Results 181 to 190 of about 41,721 (227)
Some of the next articles are maybe not open access.
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
openaire +3 more sources
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
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources