Search results

  1. 1.
    0584258 - BC 2024 RIV NL eng J - Journal Article
    Krela, Rafal - Poreba, M. - Lesniewicz, K.
    Variations in the enzymatic activity of S1-type nucleases results from differences in their active site structures.
    Biochimica et Biophysica Acta-General Subjects. Roč. 1867, č. 10 (2023), č. článku 130424. ISSN 0304-4165. E-ISSN 1872-8006
    Institutional support: RVO:60077344
    Keywords : Non-zinc-dependent activity * S1-like nuclease * Active-site * Acanthamoeba castellanii * Physcomitrella patens
    OECD category: Biochemistry and molecular biology
    Impact factor: 3, year: 2022
    Method of publishing: Open access
    https://www.sciencedirect.com/science/article/pii/S0304416523001228?via%3Dihub
    Permanent Link: https://hdl.handle.net/11104/0352320
     
     
  2. 2.
    0510417 - ÚOCHB 2020 RIV GB eng J - Journal Article
    de Vries, L. E. - Sanchez, M. I. - Groborz, K. - Kuppens, L. - Poreba, M. - Lehmann, C. - Nevins, N. - Withers-Martinez, C. - Hirst, D. J. - Yuan, F. - Arastu-Kapur, S. - Horn, Martin - Mareš, Michael - Bogyo, M. - Drag, M. - Deu, E.
    Characterization of P. falciparum dipeptidyl aminopeptidase 3 specificity identifies differences in amino acid preferences between peptide-based substrates and covalent inhibitors.
    FEBS Journal. Roč. 286, č. 20 (2019), s. 3998-4023. ISSN 1742-464X. E-ISSN 1742-4658
    R&D Projects: GA MŠMT(CZ) EF16_019/0000729
    Institutional support: RVO:61388963
    Keywords : dipeptidyl aminopeptidase * malaria * positional scanning * proteases * specificity
    OECD category: Biochemistry and molecular biology
    Impact factor: 4.392, year: 2019
    Method of publishing: Open access
    https://febs.onlinelibrary.wiley.com/doi/full/10.1111/febs.14953
    Permanent Link: http://hdl.handle.net/11104/0300925
     
     
  3. 3.
    0376236 - ÚOCHB 2013 RIV FR eng J - Journal Article
    Poreba, M. - Gajda, A. - Pícha, Jan - Jiráček, Jiří - Marschner, A. - Klein, Ch. D. - Salvesen, G. S. - Drag, M.
    S1 pocket fingerprints of human and bacterial methionine aminopeptidases determined using fluorogenic libraries of substrates and phosphorus based inhibitors.
    Biochimie. Roč. 94, č. 3 (2012), s. 704-710. ISSN 0300-9084. E-ISSN 1638-6183
    R&D Projects: GA MŠMT(CZ) LC06077
    Institutional research plan: CEZ:AV0Z40550506
    Keywords : methionine aminopeptidase * substrate library * protease * enzyme * inhibitor * substrate specificity
    Subject RIV: CC - Organic Chemistry
    Impact factor: 3.142, year: 2012
    Permanent Link: http://hdl.handle.net/11104/0208695
     
     


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