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See searches and references containing RETINYLIDENE PROTEIN!RETINYLIDENE PROTEIN
Family of proteins
Retinylidene proteins, or rhodopsins in a broad sense, are proteins that use retinal as a chromophore for light reception. They are the molecular basis
Retinylidene_protein
Vision proteins
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
Vertebrate_visual_opsin
Photoreceptive organelle
and retinylidene proteins (rhodopsins). Flavoproteins are characterized by containing flavin molecules as chromophores, whereas retinylidene proteins contain
Eyespot_apparatus
Class of light-sensitive proteins
chromophore, typically retinal. When bound to retinal, opsins become retinylidene proteins, but are usually still called opsins regardless. Most prominently
Opsin
Vitamin A aldehyde, a polyene chromophore
giving H2O. Retinylidene is the divalent group formed by removing the oxygen atom from retinal, and so opsins have been called retinylidene proteins. Opsins
Retinal
Molecular photoreceptors
receptor protein which triggers a signal transduction cascade. Chromophores found in photoreceptors include retinal (retinylidene proteins, for example
Photoreceptor_protein
Family of transmembrane proteins
pRhodopsin) belongs to the family of bacterial transmembrane rhodopsins (retinylidene proteins). In 1971, the first microbial transmembrane rhodopsin - Bacteriorhodopsin
Proteorhodopsin
Class of transport proteins
Channelrhodopsins are a subfamily of retinylidene proteins (rhodopsins) that function as light-gated ion channels. They serve as sensory photoreceptors
Channelrhodopsin
Process by which light activates retinal cells
bleaching intensities. The visual cycle occurs via G-protein coupled receptors called retinylidene proteins which consists of a visual opsin and a chromophore
Visual_phototransduction
Chemical changes in proteins following their translation from mRNA
fatty acid, polyketide, non-ribosomal peptide and leucine biosynthesis retinylidene Schiff base formation diphthamide formation (on a histidine found in
Post-translational modification
Post-translational_modification
Family of transmembrane proteins
Halorhodopsin is a seven-transmembrane retinylidene protein from microbial rhodopsin family. It is a chloride-specific light-activated ion pump found in
Halorhodopsin
Physiological process
Retinal is a chromophore that forms photosensitive retinylidene proteins when covalently bound to proteins called opsins. Retinal can be photoisomerized by
Visual_cycle
Mammalian protein found in humans
accumulation leads to formation of toxic cationic bis-pyridinium salt, N-retinylidene-N-retinyl-ethanolamine (A2E), which causes human dry and wet age-related
ABCA4
Light-sensitive receptor protein
active-site lysine in rhodopsin and implications for evolution of retinylidene proteins". Proceedings of the National Academy of Sciences of the United
Rhodopsin
Cellular players that can be activated by light
used photoactivatable proteins in scientific research, as of 2013, are photoactivatable fluorescent proteins and retinylidene proteins. Photoactivatable fluorescent
Photoactivatable_probes
Protein used by single-celled organisms
retinal molecule to residue Lys216, via a Schiff base, to create the retinylidene chromophore. Cleavage of the signal peptide, the first 13 amino acids
Bacteriorhodopsin
Amino acid
base with a conserved lysine residue, and interaction of light with the retinylidene group causes signal transduction in color vision (See visual cycle for
Lysine
Lipid-containing residue associated with aging
strong light leads to formation of toxic cationic bis-pyridinium salt, N-retinylidene-N-retinyl-ethanolamine (A2E), which causes dry and wet age-related macular
Lipofuscin
PMID 13346046. Shichi H, Somers RL (1974). "Possible involvement of retinylidene phospholipid in photoisomerization of all-trans-retinal to 11-cis-retinal"
Retinal_isomerase
Chemical compound
age-related macular degeneration (AMD) is thought to be the toxic byproduct, N-retinylidene-N-retinylethanolamine (A2E). A2E is a major chromophore in lipofuscin
Emixustat
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RETINYLIDENE PROTEIN
n.
A body now known as alkali albumin, but originally considered to be the basis of all albuminous substances, whence its name.
n.
An albuminoid substance which occurs in minute grains ("protein granules") in maturing seeds and tubers; -- supposed to be a modification of protoplasm.
a.
Of or related to protein; albuminous; proteid.
a.
Proteinaceuos.
n.
A piece of DNA, usually circular, functioning as part of the genetic material of a cell, not integrated with the chromosome and replicating independently of the chromosome, but transferred, like the chromosome, to subsequent generations. In bacteria, plasmids often carry the genes for antibiotic resistance; they are exploited in genetic engineering as the vehicles for introduction of extraneous DNA into cells, to alter the genetic makeup of the cell. The cells thus altered may produce desirable proteins which are extracted and used; in the case of genetically altered plant cells, the altered cells may grow into complete plants with changed properties, as for example, increased resistance to disease.
n.
One of the microscopic particles resembling crystals, consisting of protein matter, which occur in certain plant cells; -- called also protein crystal.
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