Wynik wyszukiwania w bazie Polska Bibliografia Lekarska GBL

Zapytanie: BUJNICKI
Liczba odnalezionych rekordów: 2



Przejście do opcji zmiany formatu | Wyświetlenie wyników w wersji do druku

1/2

Tytuł oryginału: Angiogenesis inhibitors specific for methionine aminopeptidase 2 as drugs for malaria and Leishmaniasis.
Autorzy: Zhang Peng, Nicholson Diarmuid E., Bujnicki Janusz M., Su Xinzhuan, Brendle James J., Ferdig Michael, Kyle Dennis E., Milhous Wilbur K., Chiang Peter K.
Źródło: J. Biomed. Sci. 2002: 9 (1) s.34-40, il., tab., bibliogr. 27 poz.
Sygnatura GBL: 313,488

Hasła klasyfikacyjne GBL:
  • mikrobiologia
  • farmacja

    Typ dokumentu:
  • praca doświadczalna
  • praca opublikowana za granicą
  • tytuł obcojęzyczny

    Wskaźnik treści:
  • in vitro

    Streszczenie angielskie: Methionine aminopeptidase 2(MetAP2) is responsible for the hydrolysis of the initiator methionine molecule from the majority of newly synthesized proteins. We have cloned the MetAP2 gene from the malaria parasite Plasmodium falciparum (PfMetAP2; GenBank accession number AF348320). The cloned PfMetAP2 has no intron, consists of 1,544 bp and encodes a protein of 354 amino acids with a molecular mass of 40,537 D and an overall base composition of 72.54 p.c. A + T. PfMetAP2 has 40 p.c. sequence identity with human MetAP2 and 45 p.c. identity with yeast MetAP2, and is located in chromosome 14 of P. falciparum. The three-dimensional structure of PfMetAP2 has been modeled based on the crystal structure of human MetAP2, and several amino acid side chains protruding into the binding pocket that differ between the plasmodial and human enzyme have been identified. The specific MetAP2 inhibitors, fumagilin and TNP-470, potently blocked in vitro growth of P. falciparum and Leishmania donovani, with IC50 values similar to the prototype drugs. Furthermore, in the case of P. falciparum, the chloroquine-resistant strains are equally susceptible to these two compounds.


    2/2

    Tytuł oryginału: Fold-recognition analysis predicts that the Tag protein family shares a common domain with the helix-hairpin-helix DNA glycosylases.
    Autorzy: Bujnicki Janusz M., Rychlewski Leszek
    Źródło: DNA Repair 2002: 1 (5) s.391-395, il., bibliogr. 30 poz.
    Sygnatura GBL: 304,952

    Hasła klasyfikacyjne GBL:
  • genetyka
  • mikrobiologia

    Typ dokumentu:
  • praca opublikowana za granicą
  • tytuł obcojęzyczny

    Streszczenie angielskie: The Escherichia coli protein Tag is traditionally regarded as an archetype of one of four classes of N-alkylpurine DNA glycosylases. However, its structure and phylogenetic relationship to other glycosylases emains a mystery. Fold-recognition and sequence profile analyses suggest that Tag shares the catalytic domain with helix-hairpin-helix (HhH) glycosylases such as MutY, AlkA and EndoIII, but its N- and C-termini together form a unique His2Cys2 cluster. The findings presented in this paper provide insight into sequence-structure-function relationships in the Tag family and should aid in a more precise definition of the common core of the HhH superfamily of glycosylases involved in DNA repair.

    stosując format: