Dr. Eva Kutejova

head of department

ATP-dependent proteases in mitochondria

Mitochondria play important roles in various cellular functions, including cell differentiation and cell death processes. Therefore, mitochondrial dysfunction could contribute to aging and pathogenesis of several neurodegenerative diseases and cancer. Mitochondrial proteases and chaperones control key steps of mitochondrial biogenesis by folding and proteolytic processing of many regulatory proteins. Our research focuses on biochemical, molecular and structural analyses of the properties of mitochondrial chaperones and ATP-dependent AAA proteases, the control of the nucleoid complex assembly, proteolytic processes regulating mitochondrial dynamics, and the influence of post-translational protein modifications (succinylation, phosphorylation) on mitochondrial biogenesis using yeast S. cerevisiae and human cells as model organisms.

Septin - cell division

Our work also focuses on the mechanisms of cell division regulation 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.

Study of mitophagy and apoptosis

In our work, we use the yeast S. cerevisiae as a model eukaryotic organism in a search of an answer to the question of how Mmi1/TCTP proteins interact with mitochondria and regulate the mitophagy of these organelles and apoptosis.

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.

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. 

The working group of protein crystallography and molecular dynamics is dedicated to two fundamental projects:

• Study of the structure and function of the human ryanodine receptor 2
• Study of the structure and function of industrially interesting enzymes used in biosensors

Both projects are approached primarily by combining in vitro laboratory experiments with an in silico analyses with the aim of obtaining a comprehensive view of the studied proteins.

Study of the structure and function of the human ryanodine receptor 2 

Regular heart activity is one of the basic physiological functions necessary for human life. The protein that plays a key role in this process is ryanodine receptor 2 (hRyR2), which is expressed primarily in the myocardium. It is the largest known calcium channel to date, which mediates the release of calcium from the sarcoplasmic reticulum into the cytoplasm. An increase in the concentration of Ca²⁺ in the cytoplasm of myocytes causes a cascade of reactions that condition regular cardiac activity. Incorrect function of the RyR2 channel in humans causes serious heart diseases - arrhythmias (CPVT1, ARVC/D2, SIDS, SUO). Recently, hRyR2 dysfunction has also been found to be associated with colon cancer.

In our laboratory, we study the structure and function of hRyR2 using bioinformatics, proteomics, molecular and structural biology, and biophysics. An important milestone on this path was the determination of the structure of the N-terminal domain of hRyR2 by X-ray structural and SAXS analysis. In addition, we prepared and characterized several mutants in this domain that are associated with the above-mentioned diseases. We also deal with the effect of dantrolene - a muscle relaxant standardly used in the treatment of malignant hyperthermia, and its binding to hRyR2.

Study of the structure and function of industrially interesting enzymes used in biosensors

This project deals primarily with the enzyme glucoseoxidase (GOx), which cleaves the glucose into gluconolactone and hydrogen peroxide. Because of its fast digestion, GOx has also been labeled as "the Ferrari" of the oxidoreductases. In our laboratory, we have determined the tertiary structure of GOx in both native and mutant form and we are also studying the effect of various modulators on its activity and stability.

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.

Staff

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

• Covid-19 and long covid at the molecular level - biomarkers, tools and targets for diagnosis and therapy.
  (09I03-03-V02-00047, Sep 2023 - Aug 2027)
  Principal investigator: Vladimír Leksa
• Interaction between proteases, chaperones and kinases in stress condition cause by pathological conditions.
  (APVV-19-0298, Jul 2000 - Jun 2024)
  Principal investigator: Eva Kutejová
• Interaction of Mmi1/TCTP protein with mitochondria.
  (SK-CZ-RD-21-0104, Jul 2022 - Jun 2025)
  Principal investigator: Vladimír Pevala
• LACTOFERRIN AND LACTOFERRICIN AS NATURAL PLASMIN INHIBITORS: FROM THE STRUCTURE RESOLUTION TO THERAPEUTIC APPLICATIONS.
  (2/0152/21, Jan 2021 - Dec 2024)
  Principal investigator: Vladimír Leksa
• Regulation of the interaction specificity of muti-PDZ proteins. .
  (2/0127/21, Jan 2021 - Dec 2024)
  Principal investigator: Martina Baliová
• The double-edged sword of the plasminogen system: From homeostasis maintenance to COVID-19.
  (APVV-20-0513, Aug 2021 - Jun 2025)
  Principal investigator: Vladimír Leksa
• The stipend for a scientist threatened by the war in Ukraine .
  (09I03-03-V01-00113, Jan 2023 - Dec 2025)
  Principal investigator: Tetiana Moskalets

Selected Publications

1. Kunova, N., Ondrovicova, G., Bauer, J., Krajcovicova, V., Pinkas, M., Stojkovicova, B., Havalova, H., Lukacova, V., Kohutova, L., Kostan, J., Martinakova, L., Barath, P., Kereiche, S., Kutejova, E., Pevala, V.
   Polyphosphate and tyrosine phosphorylation in the N-terminal domain of the human mitochondrial Lon protease disrupts its functions.
   (2024) Sci Rep 1: 1-.
2. Photenhauer, A.L., Villafuerte-Vega, R.C., Cerqueira, F.M., Armbruster, K.M., Marecek, F., Chen, T., Wawrzak, Z., Hopkins, J.B., Vander Kooi, C.W., Janecek, S., Ruotolo, B.T., Koropatkin, N.M.
   The Ruminococcus bromii amylosome protein Sas6 binds single and double helical alpha-glucan structures in starch.
   (2024) Nat. Struct. Mol. Biol. 31(2): 255-265.
3. Baliova, M., Jahodová, I., Jursky, F.
   A Significant Difference in Core PDZ Interactivity of SARS-CoV, SARS-CoV2 and MERS-CoV Protein E Peptide PDZ Motifs In Vitro.
   (2023) Protein J. 42: 253-262.
4. Jahodová, I., Baliova, M., Jursky, F.
   PDZ interaction of the GABA transporter GAT1 with the syntenin-1 in Neuro-2a cells..
   (2023) Neurochem. Int. 165: 105522-.
5. Janecek, S., Brumer, H., Henrissat, B.
   News, trends, and challenges in Carbohydrate-Active enZymes.
   (2023) Biologia 78(7): 1739-1740.
6. Janecek, S.
   Advances in amylases - what's going on?.
   (2023) Molecules 28: 7268-.
7. Leksa, V.
   Milky way of immunity - galactic functions of lactoferrin in host defence (meeting abstract).
   (2023) Eur. J. Immunol. 53(SI): 48-48.
8. Magyar, Z.E., Bauer, J., Bauerova-Hlinkova, V., Jóna, I., Gaburjakova, J., Gaburjakova, M., Almássy, J.
   Eu3+ detects two functionally distinct luminal Ca2+ binding sites in ryanodine receptors.
   (2023) Biophys. J. 122(17): 3516-3531.
9. Meskova, K., Martonova, K., Hrasnova, P., Sinska, K., Skrabanova, M., Fialova, L., Njemoga, S., Cehlar, O., Parmar, O., Kolenko, P., Pevala, V., Skrabana, R.
   Cost-Effective Protein Production in CHO Cells Following Polyethylenimine-Mediated Gene Delivery Showcased by the Production and Crystallization of Antibody Fabs.
   (2023) Antibodies 12: 51-.
10. Ohradanova-Repic, A., Praženicová, R., Gebetsberger, L., Moskalets, T., Skrabana, R., Cehlar, O., Tajti, G., Stockinger, H., Leksa, V.
    Time to Kill and Time to Heal: The Multifaceted Role of Lactoferrin and Lactoferricin in Host Defense.
    (2023) Pharmaceutics 15(4): 1056-.
11. Polacek, A., Janecek, S.
    Sequence-structural features and evolution of the alpha-amylase family GH119 revealed by the in silico analysis of its relatedness to the family GH57.
    (2023) Biologia 78(7): 1847-1860.
12. Stastny, D., Petriskova, L., Tahotna, D., Bauer, J., Pokorna, L., Holic, R., Valachovic, M., Pevala, V., Cockroft, S., Griac, P.
    Yeast Sec14-like lipid transfer proteins Pdr16 and Pdr17 bind and transfer lanosterol in addition to phosphatidylinositol.
    (2023) FEBS Lett. 597(4): 504-514.
13. Wang, Y., Wu, Y., Christensen, S.J., Janecek, S., Bai, Y., Moeller, M.S., Svensson, B.
    Impact of starch binding domain fusion on activities and starch product structure of 4-alpha-glucanotransferase.
    (2023) Molecules 28: 1320-.
14. Bauer, J., Zamocka, M., Majtan, J., Bauerova-Hlinkova, V.
    Glucose Oxidase, an Enzyme "Ferrari": Its Structure, Function, Production and Properties in the Light of Various Industrial and Biotechnological Applications.
    (2022) Biomolecules 12: 472-.
15. Janecek, S., Svensson, B.
    How many alpha-amylase GH families are there in the CAZy database?.
    (2022) Amylase 6: 1-10.
16. 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.
17. Marecek, F., Janecek, S.
    A novel subfamily GH13_46 of the alpha-amylase family GH13 represented by the cyclomaltodextrinase from Flavobacterium sp. No. 92.
    (2022) Molecules 27: 8735-.
18. Ohradanova-Repic, A., Skrabana, R., Gebetsberger, L., Tajti, G., Barath, P., Ondrovicova, G., Praženicová, R., Jantova, N., Hrasnova, P., Stockinger, H., Leksa, V.
    Blockade of TMPRSS2-mediated priming of SARS-CoV-2 by lactoferricin.
    (2022) Front Immunol Aug 23;13(958581): online-.
19. Bauer, J., Žoldák, G.
    Interpretation of Single-Molecule Force Experiments on Proteins Using Normal Mode Analysis.
    (2021) Nanomaterials 11: 2795-.
20. 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.
21. 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-.
22. 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-.
23. 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-.
24. 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.
25. 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-.
26. 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-.
27. Urbanikova, L.
    CE16 acetylesterases: in silico analysis, catalytic machinery prediction and comparison with related SGNH hydrolases.
    (2021) 3 Biotech 11: 84-.
28. Baliova, M., Jursky, F.
    Comparison of SynCAM1/CADM1 PDZ interactions with MUPP1 using mammalian and bacterial pull-down systems.
    (2020) Brain Behav. 10: e01587-.
29. 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.
30. Baliova, M., Jursky, F.
    Phosphorylation of Serine 157 Protects the Rat Glycine Transporter GlyT2 from Calpain Cleavage.
    (2020) J. Mol. Neurosci. 70: 1216-1224.
31. 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.
32. 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-.
33. Farkasovsky, M.
    Septin architecture and function in budding yeast.
    (2020) Biol. Chem. 401: 903-919.
34. Gabrisko, M.
    The in silico characterization of neutral alpha-glucosidase C (GANC) and its evolution from GANAB.
    (2020) Gene 726: 144192-.
35. 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-.
36. Janecek, S., Zamocka, B.
    A new GH13 subfamily represented by the alpha-amylase from the halophilic archaeon Haloarcula hispanica.
    (2020) Extremophiles 24: 207-217.
37. 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.
38. 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.
39. 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-.
40. 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-.
41. 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-.
42. 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.
43. Bauer, J., Pavlovič, J., Bauerova-Hlinkova, V.
    Normal Mode Analysis as a Routine Part of a Structural Investigation.
    (2019) Molecules 24: 1-20.
44. 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-.
45. 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.
46. 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.
47. 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.
48. 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.
49. 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.
50. 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.
51. 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.
52. 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.
53. 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.
54. Kuchtova, A., Gentry, M.S., Janecek, S.
    The unique evolution of the carbohydrate-binding module CBM20 in laforin.
    (2018) FEBS Lett. 592: 586-598.
55. Kutejova, E.
    Mitochondrial Lon protease-unique structure and essential function in mammalian cells.
    (2018) Integr Cancer Sci Therap 5: 1-2.
56. 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.
57. Martinovicova, M., Janecek, S.
    In silico analysis of the alpha-amylase family GH57: eventual subfamilies reflecting enzyme specificities.
    (2018) 3 Biotech 8: 307-.
58. 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-.
59. Petrovcikova, E., Vicikova, K., Leksa, V.
    Extracellular vesicles ? biogenesis, composition, function, uptake and therapeutic applications.
    (2018) Biologia 73: 437-448.
60. 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.
61. 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.
62. 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.
63. 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.
64. 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.
65. 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.
66. 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.
67. 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-.
68. 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-.
69. 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.
70. Janecek, S., Svensson, B.
    Amylolytic glycoside hydrolases.
    (2016) Cell. Mol. Life Sci. 73: 2601-2602.
71. Juhasova, A., Baliova, M., Jursky, F.
    A Dynamic Interaction of Coomassie Dye with the Glycine Transporters N-termini.
    (2016) Protein J. 35: 371-378.
72. 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.
73. Kuchtova, A., Janecek, S.
    Domain evolution in enzymes of the neopullulanase subfamily.
    (2016) Microbiology-(UK) 162(12): 2099-2115.
74. 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.
75. 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.
76. 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.
77. 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.
78. 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.
79. 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.
80. Jursky, F., Baliova, M., Juhasova, A.
    Structural insights into the benzophenanthridines binding to human glycine transporter GlyT1.
    (2015) Eur. J. Pharmacol. 765: 1-6.
81. 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.
82. 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.
83. 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.
84. 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.
85. 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.
86. 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.
87. 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.
88. 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.
89. 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.
90. Majzlova, K., Janecek, S.
    Two structurally related starch-binding domain families CBM25 and CBM26.
    (2014) Biologia 69(9): 1087-1096.
91. 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.
92. Mihalikova, A., Baliova, M., Jursky, F.
    Calcium Dependent Interaction of Calmodulin with the GlyT1 C-terminus.
    (2014) Neurochem. Res. 39(11): 2225-2233.
93. 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.
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94. 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.
95. 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-.
96. 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.
97. 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.
98. 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.
99. 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.
100. 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-.
101. 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-.
102. 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.
103. 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.
104. 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.
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105. 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.
106. 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.
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107. Ambro, L., Pevala, V., Bauer, J., Kutejova, E.
     The influence of ATP-dependent proteases on a variety of nucleoid-associated processes.
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108. Blesak, K., Janecek, S.
     Sequence fingerprints of enzyme specificities from the glycoside hydrolase family GH57.
     (2012) Extremophiles 16(3): 497-506.
109. 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.
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110. 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.
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111. Jursky, F., Baliova, M., Mihalikova, A.
     Molecular basis for differential glycine transporters sensitivity to sanguinarine .
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112. 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.
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113. 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.
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114. 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.
115. 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.
116. 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.
117. Jursky, F., Baliova, M.
     Differential effect of the benzophenanthridine alkaloids sanguinarine and chelerythrine on glycine transporters.
     (2011) Neurochem. Int. 58: 641-647.
118. 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.
119. Baliova, M., Jursky, F.
     Calcium dependent modification of distal C-terminal sequences of glycine transporter GlyT1.
     (2010) Neurochem. Int. 57: 254-261.
120. 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..
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121. 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.
122. 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.
123. 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.
124. 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.
125. 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.
126. 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.
127. 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.
128. 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.
129. 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.
130. Franekova, V., Baliova, M., Jursky, F.
     Truncation of human dopamine transporter by protease calpain.
     (2008) Neurochem. Int. 52: 1436-1441.
131. 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.
132. 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.
133. 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.
134. 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-.
135. 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.
136. 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.
137. 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.
138. 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.
139. 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.
140. Machovic, M., Janecek, S.
     Starch-binding domains in the post-genome era.
     (2006) Cell. Mol. Life Sci. 63(23): 2710-2721.
141. Machovic, M., Janecek, S.
     The evolution of putative starch-binding domains.
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142. Baliova, M., Jursky, F.
     Calpain Sensitive Regions in the N-terminal Cytoplasmic Domains of Glycine Transporters GlyT1A and GlyT1B.
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143. 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.
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144. 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.
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145. 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.
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146. 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.
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147. Baliova, M., Betz, H., Jursky, F.
     Calpain-mediated proteolytic cleavage of the neuronal glycine transporter, GlyT2.
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148. 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.
149. Baliova, M., Jursky, F.
     Phosphatase inhibitors influence proteolytic cleavage pattern of Glycine transporter GlyT2 N-terminus.
     (2004) Biologia 59(6): 843-845.
150. 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.
151. 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.
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152. 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.
153. 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.
154. 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.
155. 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.
156. 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.
157. Janecek, S.
     A motif of a microbial starch-binding domain found in human genethonin.
     (2002) Bioinformatics 18(11): 1534-1537.
158. Janecek, S.
     How many conserved sequence regions are there in the alpha-amylase family?.
     (2002) Biologia 57(Suppl. 11): 29-41.
159. 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.
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