Results 181 to 190 of about 61,046 (231)
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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
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
Rhodopsin maturation antagonized by dominant rhodopsin mutants
Visual Neuroscience, 1998ninaED1, a dominant allele of the major Drosophila rhodopsin gene, expresses a rhodopsin that is predominantly recovered in a 80-kD complex that likely represents rhodopsin dimers. By driving either ninaED1 or ninaE+ expression from a heat-shock promoter, we show that the 80-kD rhodopsin complex forms immediately after gene activation.
P, Kurada +4 more
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
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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
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
exaly +3 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
exaly +3 more sources
Journal of Supramolecular Structure, 1973
AbstractPurified, lipid‐free rhodopsin has been incorporated into bilayers of natural and synthetic phosphatidyl cholines and a natural digalactosyl diglyceride. Successful incorporation and high regenerability of rhodopsin appears to depend on the nature of the hydrocarbon chains and not specifically on the type of polar head group of the lipids ...
K, Hong, Y S, Chen, W L, Hubbell
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AbstractPurified, lipid‐free rhodopsin has been incorporated into bilayers of natural and synthetic phosphatidyl cholines and a natural digalactosyl diglyceride. Successful incorporation and high regenerability of rhodopsin appears to depend on the nature of the hydrocarbon chains and not specifically on the type of polar head group of the lipids ...
K, Hong, Y S, Chen, W L, Hubbell
openaire +2 more sources
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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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
openaire +2 more sources