Projects funded by the NCN

Information on the principal investigator and host institution

Information of the project and the call

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Novel L-asparaginases as potential therapeutic agents and antimicrobial targets: structural and functional studies of enzymes with dual implications for drug design

2020/37/B/NZ1/03250

Keywords:

asparaginase leukemia fungal infections enzyme inhibitors protein crystallography

Descriptors:

  • NZ1_004:
  • NZ1_002:
  • NZ1_005:

Panel:

NZ1 - Molecular biology, structural biology, biotechnology: molecular biology, structural biology, biotechnology

Host institution :

Instytut Chemii Bioorganicznej Polskiej Akademii Nauk

woj. wielkopolskie

Other projects carried out by the institution 

Principal investigator (from the host institution):

prof. Mariusz Jaskólski 

Number of co-investigators in the project: 7

Call: OPUS 19 - announced on 2020-03-16

Amount awarded: 2 347 200 PLN

Project start date (Y-m-d): 2021-02-01

Project end date (Y-m-d): 2026-01-31

Project duration:: 60 months (the same as in the proposal)

Project status: Pending project

Project description

Download the project description in a pdf file

Note - project descriptions were prepared by the authors of the applications themselves and placed in the system in an unchanged form.

Information in the final report

  • Publication in academic press/journals (12)
  1. Substrate affinity is not crucial for therapeutic L-asparaginases: antileukemic activity of novel bacterial enzymes
    Authors:
    A.Ściuk, K.Wątor, I.Staroń, P.Worsztynowicz, K.Pokrywka, M.Kilichowska, K.Pietruszewska, Z.Mazurek, A.Skalniak, K.Lewandowski, M.Jaskólski, J.I.Loch, M.Surmiak
    Academic press:
    Molecules (rok: 2024, tom: 29(10), strony: 45673), Wydawca: MDPI
    Status:
    Published
    DOI:
    10.3390/molecules29102272 - link to the publication
  2. Crystal structures of the elusive Rhizobium etli l-asparaginase reveal a peculiar active site
    Authors:
    2 J.I.Loch, B.Imiolczyk, J.Sliwiak, A.Wantuch, M.Bejger, M.Gilski, M.Jaskolski
    Academic press:
    NATURE COMMUNICATIONS (rok: 2021, tom: 12, strony: Article Number 6717), Wydawca: Nature Publishing Group
    Status:
    Published
    DOI:
    10.1038/s41467-021-27105-x - link to the publication
  3. Structural and biophysical aspects of l-asparaginases: a growing family with amazing diversity
    Authors:
    1 J.Loch, M.Jaskolski
    Academic press:
    IUCRJ (rok: 2021, tom: 8, strony: 514-531), Wydawca: INT UNION CRYSTALLOGRAPHY
    Status:
    Published
    DOI:
    10.1107/S2052252521006011 - link to the publication
  4. Rhizobium etli has two L-asparaginases with low sequence identity but similar structure and catalytic center
    Authors:
    J.I.Loch, P.Worsztynowicz, J.Sliwiak, M.Grzechowiak, B.Imiolczyk, K.Pokrywka, M.Chwastyk, M.Gilski, M.Jaskolski
    Academic press:
    Acta Cryst. D (rok: 2023, tom: D79, strony: 775-791), Wydawca: IUCr Journals
    Status:
    Published
    DOI:
    10.1107/S2059798323005648 - link to the publication
  5. Biochemical characterization of L-asparaginase isoforms from Rhizobium etli - the boosting effect of zinc
    Authors:
    J.Sliwiak, P.Worsztynowicz, K.Pokrywka, M.Grzechowiak, J.I.Loch, M.Jaskolski
    Academic press:
    Frontiers in Chemistry (rok: 2024, tom: 12, strony: 45671), Wydawca: Frontiers
    Status:
    Published
    DOI:
    10.3389/fchem.2024.1373312 - link to the publication
  6. Towards a dependable dataset of structures for L-asparaginase research
    Authors:
    A.Wlodawer, Z.Dauter, J.Lubkowski, J.Loch, D.Brzezinski, M.Gilski, M.Jaskolski
    Academic press:
    Acta Crystallographica Section D (rok: 2024, tom: 80, strony: 506-527), Wydawca: IUCr Journals
    Status:
    Published
    DOI:
    10.1107/S2059798324005461 - link to the publication
  7. Rhizobium etli has two L-asparaginases with low sequence identity but similar structure and catalytic center
    Authors:
    J.I.Loch, P.Worsztynowicz, J.Sliwiak, M.Grzechowiak, B.Imiolczyk, K.Pokrywka, M.Chwastyk, M.Gilski, M.Jaskolski
    Academic press:
    Acta Cryst. D (rok: 2023, tom: D79, strony: 775-791), Wydawca: IUCr Journals
    Status:
    Published
    DOI:
    10.1107/S2059798323005648 - link to the publication
  8. Crystal structures of the elusive Rhizobium etli l-asparaginase reveal a peculiar active site
    Authors:
    2 J.I.Loch, B.Imiolczyk, J.Sliwiak, A.Wantuch, M.Bejger, M.Gilski, M.Jaskolski
    Academic press:
    NATURE COMMUNICATIONS (rok: 2021, tom: 12, strony: Article Number 6717), Wydawca: Nature Publishing Group
    Status:
    Published
    DOI:
    10.1038/s41467-021-27105-x - link to the publication
  9. Massive annotation of bacterial l-asparaginases reveals their puzzling distribution and frequent gene transfer events
    Authors:
    3 A.Zielezinski, J.Loch, W.M.Karłowski, M.Jaskolski
    Academic press:
    Nature (rok: 2022, tom: nie dotyczy, strony: nie dotyczy), Wydawca: Springer Nature
    Status:
    Published
    DOI:
    10.1038/s41598-022-19689-1 - link to the publication
  10. Structural and biophysical aspects of l-asparaginases: a growing family with amazing diversity
    Authors:
    1 J.Loch, M.Jaskolski
    Academic press:
    IUCRJ (rok: 2021, tom: 8, strony: 514-531), Wydawca: INT UNION CRYSTALLOGRAPHY
    Status:
    Published
    DOI:
    10.1107/S2052252521006011 - link to the publication
  11. Probing the active site of Class 3 L-asparaginase by mutagenesis. I. Tinkering with the zinc coordination site of ReAV
    Authors:
    K.Pokrywka, P.Worsztynowicz, J.Sliwiak, M.Grzechowiak, J.I.Loch, M.Ruszkowski, M.Gilski, M.Jaskolski
    Academic press:
    Frontiers in Chemistry (rok: 2024, tom: 12, strony: 45672), Wydawca: Frontiers
    Status:
    Published
    DOI:
    10.3389/fchem.2024.1381032 - link to the publication
  12. Massive annotation of bacterial l-asparaginases reveals their puzzling distribution and frequent gene transfer events
    Authors:
    3 A.Zielezinski, J.Loch, W.M.Karłowski, M.Jaskolski
    Academic press:
    Nature (rok: 2022, tom: nie dotyczy, strony: nie dotyczy), Wydawca: Springer Nature
    Status:
    Published
    DOI:
    10.1038/s41598-022-19689-1 - link to the publication

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