Results 201 to 210 of about 38,017 (242)
Some of the next articles are maybe not open access.
Journal of Biochemistry, 1999
Following the discovery of the bacteriorhodopsin proton pump in Halobacterium halobium (salinarum), not only the halorhodopsin halide pump and two photosensor rhodopsins (sensory rhodopsin and phoborhodopsin) in the same species, but also homologs of these four rhodopsins in strains of other genera of Halobacteriaceae have been reported.
Y, Mukohata +3 more
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Following the discovery of the bacteriorhodopsin proton pump in Halobacterium halobium (salinarum), not only the halorhodopsin halide pump and two photosensor rhodopsins (sensory rhodopsin and phoborhodopsin) in the same species, but also homologs of these four rhodopsins in strains of other genera of Halobacteriaceae have been reported.
Y, Mukohata +3 more
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Rhodopsin and Phototransduction
1993Publisher Summary When light strikes a rod photoreceptor cell in the retina, rhodopsin molecules become photoexcited and a series of biochemical events rapidly follows. Photoexcited rhodopsin activates a G protein, transducin, which in turn activates a cyclic guanosine monophosphate (cGMP)-phosphodiesterase (PDE).
P A, Hargrave, J H, McDowell
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Nature New Biology, 1973
THE structure of the ROS disk membrane is an open question and more data are needed to resolve it. Essential new data are rapidly becoming available and after answering Vanderkooi's criticisms of our previous interpretation1 we shall briefly comment on the current data.
E A, Dratz, S, Schwartz
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THE structure of the ROS disk membrane is an open question and more data are needed to resolve it. Essential new data are rapidly becoming available and after answering Vanderkooi's criticisms of our previous interpretation1 we shall briefly comment on the current data.
E A, Dratz, S, Schwartz
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Photoisomerization in Rhodopsin
Biochemistry (Moscow), 2001This article reviews the primary reaction processes in rhodopsin, a photoreceptive pigment for twilight vision. Rhodopsin has an 11-cis retinal as the chromophore, which binds covalently with a lysine residue through a protonated Schiff base linkage.
H, Kandori, Y, Shichida, T, Yoshizawa
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Radioimmunoassay for rhodopsin
Experimental Eye Research, 1980Abstract A radioimmunoassay for rhodopsin was devised using [125I]rhodopsin and antibody to purified bovine rhodopsin in a double antibody procedure that can quantify the concentration of this visual pigment when present in picomolar amounts. The method demonstrated a high degree of sensitivity, reproducibility, and specificity, and is applicable to ...
B B, Lentrichia +2 more
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Rhodopsin phosphorylation and its role in photoreceptor function
Vision Research, 1998 Light-stimulated phosphorylation of rhodopsin was first described 25 years ago. This paper reviews the progress that has been made towards (i) understanding the nature of the enzymes that phosphorylate and dephosphorylate rhodopsin (ii) identifying the ...
James B Hurley
exaly +2 more sources
2018
Microbial rhodopsins (MRs) are a large family of photoactive membrane proteins, found in microorganisms belonging to all kingdoms of life, with new members being constantly discovered. Among the MRs are light-driven proton, cation and anion pumps, light-gated cation and anion channels, and various photoreceptors.
Ivan, Gushchin, Valentin, Gordeliy
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Microbial rhodopsins (MRs) are a large family of photoactive membrane proteins, found in microorganisms belonging to all kingdoms of life, with new members being constantly discovered. Among the MRs are light-driven proton, cation and anion pumps, light-gated cation and anion channels, and various photoreceptors.
Ivan, Gushchin, Valentin, Gordeliy
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Deactivation of Photoactivated Rhodopsin by Rhodopsin-Kinase and Arrestin
Journal of Receptor Research, 1987Photoactivated rhodopsin (R) catalyses, by repetitively interacting with many copies of a guanosine nucleotide binding protein (transducin), the amplified binding of GTP to transducin molecules which then activate cyclic GMP phosphodiesterase. Electrophysiologists recently have shown that cyclic GMP keeps ion channels in the plasma membrane of the rod ...
H, Kühn, U, Wilden
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Thermal decomposition of rhodopsin, photoregenerated rhodopsin and P470
Vision Research, 1968Abstract The thermal stabilities of rhodopsin and photoregenerated rhodopsin in the temperature range 40–60°C are determined and found to be the same. The thermal decomposition of P470, produced by photolysis of metarhodopsin II, is measured in the temperature range 23–40°C.
B N, Baker, T P, Williams
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Phosphorylation of rhodopsin: Most rhodopsin molecules are not phosphorylated
Biochemical and Biophysical Research Communications, 1974Abstract Phosphorylation of rod membrane proteins is a light-dependent reaction. Most rhodopsin molecules, however, are not phosphorylated. The protein that is highly phosphorylated (>3 moles phosphate per mole phosphorylated protein) appears to be a rhodopsin species that is different from the rest or is located in different parts of the rod ...
H, Shichi, R L, Somers, P J, O'Brien
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