Results 191 to 200 of about 38,017 (242)
Optoretinography reveals rapid rod photoreceptor movement upon rhodopsin activation. [PDF]
Light Sci ApplLi H +10 more
europepmc +1 more source
Profound Effect of Light on Cysts in X-Linked Retinoschisis. [PDF]
Invest Ophthalmol Vis SciHassan S +10 more
europepmc +1 more source
ON RHODOPSIN IN SOLUTION [PDF]
Journal of General Physiology, 1938 1. The properties of rhodopsin in solution have been examined in preparations from marine fishes, frogs, and mammals. 2. The bleaching of neutral rhodopsin in solution includes a photic and at least three thermal ("dark") processes. Thermal reactions account for approximately half the total fall in extinction at 500 mµ. 3.
George Wald, Wald George
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Journal of Cell Science, 2021
ABSTRACTRhodopsins are photoreceptive membrane proteins consisting of a common heptahelical transmembrane architecture that contains a retinal chromophore. Rhodopsin was first discovered in the animal retina in 1876, but a different type of rhodopsin, bacteriorhodopsin, was reported to be present in the cell membrane of an extreme halophilic archaeon ...
Takashi Nagata, Keiichi Inoue
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ABSTRACTRhodopsins are photoreceptive membrane proteins consisting of a common heptahelical transmembrane architecture that contains a retinal chromophore. Rhodopsin was first discovered in the animal retina in 1876, but a different type of rhodopsin, bacteriorhodopsin, was reported to be present in the cell membrane of an extreme halophilic archaeon ...
Takashi Nagata, Keiichi Inoue
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Rhodopsin and phototransduction
Journal of Photochemistry and Photobiology B: Biology, 1999Recent studies on rhodopsin structure and function are reviewed and the properties of vertebrate as well as invertebrate rhodopsin described. Open issues such as the 'red shift' of the absorbance spectra are emphasized in the light of the present model of the retinal-binding pocket. The processes that restore the rhodopsin content in photoreceptors are
I M Pepe
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2022
The first microbial rhodopsin, a light-driven proton pump bacteriorhodopsin from Halobacterium salinarum (HsBR), was discovered in 1971. Since then, this seven-α-helical protein, comprising a retinal molecule as a cofactor, became a major driver of groundbreaking developments in membrane protein research.
Gordeliy, V. +9 more
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The first microbial rhodopsin, a light-driven proton pump bacteriorhodopsin from Halobacterium salinarum (HsBR), was discovered in 1971. Since then, this seven-α-helical protein, comprising a retinal molecule as a cofactor, became a major driver of groundbreaking developments in membrane protein research.
Gordeliy, V. +9 more
openaire +3 more sources
THE MOLECULAR WEIGHT OF RHODOPSIN AND THE NATURE OF THE RHODOPSIN-DIGITONIN COMPLEX [PDF]
Journal of General Physiology, 1954 The sedimentation behavior of aqueous solutions of digitonin and of cattle rhodopsin in digitonin has been examined in the ultracentrifuge. In confirmation of earlier work, digitonin was found to sediment as a micelle (D-1) with an s20 of about 6.35 Svedberg units, and containing at least 60 molecules.
Ruth Hubbard, Hubbard Ruth
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Experimental Eye Research, 1974
Abstract The particulate oxido-reductase of cattle rod outer segment membranes, most likely involved in the rhodopsin cycle, appears to be quite stereospecific. It is shown that 11-cis-retinol is only oxidized by this enzyme after previous isomerization, since incubation with 11-cis-retinol and NADP+ only yields all-trans-retinal and a minor amount ...
F J, Daemen, J P, Rotmans, S L, Bonting
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Abstract The particulate oxido-reductase of cattle rod outer segment membranes, most likely involved in the rhodopsin cycle, appears to be quite stereospecific. It is shown that 11-cis-retinol is only oxidized by this enzyme after previous isomerization, since incubation with 11-cis-retinol and NADP+ only yields all-trans-retinal and a minor amount ...
F J, Daemen, J P, Rotmans, S L, Bonting
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Science, 1958
Human rhodopsin in aqueous solution has λ max. of 493 mμ and is lower in the spectrum than the rhodopsins of all other known vertebrates, with the exception of certain deep-sea fishes. Its molar extinction is 40,000 ± 800. Like other rhodopsins, it bleaches to a mixture of opsin and all- trans
G, WALD, P K, BROWN
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Human rhodopsin in aqueous solution has λ max. of 493 mμ and is lower in the spectrum than the rhodopsins of all other known vertebrates, with the exception of certain deep-sea fishes. Its molar extinction is 40,000 ± 800. Like other rhodopsins, it bleaches to a mixture of opsin and all- trans
G, WALD, P K, BROWN
openaire +2 more sources