|
Iodopsin
Vertebrate visual opsins are a subclass of ciliary opsins and mediate visual system, vision in vertebrates. They include the opsins in human rod cell, rod and cone cells. They are often abbreviated to ''opsin'', as they were the first opsins discovered and are still the most widely studied opsins. Opsins Opsin refers strictly to the apoenzyme, apoprotein (without bound retinal). When an opsin binds retinal to form a holoprotein, it is referred to as Retinylidene protein. However, the distinction is often ignored, and opsin may refer loosely to both (regardless of whether retinal is bound). Opsins are G-protein-coupled receptors (GPCRs) and must bind retinal — typically 11-cis retinal, 11-''cis''-retinal — in order to be photosensitive, since the retinal acts as the chromophore. When the Retinylidene protein absorbs a photon, the retinal isomerizes and is released by the opsin. The process that follows the isomerization and renewal of retinal is known as the visual cyc ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Rhodopsin 3D
Rhodopsin, also known as visual purple, is a protein encoded by the RHO gene and a G-protein-coupled receptor (GPCR). It is the opsin of the rod cells in the retina and a light-sensitive receptor protein that triggers visual phototransduction in rods. Rhodopsin mediates dim light vision and thus is extremely sensitive to light. When rhodopsin is exposed to light, it immediately photobleaches. In humans, it is regenerated fully in about 30 minutes, after which the rods are more sensitive. Defects in the rhodopsin gene cause eye diseases such as retinitis pigmentosa and congenital stationary night blindness. Names Rhodopsin was discovered by Franz Christian Boll in 1876. The name rhodospsin derives from Ancient Greek () for "rose", due to its pinkish color, and () for "sight". It was coined in 1878 by the German physiologist Wilhelm Friedrich Kühne (1837-1900). When George Wald discovered that rhodopsin is a holoprotein, consisting of retinal and an apoprotein, he call ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Scotopsin
Rhodopsin, also known as visual purple, is a protein encoded by the RHO gene and a G-protein-coupled receptor (GPCR). It is the opsin of the rod cells in the retina and a light-sensitive receptor protein that triggers visual phototransduction in rods. Rhodopsin mediates dim light vision and thus is extremely sensitive to light. When rhodopsin is exposed to light, it immediately photobleaches. In humans, it is regenerated fully in about 30 minutes, after which the rods are more sensitive. Defects in the rhodopsin gene cause eye diseases such as retinitis pigmentosa and congenital stationary night blindness. Names Rhodopsin was discovered by Franz Christian Boll in 1876. The name rhodospsin derives from Ancient Greek () for "rose", due to its pinkish color, and () for "sight". It was coined in 1878 by the German physiologist Wilhelm Friedrich Kühne (1837-1900). When George Wald discovered that rhodopsin is a holoprotein, consisting of retinal and an apoprotein, he calle ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Visual System
The visual system comprises the sensory organ (the eye) and parts of the central nervous system (the retina containing photoreceptor cells, the optic nerve, the optic tract and the visual cortex) which gives organisms the sense of sight (the ability to perception, detect and process visible light) as well as enabling the formation of several non-image photo response functions. It detects and interprets information from the optical spectrum perceptible to that species to "build a representation" of the surrounding environment. The visual system carries out a number of complex tasks, including the reception of light and the formation of monocular neural representations, colour vision, the neural mechanisms underlying stereopsis and assessment of distances to and between objects, the identification of a particular object of interest, motion perception, the analysis and integration of visual information, pattern recognition, accurate motor coordination under visual guidance, and mor ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Journal Of General Physiology
''Journal of General Physiology'' is a Peer review, peer-reviewed scientific journal published by Rockefeller University Press. The journal covers biology, biological, chemical substance, chemical, or Physics, physical mechanisms of broad physiology, physiological significance. The major emphasis is on physiological problems at the Cell (biology), cellular and molecule, molecular level. Editorial history The journal was established in 1918 by Jacques Loeb. Editing duties were shared with Winthrop John Van Leuven Osterhout, Winthrop Osterhout of Harvard University. The initial rationale for the journal was stated in this extract from the 1918 announcement of publication: Under the pressure of demands of medicine and other professions, physiology has developed in the direction of an applied science, with limited opportunity for the investigation of purely theoretical problems. On the other hand, the physico-chemical methods of analyzing life phenomena have thus far made little inro ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Theria
Theria (; Greek: , wild beast) is a subclass of mammals amongst the Theriiformes. Theria includes the eutherians (including the placental mammals) and the metatherians (including the marsupials) but excludes the egg-laying monotremes. Characteristics Therian mammals give birth (''see viviparity'') to live young without a shelled egg. This is possible thanks to key proteins called syncytins which allow exchanges between the mother and its offspring through a placenta, even rudimental ones such as in marsupials. Genetic studies have suggested a viral origin of syncytins through the endogenization process. The marsupials and the placental mammals evolved from a common therian ancestor that gave live birth by suppressing the mother's immune system. While the marsupials continued to give birth to an underdeveloped fetus after a short pregnancy, the ancestors of placental mammals gradually evolved a prolonged pregnancy. Therian mammals no longer have the coracoid bone, con ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Monotreme
Monotremes () are prototherian mammals of the order Monotremata. They are one of the three groups of living mammals, along with placentals (Eutheria), and marsupials (Metatheria). Monotremes are typified by structural differences in their brains, jaws, digestive tract, reproductive tract, and other body parts, compared to the more common mammalian types. In addition, they lay eggs rather than bearing live young, but, like all mammals, the female monotremes nurse their young with milk. Monotremes have been considered members of Australosphenida, a clade that contains extinct mammals from the Jurassic and Cretaceous of Madagascar, South America, and Australia, though this is disputed. The only surviving examples of monotremes are all indigenous to Australia and New Guinea, although there is evidence that they were once more widespread, as ''Monotrematum'' is known from the Paleocene of South America. The extant monotreme species are the platypus and four species of echidnas. The ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
OPN1SW
Blue-sensitive opsin is a protein that in humans is encoded by the ''OPN1SW'' gene. See also * Opsin Animal opsins are G-protein-coupled receptors and a group of proteins made light-sensitive via a chromophore, typically retinal. When bound to retinal, opsins become Retinylidene proteins, but are usually still called opsins regardless. Most pro ... References Further reading * * * * * * * * * * G protein-coupled receptors {{transmembranereceptor-stub Color vision ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
OPN1MW
Green-sensitive opsin is a protein that in humans is encoded by the ''OPN1MW'' gene. OPN1MW2 OPN1MW2 is a duplication of the OPN1MW gene, which encodes the medium wavelength sensitive (MWS) photopsin. The gene duplication is present in about 50% of X-chromosomes, so is present in 50% of males and at least once 75% of females. It caused by ... is a similar opsin. See also * Opsin References Further reading * * * * * * * * * * * * * External links GeneReviews/NIH/NCBI/UW entry on Red-Green Color Vision Defects G protein-coupled receptors Color vision {{transmembranereceptor-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
OPN1LW
OPN1LW is a gene on the X chromosome that encodes for long wave sensitive (LWS) opsin, or red cone photopigment. It is responsible for perception of visible light in the yellow-green range on the visible spectrum (around 500-570nm). The gene contains 6 exons with variability that induces shifts in the spectral range. OPN1LW is subject to homologous recombination with OPN1MW, as the two have very similar sequences. These recombinations can lead to various vision problems, such as red-green colourblindness and blue monochromacy. The protein encoded is a G-protein coupled receptor with embedded 11-''cis''-retinal, whose light excitation causes a cis-trans conformational change that begins the process of chemical signalling to the brain. Gene OPN1LW produces red-sensitive opsin, while its counterparts, OPN1MW and OPN1SW, produce green-sensitive and blue-sensitive opsin respectively. OPN1LW and OPN1MW are on the X chromosome at position Xq28. They are in a tandem array, composed of a ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Photopic Vision
Photopic vision is the vision of the eye under well-lit conditions (luminance levels from 10 to 108 cd/m2). In humans and many other animals, photopic vision allows color perception, mediated by cone cells, and a significantly higher visual acuity and temporal resolution than available with scotopic vision. The human eye uses three types of cones to sense light in three bands of color. The biological pigments of the cones have maximum absorption values at wavelengths of about 420 nm (blue), 534 nm (bluish-green), and 564 nm (yellowish-green). Their sensitivity ranges overlap to provide vision throughout the visible spectrum. The maximum efficacy is 683 lm/W at a wavelength of 555 nm (green). By definition, light at a frequency of hertz has a luminous efficacy of 683 lm/W. The wavelengths for when a person is in photopic vary with the intensity of light. For the blue-green region (500 nm), 50% of the light reaches the image point of the retina. ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Iodopsin
Vertebrate visual opsins are a subclass of ciliary opsins and mediate visual system, vision in vertebrates. They include the opsins in human rod cell, rod and cone cells. They are often abbreviated to ''opsin'', as they were the first opsins discovered and are still the most widely studied opsins. Opsins Opsin refers strictly to the apoenzyme, apoprotein (without bound retinal). When an opsin binds retinal to form a holoprotein, it is referred to as Retinylidene protein. However, the distinction is often ignored, and opsin may refer loosely to both (regardless of whether retinal is bound). Opsins are G-protein-coupled receptors (GPCRs) and must bind retinal — typically 11-cis retinal, 11-''cis''-retinal — in order to be photosensitive, since the retinal acts as the chromophore. When the Retinylidene protein absorbs a photon, the retinal isomerizes and is released by the opsin. The process that follows the isomerization and renewal of retinal is known as the visual cyc ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Photopsin
Vertebrate visual opsins are a subclass of ciliary opsins and mediate vision in vertebrates. They include the opsins in human rod and cone cells. They are often abbreviated to ''opsin'', as they were the first opsins discovered and are still the most widely studied opsins. Opsins Opsin refers strictly to the apoprotein (without bound retinal). When an opsin binds retinal to form a holoprotein, it is referred to as Retinylidene protein. However, the distinction is often ignored, and opsin may refer loosely to both (regardless of whether retinal is bound). Opsins are G-protein-coupled receptors (GPCRs) and must bind retinal — typically 11-''cis''-retinal — in order to be photosensitive, since the retinal acts as the chromophore. When the Retinylidene protein absorbs a photon, the retinal isomerizes and is released by the opsin. The process that follows the isomerization and renewal of retinal is known as the visual cycle. Free 11-''cis''-retinal is photosensitive an ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
