Publications

  1. Ewa M. Stein, Joanna Kwiatkowska, Maciej M. Basczok, Chandra M. Gravel, Katherine E. Berry, Mikołaj Olejniczak „Determinants of RNA recognition by the FinO domain of the Escherichia coli ProQ protein”, Nucleic Acids Research (2020), PubMed
  2. Kwiatkowska J, Wroblewska Z, Johnson KA, Olejniczak M. „The binding of Class II sRNA MgrR to two different sites on matchmaker protein Hfq enables efficient competition for Hfq and annealing to regulated mRNAs.”, RNA (2018), 24(12):1761-1784
    PubMed

  3. Olejniczak M, Storz G. “ProQ/FinO-domain proteins: Another ubiquitous family of RNA matchmakers?” Mol Microbiol. (2017) Mar 30. doi: 10.1111/mmi.
    PubMed

  4. Thoduka SG, Zaleski PA, Dąbrowska Z, Równicki M, Stróżecka J, Górska A, Olejniczak M, Trylska J. "Analysis of ribosomal inter-subunit sites as targets for complementary oligonucleotides." Biopolymers. 2017 Apr;107(4). doi: 10.1002/bip.23004.
    PubMed

  5. Wroblewska Z, Olejniczak M. "Contributions of the Hfq protein to translation regulation by small noncoding RNAs binding to the mRNA coding sequence." Acta Biochim Pol. 2016;63(4):701-707. (Special Issue of KNOW  RNA Research Center in Poznan)
    PubMed

  6. Groszewska A, Wroblewska Z, Olejniczak M. "The structure of fadL mRNA and its interactions with RybB sRNA." Acta Biochim Pol. 2016;63(4):835-840. (Special Issue of KNOW  RNA Research Center in Poznan)
    PubMed

  7. Wróblewska Z, Olejniczak M. "Hfq assists small RNAs in binding to the coding sequence of ompD mRNA and in rearranging its structure", RNA (2016), 22:979-94 (2016).
    PubMed

  8. Małecka E.M., Stróżecka J., Sobańska D. and Olejniczak M. "Structure of bacterial regulatory RNAs determines their performance in competition for the chaperone protein Hfq." Biochemistry 54, 1157-70 (2015)
    PubMed

  9. Olejniczak M. "Despite similar binding to the Hfq protein regulatory RNAs widely differ in their competition performance." Biochemistry 50, 4427-4440 (2011)
    PubMed

  10. Ledoux S., Olejniczak M., Uhlenbeck O.C. "A sequence element that tunes Escherichia coli tRNA(Ala)(GGC) to ensure accurate decoding." Nat. Struct. Mol. Biol. 16(4), 359-64 (2009)
    PubMed

  11. Dale T., Fahlman R.P., Olejniczak M., Uhlenbeck O.C. "Specificity of the ribosomal A site for aminoacyl-tRNAs." Nucleic Acids Res. 37(4), 1202-10 (2009)
    PubMed

  12. Olejniczak M., Uhlenbeck O.C, „tRNA residues that have coevolved with their anticodon to ensure uniform and accurate codon recognition” Biochimie 88(8), 943-50, (2006)
    PubMed

  13. Fahlman R.P., Olejniczak M. and Uhlenbeck O.C. "Quantitative analysis of deoxynucleotide substitutions in the codon-anticodon helix." J. Mol. Biol. 355(5), 887-892, (2006)
    PubMed

  14. Olejniczak M., Dale T., Fahlman R.P. and Uhlenbeck O.C. "Idiosyncratic tuning of tRNAs to achieve uniform ribosome binding." Nat. Struct. Mol. Biol. 12(9), 788-793 (2005)
    PubMed

  15. Kuliński T., Olejniczak M., Huthoff H., Bielecki L., Pachulska K., Das A.T., Berkhout B. and Adamiak R.W. "The apical loop of the HIV-1 TAR RNA hairpin is stabilized by a cross-loop base pair. " J. Biol. Chem. 278, 38892-38901 (2003)
    PubMed

  16. Olejniczak M., Gdaniec Z., Fischer A., Grabarkiewicz T., Bielecki L. and Adamiak R. W. "The bulge region of HIV-1 TAR RNA binds metal ions in solution”, Nucleic Acids Res. 30, 4241-4249 (2002)
    PubMed