Organization Structure
Executive Body
Management Board
Supervisory Board
Scientific Board
Labour Union
PhD Study
Public Information
Journal Biologia[IF: 1.350]
Department of Microbial GeneticsBarak.jpg

Dr. Imrich Barak

head of department

Group - Microbial Genetics

Dr. Imrich Barak (group leader)

A complete, molecular understanding of the workings of any organism requires an investigation of the structure - function relationship for all proteins in the cell. Bacillus subtilis is an internationally-recognized model organism, whose physiology, biochemistry and genetics has been studied for many years. Department of Microbial Genetics projects are oriented toward studying the proteins involved in basic processes in Bacillus subtilis as cell division, sporulation and programmed cell death. Asymmetric cell division is fundamental to the development not only of multicellular organisms but also to rod-shaped bacteria that undergo a specific differentiation process called sporulation. The target proteins are especially Spo0A, SpoIIE, DivIVA, MinC, MinD, RodZ and their complexes. In case of programmed cell death we concentrate on biochemical, genetic and structural studies of toxin-antitoxin, SpoIISA-SpoIISB system. These proteins were firstly identified as part of sporulation process in Bacillus subtilis. Genetic, biochemical experiments and especially tertiary structure of above mentioned proteins would be a great contribution for our understanding of basic bacterial cell processes.

Department is also involved in studies of protein-protein interactions of sporulation specific Cot proteins which are able to form highly ordered nano-scale layers. The aim of these studies is to develop new tools and nano-array based systems to form layers from protein molecules up to the scale of nano-particles. These technologies should be tested in a few trial applications for preparation of nano-materials as well as in new bio-nanotechnologies processes.

Working group of Apidology and Apitherapy

Dr. Juraj Majtan (group leader)

Chronic, non-healing wounds are the major cause of morbidity in elderly population.  These non-healing wounds are often characterised by an excessive, and detrimental inflammatory response accompanied by bacterial colonization. Prevalence of antibiotic-resistant bacteria and bacterial biofilms in wounds is a significant problem in wound care and therefore, it urgently needs to find alternative biomedical strategies. One of these strategies represents apitherapy ? the medical use of honeybee products including medical-grade honeys, propolis and royal jelly in the treatment of chronic and infected wounds.

Laboratory of apidology and apitherapy focus on the apimedical research and characterisation the bee products-induced mechanisms of wound healing and tissue remodelling. Besides the direct antimicrobial and antibiofilm effect, bee products possess the anti-inflammatory and immunomodulatory effects. Recently, the multifunctional immunomodulatory properties of bee products on cells involved in wound healing such as monocytes, keratinocytes and fibroblasts have attracted much attention. Our laboratory together with Department of microbiology at Slovak medical university also participates on translational research through the performing in vivo experiments on an animal model or human clinical trials using a Slovak honeydew honey in wound care. An important part of our research is the quality and authenticity of honeybee products with reference to the content of individual biologically active components where we focus on the development of new qualitative/quantitative tests. A naturally increased content of bee secreted biologically active compounds in honey and royal jelly may promote to protect bee and its offspring and to wider therapeutic use of these products.


Research fellows:
     Dr. Juraj Majtan
     Dr. Imrich Barak
     Dr. Jarmila Farkasovska
     Dr. Marcela Bucekova
     Dr. Daniela Krajcikova
     Dr. Katarina Muchova
     Dr. Romana Kaliankova Chovanova
     Dr. Zuzana Chromikova
     Dr. Nada Labajova
     Veronika Bellova
     Jana Godocikova
PhD students:
     Veronika Bugarova
     Evelina Kalocsaiova
     Silvia Žarnovicanova
     Emilia Chovancova

International scientific co-operation

  1. Biological Physical Sciences Institute, University of York, York, United Kingdom
  2. Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, China
  3. Department of Chemistry, University of York, York, United Kingdom
  4. DISIT - Dipartimento di Scienze e Innovazione Tecnologica, University of Piemonte Orientale, Alessandria, Italy
  5. EPFL, Lausanne, Switzerland
  6. Royal Holloway and Bedford New College, London, United Kingdom
  7. XFEL, Hamburg, Germany

Selected Publications

  1. Chromikova, Z., Kaliankova-Chovanova, R., Tamindzija, D., Bartova, B., Radnovic, D., Bernier-Latmani, R., Barak, I.
    Implantation of Bacillus pseudomycoides Chromate Transporter Increases Chromate Tolerance in Bacillus subtilis.
    (2022) Front Microbiol 13: 842623-.
  2. Barak, I.
    Bacillus subtilis as a Model Organism to Study Basic Cell Processes.
    (2021) Microorganisms 9: 2459-.
  3. Bodik, M., Krajcikova, D., Hagara, J., Majkova, E., Barak, I., Siffalovic, P.
    Diffraction pattern of Bacillus subtilis CotY spore coat protein 2D crystals.
    (2021) Colloid Surf. B-Biointerfaces 197: 111425-.
  4. Han, H., Round, E., Schubert, R., Gul, Y., Makroczyova, J., Meza, D., Heuser, P., Aepfelbacher, M., Barak, I., Betzel, C., Fromme, P., Kursula, I., Nissen, P., Tereschenko, E., Schulz, J.
    The XBI BioLab for life science experiments at the European XFEL.
    (2021) J. Appl. Crystallogr. 54: 7-21.
  5. Krajcikova, D., Bugarova, V., Barak, I.
    Interactions of Bacillus subtilis Basement Spore Coat Layer Proteins.
    (2021) Microorganisms 9: 285-.
  6. Labajova, N., Baranova, N., Jurasek, M., Vacha, R., Loose, M., Barak, I.
    Cardiolipin-Containing Lipid Membranes Attract the Bacterial Cell Division Protein DivIVA.
    (2021) Int J Mol Sci 22: 8350-.
  7. Majtan, J., Bucekova, M., Kafantaris, I., Szweda, P., Hammer, K., Mossialos, D.
    Honey antibacterial activity: A neglected aspect of honey quality assurance as functional food.
    (2021) Trends Food Sci. Technol. 118: 870-886.
  8. Gacek-Matthews, A., Chromikova, Z., Sulyok , M., Lücking, G., Barak, I., Ehling-Schulz, M.
    Beyond Toxin Transport: Novel Role of ABC Transporter for Enzymatic Machinery of Cereulide NRPS Assembly Line.
    (2020) Mbio 11(5): e01577-20-.
  9. Muchova, K., Chromikova, Z., Barak, I.
    Linking the Peptidoglycan Synthesis Protein Complex with Asymmetric Cell Division during Bacillus subtilis Sporulation.
    (2020) Int J Mol Sci 21: 4513-.
  10. Pospisil, J., Vitovska, D., Kofronova, O., Muchova, K., Sanderova, H., Hubalek, M., Sikova, M., Modrak, M., Benada, O., Barak, I., Krasny, L.
    Bacterial nanotubes as a manifestation of cell death.
    (2020) Nat Commun 11: 4963-.
  11. Sobolev, E., Zolotarev, S., Giewekemeyer, K., Bielecki, J., Okamoto, K., Reddy, H., Andreasson, J., Ayyer, K., Barak, I., Bari, S., Barty, A., Bean, R., Bobkov, S., Chapman, H., Chojnowski, G.
    Megahertz single-particle imaging at the European XFEL.
    (2020) Commun. Phys. 3: 97-.
  12. Wollman, A., Muchova, K., Chromikova, Z., Wilkinson, A.J., Barak, I., Leake, M.
    Single-molecule optical microscopy of protein dynamics and computational analysis of images to determine cell structure development in differentiating Bacillus subtilis.
    (2020) Comp. Struct. Biotechnol. J. 18: 1474-1486.
  13. Barak, I., Muchova, K., Labajova, N.
    Asymmetric cell division during Bacillus subtilis sporulation.
    (2019) Future Microbiol. 14: 353-363.
  14. Bucekova, M., Jardekova, L., Juricova, V., Bugarova, V., Di Marco, G., Gismondi, A., Leonardi, D., Farkasovska, J., Godocikova, J., Laho, M., Klaudiny, J., Majtan, V., Canini, A., Majtan, J.
    Antibacterial activity of different blossom honeys: new findings.
    (2019) Molecules 24(8): 1573-.
  15. Tamindzija, D., Chromikova, Z., Spaic, A., Barak, I., Bernier-Latmani, R., Radnovic, D.
    Chromate tolerance and removal of bacterial strains isolated from uncontaminated and chromium-polluted environments.
    (2019) World J. Microbiol. Biotechnol. 35: 56-.
  16. Barak, I., Muchova, K.
    The positioning of the asymmetric septum during sporulation in Bacillus subtilis.
    (2018) PLoS One 13: 1-15.
  17. Bucekova, M., Juricova, V., Monton, E., Martinotti, S., Ranzato, E., Majtan, J.
    Microwave processing of honey negatively affects honey antibacterial activity by inactivation of bee-derived glucose oxidase and defensin-1.
    (2018) Food Chem 240: 1131-1136.
  18. Bucekova, M., Buriova, M., Pekarik, L., Majtan, V., Majtan, J.
    Phytochemicals-mediated production of hydrogen peroxide is crucial for high antibacterial activity of honeydew honey.
    (2018) Sci Rep 8:9061: 1-9.
  19. Bucekova, M., Juricova, V., Di Marco, G., Gismondi, A., Leonardi, D., Canini, A., Majtan, J.
    Effect of thermal liquefying of crystallised honeys on their antibacterial activities.
    (2018) Food Chem 269: 335-341.
  20. Muchova, K., Chromikova, Z., Valencikova, R., Barak, I.
    Interaction of the Morphogenic Protein RodZ with the Bacillus subtilis Min System.
    (2018) Front Microbiol 8: 1-10.
  21. Valencikova, R., Krascsenitsova, E., Labajova, N., Makroczyova, J., Barak, I.
    Clostridial DivIVA and MinD interact in the absence of MinJ.
    (2018) Anaerobe 50: 22-31.
  22. Wiedorn, M., Oberthür, D., Bean, R., Schubert, R., Werner, N., Abbey, B., Apfelbacher, M., Adriano, L., Allahgholi, A., Al-Qudami, N., Andreasson, S., aplin, S., Awel, S., Ayyer, K., Barak, I.
    Megahertz serial crystallography.
    (2018) Nat Commun 9: 4025-.
  23. Barak, I.
    Editorial: Spores and Spore Formers.
    (2017) Front Microbiol 8: 1-2.
  24. Bucekova, M., Sojka, M., Valachova, I., Martinotti, S., Ranzato, E., Szep, Z., Majtan, V., Klaudiny, J., Majtan, J.
    Bee-derived antibacterial peptide, defensin-1, promotes wound re-epithelialisation, in vitro and in vivo.
    (2017) Sci Rep 7: 7340: 1-13.
  25. Krajcikova, D., Forgac, V., Szabo, A., Barak, I.
    Exploring the interaction network of the Bacillus subtilis outer coat and crust proteins.
    (2017) Microbiol. Res. 204: 72-80.
  26. Bucekova, M., Majtan, J.
    The MRJP1 honey glycoprotein does not contribute to the overall antibacterial activity of natural honey.
    (2016) Eur. Food Res. Technol. 242: 625-629.
  27. Gabrisko, M., Barak, I.
    Evolution of the SpoIISABC Toxin-Antitoxin-Antitoxin System in Bacilli.
    (2016) Toxins 8: 1-16.
  28. Jamroskovic, J., Chromikova, Z., List, C., Barak, I., Bernier-Latmani, R.
    Variability in DPA and calcium content in the spores of Clostridium species.
    (2016) Front Microbiol 7: 1-10.
  29. Liu, H., Qiao, H., Krajcikova, D., Zhang, Z., Wang, H., Barak, I., Tang, J.
    Physical interaction and assembly of Bacillus subtilis spore coat proteins CotE and CotZ studied by atomic force microscopy.
    (2016) J. Struct. Biol. 195: 245-251.
  30. Liu, H., Krajcikova, D., Wang, N., Zhang, Z., Wang, H., Barak, I., Tang, J.
    Forces and Kinetics of the Bacillus subtilis Spore Coat Proteins CotY and CotX Binding to CotE Inspected by Single Molecule Force Spectroscopy.
    (2016) J. Phys. Chem. B 120: 1041-1047.
  31. Makroczyova, J., Jamroskovic, J., Krascsenitsova, E., Labajova, N., Barak, I.
    Oscillating behavior of Clostridium difficile Min proteins in Bacillus subtilis.
    (2016) MicrobiologyOpen 5: 387-401.
  32. Muchova, K., Chromikova, Z., Bradshaw, N., Wilkinson, A.J., Barak, I.
    Morphogenic Protein RodZ Interacts with Sporulation Specific SpoIIE in Bacillus subtilis.
    (2016) PLoS One 11: 1-21.
  33. Sojka, M., Valachova, I., Bucekova, M., Majtan, J.
    Antibiofilm efficacy of honey and bee-derived defensin-1 on multi-species wound biofilm.
    (2016) J. Med. Microbiol. 65: 337-344.
  34. Valachova, I., Bucekova, M., Majtan, J.
    Quantification of bee-derived peptide defensin-1 in honey by competitive enzyme-linked immunosorbent assay, a new approach in honey quality control.
    (2016) Czech. J. Food Sci. 34(3): 233-243.
  35. Jiang, S., Wan, Q., Krajcikova, D., Tang, J., Tzokov, S.B., Barak, I., Bullough, P.A.
    Diverse supramolecular structures formed by self-assembling proteins of the Bacillus subtilis spore coat.
    (2015) Mol. Microbiol. 97: 347-359.
  36. Liu, H., Krajcikova, D., Zhang, Z., Wang, H., Barak, I., Tang, J.
    Investigating interactions of the Bacillus subtilis spore coat proteins CotY and CotZ using single molecule force spectroscopy.
    (2015) J. Struct. Biol. 192: 14-20.
  37. Melnicakova, J., Becarova, Z., Makroczyova, J., Barak, I.
    Analysis of the Bacillus cereus SpoIIS antitoxin-toxin system reveals its three-component nature.
    (2015) Front Microbiol 6(808): 1-11.
  38. Barak, I.
    Complexity of bacterial phosphorylation interaction network.
    (2014) Front Microbiol 5: 1-2.
  39. Bucekova, M., Valachova, I., Kohutova, L., Prochazka, E., Klaudiny, J., Majtan, J.
    Honeybee glucose oxidase - its expression in honeybee workers and comparative analyses of its content and H2O2-mediated antibacterial activity in natural honeys.
    (2014) Naturwissenschaften 101: 661-670.
  40. Jamroskovic, J., Shao, P.P., Suvorova, E., Barak, I., Bernier-Latmani, R.
    Combined scanning transmission X-ray and electron microscopy for the characterization of bacterial endospores.
    (2014) FEMS Microbiol. Lett. 358: 188-193.
  41. Majtan, J.
    Honey: an immunomodulator in wound healing.
    (2014) Wound Repair Regen 22: 187-192.
  42. Makroczyova, J., Resetarova, S., Florek, P., Barak, I.
    Topology of the Bacillus subtilis SpoIISA protein and its role in toxin–antitoxin function.
    (2014) FEMS Microbiol. Lett. 358: 180-187.
  43. Barak, I., Muchova, K.
    The Role of Lipid Domains in Bacterial Cell Processes.
    (2013) Int J Mol Sci 14: 4050-4065.
  44. Barak, I.
    Open questions about the function and evolution of bacterial Min systems.
    (2013) Front Microbiol 4: 378-.
  45. Majtan, J., Bohova, J., Garcia-Villalba, R., Tomas-Barberan, F.A., Madakova, Z., Majtan, T., Majtan, V., Klaudiny, J.
    Fir honeydew honey flavonoids inhibit TNF-?-induced MMP-9 expression in human keratinocytes: a new action of honey in wound healing.
    (2013) Arch. Dermatol. Res. 305: 619-627.
  46. Melnicakova, J., Derdakova, M., Barak, I.
    A system to simultaneously detect tick-borne pathogens based on the variability of the 16S ribosomal genes.
    (2013) Parasites Vectors 6: 269-.
  47. Muchova, K., Chromikova, Z., Barak, I.
    Control of Bacillus subtilis cell shape by RodZ.
    (2013) Environ. Microbiol 15: 3259-3271.
  48. Qiao, H., Krajcikova, D., Xing, C., Lu, B., Hao, J., Ke, X., Wang, H., Barak, I., Tang, J.
    Study of the interactions between the key spore coat morphogenetic proteins CotE and SpoVID.
    (2013) J. Struct. Biol. 181: 128-135.
  49. Jamroskovic, J., Pavlendova, N., Muchova, K., Wilkinson, A.J., Barak, I.
    An Oscillating Min system in Bacillus subtilis influences asymmetric septation during sporulation.
    (2012) Microbiology-(UK) 158: 1972-1981.
  50. Koharyova, M., Barak, I., Kollarova, M.
    Expresia a purifikácia tioredoxínu 2 a tioredoxínu 3 zo Streptomyces coelicolor A3(2).
    (2012) Chem. Listy 106: 398-403.
  51. Levdikov, V.M., Blagova, E., Rawlings, A.E., Jameson, J., Tunaley, J., Hart, D.J., Barak, I., Wilkinson, A.J.
    Structure of the phosphatase domain of the cell fate determinant SpoIIE from Bacillus subtilis.
    (2012) J. Mol. Biol. 415: 343-358.
  52. Qiao, H., Krajcikova, D., Liu, C., Li, Y., Wang, H., Barak, I., Tang, J.
    The interactions of spore coat morphogenetic proteins studied by single-molecular recognition force spectroscopy.
    (2012) Chem.-Asian J. 7: 725-731.
  53. Florek, P., Levdikov, V.M., Blagova, E., Lebedev, A.A., Skrabana, R., Pavelcikova, P., Resetarova, S., Barak, I., Wilkinson, A.J.
    The Structure and Interactions of SpoIISA and SpoIISB, a Toxin - Antitoxin System in B. subtilis.
    (2011) J. Biol. Chem. 286(8): 6808-6819.
  54. Gundogdu, M.E., Kawai, Y., Pavlendova, N., Ogasawara, N., Errington, J., Scheffers, D.J., Hamoen, L.W.
    Large ring polymers align FtsZ polymers for normal septum formation.
    (2011) Embo J. 30(3): 617-626.
  55. Muchova, K., Wilkinson, A.J., Barak, I.
    Changes of lipid domains in Bacillus subtilis cells with disrupted cell wall peptidoglycan.
    (2011) FEMS Microbiol. Lett. 325(1): 92-98.
  56. Muchova, K., Jamroskovic, J., Barak, I.
    Lipid domains in Bacillus subtilis anucleate cells.
    (2010) Res. Microbiol. 161(9): 783-790.
  57. Pavlendova, N., Muchova, K., Barak, I.
    Expression of Escherichia coli Min system in Bacillus subtilis and its effect on cell division.
    (2010) FEMS Microbiol. Lett. 302(1): 58-68.
  58. Rawlings, A.E., Levdikov, V.M., Blagova, E., Colledge, V.L., Mas, P.J., Tunaley, J., Vavrova, L., Wilson, K.S., Barak, I., Hart, D.J., Wilkinson, A.J.
    Expression of soluble, active fragments of the morphogenetic protein SpoIIE from Bacillus subtilis using a library-based construct screen.
    (2010) Protein Eng. Des. Sel. 23(11): 817-825.
  59. Resetarova, S., Florek, P., Muchova, K., Wilkinson, A.J., Barak, I.
    Expression and localization of SpoIISA toxin during the life cycle of Bacillus subtilis.
    (2010) Res. Microbiol. 161(9): 750-756.
  60. Vavrova, L., Muchova, K., Barak, I.
    Comparison of different Bacillus subtilis expression systems.
    (2010) Res. Microbiol. 161(9): 791-797.
  61. Krajcikova, D., Lukacova, M., Mullerova, D., Cutting, S., Barak, I.
    Searching for Protein-Protein Interactions Within the Bacillus subtilis Spore Coat.
    (2009) J. Bacteriol. 191(10): 3212-3219.
  62. Mullerova, D., Krajcikova, D., Barak, I.
    Interactions between Bacillus subtilis early spore coat morphogenetic proteins.
    (2009) FEMS Microbiol. Lett. 299: 74-85.
  63. Barak, I., Muchova, K., Wilkinson, A.J., O Toole, P.J., Pavlendova, N.
    Lipid spirals in Bacillus subtilis and their role in cell division.
    (2008) Mol. Microbiol. 68: 1315-1327.
  64. Florek, P., Muchova, K., Pavelcikova, P., Barak, I.
    Expression of functional Bacillus SpoIISAB toxin-antitoxin modules in Escherichia coli.
    (2008) FEMS Microbiol. Lett. 278: 177-184.
  65. Kocianova, E., Blaskovic, D., Smetanova, K., Schwarzova, K., Boldis, V., Kostanova, Z., Mullerova, D., Barak, I.
    Comparison of an oligo-chip based assay with PCR method to measure the prevalence of tick-borne pathogenic bacteria in central Slovakia.
    (2008) Biologia 63: 34-37.
  66. Lukacova, M., Barak, I., Kazar, J.
    Role of structural variations of polysacharide antigens in the pathogenicity of Gram-negative bacteria.
    (2008) Clin. Microbiol. Infect. 14: 200-206.
  67. Zweers, J.C., Barak, I., Becher, D., Driessen, A.J., Hecker, M., Kontinen, V.P., Saller, M.J., Vavrova, L., van Dijl, J.M.
    Towards the development of Bacillus subtilis as a cell factory for membrane proteins and protein complexes.
    (2008) Microb. Cell. Fact. 7: 10-.
  68. Barak, I., Wilkinson, A.J.
    Division site recognition in Escherichia coli and Bacillus subtilis.
    (2007) Fems Microbiol. Rev. 31: 311-326.
  69. Pavlendova, N., Muchova, K., Barak, I.
    Chromosome Segregation in Bacillus subtilis.
    (2007) Folia Microbiol. 52: 563-572.
  70. Tang, J., Krajcikova, D., Zhu, R., Ebner, A., Cutting, S., Gruber, H.J., Barak, I., Hinterdorfer, P.
    Atomic force microscopy imaging and single molecule recognition force spectroscopy of coat proteins on the surface of Bacillus subtilis spore .
    (2007) J. Mol. Recognit. 20(6): 483-489.
  71. Barbaro, M., Bonfiglio, A., Raffo, L., Alessandrini, P., Facci, P., Barak, I.
    A CMOS, fully integrated sensor for electronic detection of DNA hybridization.
    (2006) IEEE Electron Device Lett. 27(7): 595-597.
  72. Barbaro, M., Bonfiglio, A., Raffo, L., Alessandrini, P., Facci, P., Barak, I.
    Fully electronic DNA hybridization detection by a standard CMOS biochip.
    (2006) Sens. Actuator B-Chem. 118(1-2): 41-46.
  73. Stefankova, P., Perecko, D., Barak, I., Kollarova, M.
    The thioredoxin system from Streptomyces coelicolor.
    (2006) J. Basic Microbiol. 46(1): 47-55.
  74. Alessandrini, A., de Renzi, V., Berti, L., Barak, I., Facci, P.
    Chemically homogeneous, silylated surfaces for effective DNA binding and hybridization.
    (2005) Surf. Sci. 582: 202-208.
  75. Barak, I., Ricca, E., Cutting, S.
    From fundamental studies of sporulation to applied spore research.
    (2005) Mol. Microbiol. 55: 330-338.
  76. Barak, I., Wilkinson, A.J.
    Where asymmetry in gene expression originates.
    (2005) Mol. Microbiol. 57: 611-620.
  77. Blaskovic, D., Barak, I.
    DNA chips for detection of bacterial pathogens.
    (2005) Biologia 60: 239-249.
  78. Blaskovic, D., Barak, I.
    Oligo-chip based assay for detection of tick-borne bacteria causing diseases in humans.
    (2005) FEMS Microbiol. Lett. 243: 473-478.
  79. Kollarova, M., Stefankova, P., Maderova, J., Barak, I., Otwinowski, Z.
    Thioredoxin system of Streptomyces coelicolor.
    (2005) FEBS J. 272: 378-378.
  80. Stefankova, P., Kollarova, M., Barak, I.
    Thioredoxin - Structural and Functional Complexity.
    (2005) Gen. Physiol. Biophys. 24: 3-11.
  81. Stefankova, P., Maderova, J., Barak, I., Kollarova, M., Otwinowski, Z.
    Expression, purification and X-ray crystallographic analysis of thioredoxin from Streptomyces coelicolor.
    (2005) Acta Crystallographica Sect. F-Struct. Biol. Cryst. Commun. 61: 164-168.
  82. Barak, I., Florek, P., Muchova, K., Pribisova, L., Chromikova, Z.
    Bacterial cell division proteins – structure and function.
    (2004) Mater. Struct. 11: 7-11.
  83. Krajcikova, D., Hartley, R.W.
    A new member of the bacterial ribonuclease inhibitor family from Saccharopolyspora erythraea.
    (2004) FEBS Lett. 557(1-3): 164-168.
  84. Muchova, K., Lewis, R.J., Perecko, D., Brannigan, J.A., Ladds, J.C., Leech, A., Wilkinson, A.J., Barak, I.
    Dimer induced signal propagation in Spo0A.
    (2004) Mol. Microbiol. 53(3): 829-842.
  85. Pribisova, L., Muchova, K., Barak, I.
    Cloning and biochemical characterization of DivIVA protein from Bacillus stearotermophilus.
    (2004) Biologia 59: 391-398.
  86. 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.
  87. Howe, D., Melnicakova, J., Barrows, L.F., Barak, I., Heinzen, R.A.
    Fusogenicity of the Coxiella burnetii parasitophorous vacuole .
    (2003) Ann.NY Acad.Sci. 990: 556-562.
  88. Howe, D., Melnicakova, J., Barak, I., Heinzen, R.A.
    Maturation of the Coxiella burnetii Parasitophorous vacuole requires bacterial protein synthesis but not replication.
    (2003) Cell Microbiol. 5: 469-480.
  89. Kuznetsova, S., Tokarevich, N., Lukacova, M., Koloskov, A., Freidlin, I.
    Influence of inactivated Coxiella burnetii on production of proinflammatory cytokines by blood cells from healthy donors.
    (2003) Ann.NY Acad.Sci. 990: 500-504.
  90. Ladds, J.C., Muchova, K., Blaskovic, D., Lewis, R.J., Brannigan, J.A., Wilkinson, A.J., Barak, I.
    The response regulator Spo0A from Bacillus subtilis is efficiently phosphorylated in Escherichia coli.
    (2003) FEMS Microbiol. Lett. 223: 153-157.
  91. Melnicakova, J., Lukacova, M., Howe, D., Heinzen, R.A., Barak, I.
    Identification of Coxiella burnetii RpoS-dependent promoters.
    (2003) Ann.NY Acad.Sci. 990: 591-595.
  92. Chromikova, Z., Barak, I.
    Gene asymmetry during sporulation process of Bacillus subtilis.
    (2002) Biologia 57: 707-712.
  93. Florek, P., Muchova, K., Barak, I.
    Truncated Spo0A transcription activities in Bacillus subtilis.
    (2002) Biologia 57: 805-811.
  94. Lukacova, M., Melnicakova, J., Quevedo-Diaz, M.A., Barak, I.
    Coxiella burnetii as a query microorganism.
    (2002) Biologia 57: 713-720.
  95. Arigoni, F., Guerout-Fleury, A.M., Barak, I., Stragier, P.
    The SpoIIE phosphatase, the sporulation septum, and the establishment of forespore-specific transcription in Bacillus subtilis: a reassessment.
    (1999) Mol. Microbiol. 31: 1407-1416.
  96. Frandsen, N., Barak, I., Karmazyn-Campelli, C., Stragier, P.
    Transient gene asymmetry during sporulation and establishment of cell specificity in Bacillus subtilis.
    (1999) Genes Dev. 13: 394-399.
  97. Kormanec, J., Homerova, D., Barak, I., Sevcikova, B.
    A new gene, sigG, encoding a putative alternative sigma factor of Streptomyces coelicolor A3(2).
    (1999) FEMS Microbiol. Lett. 172(2): 153-158.
  98. Muchova, K., Lewis, R.J., Brannigan, J.A., Offen, W., Brown, D.P., Barak, I., Youngman, P., Wilkinson, A.J.
    Cloning, purification and crystallisation of discrete domains of Spo0A, the primary sporulation response regulator of Bacillus.
    (1999) Acta Crystallogr. D 55: 671-676.
  99. Barak, I., Prepiak, P., Schmeisser, F.
    Protein localisation and protein-protein contact during asymmetric cell division in Bacillus subtilis.
    (1998) Gen. Physiol. Biophys. 17: 37-40.
  100. Muchova, K., Lewis, R.J., Brannigan, J.A., Schmeisser, F., Wilkinson, A.J., Barak, I.
    Primary sporulation response regulator Spo0A.
    (1998) Gen. Physiol. Biophys. 17: 34-36.
  101. Rezuchova, B., Barak, I., Kormanec, J.
    Disruption of a sigma factor gene, sigF, affects an intermediate stage of spore pigment production in Streptomyces aureofaciens.
    (1997) FEMS Microbiol. Lett. 153(2): 371-377.
  102. Barak, I., Youngman, P.
    SpoIIE mutants of Bacillus subtilis comprises two distinct phenotypic classes consistent with a dual functional role for the SpoIIE protein.
    (1996) J. Bacteriol. 178: 4984-4989.
  103. Barak, I., Behari, J., Olmedo, G., Guzmán, P., Castro, E., Brown, D.P., Walker, D., Westpheling, J., Youngman, P.
    Structure and function of the Bacillus SpoIIE protein and its localization to sites of sporulation septum assembly.
    (1996) Mol. Microbiol. 19: 1047-1060.
  104. Walker, D., Burke, V.J., Barak, I., Avise, J.C.
    A comparison of mtDNA restriction sites vs. control region sequences in phylogeographic assessment of the musk turtle (Sternotherus minor).
    (1995) Mol.Ecol. 4: 365-373.
  105. Barak, I., Koptides, M., Jucovic, M., Sisova, M., Timko, J.
    Construction of a promoter-probe shuttle vector for Escherichia coli and brevibacteria.
    (1990) Gene 95(1): 133-135.
  106. Barak, I.
    Molecular-biological aspects of L-lysine biosynthesis in coryneform bacteria.
    (1989) Biophys. J. 44: 1197-1209.