Elsevier

Vision Research

Volume 26, Issue 12, 1986, Pages 1881-1895
Vision Research

Molecular biology of the visual pigments

https://doi.org/10.1016/0042-6989(86)90115-XGet rights and content

First page preview

First page preview
Click to open first page preview

References (76)

  • KoikeS. et al.

    Isolation and nucleo-tide sequence of a partial cDNA clone for bovine opsin

    Biochem. biophys. Res. Commun.

    (1983)
  • KühnH.

    Interactions between photoexcited rhodopsin and light-activated enzymes in rods

    Prog. Retinal Res.

    (1984)
  • KyteJ. et al.

    A simple method for displaying the hydropathic character of a protein

    J. Molec. Biol.

    (1982)
  • NathansJ. et al.

    Isolation, sequence analysis and intro-nexon arrangement of the gene encoding bovine rhodopsin

    Cell

    (1983)
  • O'TousaJ.E. et al.

    The Drosophila nina E gene encodes an opsin

    Cell

    (1985)
  • PappinD.J.C. et al.

    A structural model for ovine rhodopsin

    Int. J. Biol. Macromol.

    (1984)
  • PaulsenR. et al.

    Light-activated phosphorylation of cephalopod rhodopsin

    FEBS Lett.

    (1978)
  • RothschildK.J. et al.

    A spectroscopic study of rhodopsin alpha-helix orientation

    Biophys. J.

    (1980)
  • SchwartzS. et al.

    An analysis of lamellar x-ray diffraction from disordered membrane multilayers with application to data from retinal rod outer segments

    Biophys. J.

    (1975)
  • YoungD. et al.

    Isolation and characterization of a new cellular oncogene encoding a protein with multiple potential transmembrane domains

    Cell

    (1986)
  • ZukerC.S. et al.

    Isolation and structure of a rhodopsin gene from D. melanogaster

    Cell

    (1985)
  • AlbertA.D. et al.

    Independent structural domains in the membrane protein bovine rhodopsin

    Biochemistry

    (1978)
  • ArgosP. et al.

    Structural prediction of membrane bound proteins

    Eur. J. Biochem.

    (1982)
  • BachrW. et al.

    Characterization of bovine rhodopsin mRNA and cDNA

    Biophys. J.

    (1983)
  • BagleyK.A. et al.

    Fourier-transform infrared difference spectroscopy of rhodopsin and its photo-products at low temperature

    Biochemistry

    (1985)
  • BenovicJ.L. et al.

    Light-dependent phosphorylation or rhodopsin by β-adrenergic receptor kinase

    Nature, Lond.

    (1986)
  • BitenskyM.W. et al.

    Functional exchange of components between light-activated photoreceptor phosphodiesterase and hormone-activated adenylate cyclase systems

  • BlumenfeldA. et al.

    Light-activated guanosinetriphosphatase in Musca eye membranes resembles the prolonged depolarizing afterpotential in photoreceptor cells

  • ChabreM.

    Molecular mechanism of visual photo-transduction in retinal rod cells

    Ann. Rev. Biophys. Chem.

    (1985)
  • ChabreM. et al.

    Orientation of aromatic residues in rhodopsin. Rotation of one tryptophan upon the meta I—meta II transition after illumination

    Photochem. Photobiol.

    (1979)
  • CobbsW.H. et al.

    Cyclic GMP increases photocurrent and light sensitivity of retinal cones

    Nature, Lond.

    (1985)
  • CorlessJ.M. et al.

    Two-dimensional rhodopsin crystals from disk membranes of frog retinal rod outer segments

  • DavisonM.D. et al.

    Modification of ovine opsin with the photosensitive hydrophobic probe I-azido-4-[125I]iodobenzene

    Biochem. J.

    (1986)
  • DixonR.A.F. et al.

    Cloning of the gene and cDNA for mammalian β-adrenergic receptor and homology with rhodopsin

    Nature, Lond.

    (1986)
  • DoolittleR.F.

    Proteins

    Scient. Am.

    (1985)
  • FesenkoE.F. et al.

    Induction by cyclic GMP of cationic conductance in plasma membrane of retinal rod outer segment

    Nature, Lond.

    (1985)
  • FindlayJ.B.C.

    The biosynthetic, functional and evolutionary implications of the structure of rhodopsin

  • FungB.K.-K.

    The light-activated cyclic GMP phosphodiesterase system in retinal rods

  • Cited by (226)

    • Targeted differential illumination improves reproductive traits of broiler breeder males

      2021, Poultry Science
      Citation Excerpt :

      Photons of light absorbed through these photoreceptors are converted into neural signals through photochemical changes in the retina whereby opsin–protein complexes are isomerized after binding with vitamin A (Hart, 2001). These signals are used to activate, enhance or decelerate many biological processes in chickens (Applebury and Hargrave, 1986). However, studies have shown that in domestic fowl, among other bird species, in contrast to mammals, longer wavelengths are capable of penetrating directly through the skull and tissues to the hypothalamus, which contains photoreceptors known as extraretinal photoreceptors (ERPR) (Foster and Hankins, 2002).

    • Spectrum-frequency and genotype–phenotype analysis of rhodopsin variants

      2021, Experimental Eye Research
      Citation Excerpt :

      Rhodopsin, encoded by RHO, is an archetypal G protein-coupled receptor with seven transmembrane (TM) α-helices (Palczewski, 2000; Probst et al., 1992). There is an opsin binding site in the seventh TM domain of rhodopsin, from amino acid 290 to amino acid 306 (Applebury and Hargrave, 1986; Shen et al., 1994). This forms an α-helices pocket.

    • Targeted differential monochromatic lighting improves broiler breeder reproductive performance

      2020, Poultry Science
      Citation Excerpt :

      All photoreceptors contain opsins—protein complexes that binds to vitamin-A— that isomerizes in response to light (Bownds, 1967; Hart, 2001). Isomerization allows the opsin molecule to bind a protein involved in signal transfer to the brain—resulting in a biochemical cascade that changes neurotransmitter release from the photoreceptor (Applebury and Hargrave, 1986). The neuroendocrine response to photostimulation is expressed by release of gonadotropin-releasing hormone (GnRH) from the hypothalamus.

    • Molecular chaperones and photoreceptor function

      2008, Progress in Retinal and Eye Research
    View all citing articles on Scopus
    View full text