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Wyszukujesz frazę "Ciarkowski, Jerzy" wg kryterium: Autor

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    Wyświetlanie 1-10 z 10
    Tytuł:
    Interaction of class A G protein-coupled receptors with G protein.
    Autorzy:
    Ślusarz, Rafał
    Ciarkowski, Jerzy
    Powiązania:
    https://bibliotekanauki.pl/articles/1043328.pdf
    Data publikacji:
    2004
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    GPCR class A
    GPCR activation
    G protein
    Opis:
    A model for interaction of class A G protein-coupled receptor with the G protein Gα subunit is proposed using the rhodopsin-transducin (RD/Gt) prototype. The model combines the resolved interactions/distances, essential in the active RD*/Gt system, with the structure of Gtα C-terminal peptide bound to RD* while stabilizing it. Assuming the interactions involve conserved parts of the partners, the model specifies the conserved Helix 2 non-polar X- - -X, Helix 3 DRY and Helix 7/8 NP- -Y- - F RD* motifs interacting with the Gtα C-terminal peptide, in compliance with the structure of the latter. A concomitant role of Gtα and Gtγ>C-termini in stabilizing RD* could possibly be resolved assuming a receptor dimer as requisite for G protein activation.
    Źródło:
    Acta Biochimica Polonica; 2004, 51, 1; 129-136
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    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
    Tytuł:
    Signal transmission via G protein-coupled receptors in the light of rhodopsin structure determination.
    Autorzy:
    Ciarkowski, Jerzy
    Drabik, Piotr
    Giełdoń, Artur
    Kaźmierkiewicz, Rajmund
    Ślusarz, Rafał
    Powiązania:
    https://bibliotekanauki.pl/articles/1044085.pdf
    Data publikacji:
    2001
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    signal transduction
    neurohypophyseal receptors
    molecular modeling
    GPCRs
    Opis:
    G protein-coupled receptors (GPCRs) transducing diverse external signals to cells via activation of heterotrimeric GTP-binding (G) proteins, estimated to mediate actions of 60% of drugs, had been resistant to structure determination until summer 2000. The first atomic-resolution experimental structure of a GPCR, that of dark (inactive) rhodopsin, thus provides a trustworthy 3D prototype for antagonist-bound forms of this huge family of proteins. In this work, our former theoretical GPCR models are evaluated against the new experimental template. Subsequently, a working hypothesis regarding the signal transduction mechanism by GPCRs is presented.
    Źródło:
    Acta Biochimica Polonica; 2001, 48, 4; 1203-1207
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Molecular docking-based test for affinities of two ligands toward vasopressin and oxytocin receptors.
    Autorzy:
    Ślusarz, Rafał
    Kaźmierkiewicz, Rajmund
    Giełdoń, Artur
    Lammek, Bernard
    Ciarkowski, Jerzy
    Powiązania:
    https://bibliotekanauki.pl/articles/1044173.pdf
    Data publikacji:
    2001
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    simulated annealing
    bioligand docking
    GPCR receptor/bioligand interaction
    molecular dynamics
    Opis:
    Molecular docking simulations are now fast developing area of research. In this work we describe an effective procedure of preparation of the receptor-ligand complexes. The amino-acid residues involved in ligand binding were identified and described.
    Źródło:
    Acta Biochimica Polonica; 2001, 48, 1; 131-135
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Molecular modelling study of the role of cholesterol in the stimulation of the oxytocin receptor.
    Autorzy:
    Politowska, Ewa
    Kaźmierkiewicz, Rajmund
    Wiegand, Volker
    Fahrenholz, Falk
    Ciarkowski, Jerzy
    Powiązania:
    https://bibliotekanauki.pl/articles/1044168.pdf
    Data publikacji:
    2001
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    cholesterol
    AutoDock 2.4
    cholecystokinin receptor type β
    oxytocin receptor
    GPCR
    sterols
    Opis:
    Cholesterol, an integral component of membranes in Eucaryota, is a modifier of membrane properties. In vivo studies have demonstrated that cholesterol can also modulate activities of some G protein-coupled receptors (GPCRs), which are integral membrane proteins. This can result either from an effect of cholesterol on the membrane fluidity or from specific interactions of the membrane cholesterol with the receptor, as recently demonstrated for the cholecystokinin type β (CCKRβ) or the oxytocin receptor (OTR). Using molecular modelling, we studied conformational preferences of cholesterol and several of its analogues. Subsequently, we simulated the distributions of their preferred conformations around the surface of OTR, CCKRβ and a chimeric oxytocin/cholecystokinin receptor. Consequently, we suggest residues on the surface of OTR which are potentially significant in the OTR/cholesterol interaction.
    Źródło:
    Acta Biochimica Polonica; 2001, 48, 1; 83-93
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Theoretical studies of binding modes of two covalent inhibitors of cysteine proteases.
    Autorzy:
    Drabik, Piotr
    Politowska, Ewa
    Czaplewski, Cezary
    Kasprzykowski, Franciszek
    Łankiewicz, Leszek
    Ciarkowski, Jerzy
    Powiązania:
    https://bibliotekanauki.pl/articles/1044228.pdf
    Data publikacji:
    2000
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    cysteine proteases
    covalent protease inhibitors
    constrained simulated annealing
    papain
    molecular dynamics
    Opis:
    Physiological and pathological roles of cysteine proteases make them important targets for inhibitor development. Although highly potent inhibitors of this group of enzymes are known, their major drawback is a lack of sufficient specificity. Two cysteine protease covalent inhibitors, viz. (i) Z-RL-deoxo-V-peptide-epoxysuccinyl hybrid, and (ii) Z-RLVG-methyl-, have been developed and modeled in the catalytic pocket of papain, an archetypal thiol protease. A number of configurations have been generated and relaxed for each system using the AMBER force field. The catalytic pockets S3 and S4 appear rather elusive in view of the observed inhibitors' flexibility. This suggest rather limited chances for the development of selective structure-based inhibitors of thiol proteases, designed to exploit differences in the structure of catalytic pockets of various members of this family.
    Źródło:
    Acta Biochimica Polonica; 2000, 47, 4; 1061-1066
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Structural studies of cysteine proteases and their inhibitors.
    Autorzy:
    Grzonka, Zbigniew
    Jankowska, Elżbieta
    Kasprzykowski, Franciszek
    Kasprzykowska, Regina
    Łankiewicz, Leszek
    Wiczk, Wiesław
    Wieczerzak, Ewa
    Ciarkowski, Jerzy
    Drabik, Piotr
    Janowski, Robert
    Kozak, Maciej
    Jaskólski, Mariusz
    Grubb, Anders
    Powiązania:
    https://bibliotekanauki.pl/articles/1044158.pdf
    Data publikacji:
    2001
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    cysteine proteases
    structure-activity relationship
    cystatins
    synthetic inhibitors
    Opis:
    Cysteine proteases (CPs) are responsible for many biochemical processes occurring in living organisms and they have been implicated in the development and progression of several diseases that involve abnormal protein turnover. The activity of CPs is regulated among others by their specific inhibitors: cystatins. The main aim of this review is to discuss the structure-activity relationships of cysteine proteases and cystatins, as well as of some synthetic inhibitors of cysteine proteases structurally based on the binding fragments of cystatins.
    Źródło:
    Acta Biochimica Polonica; 2001, 48, 1; 1-20
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-10 z 10

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