584-2593.
  81. Borko, L., Kostan, J., Zahradnikova, A., Pevala, V., Gasperik, J., Hostinova, E., Urbanikova, L., Djinović-Carugo, K., Bauerova-Hlinkova, V., Sevcik, J.
    Human Cardiac Ryanodine Receptor: Preparation, Crystallization and Preliminary X-ray Analysis of the N-terminal Region.
    (2013) Protein Pept. Lett. 20(11): 1211-1216.
  82. Faltinova, A., Zahradnikova, A.
    Modification of cardiac RYR2 gating by a peptide from the central domain of the RYR2.
    (2013) Cent. Eur. J. Biol. 8(12): 1164-1171.
  83. Jursky, F., Baliova, M.
    Expression and purification of recombinant calpain-derived N-terminal peptides from glycine transporter GlyT2 .
    (2013) Protein Expr. Purif. 88(1): 143-149.
  84. Kadlcik, S., Kucera, T., Chalupska, D., Gazak, R., Koberska, M., Ulanova, D., Kopecky, J., Kutejova, E., Najmanova, L., Janata, J.
    Adaptation of an L-Proline Adenylation Domain to Use 4- Propyl-L-Proline in the Evolution of Lincosamide Biosynthesis.
    (2013) PLoS One 8: e84902-.
  85. Kucera, T., Otyepka, M., Matuskova, A., Samad, A., Kutejova, E., Janata, J.
    A Computational Study of the Glycine-Rich Loop of Mitochondrial Processing Peptidase.
    (2013) PLoS One 8: e74518-.
  86. Majzlova, K., Pukajova, Z., Janecek, S.
    Tracing the evolution of the alpha-amylase subfamily GH13_36 covering the amylolytic enzymes intermediate between oligo-1,6-glucosidases and neopullulanases.
    (2013) Carbohydr. Res. 367: 48-57.
  87. Najmanova, L., Kutejova, E., Kadlec, J., Polan, M., Olsovska, J., Benada, O., Novotna, J., Kamenik, Z., Halada, P., Bauer, J., Janata, J.
    Characterization of N-Demethyllincosamide Methyltransferases LmbJ and CcbJ.
    (2013) ChemBioChem 14: 2259-2262.
  88. Novotna, J., Olsovska, J., Novak, P., Mojzes, P., Chaloupkova, R., Kamenik, Z., Spizek, J., Kutejova, E., Mareckova, M., Tichy, P., Damborsky, J., Janata, J.
    Lincomycin Biosynthesis Involves a Tyrosine Hydroxylating Heme Protein of an Unusual Enzyme Family.
    (2013) PLoS One 8(12): e79974-.
  89. Pancik, P., Bauerova-Hlinkova, V., Kudelova, M.
    Purification of recombinant M3 proteins of murine gammaherpesviruses 68 and 72 expressed in Escherichia coli.
    (2013) Acta Virol. 57: 59-68.
  90. Puspasari, F., Radjasa, O.K., Noer, A.S., Nurachman, Z., Syah, Y.M., van der Maarel, M.J., Dijkhuizen, L., Janecek, S., Natalia, D.
    Raw starch–degrading alpha-amylase from Bacillus aquimaris MKSC 6.2: isolation and expression of the gene, bioinformatics and biochemical characterization of the recombinant enzyme.
    (2013) J. Appl. Microbiol. 114: 108-120.
  91. Ambro, L., Pevala, V., Bauer, J., Kutejova, E.
    The influence of ATP-dependent proteases on a variety of nucleoid-associated processes.
    (2012) J. Struct. Biol. 179: 181-192.
  92. Blesak, K., Janecek, S.
    Sequence fingerprints of enzyme specificities from the glycoside hydrolase family GH57.
    (2012) Extremophiles 16(3): 497-506.
  93. Janecek, S., Kuchtova, A.
    In silico identification of catalytic residues and domain fold of the family GH119 sharing the catalytic machinery with the alpha-amylase family GH57.
    (2012) FEBS Lett. 586(19): 3360-3366.
  94. Jung, T.Y., Li, D., Park, J.T., Yoon, S.M., Tran, P.L., Oh, B.H., Janecek, S., Park, S.G., Woo, E.J., Park, K.H.
    Association of novel domain in active site of archaic hyperthermophilic maltogenic amylase from Staphylothermus marinus.
    (2012) J. Biol. Chem. 278(11): 7979-7989.
  95. Jursky, F., Baliova, M., Mihalikova, A.
    Molecular basis for differential glycine transporters sensitivity to sanguinarine .
    (2012) Toxicol. Lett. 212(3): 262-267.
  96. Leksa, V., Pfisterer, K., Ondrovicova, G., Binder, B., Lakatošová, S., Donner, C., Schiller, H.B., Zwirzitz, A., Mrvová, K., Pevala, V., Kutejova, E., Stockinger, H.
    Dissecting Mannose 6-Phosphate-Insulin-like Growth Factor 2 Receptor Complexes That Control Activation and Uptake of Plasminogen in Cells.
    (2012) J. Biol. Chem. 287(27): 22450-22462.
  97. Sedlacek, J., Fabry, M., Sieglova, I., Kral, V., Uhnakova, B., Mudra, M., Kronrad, L., Sawicka, A., Mikolajczak, R., Rezacova, P.
    Recombinant fragment of an antibody tailored for direct radioiodination.
    (2012) J. Label. Compd. Radiopharm. 55(1): 52-56.
  98. Skrabana, R., Cehlar, O., Flachbartova, Z., Kovac, A., Sevcik, J., Novak, M.
    Crystallization and preliminary X-ray diffraction analysis of two peptides from Alzheimer PHF in complex with the MN423 antibody Fab fragment.
    (2012) Acta Crystallographica Sect. F-Struct. Biol. Cryst. Commun. 68(10): 1186-1190.
  99. Janecek, S., Blesak, K.
    Sequence-structural features and evolutionary relationships of family GH57 alpha-amylases and their putative alpha-amylase-like homologues.
    (2011) Protein J. 30(6): 429-435.
  100. Janecek, S., Svensson, B., MacGregor, E.A.
    Structural and evolutionary aspects of two families of non-catalytic domains present in starch and glycogen binding proteins from microbes, plants and animals.
    (2011) Enzyme Microb. Technol. 49(5): 429-440.
  101. Jursky, F., Baliova, M.
    Differential effect of the benzophenanthridine alkaloids sanguinarine and chelerythrine on glycine transporters.
    (2011) Neurochem. Int. 58: 641-647.
  102. Leksa, V., Loewe, R., Binder, B., Schiller, H.B., Eckerstorfer, P., Forster, F., Soler-Cardona, A., Ondrovicova, G., Kutejova, E., Steinhuber, A., Breuss, J., Drach, J., Petzelbauer, P., Binder, B.R., Stockinger, H.
    Soluble M6P/IGF2R released by TACE controls angiogenesis via blocking plasminogen activation. .
    (2011) Circ.Res. 108(6): 676-685.
  103. Baliova, M., Jursky, F.
    Calcium dependent modification of distal C-terminal sequences of glycine transporter GlyT1.
    (2010) Neurochem. Int. 57: 254-261.
  104. Dvoráková-Holá, K., Matuskova, A., Kubala, M., Otyepka, M., Kucera, T., Vecer, J., Herman, P., Parkhomenko, N., Kutejova, E., Janata, J.
    Glycine-rich loop of mitochondrial processing peptidase alpha-subunit is responsible for substrate recognition by a mechanism analogous to mitochondrial receptor Tom20..
    (2010) J. Mol. Biol. 396(5): 1197-1210.
  105. García-Nafría, J., Ondrovicova, G., Blagova, E., Levdikov, V.M., Bauer, J., Suzuki, C.K., Kutejova, E., Wilkinson, A.J., Wilson, K.S.
    Structure of the catalytic domain of the human mitochondrial Lon protease: Proposed relation of oligomer formation and activity.
    (2010) Protein Sci. 19(5): 987-999.
  106. Godany, A., Majzlova, K., Horvathova, V., Vidova, B., Janecek, S.
    Tyrosine 39 of GH13 alpha-amylase from Thermococcus hydrothermalis contributes to its thermostability.
    (2010) Biologia 65(3): 408-415.
  107. Hostinova, E., Janecek, S., Gasperik, J.
    Gene sequence, bioinformatics and enzymatic characterization of alpha-amylase from Saccharomycopsis fibuligera KZ.
    (2010) Protein J. 29(5): 355-364.
  108. Baliova, M., Knab, A., Franekova, V., Jursky, F.
    Modification of the cytosolic regions of GABA transporter GAT1 by calpain.
    (2009) Neurochem. Int. 55(5): 288-294.
  109. Christiansen, C., Abou Hachem, M., Janecek, S., Viksoe-Nielsen, A., Blennow, A., Svensson, B.
    The carbohydrate-binding module family 20 – diversity, structure, and function.
    (2009) FEBS J. 276(18): 5006-5029.
  110. Gabrisko, M., Janecek, S.
    Looking for the ancestry of the heavy-chain subunits of heteromeric amino acid transporters rBAT and 4F2hc within the GH13 alpha-amylase family.
    (2009) FEBS J. 276(24): 7265-7278.
  111. Muhammad, A., Schiller, H.B., Forster, H.H., Eckerstorfer, P., Geyeregger, R., Leksa, V., Zlabinger, G.J., Sibilia, M., Sonnleitner, A., Paster, W., Stockinger, H.
    Sequential Cooperation of CD2 and CD48 in the Buildup of the Early TCR Signalosome.
    (2009) J. Immunol. 182(12): 7672-7680.
  112. Probst, O.C., Puxbaum, V., Svoboda, B., Leksa, V., Stockinger, H., Mikula, M., Mikulits, W., Mach, L.
    The mannose 6-phosphate/insulin-like growth factor II receptor restricts the tumourigenicity and invasiveness of squamous cell carcinoma cells..
    (2009) Int. J. Cancer 124(11): 2559-2567.
  113. Schiller, H.B., Szekeres, A., Binder, B.R., Stockinger, H., Leksa, V.
    Mannose 6-phosphate/insulin-like growth factor 2 receptor limits cell invasion by controlling alphaVbeta3 integrin expression and proteolytic processing of urokinase-type plasminogen activator receptor..
    (2009) Mol. Biol. Cell 20(3): 745-756.
  114. Franekova, V., Baliova, M., Jursky, F.
    Truncation of human dopamine transporter by protease calpain.
    (2008) Neurochem. Int. 52: 1436-1441.
  115. Godany, A., Vidova, B., Janecek, S.
    The unique glycoside hydrolase family 77 amylomaltase from Borrelia burgdorferi with only catalytic triad conserved.
    (2008) FEMS Microbiol. Lett. 284(1): 84-91.
  116. Hlinkova, V., Xing, G.X., Bauer, J., Shin, Y.J., Dionne, I., Rajashankar, K.R., Bell, S.D., Ling, H.
    Structures of monomeric, dimeric and trimeric PCNA: PCNA-ring assembly and opening.
    (2008) Acta Crystallogr. D D64: 941-949.
  117. Khunkaewla, P., Schiller, H.B., Paster, W., Leksa, V., Cermák, L., Andera, L., Horejsi, V., Stockinger, H.
    LFA-1-mediated leukocyte adhesion regulated by interaction of CD43 with LFA-1 and CD147.
    (2008) Mol. Immunol. 45(6): 1703-1711.
  118. Smid, O., Matuskova, A., Harris, S.R., Kucera, T., Novotny, M., Horvathova, V., Hrdy, I., Kutejova, E., Hirt, R.P., Embley, M., Janata, J., Tachezy, J.
    Reductive Evolution of the Mitochondrial Processing Peptidases of the Unicellular Parasites Trichomonas vaginalis and Giardia intestinalis.
    (2008) PLoS Pathog. 4(12): e1000243-.
  119. Janecek, S., Svensson, B., MacGregor, E.A.
    A remote but significant sequence homology between glycoside hydrolase clan GH-H and family GH31.
    (2007) FEBS Lett. 581(7): 1261-1268.
  120. Jiang, Z., Li, B., Jursky, F., Shen, W.
    Differential distribution of glycine transporters in Muller cells and neurons in amphibian retinas.
    (2007) Visual Neurosci. 24(2): 157-168.
  121. Lu, B., Yadav, S., Shah, P.G., Liu, T., Tian, B., Pukszta, S., Villaluna, N., Kutejova, E., Newlon, C.S., Santos, J.H., Suzuki, C.K.
    Roles for the Human ATP-dependent Lon Protease in Mitochondrial DNA Maintenance.
    (2007) J. Biol. Chem. 282(24): 17363-17374.
  122. van der Kaaij, R.M., Janecek, S., van der Maarel, M.J., Dijkhuizen, L.
    Phylogenetic and biochemical characterization of a novel cluster of intracellular fungal alpha-amylase enzymes.
    (2007) Microbiology-(UK) 153(12): 4003-4015.
  123. Csokova, N., Skrabana, R., Urbanikova, L., Kovacech, B., Popov, A., Sevcik, J., Novak, M.
    Preparation, crystallization and preliminary X-ray analysis of the Fab fragment of monoclonal antibody MN423, revealing the structural aspects of Alzheimer’s paired helical filaments.
    (2006) Protein Pept. Lett. 13(9): 941-944.
  124. Machovic, M., Janecek, S.
    The evolution of putative starch-binding domains.
    (2006) FEBS Lett. 580(27): 6349-6356.
  125. Machovic, M., Janecek, S.
    Starch-binding domains in the post-genome era.
    (2006) Cell. Mol. Life Sci. 63(23): 2710-2721.
  126. Baliova, M., Jursky, F.
    Calpain Sensitive Regions in the N-terminal Cytoplasmic Domains of Glycine Transporters GlyT1A and GlyT1B.
    (2005) Neurochem. Res. 30: 1093-1100.
  127. Leksa, V., Godar, S., Schiller, H.B., Feurtbauer, E., Muhammad, A., Slezakova, K., Horejsi, V., Steinstein, P., Weidle, U.H., Binder, B.R., Stockinger, H.
    TGF-beta-induced apoptosis in endothelial cells mediated by M6P/IGFII-R and mini-plasminogen.
    (2005) J. Cell Sci. 118(19): 4577-4586.
  128. Machovic, M., Svensson, B., MacGregor, E.A., Janecek, S.
    A new clan of CBM families based on bioinformatics of starch-binding domains from families CBM20 and CBM21.
    (2005) FEBS J. 272(21): 5497-5513.
  129. Ondrovicova, G., Liu, T., Singh, K., Tian, B., Li, H., Gakh, O., Perecko, D., Janata, J., Granot, Z., Orly, J., Kutejova, E., Suzuki, C.K.
    Cleavage site selection within a folded substrate by the mitochondrial ATPdependent Lon protease.
    (2005) J. Biol. Chem. 280: 25103-25110.
  130. Alston, R.W., Urbanikova, L., Sevcik, J., Lasagna, M., Reinhart, G.D., Scholtz, J.M., Pace, C.N.
    Contribution of single tryptophan residues to the fluorescence and stability of ribonuclease Sa.
    (2004) Biophys. J. 87: 4036-4047.
  131. Baliova, M., Betz, H., Jursky, F.
    Calpain-mediated proteolytic cleavage of the neuronal glycine transporter, GlyT2.
    (2004) J. Neurochem. 88: 227-232.
  132. Baliova, M., Jursky, F.
    Use of calpain for native GlyT2 N-terminal region separation and its potential use in transporter N-terminus interaction studies.
    (2004) Biologia 59(6): 839-842.
  133. Baliova, M., Jursky, F.
    Phosphatase inhibitors influence proteolytic cleavage pattern of Glycine transporter GlyT2 N-terminus.
    (2004) Biologia 59(6): 843-845.
  134. Janata, J., Hola, K., Kubala, M., Gakh, O., Parkhomenko, N., Matuskova, A., Kutejova, E., Amler, E.
    Substrate evokes translocation of both domains in the mitochondrial processing peptidase alpha-subunit during which the C-terminus acts as a stabilizing element.
    (2004) Biochem. Biophys. Res. Commun. 316(1): 211-217.
  135. Liu, T., Lu, B., Lee, I., Ondrovicova, G., Kutejova, E., Suzuki, C.K.
    DNA and RNA binding by the mitochondrial Lon protease is regulated by nucleotide and protein substrate.
    (2004) J. Biol. Chem. 279: 13902-13910.
  136. Sevcik, J., Urbanikova, L., Kostan, J., Janda, L., Wiche, G.
    Actin-binding domain of mouse plectin: crystal structure and binding to vimentin.
    (2004) Eur. J. Biochem. 271: 1873-1884.
  137. Stahlberg, H., Kutejova, E., Muchova, K., Gregorini, M., Lustig, A., Muller, S.A., Olivieri, V., Engel, A., Wilkinson, A.J., Barak, I.
    Oligomeric structure of the Bacillus subtilis cell division protein DivIVA determined by transmission electron microscopy.
    (2004) Mol. Microbiol. 52: 1281-1290.
  138. Zona, R., Chang-Pi-Hin, F., O'Donohue, M.J., Janecek, S.
    Bioinformatics of the family 57 glycoside hydrolases and identification of catalytic residues in amylopullulanase from Thermococcus hydrothermalis.
    (2004) Eur. J. Biochem. 271(14): 2863-2872.
  139. Horecka, T., Perecko, D., Kutejova, E., Mikulasova, D., Kollarova, M.
    The activities of the two thioredoxins from Streptomyces aureofaciens are not interchangeable.
    (2003) J. Basic Microbiol. 43(1): 62-67.
  140. Janecek, S., Svensson, B., MacGregor, E.A.
    Relation between domain evolution, specificity, and taxonomy of the a-amylase family members containing a C-terminal starch-binding domain.
    (2003) Eur. J. Biochem. 270(4): 635-345.
  141. Janecek, S.
    A motif of a microbial starch-binding domain found in human genethonin.
    (2002) Bioinformatics 18(11): 1534-1537.
  142. Janecek, S.
    How many conserved sequence regions are there in the alpha-amylase family?.
    (2002) Biologia 57(Suppl. 11): 29-41.
  143. Mertova, J., Almasiova, M., Perecko, D., Bilka, F., Benesova, M., Bezakova, L., Psenak, M., Kutejova, E.
    ATP-dependent Lon protease from maize mitochondria - comparison with the other Lon proteases.
    (2002) Biologia 57(6): 739-745.
  144. Oslancova, A., Janecek, S.
    Oligo-1,6-glucosidase and neopullulanase enzyme subfamilies from the a-amylase family defined by the fifth conserved sequence region.
    (2002) Cell. Mol. Life Sci. 59(11): 1945-1959.
  145. Sevcik, J., Urbanikova, L., Leland, P.A., Raines, R.T.
    X-ray structure of two crystalline forms of a Streptomycete ribonuclease with cytotoxic activity.
    (2002) J. Biol. Chem. 277: 47325-47330.
  146. Urbanikova, L., Janda, L., Popov, A., Wiche, G., Sevcik, J.
    Purification, crystallization and preliminary X-ray analysis of the plectin actin binding domain.
    (2002) Acta Crystallogr. D 58: 1368-1370.
  147. MacGregor, E.A., Janecek, S., Svensson, B.
    Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes.
    (2001) Biochim. Biophys. Acta 1546(1): 1-20.
  148. Pace, C.N., Horn, G., Hebert, E.J., Bechert, J., Shaw, K., Urbanikova, L., Scholtz, J.M., Sevcik, J.
    Tyrosine Hydrogen Bonds Make a Large Contribution to Protein Stability.
    (2001) J. Mol. Biol. 312: 393-404.
  149. Janecek, S., Svensson, B., Russell, R.R.
    Location of repeat elements in glucansucrases of Leuconostoc and Streptococcus species.
    (2000) FEMS Microbiol. Lett. 192(1): 53-57.
  150. Janecek, S., Sevcik, J.
    The evolution of starch-binding domain.
    (1999) FEBS Lett. 456(1): 119-125.
  151. Janecek, S., Leveque, E., Belarbi, A., Haye, B.
    Close evolutionary relatedness of alpha-amylases from Archaea and plants.
    (1999) J. Mol. Evol. 48(4): 421-426.
  152. Stahlberg, H., Kutejova, E., Suda, K., Wolpensinger, B., Lustig, A., Schatz, G., Engel, A., Suzuki, C.K.
    Mitochondrial Lon of Saccharomyces cerevisiae is a ring-shaped protease with seven flexible subunits.
    (1999) Proc. Natl. Acad. Sci. U. S. A. 96: 6787-6790.
  153. Sevcik, J., Urbanikova, L., Dauter, Z., Wilson, K.S.
    Recognition of RNase Sa by the inhibitor barstar: Crystal structure of the complex at 1.7 A resolution.
    (1998) Acta Crystallogr. D 54: 954-963.
  154. Urbanikova, L., Sevcik, J.
    Crystallization and preliminary X-ray investigation of the complex of RNase Sa with wild-type barstar.
    (1998) Acta Crystallogr. D 54: 403-404.
  155. Urbanikova, L., Sevcik, J.
    Crystal structure of the complex RNase Sa - barstar at 1.7 A resolution.
    (1998) Gen. Physiol. Biophys. 17: 12-15.
  156. van Dijl, J.M., Kutejova, E., Suda, K., Perecko, D., Schatz, G., Suzuki, C.K.
    The ATPase and protease domains of yeast mitochondrial Lon: roles in proteolysis and respiration-dependent growth.
    (1998) Proc. Natl. Acad. Sci. U. S. A. 95: 10584-10589.
  157. Janecek, S., Svensson, B., Henrissat, B.
    Domain evolution in the alpha-amylase family.
    (1997) J. Mol. Evol. 45(3): 322-331.
  158. Janecek, S.
    Alpha-amylase family: molecular biology and evolution.
    (1997) Prog. Biophys. Mol. Biol. 67(1): 67-97.
  159. Benesova, M., Durcova, G., Kuzela, S., Kutejova, E., Psenak, M.
    Spinach chloroplast ATP-dependent endopeptidase Ti-like protease .
    (1996) Phytochemistry 41: 65-69.
  160. Janecek, S., MacGregor, E.A., Svensson, B.
    Characteristic differences in the primary structure allow discrimination of cyclodextrin glucanotransferases from alpha-amylases.
    (1995) Biochem J. 305(2): 685-686.
  161. Suzuki, C.K., Kutejova, E., Suda, K.
    Analysis and purification of ATP-dependent mitochondrial lon protease of Saccharomyces cerevisiae.
    (1995) Methods Enzymol. 260: 486-494.
  162. Halgasova, N., Kutejova, E., Timko, J.
    Purification and some characteristics of the acetylxylan esterase from Schizophyllum commune.
    (1994) Biochem J. 298: 751-755.
  163. Janecek, S.
    Sequence similarities and evolutionary relationships of microbial, plant and animal alpha-amylases.
    (1994) Eur. J. Biochem. 224(2): 519-524.
  164. Janecek, S.
    Parallel beta/alpha-barrels of alpha-amylase, cyclodextrin glycosyltransferase and oligo-1,6-glucosidase versus the barrel of beta-amylase: evolutionary distance is a reflection of unrelated sequences.
    (1994) FEBS Lett. 353(2): 119-123.
  165. Kutejova, E., Durcova, G., Surovkova, E., Kuzela, S.
    Yeast mitochondrial ATP-dependent protease: purification and comparison with the homologous rat enzyme and the bacterial ATP-dependent protease La.
    (1993) FEBS Lett. 329: 47-50.
  166. Vanat, I., Pristas, P., Kutejova, E., Judova, J., Godany, A., Javorsky, P.
    SbvI restriction endonuclease from Streptococcus bovis.
    (1993) Lett. Appl. Microbiol. 17(6): 297-299.
  167. Janecek, S.
    New conserved amino acid region of alpha-amylases in the third loop of their (beta/alpha)8-barrel domains.
    (1992) Biochem J. 288(3): 1069-1070.