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Wyszukujesz frazę "protein phosphatase 2A" wg kryterium: Temat

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    Wyświetlanie 1-4 z 4
    Tytuł:
    Interaction of maize (Zea mays) protein phosphatase 2A with tubulin
    Autorzy:
    Awotunde, Olubunmi
    Lechward, Katarzyna
    Krajewska, Katarzyna
    Żołnierowicz, Stanisław
    Muszyńska, Grażyna
    Powiązania:
    https://bibliotekanauki.pl/articles/1043655.pdf
    Data publikacji:
    2003
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    protein phosphatase 2A
    tubulin
    protein-protein interaction
    plant cytoskeleton organization
    maize
    Opis:
    Immunological and biochemical evidence has been obtained for an interaction of maize protein phosphatase 2A (PP2A) holoenzyme with tubulin. Tubulin co-purifies with maize seedling PP2A. Affinity chromatography of the maize PP2A preparation on immobilized tubulin revealed two peaks of phosphorylase a phosphatase activity. In one of the peaks, the catalytic (C) and constant regulatory (A) subunits of PP2A were identified by Western blotting. The subunits (C and A) of PP2A were co-immunoprecipitated from maize seedlings homogenate by an anti-α-tubulin antibody. The interaction of plant PP2A with tubulin indicates a possible role of reversible protein phosphorylation in the dynamic structure of plant cytoskeleton.
    Źródło:
    Acta Biochimica Polonica; 2003, 50, 1; 131-138
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Protein phosphatase 2A: Variety of forms and diversity of functions
    Autorzy:
    Lechward, Katarzyna
    Awotunde, Olubunmi
    Świątek, Wojciech
    Muszyńska, Grażyna
    Powiązania:
    https://bibliotekanauki.pl/articles/1044037.pdf
    Data publikacji:
    2001
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    protein phosphatase 2A
    signal transduction
    protein-protein interactions
    reversible phosphorylation
    cell cycle
    carcinogenesis.
    Opis:
    Protein phosphatase 2A (PP2A) comprises a diverse family of phosphoserine-and phosphothreonine-specific phosphatases present in all eukaryotic cells. All forms of PP2A contain a catalytic subunit (PP2Ac) which forms a stable complex with the structural subunit PR65/A. The heterodimer PP2Ac-PR65/A associates with regulatory proteins, termed variable subunits, in order to form trimeric holoenzymes attributed with distinct substrate specificity and targeted to different subcellular compartments. PP2Ac activity can be modulated by reversible phosphorylation on Tyr307 and methylation on C-terminal Leu309. Studies on PP2A have shown that this enzyme may be implicated in the regulation of metabolism, transcription, RNA splicing, translation, differentiation, cell cycle, oncogenic transformation and signal transduction.
    Źródło:
    Acta Biochimica Polonica; 2001, 48, 4; 921-933
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    PP2A phosphatase interacts with CPK kinase and regulates pathogenesis responses triggered by intracellular ROS signals
    Autorzy:
    Kangasjarvi, S.
    Denessiouk, K.
    Trotta, A.
    Konert, G.
    Rahikainen, M.
    Li, S.
    Mhamdi, A.
    Noctor, G.
    Powiązania:
    https://bibliotekanauki.pl/articles/80995.pdf
    Data publikacji:
    2013
    Wydawca:
    Polska Akademia Nauk. Czytelnia Czasopism PAN
    Tematy:
    conference
    protein phosphatase 2A
    calcium-dependent protein kinase
    reactive oxygen species
    organelle
    protein kinase
    plant immunity
    Arabidopsis
    Źródło:
    BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2013, 94, 2
    0860-7796
    Pojawia się w:
    BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Theoretical models of catalytic domains of protein phosphatases 1 and 2A with Zn2+ and Mn2+ metal dications and putative bioligands in their catalytic centers.
    Autorzy:
    Woźniak-Celmer, Edyta
    Ołdziej, Stanisław
    Ciarkowski, Jerzy
    Powiązania:
    https://bibliotekanauki.pl/articles/1044161.pdf
    Data publikacji:
    2001
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    protein phosphatase inhibitors
    constrained simulated annealing
    protein phosphatase 1A and 2B
    molecular dynamics
    homology modeling
    Opis:
    The oligomeric metalloenzymes protein phosphatases dephosphorylate OH groups of Ser/Thr or Tyr residues of proteins whose actions depend on the phosphorus signal. The catalytic units of Ser/Thr protein phosphatases 1, 2A and 2B (PP1c, PP2Ac and PP2Bc, respectively), which exhibit about 45% sequence similarity, have their active centers practically identical. This feature strongly suggests that the unknown structure of PP2Ac could be successfully homology-modeled from the known structures of PP1c and/or PP2Bc. Initially, a theoretical model of PP1c was built, including a phosphate and a metal dication in its catalytic site. The latter was modeled, together with a structural hydroxyl anion, as a triangular pseudo-molecule (Zno or Mno), composed of two metal cations (double Zn2+ or Mn2+, respectively) and the OH- group. To the free PP1c two inhibitor sequences R29RRRPpTPAMLFR40 of DARPP-32 and R30RRRPpTPATLVLT42 of Inhibitor-1, and two putative substrate sequences LRRApSVA and QRRQRKpRRTI were subsequently docked. In the next step, a free PP2Ac model was built via homology re-modeling of the PP1c template and the same four sequences were docked to it. Thus, together, 20 starting model complexes were built, allowing for combination of the Zno and Mno pseudo-molecules, free enzymes and the peptide ligands docked in the catalytic sites of PP1c and PP2Ac. All models were subsequently subjected to 250-300 ps molecular dynamics using the AMBER 5.0 program. The equilibrated trajectories of the final 50 ps were taken for further analyses. The theoretical models of PP1c complexes, irrespective of the dication type, exhibited increased mobilities in the following residue ranges: 195-200, 273-278, 287-209 for the inhibitor sequences and 21-25, 194-200, 222-227, 261, 299-302 for the substrate sequences. Paradoxically, the analogous PP2Ac models appeared much more stable in similar simulations, since only their "prosegment" residues 6-10 and 14-18 exhibited an increased mobility in the inhibitor complexes while no areas of increased mobility were found in the substrate complexes. Another general observation was that the complexes with Mn dications were more stable than those with Zn dications for both PP1c and PP2Ac units.
    Źródło:
    Acta Biochimica Polonica; 2001, 48, 1; 35-52
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-4 z 4

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