Results 241 to 250 of about 69,355 (271)
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Halobacterial Rhodopsins

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

Human Rhodopsin

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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Rhodopsin maturation antagonized by dominant rhodopsin mutants

Visual Neuroscience, 1998
ninaED1, 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

Microbial Rhodopsins

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

Rhodopsin–lipid interactions

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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Photoisomerization in Rhodopsin

Biochemistry (Moscow), 2001
This 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
openaire   +2 more sources

Rhodopsin and Phototransduction

1993
Publisher 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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Where is Rhodopsin?

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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Radioimmunoassay for rhodopsin

Experimental Eye Research, 1980
Abstract 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

2015
Part I: Historical Overview 1. The G Protein-Coupled Receptor Rhodopsin: A Historical Perspective Lukas Hofmann and Krzysztof Palczewski Part II: Rhodopsin Expression, Regeneration and Purification for Structural Studies 2. Rhodopsin Purification from Dark Adapted Bovine Retina Elise Blankenship and David T. Lodowski 3.
openaire   +1 more source

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