Informacja

Drogi użytkowniku, aplikacja do prawidłowego działania wymaga obsługi JavaScript. Proszę włącz obsługę JavaScript w Twojej przeglądarce.

English (EN)·Polski (PL)·Yкраїнський (UK)
Przejdź do strony domowej biblioteki Centralna Biblioteka Wojskowa Link otwiera się w nowym oknie Logo biblioteki Prolib Integro - strona głównaCentralna Biblioteka Wojskowa

Wyszukujesz frazę "Sikora, Jacek" wg kryterium: Autor

  Lista filtrów
Wyrównaj
    Wyświetlanie 1-2 z 2
    Tytuł:
    Polish publishers Open Access policies database - functionalities and role in the implementation of openness policies
    Autorzy:
    Leszczewicz, Agnieszka
    Stankevic, Magdalena
    Sikora, Jacek
    Powiązania:
    https://bibliotekanauki.pl/articles/1991142.pdf
    Data publikacji:
    2021-12-30
    Wydawca:
    Politechnika Gdańska
    Tematy:
    publishing policy
    Polish Publishers Open Access Policy
    Open Access
    Plan S
    publication model
    scientific disciplines
    Opis:
    The aim of the article is to present a base of Polish Publishers Open Access Policies as a tool supporting the scientific community in the implementation of openness policies. It is the first national platform to gather and analyze a publishing policy in the field of Open Access to Polish scientific journals. For scientists, it is a tool for searching for a Polish journal meeting certain criteria. It enables grant recipients to verify whether the journal meets the principles of Plan S. The database also provides information on the principles of using intellectual property.The functionalities of the database were analyzed based on NCN’s policy comparing them with the principles of publishing research results in Open Access. The specific criteria used in the Polish Publishers Open Access Policies database were compared with other databases: Arianta, SHERPA/RoMEO. The analysis shows that the Polish Publishers Open Access Policy is the only national database for Polish scientific journals, bringing together in one place information necessary for the scientific community on publication in Open Access. The database facilitates project preparation and implementation. Academic librarians, promoting the idea of Open Science, support the scientific community at each stage of the activity described, providing tools, knowledge base and competences.
    Źródło:
    TASK Quarterly. Scientific Bulletin of Academic Computer Centre in Gdansk; 2021, 25, 4; 473-490
    1428-6394
    Pojawia się w:
    TASK Quarterly. Scientific Bulletin of Academic Computer Centre in Gdansk
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Altered mouse leukemia L1210 thymidylate synthase, associated with cell resistance to 5-fluoro-dUrd, is not mutated but rather reflects posttranslational modification
    Autorzy:
    Cieśla, Joanna
    Frączyk, Tomasz
    Zieliński, Zbigniew
    Sikora, Jacek
    Rode, Wojciech
    Powiązania:
    https://bibliotekanauki.pl/articles/1041288.pdf
    Data publikacji:
    2006
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    protein phosphorylation
    L1210
    thymidylate synthase
    posttranslational modification
    FdUrd resistance
    Opis:
    Thymidylate synthase purified from 5-fluoro-dUrd-resistant mouse leukemia L1210 cells (TSr) was less sensitive to slow-binding inhibition by 5-fluoro-dUMP than the enzyme from the parental cells (TSp), both enzyme forms differing also in sensitivity to several other dump analogues, apparent molecular weights of monomer and dimer, and temperature dependence of the catalyzed reaction. Direct sequencing of products obtained from RT-PCR, performed on total RNA isolated from the parental and 5-fluoro-dUrd-resistant cells, proved both nucleotide sequences to be identical to the mouse thymidylate synthase coding sequence published earlier (NCBI protein database access no. NP_067263). This suggests that the altered properties of TSr are caused by a factor different than protein mutation, presumably posttranslational modification. As a possibility of rat thymidylate synthase phosphorylation has been recently demonstrated (Samsonoff et al. (1997) J Biol Chem 272: 13281), the mouse enzyme amino-acid sequence was analysed, revealing several potential phosphorylation sites. In order to test possible influence of the protein phosphorylation state on enzymatic properties, endogenous TSp and TSr were purified in the presence of inhibitors of phosphatases. Although both enzyme forms were phosphorylated, as shown by electrophoretical separation followed by phosphoprotein detection, the extent of phosphorylation was apparently similar. However, the same two purified enzyme preparations, compared to the corresponding preparations purified in the absence of phosphatase inhibitors, showed certain properties, including sensitivity to the slow-binding inhibition by FdUMP, altered. Thus properties dependence on phosphorylation was indicated.
    Źródło:
    Acta Biochimica Polonica; 2006, 53, 1; 189-198
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-2 z 2

      Ta witryna wykorzystuje pliki cookies do przechowywania informacji na Twoim komputerze. Pliki cookies stosujemy w celu świadczenia usług na najwyższym poziomie, w tym w sposób dostosowany do indywidualnych potrzeb. Korzystanie z witryny bez zmiany ustawień dotyczących cookies oznacza, że będą one zamieszczane w Twoim komputerze. W każdym momencie możesz dokonać zmiany ustawień dotyczących cookies