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Wyszukujesz frazę "rhodopsin" wg kryterium: Temat

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    Wyświetlanie 1-3 z 3
    Tytuł:
    Mutations in the human rhodopsin gene and polymorphisms in peripherin-RDS gene in Lithuanian autosomal dominant retinitis pigmentosa patients
    Autorzy:
    Kucinskas, V
    Payne, A.M.
    Ambrasiene, D.
    Jurgelevicius, V.
    Steponaviciute, D.
    Arciuliene, J.V.
    Daktaraviciene, E.
    Bhattacharya, S.
    Powiązania:
    https://bibliotekanauki.pl/articles/2043868.pdf
    Data publikacji:
    1999
    Wydawca:
    Polska Akademia Nauk. Czytelnia Czasopism PAN
    Tematy:
    retinal degeneration
    polymorphism
    patient
    rhodopsin gene
    man
    retinitis pigmentosa
    mutation
    Lithuania
    Źródło:
    Journal of Applied Genetics; 1999, 40, 1; 53-61
    1234-1983
    Pojawia się w:
    Journal of Applied Genetics
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Photoreceptor guanylate cyclase variants: cGMP production under control.
    Autorzy:
    Sokal, Izabela
    Alekseev, Andrei
    Palczewski, Krzysztof
    Powiązania:
    https://bibliotekanauki.pl/articles/1043388.pdf
    Data publikacji:
    2003
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    rhodopsin
    photoreceptor cells
    guanylate cyclase
    Ca2+-binding proteins
    guanylate cyclase-activating protein
    retina
    Opis:
    Changes in the Ca2+ concentration are thought to affect many processes, including signal transduction in a vast number of biological systems. However, only in few cases the molecular mechanisms by which Ca2+ mediates its action are as well understood as in phototransduction. In dark-adapted photoreceptor cells, the equilibrium level of cGMP is maintained by two opposing activities, such as phosphodiesterase (PDE) and guanylate cyclase (GC). Upon absorption of photons, rhodopsin-G-protein-mediated activation of PDE leads to a transient decrease in [cGMP] and subsequently to lowering of [Ca2+]. In turn, lower [Ca2+] increases net production of cGMP by stimulation of GC until dark conditions are re-established. This activation of GC is mediated by Ca2+-free forms of Ca2+-binding proteins termed GC-activating proteins (GCAPs). The last decade brought the molecular identification of GCs and GCAPs in the visual system. Recent efforts have been directed toward understanding the properties of GC at the physiological and structural levels. Here, we summarize the recent progress and present a list of topics of ongoing research.
    Źródło:
    Acta Biochimica Polonica; 2003, 50, 4; 1075-1095
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    G protein-coupled receptors - recent advances
    Autorzy:
    Latek, Dorota
    Modzelewska, Anna
    Trzaskowski, Bartosz
    Palczewski, Krzysztof
    Filipek, Sławomir
    Powiązania:
    https://bibliotekanauki.pl/articles/1039641.pdf
    Data publikacji:
    2012
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    G protein-coupled receptors
    chemokine receptors
    β-adrenergic receptors
    rhodopsin
    arrestin.
    G protein
    Opis:
    The years 2000 and 2007 witnessed milestones in current understanding of G protein-coupled receptor (GPCR) structural biology. In 2000 the first GPCR, bovine rhodopsin, was crystallized and the structure was solved, while in 2007 the structure of β2-adrenergic receptor, the first GPCR with diffusible ligands, was determined owing to advances in microcrystallization and an insertion of the fast-folding lysozyme into the receptor. In parallel with those crystallographic studies, the biological and biochemical characterization of GPCRs has advanced considerably because those receptors are molecular targets for many of currently used drugs. Therefore, the mechanisms of activation and signal transduction to the cell interior deduced from known GPCRs structures are of the highest importance for drug discovery. These proteins are the most diversified membrane receptors encoded by hundreds of genes in our genome. They participate in processes responsible for vision, smell, taste and neuronal transmission in response to photons or binding of ions, hormones, peptides, chemokines and other factors. Although the GPCRs share a common seven-transmembrane α-helical bundle structure their binding sites can accommodate thousands of different ligands. The ligands, including agonists, antagonists or inverse agonists change the structure of the receptor. With bound agonists they can form a complex with a suitable G protein, be phosphorylated by kinases or bind arrestin. The discovered signaling cascades invoked by arrestin independently of G proteins makes the GPCR activating scheme more complex such that a ligand acting as an antagonist for G protein signaling can also act as an agonist in arrestin-dependent signaling. Additionally, the existence of multiple ligand-dependent partial activation states as well as dimerization of GPCRs result in a 'microprocessor-like' action of these receptors rather than an 'on-off' switch as was commonly believed only a decade ago.
    Źródło:
    Acta Biochimica Polonica; 2012, 59, 4; 515-529
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-3 z 3

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