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RhodopsinSensory RhodopsinsRhodopsins, MicrobialRetinal PigmentsG-Protein-Coupled Receptor Kinase 1Rod Cell Outer SegmentTransducinRetinaldehydeRod OpsinsLightPhotoreceptor CellsHalorhodopsinsRetinal Rod Photoreceptor CellsEye ProteinsSchiff BasesCattleRetinitis PigmentosaDark AdaptationRecoverinPhotoreceptor Cells, InvertebrateRetinaRetinal DegenerationVision, OcularOctopodiformesElectroretinographyNatronobacteriumHippocalcinPhotochemistryPhotoreceptor Cells, VertebrateBacteriorhodopsinsDarknessHydroxylamineAmino Acid SequenceMolecular Sequence DataPhotolysisSpectrophotometryNight BlindnessHalobacterium salinarumHydroxylaminesIsomerismModels, MolecularOpsinsProtein ConformationProtein Structure, Secondary3',5'-Cyclic-GMP PhosphodiesterasesKineticsLight Signal TransductionMicrospectrophotometryAnimals, Genetically ModifiedSpectrum AnalysisGTP-Binding ProteinsArchaeal ProteinsNorisoprenoidsMutationHalobacteriumDecapodiformesRetinoidsHalobacteriaceaeRetinal Cone Photoreceptor CellsReceptors, G-Protein-CoupledProtein BindingRanidae
Rhodopsin
A purplish-red, light-sensitive pigment found in RETINAL ROD CELLS of most vertebrates. It is a complex consisting of a molecule of ROD OPSIN and a molecule of 11-cis retinal (RETINALDEHYDE). Rhodopsin exhibits peak absorption wavelength at about 500 nm.
Sensory Rhodopsins
Photosensory rhodopsins found in microorganisms such as HALOBACTERIA. They convert light signals into biochemical information that regulates certain cellular functions such as flagellar motor activity.
Rhodopsins, Microbial
Rhodopsin molecules found in microorganisms such as ARCHAEA and PROTEOBACTERIA.
Retinal Pigments
Photosensitive protein complexes of varied light absorption properties which are expressed in the PHOTORECEPTOR CELLS. They are OPSINS conjugated with VITAMIN A-based chromophores. Chromophores capture photons of light, leading to the activation of opsins and a biochemical cascade that ultimately excites the photoreceptor cells.
G-Protein-Coupled Receptor Kinase 1
A PROTEIN-SERINE-THREONINE KINASE that is found in PHOTORECEPTOR CELLS. It mediates light-dependent PHOSPHORYLATION of RHODOPSIN and plays an important role in PHOTOTRANSDUCTION.
Rod Cell Outer Segment
The portion of a retinal rod cell situated between the ROD INNER SEGMENT and the RETINAL PIGMENT EPITHELIUM. It contains a stack of photosensitive disk membranes laden with RHODOPSIN.
Transducin
A heterotrimeric GTP-binding protein that mediates the light activation signal from photolyzed rhodopsin to cyclic GMP phosphodiesterase and is pivotal in the visual excitation process. Activation of rhodopsin on the outer membrane of rod and cone cells causes GTP to bind to transducin followed by dissociation of the alpha subunit-GTP complex from the beta/gamma subunits of transducin. The alpha subunit-GTP complex activates the cyclic GMP phosphodiesterase which catalyzes the hydrolysis of cyclic GMP to 5'-GMP. This leads to closure of the sodium and calcium channels and therefore hyperpolarization of the rod cells. EC 3.6.1.-.
Retinaldehyde
A carotenoid constituent of visual pigments. It is the oxidized form of retinol which functions as the active component of the visual cycle. It is bound to the protein opsin forming the complex rhodopsin. When stimulated by visible light, the retinal component of the rhodopsin complex undergoes isomerization at the 11-position of the double bond to the cis-form; this is reversed in "dark" reactions to return to the native trans-configuration.
Rod Opsins
Photosensitive proteins expressed in the ROD PHOTORECEPTOR CELLS. They are the protein components of rod photoreceptor pigments such as RHODOPSIN.
Light
That portion of the electromagnetic spectrum in the visible, ultraviolet, and infrared range.
Photoreceptor Cells
Specialized cells that detect and transduce light. They are classified into two types based on their light reception structure, the ciliary photoreceptors and the rhabdomeric photoreceptors with MICROVILLI. Ciliary photoreceptor cells use OPSINS that activate a PHOSPHODIESTERASE phosphodiesterase cascade. Rhabdomeric photoreceptor cells use opsins that activate a PHOSPHOLIPASE C cascade.
Halorhodopsins
Light driven chloride ion pumps that are ubiquitously found in halophilic archaea (HALOBACTERIALES).
Retinal Rod Photoreceptor Cells
Photosensitive afferent neurons located in the peripheral retina, with their density increases radially away from the FOVEA CENTRALIS. Being much more sensitive to light than the RETINAL CONE CELLS, the rod cells are responsible for twilight vision (at scotopic intensities) as well as peripheral vision, but provide no color discrimination.
Eye Proteins
Schiff Bases
Condensation products of aromatic amines and aldehydes forming azomethines substituted on the N atom, containing the general formula R-N:CHR. (From Grant & Hackh's Chemical Dictionary, 5th ed)
Cattle
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
Retinitis Pigmentosa
Hereditary, progressive degeneration of the neuroepithelium of the retina characterized by night blindness and progressive contraction of the visual field.
Dark Adaptation
Adjustment of the eyes under conditions of low light. The sensitivity of the eye to light is increased during dark adaptation.
Recoverin
A neuronal calcium-sensor protein that is found in ROD PHOTORECEPTORS and CONE PHOTORECEPTORS. It interacts with G-PROTEIN-COUPLED RECEPTOR KINASE 1 in a Ca2+ dependent manner and plays an important role in PHOTOTRANSDUCTION.
Photoreceptor Cells, Invertebrate
Specialized cells in the invertebrates that detect and transduce light. They are predominantly rhabdomeric with an array of photosensitive microvilli. Illumination depolarizes invertebrate photoreceptors by stimulating Na+ influx across the plasma membrane.
Retina
The ten-layered nervous tissue membrane of the eye. It is continuous with the OPTIC NERVE and receives images of external objects and transmits visual impulses to the brain. Its outer surface is in contact with the CHOROID and the inner surface with the VITREOUS BODY. The outer-most layer is pigmented, whereas the inner nine layers are transparent.
Retinal Degeneration
A retrogressive pathological change in the retina, focal or generalized, caused by genetic defects, inflammation, trauma, vascular disease, or aging. Degeneration affecting predominantly the macula lutea of the retina is MACULAR DEGENERATION. (Newell, Ophthalmology: Principles and Concepts, 7th ed, p304)
Vision, Ocular
The process in which light signals are transformed by the PHOTORECEPTOR CELLS into electrical signals which can then be transmitted to the brain.
Octopodiformes
A superorder in the class CEPHALOPODA, consisting of the orders Octopoda (octopus) with over 200 species and Vampyromorpha with a single species. The latter is a phylogenetic relic but holds the key to the origins of Octopoda.
Electroretinography
Recording of electric potentials in the retina after stimulation by light.
Natronobacterium
A genus of rod-shaped, extremely halophilic HALOBACTERIACEAE which grows in alkaline conditions. They are strictly aerobic and some strains are motile. Natronobacterium is found in soda lakes, alkaline salterns, and soda soils.
Hippocalcin
A neuronal calcium-sensor protein that was initially found in the NEURONS of the HIPPOCAMPUS. It interacts with NEURONAL APOPTOSIS-INHIBITORY PROTEIN.
Photochemistry
Photoreceptor Cells, Vertebrate
Specialized PHOTOTRANSDUCTION neurons in the vertebrates, such as the RETINAL ROD CELLS and the RETINAL CONE CELLS. Non-visual photoreceptor neurons have been reported in the deep brain, the PINEAL GLAND and organs of the circadian system.
Bacteriorhodopsins
Rhodopsins found in the PURPLE MEMBRANE of halophilic archaea such as HALOBACTERIUM HALOBIUM. Bacteriorhodopsins function as an energy transducers, converting light energy into electrochemical energy via PROTON PUMPS.
Darkness
The absence of light.
Hydroxylamine
A colorless inorganic compound (HONH2) used in organic synthesis and as a reducing agent, due to its ability to donate nitric oxide.
Amino Acid Sequence
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Molecular Sequence Data
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Photolysis
Chemical bond cleavage reactions resulting from absorption of radiant energy.
Spectrophotometry
The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.
Night Blindness
Failure or imperfection of vision at night or in dim light, with good vision only on bright days. (Dorland, 27th ed)
Halobacterium salinarum
A species of halophilic archaea found in salt lakes. Some strains form a PURPLE MEMBRANE under anaerobic conditions.
Hydroxylamines
Organic compounds that contain the (-NH2OH) radical.
Isomerism
The phenomenon whereby certain chemical compounds have structures that are different although the compounds possess the same elemental composition. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
Models, Molecular
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
Opsins
Photosensitive proteins in the membranes of PHOTORECEPTOR CELLS such as the rods and the cones. Opsins have varied light absorption properties and are members of the G-PROTEIN-COUPLED RECEPTORS family. Their ligands are VITAMIN A-based chromophores.
Protein Conformation
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
Protein Structure, Secondary
The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.
3',5'-Cyclic-GMP Phosphodiesterases
Enzymes that catalyze the hydrolysis of cyclic GMP to yield guanosine-5'-phosphate.
Kinetics
The rate dynamics in chemical or physical systems.
Light Signal Transduction
The conversion of absorbed light energy into molecular signals.
Microspectrophotometry
Analytical technique for studying substances present at enzyme concentrations in single cells, in situ, by measuring light absorption. Light from a tungsten strip lamp or xenon arc dispersed by a grating monochromator illuminates the optical system of a microscope. The absorbance of light is measured (in nanometers) by comparing the difference between the image of the sample and a reference image.
Animals, Genetically Modified
ANIMALS whose GENOME has been altered by GENETIC ENGINEERING, or their offspring.
Spectrum Analysis
The measurement of the amplitude of the components of a complex waveform throughout the frequency range of the waveform. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
GTP-Binding Proteins
Regulatory proteins that act as molecular switches. They control a wide range of biological processes including: receptor signaling, intracellular signal transduction pathways, and protein synthesis. Their activity is regulated by factors that control their ability to bind to and hydrolyze GTP to GDP. EC 3.6.1.-.
Archaeal Proteins
Proteins found in any species of archaeon.
Norisoprenoids
Thirteen-carbon butene cyclohexene degradation products formed by the cleavage of CAROTENOIDS. They contribute to the flavor of some FRUIT. Ionone should not be confused with the similarly named ionol.
Mutation
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
Halobacterium
A genus of HALOBACTERIACEAE whose growth requires a high concentration of salt. Binary fission is by constriction.
Decapodiformes
A superorder of CEPHALOPODS comprised of squid, cuttlefish, and their relatives. Their distinguishing feature is the modification of their fourth pair of arms into tentacles, resulting in 10 limbs.
Retinoids
A group of tetraterpenes, with four terpene units joined head-to-tail. Biologically active members of this class are used clinically in the treatment of severe cystic ACNE; PSORIASIS; and other disorders of keratinization.
Halobacteriaceae
A family of extremely halophilic archaea found in environments with high salt concentrations, such as salt lakes, evaporated brines, or salted fish. Halobacteriaceae are either obligate aerobes or facultative anaerobes and are divided into at least twenty-six genera including: HALOARCULA; HALOBACTERIUM; HALOCOCCUS; HALOFERAX; HALORUBRUM; NATRONOBACTERIUM; and NATRONOCOCCUS.
Retinal Cone Photoreceptor Cells
Photosensitive afferent neurons located primarily within the FOVEA CENTRALIS of the MACULA LUTEA. There are three major types of cone cells (red, blue, and green) whose photopigments have different spectral sensitivity curves. Retinal cone cells operate in daylight vision (at photopic intensities) providing color recognition and central visual acuity.
Receptors, G-Protein-Coupled
The largest family of cell surface receptors involved in SIGNAL TRANSDUCTION. They share a common structure and signal through HETEROTRIMERIC G-PROTEINS.
Protein Binding
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
Ranidae
The family of true frogs of the order Anura. The family occurs worldwide except in Antarctica.

Arrestin function in G protein-coupled receptor endocytosis requires phosphoinositide binding. (1/2465)

Internalization of agonist-activated G protein-coupled receptors is mediated by non-visual arrestins, which also bind to clathrin and are therefore thought to act as adaptors in the endocytosis process. Phosphoinositides have been implicated in the regulation of intracellular receptor trafficking, and are known to bind to other coat components including AP-2, AP180 and COPI coatomer. Given these observations, we explored the possibility that phosphoinositides play a role in arrestin's function as an adaptor. High-affinity binding sites for phosphoinositides in beta-arrestin (arrestin2) and arrestin3 (beta-arrestin2) were identified, and dissimilar effects of phosphoinositide and inositol phosphate on arrestin interactions with clathrin and receptor were characterized. Alteration of three basic residues in arrestin3 abolished phosphoinositide binding with complete retention of clathrin and receptor binding. Unlike native protein, upon agonist activation, this mutant arrestin3 expressed in COS1 cells neither supported beta2-adrenergic receptor internalization nor did it concentrate in coated pits, although it was recruited to the plasma membrane. These findings indicate that phosphoinositide binding plays a critical regulatory role in delivery of the receptor-arrestin complex to coated pits, perhaps by providing, with activated receptor, a multi-point attachment of arrestin to the plasma membrane.  (+info)

Two light-activated conductances in the eye of the green alga Volvox carteri. (2/2465)

Photoreceptor currents of the multicellular green alga Volvox carteri were analyzed using a dissolver mutant. The photocurrents are restricted to the eyespot region of somatic cells. Photocurrents are detectable from intact cells and excised eyes. The rhodopsin action spectrum suggests that the currents are induced by Volvox rhodopsin. Flash-induced photocurrents are a composition of a fast Ca2+-carried current (PF) and a slower current (PS), which is carried by H+. PF is a high-intensity response that appears with a delay of less than 50 micros after flash. The stimulus-response curve of its initial rise is fit by a single exponential and parallels the rhodopsin bleaching. These two observations suggest that the responsible channel is closely connected to the rhodopsin, both forming a tight complex. At low flash energies PS is dominating. The current delay increases up to 10 ms, and the PS amplitude saturates when only a few percent of the rhodopsin is bleached. The data are in favor of a second signaling system, which includes a signal transducer mediating between rhodopsin and the channel. We present a model of how different modes of signal transduction are accomplished in this alga under different light conditions.  (+info)

Structure and function in rhodopsin: kinetic studies of retinal binding to purified opsin mutants in defined phospholipid-detergent mixtures serve as probes of the retinal binding pocket. (3/2465)

In the current standard procedure for preparation of mammalian rhodopsin mutants, transfected COS-1 cells expressing the mutant opsin genes are treated with 5 microM 11-cis-retinal before detergent solubilization for purification. We found that binding of 11-cis-retinal to opsin mutants with single amino acid changes at Trp-265 (W265F,Y,A) and a retinitis pigmentosa mutant (A164V) was far from complete and required much higher concentrations of 11-cis-retinal. By isolation of the expressed opsins in a stable form, kinetic studies of retinal binding to the opsins in vitro have been carried out by using defined phospholipid-detergent mixtures. The results show wide variation in the rates of 11-cis-retinal binding. Thus, the in vitro reconstitution procedure serves as a probe of the retinal-binding pocket in the opsins. Further, a method is described for purification and characterization of the rhodopsin mutants after retinal binding to the opsins in vitro.  (+info)

Structure and function in rhodopsin: further elucidation of the role of the intradiscal cysteines, Cys-110, -185, and -187, in rhodopsin folding and function. (4/2465)

The disulfide bond between Cys-110 and Cys-187 in the intradiscal domain is required for correct folding in vivo and function of mammalian rhodopsin. Misfolding in rhodopsin, characterized by the loss of ability to bind 11-cis-retinal, has been shown to be caused by an intradiscal disulfide bond different from the above native disulfide bond. Further, naturally occurring single mutations of the intradiscal cysteines (C110F, C110Y, and C187Y) are associated with retinitis pigmentosa (RP). To elucidate further the role of every one of the three intradiscal cysteines, mutants containing single-cysteine replacements by alanine residues and the above three RP mutants have been studied. We find that C110A, C110F, and C110Y all form a disulfide bond between C185 and C187 and cause loss of retinal binding. C185A allows the formation of a C110-C187 disulfide bond, with wild-type-like rhodopsin phenotype. C187A forms a disulfide bond between C110 and C185 and binds retinal, and the pigment formed has markedly altered bleaching behavior. However, the opsin from the RP mutant C187Y forms no rhodopsin chromophore.  (+info)

The GTPase activating factor for transducin in rod photoreceptors is the complex between RGS9 and type 5 G protein beta subunit. (5/2465)

Proteins of the regulators of G protein signaling (RGS) family modulate the duration of intracellular signaling by stimulating the GTPase activity of G protein alpha subunits. It has been established that the ninth member of the RGS family (RGS9) participates in accelerating the GTPase activity of the photoreceptor-specific G protein, transducin. This process is essential for timely inactivation of the phototransduction cascade during the recovery from a photoresponse. Here we report that functionally active RGS9 from vertebrate photoreceptors exists as a tight complex with the long splice variant of the G protein beta subunit (Gbeta5L). RGS9 and Gbeta5L also form a complex when coexpressed in cell culture. Our data are consistent with the recent observation that several RGS proteins, including RGS9, contain G protein gamma-subunit like domain that can mediate their association with Gbeta5 (Snow, B. E., Krumins, A. M., Brothers, G. M., Lee, S. F., Wall, M. A., Chung, S., Mangion, J., Arya, S., Gilman, A. G. & Siderovski, D. P. (1998) Proc. Natl. Acad. Sci. USA 95, 13307-13312). We report an example of such a complex whose cellular localization and function are clearly defined.  (+info)

Molecular genetic study of autosomal dominant retinitis pigmentosa in Lithuanian patients. (6/2465)

Lithuanian patients with visual problems were clinically examined for retinitis pigmentosa (RP). A total of 33 unrelated families with autosomal dominant RP (adRP) were identified. Screening for mutations in the rhodopsin (RHO) and peripherin/RDS (RDS) genes was performed using DNA heteroduplex analysis. Direct DNA sequencing in the cases of heteroduplex formation showed the presence of the following mutations and polymorphisms in 14 adRP patients: RHO gene - Lys248Arg (1 case), and Pro347Leu (2 cases); RDS gene - Glu304Gln (12 cases), Lys310Arg (5 cases), and Gly338Asp (12 cases). The presence of these mutations (except Lys248Arg in the RHO gene) was confirmed by relevant restriction enzyme digestion. The frequency of the RDS gene mutations Glu304Gln and Gly338Asp was estimated to be 36.4%, while mutation Lys310Arg was less frequent (15.2%). These 3 RDS gene mutations appear to be polypeptide polymorphisms not related to adRP.  (+info)

Abnormal photoresponses and light-induced apoptosis in rods lacking rhodopsin kinase. (7/2465)

Phosphorylation is thought to be an essential first step in the prompt deactivation of photoexcited rhodopsin. In vitro, the phosphorylation can be catalyzed either by rhodopsin kinase (RK) or by protein kinase C (PKC). To investigate the specific role of RK, we inactivated both alleles of the RK gene in mice. This eliminated the light-dependent phosphorylation of rhodopsin and caused the single-photon response to become larger and longer lasting than normal. These results demonstrate that RK is required for normal rhodopsin deactivation. When the photon responses of RK-/- rods did finally turn off, they did so abruptly and stochastically, revealing a first-order backup mechanism for rhodopsin deactivation. The rod outer segments of RK-/- mice raised in 12-hr cyclic illumination were 50% shorter than those of normal (RK+/+) rods or rods from RK-/- mice raised in constant darkness. One day of constant light caused the rods in the RK-/- mouse retina to undergo apoptotic degeneration. Mice lacking RK provide a valuable model for the study of Oguchi disease, a human RK deficiency that causes congenital stationary night blindness.  (+info)

Reciprocity between light intensity and rhodopsin concentration across the rat retina. (8/2465)

1. If a purpose of photostasis - absorption of a constant number of photons by the retina, regardless of incident light levels - is to maintain rods at saturation during the light period, then in retinal regions where light intensity is low, rhodopsin concentration should be high, and vice versa. 2. Our ocular transmission photometric measurements revealed that the distribution of light intensity across the rat retina was not as simple as had been thought and, furthermore, that the local concentration of rhodopsin had a high negative correlation with the light intensity. 3. The reciprocity between these two parameters leads to nearly uniform rates of photon absorption in rods across the retina.  (+info)

New understanding of rhodopsin in retinal degeneration and high gain phosphorylation :: University of Southern California...
Through the experiments described in this thesis, I strived to obtain a better understanding the function of rhodopsin in retinal degeneration and light adaptation. Over 100 rhodopsin mutation alleles have been associated with autosomal dominant retinitis pigmentosa (ADRP), a blindness disorder that affects one in 3000 people globally. These mutations appear to cause photoreceptor cell death through diverse molecular mechanisms. We show that Lys296Glu (K296E), a rhodopsin mutation associated with ADRP, forms a stable complex with arrestin that is toxic to mouse rod photoreceptors. This cell death pathway appears to be conserved from flies to mammals. Accumulation of stable rhodopsin/arrestin complexes in the inner segment may be an important mechanism for triggering cell death in the mammalian photoreceptor cells. Abnormal turnover of rhodopsin mutants could also underlie a mechanism leading to cell death. In order to investigate rhodopsin turnover rate, rhodopsin was tagged with a special ...
http://digitallibrary.usc.edu/cdm/compoundobject/collection/p15799coll127/id/39461/rec/14
Effects of rhodopsin phosphorylation on dark adaptation and the recovery of sensitivityEffects of rhodopsin phosphorylation on dark adaptation and the recovery of sensitivity
Vision requires the photoreceptors in the eye to rapidly respond to changes in light intensity. These processes are accomplished within rod photoreceptors by the visual pigment rhodopsin that initiates a downstream signaling cascade called phototransduction. Rhodopsin is composed of an apoprotein opsin that is covalently bonded with light sensitive 11-cis retinal. Rhodopsin is activated when 11-cis retinal is photoisomerized into all-trans retinal. This isomerization initiates the phototransduction cascade that culminates in a change in current at the plasma membrane. Rhodopsin, once activated (bleached), can no longer absorb photons to activate phototransduction, and must be regenerated through the visual cycle. To enable the photoreceptors to respond to rapid changes in light intensities, phototransduction must terminate in a timely manner. Deactivation involves phosphorylation of activated rhodopsin by rhodopsin kinase, and then binding of visual arrestin. Exposing rods to daylight bleaches ...
https://open.bu.edu/handle/2144/16720
Effects of rhodopsin phosphorylation on dark adaptation and the recovery of sensitivityEffects of rhodopsin phosphorylation on dark adaptation and the recovery of sensitivity
Vision requires the photoreceptors in the eye to rapidly respond to changes in light intensity. These processes are accomplished within rod photoreceptors by the visual pigment rhodopsin that initiates a downstream signaling cascade called phototransduction. Rhodopsin is composed of an apoprotein opsin that is covalently bonded with light sensitive 11-cis retinal. Rhodopsin is activated when 11-cis retinal is photoisomerized into all-trans retinal. This isomerization initiates the phototransduction cascade that culminates in a change in current at the plasma membrane. Rhodopsin, once activated (bleached), can no longer absorb photons to activate phototransduction, and must be regenerated through the visual cycle. To enable the photoreceptors to respond to rapid changes in light intensities, phototransduction must terminate in a timely manner. Deactivation involves phosphorylation of activated rhodopsin by rhodopsin kinase, and then binding of visual arrestin. Exposing rods to daylight bleaches ...
https://open.bu.edu/handle/2144/16720?show=full
Rhodopsin 7-The unusual Rhodopsin in Drosophila [PeerJ]Rhodopsin 7-The unusual Rhodopsin in Drosophila [PeerJ]
Rhodopsins are the major photopigments in the fruit fly Drosophila melanogaster. Drosophila express six well-characterized Rhodopsins (Rh1-Rh6) with distinct absorption maxima and expression pattern. In 2000, when the Drosophila genome was published, a novel Rhodopsin gene was discovered: Rhodopsin 7 (Rh7). Rh7 is highly conserved among the Drosophila genus and is also found in other arthropods. Phylogenetic trees based on protein sequences suggest that the seven Drosophila Rhodopsins cluster in three different groups. While Rh1, Rh2 and Rh6 form a
https://peerj.com/articles/2427/
Three cytoplasmic loops of rhodopsin interact with transducin | PNASThree cytoplasmic loops of rhodopsin interact with transducin | PNAS
Rhodopsin is a member of an ancient class of receptors that transduce signals through their interaction with guanine nucleotide-binding proteins (G proteins). We have mapped the sites of interaction of rhodopsin with its G protein, which by analogy suggests how other members of this class of receptors may interact with their G proteins. Three regions of rhodopsins cytoplasmic surface interact with the rod cell G protein transducin (Gt). These are (i) the second cytoplasmic loop, which connects rhodopsin helices III and IV, (ii) the third cytoplasmic loop, which connects rhodopsin helices V and VI, and (iii) a putative fourth cytoplasmic loop formed by amino acids 310-321, as the carboxyl-terminal sequence emerges from helix VII and anchors to the lipid bilayer via palmitoylcysteines 322 and 323. Evidence for these regions of interaction of rhodopsin and Gt comes from the ability of synthetic peptides comprising these regions to compete with metarhodopsin II for binding to Gt. A spectroscopic ...
https://www.pnas.org/content/86/18/6878?ijkey=24ad4046c642c1bc92b20198553a96fd95fad60d&keytype2=tf_ipsecsha
Highly conserved glutamic acid in the extracellular IV-V loop in rhodopsins acts as the counterion in retinochrome, a member of...Highly conserved glutamic acid in the extracellular IV-V loop in rhodopsins acts as the counterion in retinochrome, a member of...
To examine whether the glutamic acid at position 181 affects the absorption characteristics of vertebrate rhodopsins, we replaced the glutamic acid with glutamine in bovine rhodopsin (Fig. 4). The replacement caused an ≈10-nm red shift of absorption maximum, but the addition of chloride shifted the maximum back to that of the WT. This absorption maximum of E181Q in the presence of chloride is consistent with a previous report on this mutant (18). In contrast, the E113Q mutant had its absorption maximum at ≈380 nm, and the addition of chloride caused an increase in absorbance at ≈500 nm (Fig. 4). Taken together with the recent rhodopsin structure (30), these results suggested that Glu-181 in bovine rhodopsin is not the counterion but is located near the region including Schiff base to affect absorption characteristics. The electrostatic character of Glu-181 is compensated by the addition of chloride when Glu-181 was replaced with glutamine. Interestingly, the effect of replacement of ...
https://www.pnas.org/content/97/26/14263?ijkey=12e36608261315b6b981247902d7b03211b40a52&keytype2=tf_ipsecsha
Rod/cone dysplasia in Irish setters. Presence of an altered rhodopsin | Biochemical JournalRod/cone dysplasia in Irish setters. Presence of an altered rhodopsin | Biochemical Journal
On the basis of the amino acid sequence of bovine rhodopsin, a series of peptides from the C-terminus (Rhod-4 and Rhod-1) and external loops (Rhod-10) were synthesized. Rabbit antisera to these peptides recognize the rhodopsin molecule in whole retina from 8-week-old normal and affected rcdl (rod/cone-dysplasic) Irish setters (8- and 4-weeks-old). When the rhodopsin content was equalized by using a solid-phase radioimmunoassay, the reaction with anti-peptide antisera to the C-terminal octapeptide (residues 341-348) is severely decreased in the rcdl-dog retinas. The results of mixing experiments suggest that this is not due to proteolytic clipping of the rhodopsin C-terminus from the affected dogs. Treatment of retinas with 1.0 mM-NaF, a phosphatase inhibitor, or pretreatment with alkaline and acid phosphatases does alter the reaction of the rhodopsin with anti-rhodopsin antisera. This suggests that the decreased reaction of the affected rhodopsin with the anti-peptide antisera may partially ...
http://www.biochemj.org/content/250/2/335
Imaging rhodopsin molecular contrast in vivo by optical coherence tomography | IOVS | ARVO JournalsImaging rhodopsin molecular contrast in vivo by optical coherence tomography | IOVS | ARVO Journals
Rhodopsin, the light-sensing molecule in the outer segments of rod photoreceptors, is responsible for converting light into neuronal signals in a process known as phototransduction. After absorbing a photon, rhodopsin undergoes conformational changes with a dramatic shift in its absorption spectrum: the maximum absorption peak shifts from 500 nm to 380 nm. This absorption change, known as rhodopsin photo-bleaching, provides a contrast to image rhodopsin. We report a novel 3-D retinal densitometry technique based on visible-light OCT for in vivo molecular imaging of rhodopsin. The system uses a light source centered at 532 nm closing to the peak absorption wavelength. With a bandwidth of 9.3 nm the system achieved a depth resolution of 13 micro-meters in air. The depth resolution allows the visualization and segmentation of the location where the absorption change occurs and provides an accurate assessment of rhodopsin content.. ...
http://iovs.arvojournals.org/article.aspx?articleid=2335313
Microbial and viral-like rhodopsins present in coastal marine sediments from four polar and subpolar regions. - NextBio article
Rhodopsins are broadly distributed. In this work, we analyzed 23 metagenomes corresponding to marine sediment samples from four regions that share cold climate conditions (Norway; Sweden; Argentina and Antarctica). In order to investigate the genes evolution of viral rhodopsins, an initial set of 6224 bacterial rhodopsin sequences according to COG5524 were retrieved from the 23 metagenomes. After selection by the presence of transmembrane domains and alignment, 123 viral (51) and non-viral (72) sequences (>50 amino acids) were finally included in further analysis. Viral rhodopsin genes were homologs of Phaeocystis globosa virus and Organic lake Phycodnavirus. Non-viral microbial rhodopsin genes were ascribed to Bacteroidetes, Planctomycetes, Firmicutes, Actinobacteria, Cyanobacteria, Proteobacteria, Deinococcus-Thermus and Cryptophyta and Fungi. A rescreening using Blastp, using as queries the viral sequences previously described, retrieved 30 sequences (>100 amino acids). Phylogeographic ...
http://www.nextbio.com/b/search/article.nb?id=27815287
BU Molecular Biophysics GroupBU Molecular Biophysics Group
Visual rhodopsins in vertebrates undergo irreversible structural changes leading to a loss of the chromophore (bleaching) when triggered by light, whereas microbial rhodopsins undergo a series of cyclic changes comprising a photocycle, eventually returning back to their initial state. The photocycle can take anywhere from milliseconds to several seconds, depending on the type of rhodopsin.. The physiological functions of rhodopsins vary widely. Visual rhodopsins found in the rod and cone cells of your eyes function as the primary light receptors in vision due to their role in activating G-proteins, which through a biochemical cascade control cyclic-nucleotide regulated ion channels. Light signaling rhodopsins called sensory rhodopsins are also present in microbes. For example, sensory rhodopsins I and II initiate either negative or positive phototaxis, signaling the cell to move away from or towards a light source depending on its wavelength. In this case sensory rhodopsins activate transducer ...
http://physics.bu.edu/mbl/
Essential role of the carboxyl-terminus for proper rhodopsin trafficking and enlightenment to the pathway(s) causing retinal...
Retinitis pigmentosa (RP) is a heterogeneous group of inherited eye diseases that is typified by initial night blindness and loss of peripheral vision and eventually culminates into total blindness. This retinal disorder afflicts around 1 in 4000 people worldwide. Mutations in the carboxyl-terminus of rhodopsin have been linked to autosomal dominant RP (ADRP). In this study, we have investigated two truncated rhodopsin mutants, S334ter and Q344ter. Both mutants have demonstrated that the presence of the QVAPA domain is necessary for proper rhodopsin localization and ROS formation. However, the retention of the phosphorylation sites in the Q344ter (and not in the S334ter) has allowed us to demonstrate the light-activation capability of mislocalized rhodopsin. More pertinent to ADRP patients, the retention of these phosphorylation sites in Q344ter also contributes to light-accelerated retinal degeneration through a mechanism first described in Drosophila, the accumulation of the rhodopsin/arrestin ...
http://digitallibrary.usc.edu/cdm/compoundobject/collection/p15799coll127/id/548940/rec/18
Search BRITE
Target-based classification of drugs [BR:br08310] G Protein-coupled receptors Rhodopsin family Histamine HRH1 [HSA:3269] [KO:K04149] D06021 Tecastemizole (USAN/INN ...
https://www.genome.jp/kegg-bin/search_brite?option=-a&search_string=D06021
Orientation of Intermediates in the Bleaching of Shear-Oriented Rhodopsin | JGPOrientation of Intermediates in the Bleaching of Shear-Oriented Rhodopsin | JGP
Cattle rhodopsin can be highly oriented by shearing a wet paste of digitonin micelles of this visual pigment between two quartz slides. This orients the rhodopsin micelles so that their chromophores lie mainly parallel to the direction of shear. In such preparations the orientation of rhodopsin and intermediates of its bleaching by light have been measured with plane-polarized light from -195°C to room temperature. The chromophore maintains essentially the same orientation as in rhodopsin in all the intermediates of bleaching: bathorhodopsin (prelumirhodopsin), lumirhodopsin, and metarhodopsins I and II. When, however, the retinaldehyde chromophore is hydrolyzed from opsin in the presence of hydroxylamine, the retinaldehyde oxime that results rotates so as to lie mainly across the direction of shear. That is, the retinal oxime, though free, orients itself upon the oriented matrix of the opsin-digitonin micelles. These experiments show the rhodopsin-digitonin micelle to be markedly asymmetric, ...
http://jgp.rupress.org/content/62/5/509
Characterization of two dominant alleles of the major rhodopsin-encoding gene ninaE in DrosophilaCharacterization of two dominant alleles of the major rhodopsin-encoding gene ninaE in Drosophila
In heterozygous mutant flies, there is loss of wild-type rhodopsin immunoreactivity on a western assay but less reduction using slot blot analysis. This suggests that mutant rhodopsin is likely inducing the misfolding and insolubility of wild-type rhodopsin. Localization of rhodopsin revealed that i …
https://pubmed.ncbi.nlm.nih.gov/22194648/?dopt=Abstract
Next-generation sequencing in health-care delivery: lessons from the functional analysis of rhodopsin. - Nuffield Department of...
PURPOSE: The interpretation of genetic information has always been challenging, but next-generation sequencing produces data on such a vast scale that many more variants of uncertain pathogenicity will be found. We exemplify this issue with reference to human rhodopsin, in which pathogenic mutations can lead to autosomal dominant retinitis pigmentosa. METHODS: Rhodopsin variants, with unknown pathogenicity, were found in patients by next-generation and Sanger sequencing and a multidisciplinary approach was used to determine their functional significance. RESULTS: Four variants in rhodopsin were identified: F45L, P53R, R69H, and M39R, with the latter two substitutions being novel. We investigated the cellular transport and photopigment function of all four human substitutions and found that the F45L and R69H variants behave like wild-type and are highly unlikely to be pathogenic. By contrast, P53R (a de novo change) and M39R were retained in the endoplasmic reticulum with significantly reduced
https://www.ndcn.ox.ac.uk/publications/342307
Next-generation sequencing in health-care delivery: lessons from the functional analysis of rhodopsin. - Oxford Neuroscience
PURPOSE: The interpretation of genetic information has always been challenging, but next-generation sequencing produces data on such a vast scale that many more variants of uncertain pathogenicity will be found. We exemplify this issue with reference to human rhodopsin, in which pathogenic mutations can lead to autosomal dominant retinitis pigmentosa. METHODS: Rhodopsin variants, with unknown pathogenicity, were found in patients by next-generation and Sanger sequencing and a multidisciplinary approach was used to determine their functional significance. RESULTS: Four variants in rhodopsin were identified: F45L, P53R, R69H, and M39R, with the latter two substitutions being novel. We investigated the cellular transport and photopigment function of all four human substitutions and found that the F45L and R69H variants behave like wild-type and are highly unlikely to be pathogenic. By contrast, P53R (a de novo change) and M39R were retained in the endoplasmic reticulum with significantly reduced
https://www.neuroscience.ox.ac.uk/publications/342307
NMR Study of Arrestin-1 Binding to Rhodopsin | IOVS | ARVO JournalsNMR Study of Arrestin-1 Binding to Rhodopsin | IOVS | ARVO Journals
Purpose: : The arrestin-receptor interaction is a complex multi-step process. Arrestins undergo global conformational changes upon binding to their cognate receptors, but the conformation of active, receptor-bound arrestins remains unknown. We identified arrestin-1 elements engaged by different functional forms of rhodopsin and the conformational changes induced by receptor binding. Methods: : We used solution nuclear magnetic resonance (NMR) spectroscopy of 15N-labeled arrestin-1, free and in the presence of light activated (Rh*), phosphorylated light activated rhodopsin (P-Rh*), and phospho-opsin (P-Ops) in bicelles. Results: : Solution NMR was used to assign ~40% of arrestin-1 backbone resonances. Native rhodopsin-containing disc membranes are too large for NMR, whereas detergents that solubilize rhodopsin denature arrestin-1. Bicelles, where bilayered lipid discs are edge-stabilized by detergent, provide a native membrane-like environment for rhodopsin and preserve arrestin-1 structure and ...
http://iovs.arvojournals.org/article.aspx?articleid=2356765
Frontiers | Early Events in Retinal Degeneration Caused by Rhodopsin Mutation or Pigment Epithelium Malfunction: Differences...Frontiers | Early Events in Retinal Degeneration Caused by Rhodopsin Mutation or Pigment Epithelium Malfunction: Differences...
To study the course of photoreceptor cell death and macro and microglial reactivity in two rat models of retinal degeneration with different etiologies. Retinas from P23H-1 (rhodopsin mutation) and Royal College of Surgeon (RCS, pigment epithelium malfunction) rats and age-matched control animals (Sprague-Dawley and Pievald Viro Glaxo, respectively) were cross-sectioned at different postnatal ages (from P10 to P60) and rhodopsin, L/M- and S- opsin, ionized calcium-binding adapter molecule 1 (Iba1), glial fibrillary acid protein (GFAP), and proliferating cell nuclear antigen (PCNA) proteins were immunodetected. Photoreceptor nuclei rows and microglial cells in the different retinal layers were quantified.Photoreceptor degeneration starts earlier and progresses quicker in P23H-1 than in RCS rats. In both models, microglial cell activation occurs simultaneously with the initiation of photoreceptor death while GFAP over-expression starts later. As degeneration progresses, the numbers of microglial cells
https://www.frontiersin.org/articles/10.3389/fnana.2017.00014/full
Eukaryotic G protein-coupled receptors as descendants of prokaryotic sodium-translocating rhodopsins | Biology Direct | Full...Eukaryotic G protein-coupled receptors as descendants of prokaryotic sodium-translocating rhodopsins | Biology Direct | Full...
Microbial rhodopsins and G-protein coupled receptors (GPCRs, which include animal rhodopsins) are two distinct (super) families of heptahelical (7TM) membrane proteins that share obvious structural similarities but no significant sequence similarity. Comparison of the recently solved high-resolution structures of the sodium-translocating bacterial rhodopsin and various Na+-binding GPCRs revealed striking similarity of their sodium-binding sites. This similarity allowed us to construct a structure-guided sequence alignment for the two (super)families, which highlighted their evolutionary relatedness. Our analysis supports a common underlying molecular mechanism for both families that involves a highly conserved aromatic residue playing a pivotal role in rotation of the 6th transmembrane helix. This article was reviewed by Oded Beja, G. P. S. Raghava and L. Aravind.
https://biologydirect.biomedcentral.com/articles/10.1186/s13062-015-0091-4
Death of photoreceptors in organotypic retinal explant cultures: implication of rhodopsin accumulation and endoplasmic...Death of photoreceptors in organotypic retinal explant cultures: implication of rhodopsin accumulation and endoplasmic...
Here we suggest that endoplasmic reticulum (ER)-stress may be induced following aberrant rhodopsin accumulation in photoreceptors in explanted rat retinas. Rhodopsin accumulation was accompanied by increased phosphorylation of pancreatic ER-kinase and eukaryotic initiator factor 2α as well as increased levels of C/EBP homologous protein, glucose-regulated protein 78 and eventually increased cleaved caspase-12 and cleaved caspase-3. Glucose-regulated protein 78, pancreatic ER-kinase, caspase-12 and cleaved caspase-3 were present in photoreceptors, indicating that ER-stress and apoptosis are induced in this cell population. These results suggest that ER-stress and subsequent apoptosis is induced in healthy photoreceptors, presumably by aberrant accumulation of rhodopsin and the phosphorylation of eukaryotic initiator factor 2α. The explant culture system may allow investigations of neuroprotective strategies.. ...
http://lnu.diva-portal.org/smash/record.jsf?faces-redirect=true&language=no&searchType=SIMPLE&query=&af=%5B%5D&aq=%5B%5B%5D%5D&aq2=%5B%5B%5D%5D&aqe=%5B%5D&pid=diva2%3A579080&noOfRows=50&sortOrder=author_sort_asc&sortOrder2=title_sort_asc&onlyFullText=false&sf=all
RhodopsinRhodopsin
Rhodopsin Rhodopsin (opsin 2, rod pigment) (retinitis pigmentosa 4, autosomal dominant) Sensory rhodopsin II (rainbow colored) embedded in a lipid bilayer
https://www.bionity.com/en/encyclopedia/Rhodopsin.html
Molecular mechanism of phospholipid scrambling by rhodopsin - Anant MenonMolecular mechanism of phospholipid scrambling by rhodopsin - Anant Menon
The visual pigment rhodopsin is a constitutively active lipid scramblase capable of moving phospholipids rapidly between the leaflets of a membrane bilayer. Thi...
https://grantome.com/grant/NIH/R21-EY028314-01
Photocyclic behavior of rhodopsin induced by an atypical isomerization mechanismPhotocyclic behavior of rhodopsin induced by an atypical isomerization mechanism
Vertebrate rhodopsin (Rh) contains 11-|i|cis|/i|-retinal as a chromophore to convert light energy into visual signals. On absorption of light, 11-|i|cis|/i|-retinal is isomerized to all-|i|trans|/i|-retinal, constituting a one-way reaction that activates transducin (G|sub|t|/sub|) followed by chromo …
https://pubmed.ncbi.nlm.nih.gov/28289214/
Rhodopsin/lipid hydrophobic match... preview & related info | MendeleyRhodopsin/lipid hydrophobic match... preview & related info | Mendeley
(2015) Soubias et al. Biophysical Journal. Abstract Lipid composition of the membrane and rhodopsin packing density strongly modulate the early steps of the visual response of photoreceptor membranes. In this study, lipid-order and bovine rhodopsin function in proteoliposomes composed of the sn-1...
https://www.mendeley.com/catalogue/260341c0-9792-3178-8eee-8cf20208efe2/
Biophysikalische Chemie - Institut für Biologie
The topic of the research group „Biophysical Chemistry is the investigation of reaction mechanisms of various photoreceptors with spectroscopic methods, particulary with UV/ Vis and static and time resolved FTIR spectroscopy in the time range from ns to seconds. In order to improve the spectroscopic performance we also develop new advanced spectroscopic techniques. We focus on three types of photoreceptors: Vetrebrate rhodopsin, channelrhodoposins and phytochromes. In the case of vertebrate rhodopsin we concentrate on the light induced activation and deactivation and on the mechanism of G-protein binding, since many severe eye diseases are linked to deviations in these processes caused by mutations of the receptor. Channelrhodopsins are light-gated ion channels that are widely used in optogenetics, since they allow the precise control of neuronal activity by light. Phytochromes are photoreceptors in plants and bacteria. They are bimodal photoswitches that control important physiological ...
https://www.biologie.hu-berlin.de/de/gruppen/biophyschem_portal
Characterization of an Unconventional Rhodopsin from the Freshwater Actinobacterium Rhodoluna lacicolaCharacterization of an Unconventional Rhodopsin from the Freshwater Actinobacterium Rhodoluna lacicola
Publisher: American Society for Microbiology.. Date Issued: 2015-06-08. Abstract: Rhodopsin-encoding microorganisms are common in many environments. However, knowing that rhodopsin genes are present provides little insight into how the host cells utilize light. The genome of the freshwater actinobacterium, Rhodoluna lacicola encodes a rhodopsin of the uncharacterized actinorhodopsin family. We hypothesized that actinorhodopsin was a light-activated proton pump, and confirmed this by heterologously expressing R. lacicola actinorhodopsin in retinal-producing Escherichia coli. However, cultures of R. lacicola did not pump protons, even though actinorhodopsin mRNA and protein were both detected. Proton pumping in R. lacicola was induced by providing exogenous retinal, suggesting that the cells lacked the retinal cofactor. We used HPLC and oxidation of accessory pigments to confirm that R. lacicola does not synthesize retinal. These results suggest that in some organisms, the actinorhodopsin gene is ...
https://udspace.udel.edu/handle/19716/17226
Complexes between photoactivated rhodopsin and transducin: progress and questions | Biochemical JournalComplexes between photoactivated rhodopsin and transducin: progress and questions | Biochemical Journal
Activation of GPCRs (G-protein-coupled receptors) leads to conformational changes that ultimately initiate signal transduction. Activated GPCRs transiently combine with and activate heterotrimeric G-proteins resulting in GTP replacement of GDP on the G-protein α subunit. Both the detailed structural changes essential for productive GDP/GTP exchange on the G-protein α subunit and the structure of the GPCR-G-protein complex itself have yet to be elucidated. Nevertheless, transient GPCR-G-protein complexes can be trapped by nucleotide depletion, yielding an empty-nucleotide G-protein-GPCR complex that can be isolated. Whereas early biochemical studies indicated formation of a complex between G-protein and activated receptor only, more recent results suggest that G-protein can bind to pre-activated states of receptor or even couple transiently to non-activated receptor to facilitate rapid responses to stimuli. Efficient and reproducible formation of physiologically relevant, conformationally ...
http://www.biochemj.org/content/428/1/1
Gorbatyuk, Mol Vis 2005; 11:648-656. Figure 1.Gorbatyuk, Mol Vis 2005; 11:648-656. Figure 1.
Figure 1. Kinetic analysis of ribozyme Rz397. A: Hammerhead ribozyme 397 was designed to cleave following residue 397 in dog rhodopsin mRNA and in the analogous position (333) in mouse rhodopsin mRNA. B: Using an oligonucleotide substrate in tenfold excess of ribozyme, Rz397 reached a cleavage plateau at approximately 10 min in 5 mM MgCl2. The data points are from duplicate determinations that varied by less than 10%. C: Using 10 nM ribozyme, kobs was measured as a function of substrate concentration (from 0.1 to 15 μM). The data points are the average of duplicate determinations that varied by less than 10%. The Vmax was determined to be 19.5 nM/min and the KM was 910 nM using a double reciprocal plot of these data (not shown).. ...
http://www.molvis.org/molvis/v11/a77/gorbatyuk-fig1.html
HORTICULTURE CLINICHORTICULTURE CLINIC
The photoreceptors in Drosophila express a variety of rhodopsin isoforms. The R1-R6 photoreceptor cells express Rhodopsin1 (Rh1) which absorbs blue light (480 nm). The R7 and R8 cells express a combination of either Rh3 or Rh4 which absorb UV light (345 nm and 375 nm), and Rh5 or Rh6 which absorb blue (437 nm) and green (508 nm) light respectively. Each rhodopsin molecule consists of an opsin protein covalently linked to a carotenoid chromophore, 11-cis-3-hydroxyretinal. [12]. As in vertebrate vision, visual transduction in invertebrates occurs via a G protein-coupled pathway. However, in vertebrates the G protein is transducin, while the G protein in invertebrates is Gq (dgq in Drosophila). When rhodopsin (Rh) absorbs a photon of light its chromophore, 11-cis-3-hydroxyretinal, is isomerized to all-trans-3-hydroxyretinal. Rh undergoes a conformational change into its active form, metarhodopsin. Metarhodopsin activates Gq, which in turn activates a phospholipase Cβ (PLCβ) known as NorpA.. PLCβ ...
http://horticlinic.blogspot.com
what vitamin a compounds bind with opsin to form rhodopsin? - nomadconvoy.cowhat vitamin a compounds bind with opsin to form rhodopsin? - nomadconvoy.co
Looking for what vitamin a compounds bind with opsin to form rhodopsin? images? Dont panic, and download free what vitamin a compounds bind with opsin to form rhodopsin? wallpapers weve created for you.
http://nomadconvoy.co/what-vitamin-a-compounds-bind-with-opsin-to-form-rhodopsin
Results for pfam00001Results for pfam00001
7 transmembrane receptor (rhodopsin family). This family contains, amongst other G-protein-coupled receptors (GCPRs), members of the opsin family, which have been considered to be typical members of the rhodopsin superfamily. They share several motifs, mainly the seven transmembrane helices, GCPRs of the rhodopsin superfamily. All opsins bind a chromophore, such as 11-cis-retinal. The function of most opsins other than the photoisomerases is split into two steps: light absorption and G-protein activation. Photoisomerases, on the other hand, are not coupled to G-proteins - they are thought to generate and supply the chromophore that is used by visual opsins. ...
http://bioinf.umbc.edu/dmdm/generatelogo.php?domain=7tm_1&accession=pfam00001&prot=1351831
Rhodopsin-like receptors Forum
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β2-Adrenergic Receptor Structures | Science Signalingβ2-Adrenergic Receptor Structures | Science Signaling
Heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptors (GPCRs) are transmembrane proteins that respond to diverse extracellular stimuli to trigger many different cellular responses. They are important pharmacological targets, but drug design has been hampered because structural information is only available for the rather distinctive member of this family, rhodopsin (see the Perspective by Ranganathan). Three studies now provide structural insights into another GPCR, the human β2-adrenergic receptor. All three groups crystallized the protein in the presence of an inverse agonist that stabilizes the inactive conformation of the receptor. Rosenbaum et al. stabilized the protein for crystallization by protein engineering and analyzed mutagenesis data in the context of the structure to provide insight into how ligand binding is coupled. Cherezov et al. describe in detail the 2.4 Å structure of the fusion protein and how it compares to the rhodopsin structure. Rasmussen et ...
https://stke.sciencemag.org/content/2007/414/tw434
Molecular Biology of Light Transduction by the Mammalian Photoreceptor, RhodopsinMolecular Biology of Light Transduction by the Mammalian Photoreceptor, Rhodopsin
Rhodopsin, the vertebrate photoreceptor, is a prototypic molecule in the largest family of G-protein coupled receptors (GPCR). Like all receptors of this family, it contains three distinct domains: the cytoplasmic (intracellular) domain that is involve
http://www.jbsdonline.com/c3009/c4004/molecular-biology-light-transduction-mammalian-photoreceptor-rhodopsin-p10031.html
The rhodopsin cycle in the developing vertebrate retina. II. Correla- by L L. Caravaggio and S L. BontingThe rhodopsin cycle in the developing vertebrate retina. II. Correla- by L L. Caravaggio and S L. Bonting
Caravaggio, L L. and Bonting, S L., The rhodopsin cycle in the developing vertebrate retina. II. Correla- tive study in normal mice and in mice with hereditary retinal degeneration. (1963). Subject Strain Bibliography 1963. 195 ...
https://mouseion.jax.org/ssbb1963/195/
Network-level analysis of light adaptation in rod cells under normal and altered conditionsNetwork-level analysis of light adaptation in rod cells under normal and altered conditions
article{e5525a34-aaf1-4c93-881a-2c67536c98c2, abstract = {Photoreceptor cells finely adjust their sensitivity and electrical response according to changes in light stimuli as a direct consequence of the feedback and regulation mechanisms in the phototransduction cascade. In this study, we employed a systems biology approach to develop a dynamic model of vertebrate rod phototransduction that accounts for the details of the underlying biochemistry. Following a bottom-up strategy, we first reproduced the results of a robust model developed by Hamer et al. (Vis. Neurosci., 2005, 22(4), 417), and then added a number of additional cascade reactions including: (a) explicit reactions to simulate the interaction between the activated effector and the regulator of G-protein signalling (RGS); (b) a reaction for the reformation of the G-protein from separate subunits; (c) a reaction for rhodopsin (R) reconstitution from the association of the opsin apoprotein with the 11-cis-retinal chromophore; (d) ...
https://lup.lub.lu.se/search/publication/1490646
PROSITEPROSITE
Bacterial rhodopsins [1,2,3] are a family of retinal-containing proteins found in extremely halophilic bacteria which provide light-dependent ion transport and sensory functions for these organisms. Bacterial rhodopsins are integral membrane proteins with seven transmembrane regions. The retinal choromophore is covalently linked, via a Schiffs base, to the epsilon-amino group of a conserved lysine residue in the middle of the last transmembrane helix (called helix G). There are at least three types of bacterial rhodopsins: ...
https://prosite.expasy.org/doc/PS00327
Thermo Scientific Lab Vision Rhodopsin (Opsin) Ab-1, Mouse Monoclonal Antibody | Fisher ScientificThermo Scientific Lab Vision Rhodopsin (Opsin) Ab-1, Mouse Monoclonal Antibody | Fisher Scientific
Shop a large selection of products and learn more about Thermo Scientific Lab Vision Rhodopsin (Opsin) Ab-1, Mouse Monoclonal Antibody 200µL; 1mg/mL; Unlabeled; Purified
https://www.fishersci.com/shop/products/rhodopsin-opsin-ab-1-mouse-monoclonal-antibody/ms1233pabx?tab=document
Background Membrane proteins (MPs) play crucial roles in signal transduction. rhodopsin | ATR inhibitors VE-821 and VX-970...Background Membrane proteins (MPs) play crucial roles in signal transduction. rhodopsin | ATR inhibitors VE-821 and VX-970...
Background Membrane proteins (MPs) play crucial roles in signal transduction. rhodopsin was not affected by the target MPs and both could coexist in the membrane stacks. Heterologous expression levels reached about 270 to 500 pmol/mg total MP, resulting in 0.2C0.4 mg purified target MP from 1 107390-08-9 supplier g of fly heads. The metabotropic glutamate receptor and human serotonin transporter - both involved in synaptic transmission - showed native pharmacological characteristics and could be purified to homogeneity as a prerequisite for further studies. Significance We demonstrate expression in PRCs as an efficient and inexpensive tool for the large scale production of functional eukaryotic MPs. The travel eye system offers a number of advantages over conventional expression systems and paves the way for in-depth analyses of eukaryotic MPs that have so far not been accessible to biochemical and biophysical studies. Introduction Membrane proteins (MPs) represent more than 30% of the cell ...
http://icrs-world-congress.org/background-membrane-proteins-mps-play-crucial-roles-in-signal-transduction-rhodopsin/
Reviews - WebvisionReviews - Webvision
This is a great review paper on the role of rhodopsin trafficking and its influence on retinal degenerative disease by TJ Hollingsworth and Alecia Gross. Rhodopsin delocalization in rod photoreceptors has been recognized for some time as one of the first indications of retinal photoreceptor cell stress in retinal degenerative diseases, so I was intrigued when seeing this paper come up in PubMed. Continue reading Review: Defective Trafficking of Rhodopsin and Its Role In Retinal Degenerations. ...
https://webvision.med.utah.edu/category/reviews/
Weiss, Mol Vis 1998; 4:27. Figure 5.Weiss, Mol Vis 1998; 4:27. Figure 5.
Figure 5. Phosphorylation of bovine rhodopsin by GRK7 and GRK1.. Extracts from nontransfected (NT) HEK-293 cells or cells expressing bovine GRK1 or ground squirrel GRK7 were used to phosphorylate bovine ROS membranes as described in the Methods. ROS membranes containing bovine rhodopsin were incubated with [[gamma]32P]ATP in the presence (+) or absence (-) of light, then electrophoresed on a 10% SDS-polyacrylamide gel. Phosphorylation was visualized by phosphorimage analysis. The numbers at left represent protein molecular size markers (Biorad, Hercules, CA).. ...
http://www.molvis.org/molvis/v4/a27/weiss-fig5.html
PROSITEPROSITE
Visual pigments [1,2] are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to the chromophore cis-retinal. Vision is effected through the absorption of a photon by cis-retinal which is isomerized to trans-retinal. This isomerization leads to a change of conformation of the protein. Opsins are integral membrane proteins with seven transmembrane regions that belong to family 1 of G-protein coupled receptors (see ,PDOC00210,). In vertebrates four different pigments are generally found. Rod cells, which mediate vision in dim light, contain the pigment rhodopsin. Cone cells, which function in bright light, are responsible for color vision and contain three or more color pigments (for example, in mammals: red, blue and green). In Drosophila, the eye is composed of 800 facets or ommatidia. Each ommatidium contains eight photoreceptor cells (R1-R8): the R1 to R6 cells are outer cells, R7 and R8 inner cells. Each of the three types of cells ...
https://prosite.expasy.org/doc/PS00238
Team:TU-Delft/Modeling/StructuralModeling - 2012.igem.orgTeam:TU-Delft/Modeling/StructuralModeling - 2012.igem.org
Below is the initial modeling approach described, applied to all olfactory receptors used in our research, unless written otherwise.. 1. Firstly, the in silico simulations have to be redone in YASARA in order to produce similar results as reported.[2] This involves the modeling of the olfactory receptor hOR2AG1 by using the crystal structure of the bovine rhodopsin. An alignment executed by BLAST [REF] between the two sequences gives multiple gaps in the helices of the crystal scructure. By shifting the gaps to the nearest extra- or intercellular loop, these helices are preserved. This swapping method is completed by swapping the residues of bovine rhodopsin into the residues of the desired protein. Next, the binding cavities of the receptor must be defined and examined if it is similar. Run a 10 ns MD without any ligand and analyze if the binding niche shrinks in volume.. By docking the ligand amyl butyrate, used in the paper, in the binding niche of the hOR2AG1 olfactory receptor, and ...
http://2012.igem.org/wiki/index.php?title=Team:TU-Delft/Modeling/StructuralModeling&diff=prev&oldid=212941
Team:TU-Delft/Modeling/StructuralModeling - 2012.igem.orgTeam:TU-Delft/Modeling/StructuralModeling - 2012.igem.org
Below is the initial modeling approach described, applied to all olfactory receptors used in our research, unless written otherwise.. 1. Firstly, the in silico simulations have to be redone in YASARA in order to produce similar results as reported [2]. This involves the modeling of the olfactory receptor Homo sapiens OR2AG1 by using the crystal structure of the bovine rhodopsin. An alignment executed by BLAST between the two sequences gives multiple gaps in the helices of the crystal scructure. By shifting the gaps to the nearest extra- or intercellular loop, these helices are preserved. This swapping method is completed by swapping the residues of bovine rhodopsin into the residues of the desired protein. Next, the binding cavities of the receptor must be defined and examined if it is similar. A 10 ns MD run is executed without any ligand and the result is analyzed to see if the binding niche shrinks in volume.. By docking the ligand amyl butyrate in the binding niche of the Homo sapiens OR2AG1 ...
http://2012.igem.org/wiki/index.php?title=Team:TU-Delft/Modeling/StructuralModeling&diff=prev&oldid=237396
Schizorhodopsins: A family of rhodopsins from Asgard archaea that function as light-driven inward H+ pumps | Science AdvancesSchizorhodopsins: A family of rhodopsins from Asgard archaea that function as light-driven inward H+ pumps | Science Advances
SzR was first identified in Asgardarchaeota and is phylogenetically positioned between typical microbial rhodopsins and HeRs (Fig. 1). In this study, we showed that SzR is a new type of light-driven inward H+ pump (Fig. 2). XeR was previously reported as an inward H+ pump in the typical microbial rhodopsin family (9-11). Although the sequential homology between the two subfamilies is low (SzR1 and PoXeR show 15.7% identity and 42.6% similarity), the trimeric structure and the photocycle with a large M accumulation not accompanied by N and O intermediates of SzR are similar to those reported for XeR (9-11), despite a large phylogenetic distance between them. This suggests that XeR and SzR underwent convergent evolution at the molecular level to achieve the same biological function. The differences and similarities between SzR and XeR are listed in Fig. 6C. Asgardarchaeota contain not only SzRs but also typical microbial rhodopsins with a DTK motif in helix C and HeRs (8). Although the function of ...
https://advances.sciencemag.org/content/6/15/eaaz2441
Global Optogenetic Activation of Inhibitory Interneurons during Epileptiform Activity | Journal of NeuroscienceGlobal Optogenetic Activation of Inhibitory Interneurons during Epileptiform Activity | Journal of Neuroscience
In this study, we show, for the first time, that global optogenetic activation of mixed interneuron populations effectively suppresses epileptiform activity in the hippocampus because of inhibition of principal cells by GABA released from these interneurons. In support, simultaneous optogenetic activation of several subpopulations of interneurons is more efficient in suppressing epileptiform activity than stimulation of PV or SST interneurons alone. Therefore, we propose that targeting large numbers of inhibitory interneurons with optogenetics, as opposed to specific subpopulations, could represent a better alternative strategy to control seizures.. Certain subclasses of inhibitory interneurons (including PV interneurons) are responsible for generating synchrony and maintaining network oscillations (Freund and Katona, 2007). Therefore, it is possible that perturbation of their rhythmic firing by optogenetics could be accountable for stopping seizure activity. Alternatively, this effect could ...
https://www.jneurosci.org/content/34/9/3364?ijkey=06f231b44929fb7eefd85da8f9d508baf3d3ec1d&keytype2=tf_ipsecsha
Visualizing G protein activation | Science SignalingVisualizing G protein activation | Science Signaling
The G protein-coupled receptor (GPCR) rhodopsin is found in rod outer segment membranes in the retina and is composed of the apoprotein opsin covalently bound to the ligand 11-cis retinal. Exposure to light converts the ligand to all-trans retinal, which activates the receptor. Rhodopsin then couples to the G protein transducin (Gt), inducing GDP-GTP exchange at the G protein α-subunit (Gαt), which then dissociates from the Gβγ dimer to initiate downstream signaling. Gao et al. isolated rhodopsin from bovine rod outer segment membranes and mixed it with Gβ1γ1 and an engineered α-subunit, eGαt, in the presence or absence of the nanobody Nb35*, which binds to G proteins to help with structure determination. These complexes were capable of undergoing nucleotide exchange and G protein activation. The authors then used single-particle cryo-EM to solve the structures of the Nb35*-bound and Nb35*-free complexes. These structures revealed the extent of the interface between the receptor and the ...
https://stke.sciencemag.org/content/12/597/eaaz3175
JCI - Optogenetic stimulation of the auditory pathwayJCI - Optogenetic stimulation of the auditory pathway
Auditory prostheses can partially restore speech comprehension when hearing fails. Sound coding with current prostheses is based on electrical stimulation of auditory neurons and has limited frequency resolution due to broad current spread within the cochlea. In contrast, optical stimulation can be spatially confined, which may improve frequency resolution. Here, we used animal models to characterize optogenetic stimulation, which is the optical stimulation of neurons genetically engineered to express the light-gated ion channel channelrhodopsin-2 (ChR2). Optogenetic stimulation of spiral ganglion neurons (SGNs) activated the auditory pathway, as demonstrated by recordings of single neuron and neuronal population responses. Furthermore, optogenetic stimulation of SGNs restored auditory activity in deaf mice. Approximation of the spatial spread of cochlear excitation by recording local field potentials (LFPs) in the inferior colliculus in response to suprathreshold optical, acoustic, and ...
https://www.jci.org/articles/view/69050/figure/1
Retinitis pigmentosa - WikipediaRetinitis pigmentosa - Wikipedia
Retinitis pigmentosa (RP) is one of the most common forms of inherited retinal degeneration.[5] There are multiple genes that, when mutated, can cause the retinitis pigmentosa phenotype.[10] Inheritance patterns of RP have been identified as autosomal dominant, autosomal recessive, X-linked, and maternally (mitochondrially) acquired, and are dependent on the specific RP gene mutations present in the parental generation.[11] In 1989, a mutation of the gene for rhodopsin, a pigment that plays an essential part in the visual transduction cascade enabling vision in low-light conditions, was identified. The rhodopsin gene encodes a principal protein of photoreceptor outer segments. Mutations in this gene most commonly presents as missense mutations or misfolding of the rhodopsin protein, and most frequently follow autosomal dominant inheritance patterns. Since the discovery of the rhodopsin gene, more than 100 RHO mutations have been identified, accounting for 15% of all types of retinal ...
https://en.wikipedia.org/wiki/Retinitis_pigmentosa
British Library EThOS: Pharmacological therapies for rhodopsin retinitis pigmentosaBritish Library EThOS: Pharmacological therapies for rhodopsin retinitis pigmentosa
Mutations in the visual pigment protein rod opsin are the most common cause of autosomal dominant retinitis pigmentosa (ADRP) and the majority of these mutations lead to the misfolding of the protein. Patients with ADRP experience progressive loss of vision leading to blindness and at the moment no effective therapy is available. In this study I have developed a cellular model that can mimic the gain-of function and dominant-negative disease mechanisms in rhodopsin ADRP patients. Whereas wild-type rod opsin translocated to the plasma membrane of the cells, P23H mutant rod opsin misfolded was retained in the ER and accumulated in intracellular inclusions. Several pharmacological compounds were tested in this model. The retinoids 9-c/s-retinal and 11-c/s-retinal reduced inclusion incidence, alleviated cell death and promoted the translocation of the mutant protein to the plasma membrane in cells expressing P23H rod opsin. In cells co-expressing wild-type and P23H rod opsin these compounds restored ...
http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.498505
Biochemical correlates of adaptation processes in isolated frog photoreceptor membranes. | JGPBiochemical correlates of adaptation processes in isolated frog photoreceptor membranes. | JGP
Frog rod outer segments isolated in suspension can maintain much of their in vivo activity. This observation provides us with a simpler system than the intact retina for correlating biochemical and physiological changes. The relevant physiological process, a decrease of sodium permeability by illumination, is assayed as light suppression of outer segment swelling in a modified Ringers solution. We report here that this decrease is observed over approximately 4 log units of input light intensity and varies with the logarithm of intensity at light levels which bleach between 5.102 and 5.104 rhodopsin molecules/outer segment-second. In this illumination range responsiveness to light decreases as intensity increases. This sensitivity control system may be linked to light-activated rhodopsin phosphorylation, for inhibitors of this reaction increase light sensitivity. The presence of a second system, which controls the maximum amplitude of in vitro response to light, is revealed in experiments with ...
http://jgp.rupress.org/content/68/1/1
Histidine Tagging Both Allows Convenient Single-step Purification of Bovine Rhodopsin and Exerts Ionic Strength-dependent...Histidine Tagging Both Allows Convenient Single-step Purification of Bovine Rhodopsin and Exerts Ionic Strength-dependent...
inproceedings{2017HistidineTB, title={Histidine Tagging Both Allows Convenient Single-step Purification of Bovine Rhodopsin and Exerts Ionic Strength-dependent Effects on Its Photochemistry*}, author={}, year={2017 ...
https://www.semanticscholar.org/paper/Histidine-Tagging-Both-Allows-Convenient-Single-st-/942a8cb9326f31230ab42a6f0ff3a9fa19a3b809
Electronic Preresonance Stimulated Raman Scattering Imaging of Red-Shifted Proteorhodopsins: Toward Quantitation of the...Electronic Preresonance Stimulated Raman Scattering Imaging of Red-Shifted Proteorhodopsins: Toward Quantitation of the...
Voltage imaging allows mapping of the membrane potential in living cells. Yet, current intensity-based imaging approaches are limited to relative membrane potential changes, missing important information conveyed by the absolute value of the membrane voltage. This challenge arises from various factors affecting the signal intensity, such as concentration, illumination intensity, and photobleaching. Here, we demonstrate electronic preresonance hyperspectral stimulated Raman scattering (EPR-hSRS) for spectroscopic detection of the membrane voltage using a near-infrared-absorbing microbial rhodopsin expressed in E. coli. This newly developed near-infrared active microbial rhodopsin enables electronic preresonance SRS imaging at high sensitivity. By spectral profiling, we identified voltage-sensitive SRS peaks in the fingerprint region in single E. coli cells. These spectral signatures offer a new approach for quantitation of the absolute membrane voltage in living cells ...
https://repository.ubn.ru.nl/handle/2066/208620
Frontiers | Viral-Mediated Optogenetic Stimulation of Peripheral Motor Nerves in Non-human Primates | NeuroscienceFrontiers | Viral-Mediated Optogenetic Stimulation of Peripheral Motor Nerves in Non-human Primates | Neuroscience
Objective: Reanimation of muscles paralyzed by disease states such as spinal cord injury remains a highly sought therapeutic goal of neuroprosthetic research. Optogenetic stimulation of peripheral motor nerves expressing light-sensitive opsins is a promising approach to muscle reanimation that may overcome several drawbacks of traditional methods such as functional electrical stimulation (FES). However, the utility of these methods has only been demonstrated in rodents to date, while translation to clinical practice will likely first require demonstration and refinement of these gene therapy techniques in non-human primates.Approach: Three rhesus macaques were injected intramuscularly with either one or both of two optogenetic constructs (AAV6-hSyn-ChR2-eYFP and/or AAV6-hSyn-Chronos-eYFP) to transduce opsin expression in the corresponding nerves. Neuromuscular junctions were targeted for virus delivery using an electrical stimulating injection technique. Functional opsin expression was periodically
https://www.frontiersin.org/articles/10.3389/fnins.2019.00759/full
Optogenetics in the teaching laboratory: using channelrhodopsin-2 to study the neural basis of behavior and synaptic physiology...Optogenetics in the teaching laboratory: using channelrhodopsin-2 to study the neural basis of behavior and synaptic physiology...
Here we incorporate recent advances in Drosophila neurogenetics and  optogenetics into neuroscience laboratory exercises. We used the light-activated ion channel channelrhodopsin-2 (ChR2) and tissue-specific genetic expression techniques to study the neural basis of behavior in Drosophila larvae. We designed and implemented exercises using inexpensive, easy-to-use systems for delivering blue light pulses with fine temporal control. Students first examined the behavioral effects of activating glutamatergic neurons in Drosophila larvae and then recorded excitatory junctional potentials (EJPs) mediated by ChR2 activation at the larval neuromuscular junction (NMJ). Comparison of electrically and light-evoked EJPs demonstrates that the amplitudes and time courses of light-evoked EJPs are not significantly different from those generated by electrical nerve stimulation. These exercises introduce students to new genetic technology for remotely manipulating neural activity, and they simplify the ...
http://teachspatial.org/optogenetics-in-the-teaching-laboratory-using-channelrhodopsin-2-to-study-the-neural-basis-of-behavior-and-synaptic-physiology-in-drosophila/
Plus itPlus it
Our experimental approach identified rab11a as part of the major complex associated with the C-terminal targeting sequence of rhodopsin in mouse retina. Discounting the mitochondrial ant2 protein as an artifact, all of the proteins detected are known components of outer segment trafficking. A role for rab11a in rhodopsin trafficking has been reported in Drosophila melanogaster (Satoh et al., 2005) and frogs (Mazelova et al., 2009), but the direct interaction of rab11a and, specifically, the C terminus of the rhodopsin molecule has not previously been detected in vertebrate photoreceptors. The fact that this interaction is disrupted by mutations in the C terminus of rhodopsin that lead to defects in outer segment formation and retinal degeneration, including rhodopsin-EGFP and rhodopsinQ344X, suggests that the loss of rab11a binding may be the main cause of these defects.. Two other rab proteins, rab6 (Deretic and Papermaster, 1993; Shetty et al., 1998) and rab8 (Deretic et al., 1995; Moritz et ...
https://www.jneurosci.org/content/34/45/14854
B for Biology: Signal Transduction Pathway -The cGMP PathwayB for Biology: Signal Transduction Pathway -The cGMP Pathway
A small molecule is associated with rhodopsin called 11-cis retinal. This small molecule absorbs light and isomerizes to all-trans retinal. As a result, it induces a conformational change in rhodposin protein. This activated rhodopsin then activates G protein called transducin. Being a G-protein, transducin has three subunits as α, β and γ. Just to recall, the α-subunit in inactive state is bound to GDP. Since, rhodopsin activates G protein transducin, there is a conformational change where α-subunit is now bound to GTP and is in active state. This α-subunit (of transducin) bound to GTP then stimulates the activity of cGMP phosphodiesterase. Now, being a phosphodiesterase, it reduces the intracellular levels of cGMP. The cGMP has a direct effect on ion channels in plasma membrane and so when there is reduction of cGMP levels in the rod cells of retina, this is translated to nerve impulse as light by the effect of cGMP on ion channels ...
http://namrataheda.blogspot.in/2013/03/signal-transduction-pathway-cgmp-pathway.html
Receptor-Dependent G-Protein Activation in Lipidic Cubic Phase - Helmholtz-Zentrum Dresden-Rossendorf, HZDRReceptor-Dependent G-Protein Activation in Lipidic Cubic Phase - Helmholtz-Zentrum Dresden-Rossendorf, HZDR
Javier Navarro, Ehud M. Landau, Karim Fahmy. Biolpoymers 67, 2002, pp 167-177.. Abstract: The primary step in cellular signaling by G-protein-coupled receptors (GPCRs) is the interaction of the agonist-activated transmembrane receptor with an intracellular G-protein. Understanding the underlying molecular mechanisms requires the structural determination of receptor G-protein complexes that are not yet achieved. The crystal structure of the bovine photoreceptor rhodopsin, a prototypical GPCR, was solved recently and the structures of different states of engineered G-proteins were reported. Posttranslational hydrophobic modifications of G-proteins are in most cases removed for crystallization but play functional roles for interactions among G-protein subunits with receptors, as well as membranes. Bovine rhodopsin is reconstituted into lipidic cubic phases to assess their potential for crystallization of receptor G-protein complexes under conditions that may preserve the structural and functional ...
https://www.hzdr.de/db/Cms?pOid=22476&pNid=0&pLang=en
Nr2e3 - Photoreceptor-specific nuclear receptor - Mus musculus (Mouse) - Nr2e3 gene & proteinNr2e3 - Photoreceptor-specific nuclear receptor - Mus musculus (Mouse) - Nr2e3 gene & protein
Orphan nuclear receptor of retinal photoreceptor cells. Transcriptional factor that is an activator of rod development and repressor of cone development. Binds the promoter region of a number of rod- and cone-specific genes, including rhodopsin, M- and S-opsin and rod-specific phosphodiesterase beta subunit. Enhances rhodopsin expression. Represses M- and S-cone opsin expression.
https://www.uniprot.org/uniprot/Q9QXZ7
Craig Montell | MCDB | UCSB Santa BarbaraCraig Montell | MCDB | UCSB Santa Barbara
Ni JD, Baik LS, Holmes TC, Montell C. 2017. A rhodopsin in the brain functions in circadian photoentrainment in Drosophila. Nature. 545:340-344. Luo J, Shen WL, Montell C. 2017. TRPA1 mediates sensation of the rate of temperature change in Drosophila larvae. Nat Neurosci. 20:34-41. Sokabe, T, Chen HC, Luo J, Montell. 2016 Oct 4; A switch in thermal preference in Drosophila larvae depends on multiple rhodopsins. Sokabe C. Cell Rep. 17:336-344. Huang J, Liu W, Qi YX, Luo J, Montell C. 2016 Sep 12; Neuromodulation of courtship drive through tyramine-responsive neurons in the Drosophila brain. Curr Biol.; 26:2246-56. Zhang YV, Aikin TJ, Li Z, Montell C. 2016 Aug; The basis of food texture sensation in Drosophila. Neuron. 91:863-77. Walker MT, Montell C. 2016 Jul; Suppression of the motor deficit in a mucolipidosis type IV mouse model by bone marrow transplantation. Hum Mol Genet. 25:2752-2761. Chen Z, Chen HC, Montell C. 2015 Oct 20; TRP and rhodopsin transport depends on dual XPORT er chaperones ...
https://www.mcdb.ucsb.edu/people/faculty/craig-montell
Rhodopsin-like receptors - WikipediaRhodopsin-like receptors - Wikipedia
Rhodopsin-like receptors are a family of proteins that comprise the largest group of G protein-coupled receptors. G-protein-coupled receptors, GPCRs, constitute a vast protein family that encompasses a wide range of functions (including various autocrine, paracrine, and endocrine processes). They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups. GPCRs are usually described as superfamily because they embrace a group of families for which there are indications of evolutionary relationship, but between which there is no statistically significant similarity in sequence. The currently known superfamily members include the rhodopsin-like GPCRs (this family), the secretin-like GPCRs, the cAMP receptors, the fungal mating pheromone receptors, and the metabotropic glutamate receptor family. There is a specialised database for GPCRs. The rhodopsin-like GPCRs themselves represent a widespread protein family that includes hormones, ...
https://en.wikipedia.org/wiki/Rhodopsin-like_receptors
Detection of Rhodopsin Dimerization In Situ by PIE-FCCS, a Time-Resolved Fluorescence Spectroscopy | SpringerLinkDetection of Rhodopsin Dimerization In Situ by PIE-FCCS, a Time-Resolved Fluorescence Spectroscopy | SpringerLink
Rhodopsin self-associates in the plasma membrane. At low concentrations, the interactions are consistent with a monomer-dimer equilibrium (Comar et al., J Am Chem Soc 136(23):8342-8349, 2014). At high
https://link.springer.com/protocol/10.1007%2F978-1-4939-2330-4_14
Phototransduction by Vertebrate Ultraviolet Visual Pigments: Protonation of the Retinylidene Schiff Base following...Phototransduction by Vertebrate Ultraviolet Visual Pigments: Protonation of the Retinylidene Schiff Base following...
Close The Infona portal uses cookies, i.e. strings of text saved by a browser on the users device. The portal can access those files and use them to remember the users data, such as their chosen settings (screen view, interface language, etc.), or their login data. By using the Infona portal the user accepts automatic saving and using this information for portal operation purposes. More information on the subject can be found in the Privacy Policy and Terms of Service. By closing this window the user confirms that they have read the information on cookie usage, and they accept the privacy policy and the way cookies are used by the portal. You can change the cookie settings in your browser. ...
https://www.infona.pl/resource/bwmeta1.element.acs-doi-10_1021_bi025883g
Zum Mechanismus der Signalübertragung durch G-Protein gekoppelte RezeptorenZum Mechanismus der Signalübertragung durch G-Protein gekoppelte Rezeptoren
The human organism employs G protein coupled receptors (GPCRs), cell surface receptors in the plasma membrane, to transmit extracellular signals such as hormones, neurotransmitters, gustatory and olfactory signals into the interior of the cell. Specific binding of these extracellular ligands induces a conformational change in GPCRs, which allows the interaction with heterotrimeric G proteins and the catalysis of GDP/GTP nucleotide exchange in the G protein. The G protein then transmits the signal by protein-protein interaction to intracellular effector proteins. The publications summarized here on the rhodopsin/transducin system of photoreceptor cells, a model system for GPCRs/G proteins, cover three topics: 1. Methodology developments for biophysical monitoring of the interaction between rhodopsin and transducin by light scattering and evanescent field techniques, in particular surface plasmon resonance spectroscopy. 2. Formation of the active conformation of rhodopsin. The temporal sequence of ...
https://edoc.hu-berlin.de/handle/18452/14538
A point mutation of the rhodopsin gene in one form of retinitis pigmentosa. - PubMed - NCBIA point mutation of the rhodopsin gene in one form of retinitis pigmentosa. - PubMed - NCBI
PubMed comprises more than 30 million citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.
https://www.ncbi.nlm.nih.gov/pubmed/2137202?dopt=Abstract
Prof. Dr. Arzu ÇELIK | MBGProf. Dr. Arzu ÇELIK | MBG
A fundamental problem common to the development of most sensory systems is the generation of functionally distinct neuronal cell types. The visual system constitutes a unique model to study the generation of cellular diversity within an otherwise homogeneous neuronal population. We use the fly retina to dissect signaling events that regulate the late phase of eye development, in particular those that control the selective expression of different rhodopsin genes in distinct photoreceptor (PR) subtypes. In many cases it has been shown that factors important for the development of the fly retina may also play a role in the vertebrate retina. Thus, in addition to the elucidation of basic developmental processes, our studies will aid the development of tools to fight eye diseases in humans.. In Drosophila color vision is achieved by the differential expression of blue-, green-, and uv-sensitive rhodopsin molecules in R7 and R8 cells. Throughout the retina, color ommatidia fall into two classes, pale ...
http://mbg.boun.edu.tr/?q=en/node/8
Assoc. Prof. Dr. Arzu ÇELIK | MBG
A fundamental problem common to the development of most sensory systems is the generation of functionally distinct neuronal cell types. The visual system constitutes a unique model to study the generation of cellular diversity within an otherwise homogeneous neuronal population. We use the fly retina to dissect signaling events that regulate the late phase of eye development, in particular those that control the selective expression of different rhodopsin genes in distinct photoreceptor (PR) subtypes. In many cases it has been shown that factors important for the development of the fly retina may also play a role in the vertebrate retina. Thus, in addition to the elucidation of basic developmental processes, our studies will aid the development of tools to fight eye diseases in humans.. In Drosophila color vision is achieved by the differential expression of blue-, green-, and uv-sensitive rhodopsin molecules in R7 and R8 cells. Throughout the retina, color ommatidia fall into two classes, pale ...
http://www.bio.boun.edu.tr/?q=node/8
Ophthalmic Biophysical Chemistry - UCLA Health Eye Care - Los Angeles, CAOphthalmic Biophysical Chemistry - UCLA Health Eye Care - Los Angeles, CA
Dr. Hubbells research is focused on understanding the relationship between the molecular structure of a protein and the conformational changes that control its function. Of particular interest are membrane proteins that behave as molecular switches, i.e., proteins whose structures are switched to an active state by a physical or chemical signal. A primary example under study is light-activated rhodopsin, the visual pigment in photoreceptor cells of the retina. The goal is to elucidate the structure of rhodopsin, the mechanism of the molecular switch, and the regulation of this switch by associated proteins, transducin and arrestin. Recently, his research has broadened to include structure/function relationships in water-soluble proteins such as the lens protein a-crystallin and the family of retinoid carrying proteins that transport vitamin A throughout photoreceptor cells.. To investigate these proteins, Dr. Hubbells laboratory has developed the technique of site-directed spin labeling ...
https://www.uclahealth.org/Eye/ophthalmic-biophysical-chemistry
WorkoutLabs YOGA CARDS II - Intermediate: Professional Visual Study, Class Sequencing & Practice Guide Vol.2 · Plastic… -...
Product prices and availability are accurate as of the date/time indicated and are subject to change. Any price and availability information displayed on [relevant Amazon Site(s), as applicable] at the time of purchase will apply to the purchase of this product. ...
https://wealdcottage.com/product/workoutlabs-yoga-cards-ii-intermediate-professional-visual-study-class-sequencing-practice-guide-vol-2-%C2%B7-plastic-yoga-flash-cards-yoga-deck-with-sanskrit/
Cell Adhesion Archives - Research on StationResearch on Station
Retinal degenerations are the leading cause of genetically inherited blindness. One of the strategies currently being tested for the treatment is cell/tissue transplantation. As such stem cells and tissue engineered constructs are of great importance. This report describes the growth of multipotential human retinal progenitors (cell line) in a 3-D bioreactor culture vessel with (adhesive substrate) laminin coated collagen 1/cytodex beads and without adhesive substrate (beadless culture). The study demonstrates that progenitors are capable of growth and differentiation in the bioreactor with or without beads. The presence of adhesive substrate accelerates and enhances photoreceptor differentiation in the bioreactor, reflected by significantly higher level expressions of several photoreceptor specific proteins; N acetyl transferase (AaNat), rhodopsin and cone transducin GNB3. Both monomeric and dimeric forms of rhodopsin are expressed in cells attached to beads, whereas, only the monomeric form is ...
http://www.spacestationresearch.com/tag/cell-adhesion/
Klaus Gawrisch, Ph.D. | Principal Investigators | NIH Intramural Research ProgramKlaus Gawrisch, Ph.D. | Principal Investigators | NIH Intramural Research Program
Dr. Gawrischs laboratory conducts structural and functional studies on reconstituted G protein- coupled membrane receptors (GPCR) including cannabinoid receptors and the visual receptor rhodopsin. The GPCR are recombinantly expressed or purified from a natural source, reconstituted into a fluid lipid matrix with a biologically relevant composition of lipids, and receptor activation and G protein signaling investigated at functional conditions. The laboratory pays particular attention to the mechanisms by which lipids influence receptor function, especially lipids with polyunsaturated hydrocarbon chains like docosahexaenoic acid, an omega-3 fatty acid found at high concentrations in brain. The primary experimental tool of the laboratory is solid-state nuclear magnetic resonance (NMR) which is applied on the GPCR and the surrounding lipid matrix. The goal of the investigations is a better understanding of the molecular mechanisms of receptor signaling including ligand binding, structural changes ...
https://irp.nih.gov/pi/klaus-gawrisch
Crag Keeps The Light Fantastic For Photoreceptors - RedorbitCrag Keeps The Light Fantastic For Photoreceptors - Redorbit
The ability of the eye of a fruit fly (Drosophila melanogaster) to respond to light depends on a delicate ballet that keeps the supply of light sensors called rhodopsin constant as photoreceptors turn on and off in response to light exposures, said researchers from Baylor College of Medicine (www.bcm.edu) and the Jan and Dan Duncan Neurological Research Institute (http://www.nri.texaschildrens.org/) at Texas Childrens Hospital in an article that appears online in the journal PLOS Biology (http://www.plosbiology.org/home.action).. The gene Crag is key for the trafficking of rhodopsin because it is a guanine exchange factor that activates a protein called Rab11, said Dr. Hugo Bellen, professor of molecular and human genetics and director of the Program in Developmental Biology at BCM (http://www.bcm.edu/db/).. When a photon hits the membrane, it activates a protein called rhodopsin, said Bellen, also a Howard Hughes Medical Institute investigator. Exposure to another wavelength of light ...
http://www.redorbit.com/news/science/1112742563/crag-keeps-the-light-fantastic-for-photoreceptors/
Closed-loop optogenetic activation of peripheral or central neurons modulates feeding in freely moving Drosophila | eLifeClosed-loop optogenetic activation of peripheral or central neurons modulates feeding in freely moving Drosophila | eLife
The Sip-Triggered Optogenetic Behavior Enclosure (STROBE) produces robust behaviors via activation of peripheral or central neurons in the fly, and mimics key features of feeding driven by chemical taste ligands.
https://elifesciences.org/articles/45636
AN/PVS-14D, 5855-01-494-5916, Monocular, Gen 3, Night, Vision, PinnacleAN/PVS-14D, 5855-01-494-5916, Monocular, Gen 3, Night, Vision, Pinnacle
TIP: By maintaining one eye to the darkness, while using the monocular exclusively with other, will help prevent Night Blindness caused by molecules called Rhodopsin. The Rod of your eye undergoes a change in shape as it absorbs light. Rhodopsin is the chemical that allows natural Night-Vision, and is extremely sensitive. When exposed to a spectrum of light, the pigment immediately bleaches and takes about 30 minutes to regenerate fully, although most of the adaptation occurs within the first five or ten minutes in the dark. Rhodopsin in the human rods is less sensitive to the longer red wavelengths of light, so many people use red light to help preserve night vision as it only slowly depletes the eyes Rhodopsin stores in the rods and instead is viewed by the cones. One of the best features of the PVS-14 style Monocular is the Variable Gain Control Knob that works in conjunction with the Automatic Brightness Control to adjust the image for you to see it properly, without blasting your pupil ...
http://nitevis.com/SFK14_detail.htm
Research Interests | The de Lecea Lab | Stanford MedicineResearch Interests | The de Lecea Lab | Stanford Medicine
We have now applied optogenetic technology to stimulate or inhibit Hcrt neurons in vivo with high temporal resolution. Using viral gene delivery techniques, we stably express ChR2 or NpHR in Hcrt neurons and investigate the effects of optogenetic stimulation on behavior. Our work shows that optogenetic stimulation of Hcrt neurons at frequencies ,5 Hz (but not 1 Hz) is sufficient to increase the probability of an awakening event during NREM and REM sleep. This stimulation also increases neural activity in downstream arousal nuclei, such as the tuberomammilary nucleus and locus coeruleus. Current projects in the lab aim at understanding the role of Hcrts in other behaviors, as well as understanding the importance of downstream targets in mediating Hcrt functions.. Further reading:. de Lecea et al. (1998). The hypocretins: hypothalamus-specific peptides with neuroexcitatory activity. PNAS 95(1):322-7. [Abstract] [PDF] Sutcliffe & de Lecea (2002). The hypocretins: setting the arousal threshold. Nat. ...
http://med.stanford.edu/delecea/research.html
Modulating electrophysiology of motor neural networks via optogenetic stimulation during neurogenesis and synaptogenesis -...Modulating electrophysiology of motor neural networks via optogenetic stimulation during neurogenesis and synaptogenesis -...
To promote science and increase scientific awareness on recent developments around the world. Provide tools for all science loving people to enhance, educate and share their Science knowledge and skills and benefit from interaction with each other
http://sciencemission.com/site/index.php?page=news&type=view&id=publications%2Fmodulating-electrophysio&filter=22
RhodopsinRhodopsin
The Rhodopsin Protein Photoisomerization of rhodopsin, animation. Rhodopsin and the eye, summary with pictures. (CS1 German- ... Rhodopsin mediates dim light vision and thus is extremely sensitive to light. When rhodopsin is exposed to light, it ... Humans have, including rhodopsin, nine opsins, as well as cryptochrome (light-sensitive, but not an opsin). Rhodopsin, like ... Rhodopsin is made constitutively (continuously) active by some of those mutations even without light. Also wild-type rhodopsin ...
https://en.wikipedia.org/wiki/Rhodopsin
Bacterial rhodopsinBacterial rhodopsin
... may refer to: Microbial rhodopsin, also known as type-I rhodopsin Bacteriorhodopsin, a type of microbial ... rhodopsin This disambiguation page lists articles associated with the title Bacterial rhodopsin. If an internal link led you ...
https://en.wikipedia.org/wiki/Bacterial_rhodopsin
Microbial rhodopsinMicrobial rhodopsin
A marine bacterial rhodopsin has been reported to function as a proton pump. However, it also resembles sensory rhodopsin II of ... Microbial rhodopsins are, by sequence, very different from any of the GPCR families. The term bacterial rhodopsin originally ... Light-activated rhodopsin/guanylyl cyclase A phylogenetic analysis of microbial rhodopsins and a detailed analysis of potential ... Microbial rhodopsins, also known as bacterial rhodopsins are retinal-binding proteins that provide light-dependent ion ...
https://en.wikipedia.org/wiki/Microbial_rhodopsin
Rhodopsin kinaseRhodopsin kinase
... phospho-rhodopsin Mutations in rhodopsin kinase are associated with a form of night blindness called Oguchi disease. Rhodopsin ... Rhodopsin kinase is inhibited by the calcium-binding protein recoverin in a graded manner that maintains rhodopsin sensitivity ... Rhodopsin kinase is found primarily in mammalian retinal rod cells, where it phosphorylates light-activated rhodopsin, a member ... Rhodopsin kinase directly participates in the rhodopsin to activate the visual phototransduction. Studies have shown that lack ...
https://en.wikipedia.org/wiki/Rhodopsin_kinase
Rhodopsin-like receptorsRhodopsin-like receptors
... are a family of proteins that comprise the largest group of G protein-coupled receptors. G-protein- ... Rhodopsin-like GPCRs have been classified into the following 19 subgroups (A1-A19) based on a phylogenetic analysis. Chemokine ... The rhodopsin-like GPCRs themselves represent a widespread protein family that includes hormone, neuropeptide, neurotransmitter ... The currently known superfamily members include the rhodopsin-like GPCRs (this family), the secretin-like GPCRs, the cAMP ...
https://en.wikipedia.org/wiki/Rhodopsin-like_receptors
Sensory rhodopsin IISensory rhodopsin II
Structure of sensory rhodopsin II is typical for microbial rhodopsin. It consists of seven transmembrane a-helices with retinal ... Sensory rhodopsin II (SRII), also known as pharaonis phoborhodopsin (ppR), is a membrane protein of archaea, responsible ... Notable feature of sensory rhodopsin II is presence of charged residue Y199 on the surface of the hydrophobic region. This ... Sensory rhodopsin II is found in Halobacterium salinarum and Natronomonas pharaonis. ...
https://en.wikipedia.org/wiki/Sensory_rhodopsin_II
Retinal degeneration (rhodopsin mutation)Retinal degeneration (rhodopsin mutation)
These mutations affect rhodopsin transport to the outer segments of rod photoreceptor cells, rhodopsin folding, and rhodopsin ... Rhodopsin is the opsin of rod photoreceptor cells, which are the only cells in the retina that express rhodopsin and which ... The rhodopsin transcript is a pre-mRNA splicing substrate affected by PRPF31 protein, meaning that rhodopsin (RHO) is among the ... In this research null mutations in the rhodopsin kinase and arrestin genes, each of which plays a role in terminating rhodopsin ...
https://en.wikipedia.org/wiki/Retinal_degeneration_(rhodopsin_mutation)
Yuri Ovchinnikov (biochemist)Yuri Ovchinnikov (biochemist)
He contributed to the field of biophysics and biochemistry through research in rhodopsin and structural biology. "APS Member ... "Octopus rhodopsin. Amino acid sequence deduced from cDNA". FEBS Letters. 232 (1): 69-72. doi:10.1016/0014-5793(88)80388-0. ISSN ...
https://en.wikipedia.org/wiki/Yuri_Ovchinnikov_(biochemist)
RetinalRetinal
The opsin in the vertebrate rod cells is rhodopsin. The rods form disks, which contain the rhodopsin molecules in their ... rhodopsin + H2O; forms Schiff base linkage to lysine, -CH=N+H-; rhodopsin + hν → metarhodopsin II (i.e., 11-cis photoisomerizes ... Cattle rhodopsin contains 348 amino acid residues. Retinal binds as chromophore at Lys296. This lysine is conserved in almost ... Opsins are prototypical G protein-coupled receptors (GPCRs). Cattle rhodopsin, the opsin of the rod cells, was the first GPCR ...
https://en.wikipedia.org/wiki/Retinal
MelanopsinMelanopsin
Paralogs of Opn4 include OPN1LW, OPN1MW, rhodopsin and encephalopsin. Melanopsin, like all other animal opsins (e.g. rhodopsin ... The seventh helix has a lysine that corresponds to Lys2967.43 in cattle rhodopsin and that is conserved in almost all opsins. ... These sites are dephosphorylated when melanopsin is exposed to light and are unique from those that regulate rhodopsin. They ... Pitt GA, Collins FD, Morton RA, Stok P (January 1955). "Studies on rhodopsin. VIII. Retinylidenemethylamine, an indicator ...
https://en.wikipedia.org/wiki/Melanopsin
Nematode chemoreceptorNematode chemoreceptor
These receptors are distantly related to the rhodopsin-like receptors. In contrast the receptor Sro is a true rhodopsin-like ... Pitt GA, Collins FD, Morton RA, Stok P (January 1955). "Studies on rhodopsin. VIII. Retinylidenemethylamine, an indicator ... Bownds D (December 1967). "Site of attachment of retinal in rhodopsin". Nature. 216 (5121): 1178-1181. Bibcode:1967Natur. ... Collins FD (March 1953). "Rhodopsin and indicator yellow". Nature. 171 (4350): 469-471. Bibcode:1953Natur.171..469C. doi: ...
https://en.wikipedia.org/wiki/Nematode_chemoreceptor
Paul HargravePaul Hargrave
The sequencing of rhodopsin was later described as a "monumental step" toward understanding the structure of rhodopsin. At the ... Hargrave, P. A.; McDowell, J. H.; Feldmann, R. J.; Atkinson, P. H.; Rao, J. K.; Argos, P. (1984). "Rhodopsin's protein and ... Dratz, Edward; Hargrave, Paul A (1983-04-01). "The structure of rhodopsin and the rod outer segment disk membrane". Trends in ... He also pursued further research into the function of rhodopsin, including its role in visual disease such as retinitis ...
https://en.wikipedia.org/wiki/Paul_Hargrave
Tessaracoccus antarcticusTessaracoccus antarcticus
... produces rhodopsin. Zhou, Liu-Yan; Zhang, Jin-Yu; Chen, Xu-Yang; Du, Zong-Jun; Mu, Da-shuai (1 March ... nov., a rhodopsin-containing bacterium from an Antarctic environment and emended description of the genus Tessaracoccus". ...
https://en.wikipedia.org/wiki/Tessaracoccus_antarcticus
Inherent chiralityInherent chirality
Retinal, a chromophore in rhodopsin. exists in solution as a racemic pair of enantiomers due to the curvature of an achiral ...
https://en.wikipedia.org/wiki/Inherent_chirality
Anisotropic Network ModelAnisotropic Network Model
Rhodopsin, by Rader et al., 2004. - Nicotinic acetylcholine receptor, by Hung et al., 2005; Taly et al., 2005. - Auxiliary ...
https://en.wikipedia.org/wiki/Anisotropic_Network_Model
Ruth HubbardRuth Hubbard
George (1958). "The Rhodopsin System of the Squid". The Journal of General Physiology. 41 (3): 501-528. doi:10.1085/jgp.41.3. ... In the same year, the pair was awarded the Paul Karrer Gold Medal specifically for their work with rhodopsin. Hubbard made many ... Not only did he find that light absorption liberated vitamin A, he also found an intermediate of the visual pigment rhodopsin ... Her early work focused on the basic properties of rhodopsin, which is a combination of the chromophore (retinal) and a protein ...
https://en.wikipedia.org/wiki/Ruth_Hubbard
G protein-coupled receptor kinase 7G protein-coupled receptor kinase 7
Arrestin-1 bound to rhodopsin in retinal rods prevents rhodopsin activation of the transducin protein to turn off photo- ... Shichi H, Somers RL (October 1978). "Light-dependent phosphorylation of rhodopsin. Purification and properties of rhodopsin ... The related GRK1, also known as rhodopsin kinase, serves a similar function in retinal rod cells subserving dim light black-and ... primary structure of rhodopsin kinase reveals similarities to the beta-adrenergic receptor kinase". Proceedings of the National ...
https://en.wikipedia.org/wiki/G_protein-coupled_receptor_kinase_7
Congenital stationary night blindnessCongenital stationary night blindness
Only three rhodopsin mutations have been found associated with congenital stationary night blindness (CSNB). Two of these ... Dryja TP, Berson EL, Rao VR, Oprian DD (July 1993). "Heterozygous missense mutation in the rhodopsin gene as a cause of ... Rao VR, Cohen GB, Oprian DD (February 1994). "Rhodopsin mutation G90D and a molecular mechanism for congenital night blindness ... Garriga P, Manyosa J (September 2002). "The eye photoreceptor protein rhodopsin. Structural implications for retinal disease". ...
https://en.wikipedia.org/wiki/Congenital_stationary_night_blindness
Raymond C. StevensRaymond C. Stevens
Crystal structure of rhodopsin bound to arrestin determined by femtosecond X-ray laser Nature 526: 561-567 T. Hua, K. Vemuri, M ... and the human Rhodopsin-Arrestin complex. 2016: The marijuana receptor-human Cannabinoid receptor type 1 (CB1) and the human C- ... and the first structures of non-rhodopsin family GPCRs, the transmembrane domain of the human Smoothened receptor from the ...
https://en.wikipedia.org/wiki/Raymond_C._Stevens
OptogeneticsOptogenetics
reported the first rhodopsin-guanylyl cyclase gene from fungus. In 2015, Scheib et al. and Gao et al. characterized the ... Bi A, Cui J, Ma YP, Olshevskaya E, Pu M, Dizhoor AM, Pan ZH (April 2006). "Ectopic expression of a microbial-type rhodopsin ... In addition, they introduced for the first time vertebrate rhodopsin, a light-activated G protein coupled receptor, as a tool ... As its activation peak (515 nm) is close to that of Rhodopsin 1, it is necessary to carefully calibrate the optogenetic ...
https://en.wikipedia.org/wiki/Optogenetics
ChannelrhodopsinChannelrhodopsin
Bi A, Cui J, Ma YP, Olshevskaya E, Pu M, Dizhoor AM, Pan ZH (April 2006). "Ectopic expression of a microbial-type rhodopsin ... Bi A, Cui J, Ma YP, Olshevskaya E, Pu M, Dizhoor AM, Pan ZH (April 2006). "Ectopic expression of a microbial-type rhodopsin ... The extremely fast rise of the photoreceptor current after a brief light flash led to the conclusion that the rhodopsin and the ... Foster KW, Saranak J, Patel N, Zarilli G, Okabe M, Kline T, Nakanishi K (October 1984). "A rhodopsin is the functional ...
https://en.wikipedia.org/wiki/Channelrhodopsin
Purple Earth hypothesisPurple Earth hypothesis
Microbial rhodopsin Red edge DasSarma, Shiladitya; Schwieterman, Edward W. (11 October 2018). "Early evolution of purple ...
https://en.wikipedia.org/wiki/Purple_Earth_hypothesis
Visual cycleVisual cycle
... rhodopsin + H2O; forms Schiff base linkage to lysine, -CH=N+H-; rhodopsin + hν → metarhodopsin II (i.e., 11-cis photoisomerizes ... and it moves to the exit site of rhodopsin. It will not leave the opsin protein until another fresh chromophore comes to ... to all-trans): (rhodopsin + hν → photorhodopsin → bathorhodopsin → lumirhodopsin → metarhodopsin I → metarhodopsin II); ...
https://en.wikipedia.org/wiki/Visual_cycle
Protist locomotionProtist locomotion
Two archaebacterial-type rhodopsins, channelrhodopsin-1 and -2, were identified as phototaxis receptors in Chlamydomonas. Both ... Sineshchekov, O. A.; Jung, K.-H.; Spudich, J. L. (2002). "Two rhodopsins mediate phototaxis to low- and high-intensity light in ... In the best-studied green alga, Chlamydomonas reinhardtii, phototaxis is mediated by a rhodopsin pigment, as first demonstrated ... Holland, E.M.; Harz, H.; Uhl, R.; Hegemann, P. (1997). "Control of phobic behavioral responses by rhodopsin-induced ...
https://en.wikipedia.org/wiki/Protist_locomotion
Mir-708 microRNA precursor familyMir-708 microRNA precursor family
Behrman S, Acosta-Alvear D, Walter P (March 2011). "A CHOP-regulated microRNA controls rhodopsin expression". The Journal of ...
https://en.wikipedia.org/wiki/Mir-708_microRNA_precursor_family
NyctalopiaNyctalopia
In the absence of light, rhodopsin is regenerated. The body synthesizes rhodopsin from vitamin A, which is why a deficiency in ... Rods contain a receptor-protein called rhodopsin. When light falls on rhodopsin, it undergoes a series of conformational ...
https://en.wikipedia.org/wiki/Nyctalopia
Gaussian network modelGaussian network model
"Identification of core amino acids stabilizing rhodopsin". Proc. Natl. Acad. Sci. U.S.A. 101 (19): 7246-7251. Bibcode:2004PNAS ...
https://en.wikipedia.org/wiki/Gaussian_network_model
Blue cone monochromacyBlue cone monochromacy
... encoding rhodopsin, and located on chromosome 3). OPN1SW and rhodopsin are unaffected in BCM. Since BCM is caused by non- ...
https://en.wikipedia.org/wiki/Blue_cone_monochromacy
ChemotaxonomyChemotaxonomy
... has rhodopsin. In catadromous fish, which migrate from fresh water to the sea, the porphyropsin is replaced by rhodopsin. In an ... Opsins: In the vertebrates, vision is controlled by two very distinct types of opsins, porphyropsin and rhodopsin. They are ... Fresh water fishes have porphyropsin; marine ones and land vertebrates have rhodopsin. In amphibians, a tadpole living in fresh ... anadromous fish, which migrates from the sea to freshwater, the rhodopsin is replaced by porphyropsin. These examples show the ...
https://en.wikipedia.org/wiki/Chemotaxonomy
Alpha ArrestinAlpha Arrestin
Alvarez, Carlos E (2008). "On the origins of arrestin and rhodopsin". BMC Evolutionary Biology. 8 (1): 222. doi:10.1186/1471- ...
https://en.wikipedia.org/wiki/Alpha_Arrestin
Role of acidic amino acids in peptide substrates of the beta-adrenergic receptor kinase and rhodopsin kinaseRole of acidic amino acids in peptide substrates of the beta-adrenergic receptor kinase and rhodopsin kinase
... Biochemistry. 1991 ... Comparing a variety of kinases, only rhodopsin kinase and casein kinase II exhibited significant phosphorylation of the acidic ...
https://pubmed.ncbi.nlm.nih.gov/1645191/?dopt=Abstract
A rhodopsin is the functional photoreceptor for phototaxis in the unicellular eukaryote ChlamydomonasA rhodopsin is the functional photoreceptor for phototaxis in the unicellular eukaryote Chlamydomonas
If visual pigments have a common ancient origin, as is believed, then some unicellular organisms might also use a rhodopsin ... We show here that the unicellular alga Chlamydomonas does indeed use a rhodopsin photoreceptor … ... Rhodopsin is a visual pigment ubiquitous in multicellular animals. ... suggesting homology with the rhodopsins of higher organisms. This is the first demonstration of a rhodopsin photoreceptor in an ...
https://pubmed.ncbi.nlm.nih.gov/6493336/
KINETICS OF RHODOPSIN AT ROOM TEMPERATURE BY PICOSECOND SPECTROSCOPY. - Nokia Bell LabsKINETICS OF RHODOPSIN AT ROOM TEMPERATURE BY PICOSECOND SPECTROSCOPY. - Nokia Bell Labs
Nokia sites use cookies to improve and personalize your experience and to display advertisements. The sites may also include cookies from third parties. By using this site, you consent to the use of cookies. Learn more ...
https://www.bell-labs.com/institute/publications/bl7791056/
Noninvasive optical inhibition with a red-shifted microbial rhodopsin. | Scholars@DukeNoninvasive optical inhibition with a red-shifted microbial rhodopsin. | [email protected]
Noninvasive optical inhibition with a red-shifted microbial rhodopsin. ... Noninvasive optical inhibition with a red-shifted microbial rhodopsin. Journal Article (Journal Article) ...
https://scholars.duke.edu/display/pub1502321
Integration of deletion mutants of bovine rhodopsin into the membrane of the endoplasmic reticulum<...
Heymann JAW, Subramaniam S. Integration of deletion mutants of bovine rhodopsin into the membrane of the endoplasmic reticulum ... Heymann, J. A W ; Subramaniam, S. / Integration of deletion mutants of bovine rhodopsin into the membrane of the endoplasmic ... Integration of deletion mutants of bovine rhodopsin into the membrane of the endoplasmic reticulum. / Heymann, J. A W; ... Heymann, J. A. W., & Subramaniam, S. (2000). Integration of deletion mutants of bovine rhodopsin into the membrane of the ...
https://jhu.pure.elsevier.com/en/publications/integration-of-deletion-mutants-of-bovine-rhodopsin-into-the-memb-3
Rhodopsin and Indicator Yellow - WikidataRhodopsin and Indicator Yellow - Wikidata
scientific article published in Nature
https://m.wikidata.org/wiki/Q59084849
STUCTURE AND CONFORMATIONAL CHANGES OF RHODOPSIN PROTEIN - Oregon Health & Science UniversitySTUCTURE AND CONFORMATIONAL CHANGES OF RHODOPSIN PROTEIN - Oregon Health & Science University
Powered by Pure, Scopus & Elsevier Fingerprint Engine™ © 2022 Elsevier B.V We use cookies to help provide and enhance our service and tailor content. By continuing you agree to the use of cookies. Log in to Pure. ...
https://ohsu.pure.elsevier.com/en/projects/stucture-and-conformational-changes-of-rhodopsin-protein-2
Restoration of visual function in P23H rhodopsin transgenic rats by gene delivery of BiP/Grp78Restoration of visual function in P23H rhodopsin transgenic rats by gene delivery of BiP/Grp78
The P23H mutation within the rhodopsin gene (RHO) causes rhodopsin misfolding, endoplasmic reticulum (ER) stress, and activates ... Restoration of visual function in P23H rhodopsin transgenic rats by gene delivery of BiP/Grp78 Academic Article ... We have now overexpressed BiP to test the hypothesis that this chaperone promotes the trafficking of P23H rhodopsin to the cell ... In cell culture, increasing levels of BiP had no impact on the localization of P23H rhodopsin. However, BiP overexpression ...
http://scholars.uab.edu/display/pub94806
Rhodopsin - Symptoms, Causes, Treatment - NUTRITION & VITAMINS BLOGRhodopsin - Symptoms, Causes, Treatment - NUTRITION & VITAMINS BLOG
Home » Rhodopsin - Symptoms, Causes, Treatment. Rhodopsin - Symptoms, Causes, Treatment. *. July 13, 2008. ... When light energy is absorbed by rhodopsin, the rhodopsin begins within trillionths of a second to decompose. The cause of this ... Rhodopsin is a protein in the membrane of the rod photoreceptor cell in the retina of the eye. It catalyses the only light ... When the rhodopsin in the outer segment of the rod is exposed to light and begins to decompose, this decreases the outer ...
https://3r-medical.com/rhodopsin-symptoms-causes-treatment-6/
Structure of bovine rhodopsin in a trigonal crystal form.Structure of bovine rhodopsin in a trigonal crystal form.
We have determined the structure of bovine rhodopsin at 2.65 A resolution using untwinned native crystals in the space group P3 ... We have determined the structure of bovine rhodopsin at 2.65 A resolution using untwinned native crystals in the space group P3 ... Structure of bovine rhodopsin in a trigonal crystal form.. Translate. Afrikaans. Albanian. Amharic. Arabic. Armenian. ...
https://www.bioseek.eu/us/eng/research/pubmed/Structure_of_bovine_rhodopsin_in_a_trigonal_crystal_form_15491621
MedlinePlus: Genes: RMedlinePlus: Genes: R
RHO: rhodopsin. *RIT1: Ras like without CAAX 1. *RMRP: RNA component of mitochondrial RNA processing endoribonuclease ...
https://medlineplus.gov/genetics/gene-r/
Anti Rhodopsin antibody, anti OPSD antibody, opsin-2 antibody, RHO antibodyAnti Rhodopsin antibody, anti OPSD antibody, opsin-2 antibody, RHO antibody
Rhodopsin antibody for the specific detection of OPSD by immunohistochemistry using Rabbit antibody to Rhodopsin (OSR00220W) ... A synthetic peptide from human Rhodopsin conjugated to blue carrier protein was used as the antigen. The peptide is homologous ... also known as rhodopsin-related congenital stationary night blindness. Congenital stationary night blindness is a ...
https://www.osenses.com/-p-524.html
Far-red absorbing rhodopsins, insights from heterodimeric rhodopsin-cyclases - SFB 1315Far-red absorbing rhodopsins, insights from heterodimeric rhodopsin-cyclases - SFB 1315
Far-red absorbing rhodopsins, insights from heterodimeric rhodopsin-cyclases. Matthias Broser. The recently discovered ... color-tuningfluorescent proteinheterodimeric rhodopsin-cyclasemicrobial rhodopsinNIR-absorptionretinal-chromophore Share the ... Rhodopsin-cyclases from Chytridiomycota fungi show completely unexpected properties for microbial rhodopsins. These ... which is widely present in class III cyclases but is unknown for rhodopsins. NIR-sensitive retinal chromophores have greatly ...
https://www.sfb1315.de/de/publications/far-red-absorbing-rhodopsins-insights-from-heterodimeric-rhodopsin-cyclases-2/
Projects | Igor Pro by WaveMetricsProjects | Igor Pro by WaveMetrics
These projects are user-contributed packages of related Igor procedure files and XOPs (Igor extensions ...
https://www.wavemetrics.com/projects?amp%3Bproject_type=44&project_type=42&os_compatibility=26
Probing the dark state tertiary structure in the cytoplasmic domain of rhodopsin: Proximities between amino acids deduced from...
... domain of rhodopsin is presumed to be the key to the restriction of binding of transducin and rhodopsin kinase to rhodopsin. ... domain of rhodopsin is presumed to be the key to the restriction of binding of transducin and rhodopsin kinase to rhodopsin. ... domain of rhodopsin is presumed to be the key to the restriction of binding of transducin and rhodopsin kinase to rhodopsin. ... domain of rhodopsin is presumed to be the key to the restriction of binding of transducin and rhodopsin kinase to rhodopsin. ...
https://asu.pure.elsevier.com/en/publications/probing-the-dark-state-tertiary-structure-in-the-cytoplasmic-doma
IMSEAR at SEARO: Mutation analysis of codons 345 and 347 of rhodopsin gene in Indian retinitis pigmentosa patients.
More than 100 mutations have been reported till date in the rhodopsin gene in patients with retinitis pigmentosa. The present ... Dikshit M, Agarwal R. Mutation analysis of codons 345 and 347 of rhodopsin gene in Indian retinitis pigmentosa patients. ... Mutation analysis of codons 345 and 347 of rhodopsin gene in Indian retinitis pigmentosa patients. ... study was undertaken to detect the reported rhodopsin gene point mutations in Indian retinitis pigmentosa patients. We looked ...
https://imsear.searo.who.int/handle/123456789/114270
Calnexin is essential for rhodopsin maturation, Ca2+ regulation, and photoreceptor cell survival. - UW DOVS
Author(s): Rosenbaum EE, Hardie RC, Colley NJ. Calnexin is essential for rhodopsin maturation, Ca2+ regulation, and ... Here, we demonstrate a multifunctional role for calnexin as both a molecular chaperone uniquely required for rhodopsin ... Mutations in Drosophila calnexin lead to severe defects in rhodopsin (Rh1) expression, whereas other photoreceptor cell ... Calnexin is essential for rhodopsin maturation, Ca2+ regulation, and photoreceptor cell survival. ...
https://www.ophth.wisc.edu/blog/2006/01/19/calnexin-is-essential-for-rhodopsin-maturation-ca2-regulation-and-photoreceptor-cell-survival/
Automated QM/MM Screening of Rhodopsin Variants with Enhanced Fluorescence. | J Chem Theory Comput;19(1): 293-310, 2023 Jan 10...Automated QM/MM Screening of Rhodopsin Variants with Enhanced Fluorescence. | J Chem Theory Comput;19(1): 293-310, 2023 Jan 10...
Automated QM/MM Screening of Rhodopsin Variants with Enhanced Fluorescence. Automated QM/MM Screening of Rhodopsin Variants ... models of rhodopsins to be used as fluorescent probes based on the automatic rhodopsin modeling protocol (a-ARM). Such "a-ARM ... The implementation and performance of the protocol are benchmarked using different sets of rhodopsin variants whose absorption ... protocol reproduces the observed trends in fluorescence and it is capable of selecting novel potentially fluorescent rhodopsins ...
https://pesquisa.bvsalud.org/portal/resource/pt/mdl-36516450
CEF-MC : Study suggests paradigm shift about the way microbial rhodopsins functionCEF-MC : Study suggests paradigm shift about the way microbial rhodopsins function
Study suggests paradigm shift about the way microbial rhodopsins function. April 2019. Proteorhodopsins are found in marine ... Like many microbial rhodopsins, proteorhodopsins have seven transmembrane helices and form oligomers. Salt bridge contacts ... These findings suggest a paradigm shift regarding the way microbial rhodopsins function. ...
https://www.cef-mc.de/index.php?id=67&L=842&tx_ttnews%5Btt_news%5D=619&cHash=611a8ca6e22eb66b5472548e12801241
PDF] N-body Information Theory (NbIT) Analysis of Rigid-Body Dynamics in Intracellular Loop 2 of the 5-HT2A Receptor | Semantic...PDF] N-body Information Theory (NbIT) Analysis of Rigid-Body Dynamics in Intracellular Loop 2 of the 5-HT2A Receptor | Semantic...
Crystal structure of rhodopsin: a G-protein-coupled receptor.. *R. Stenkamp, D. Teller, K. Palczewski ... Although the location of carazolol in the β2-adrenergic receptor is very similar to that of retinal in rhodopsin, structural ...
https://www.semanticscholar.org/paper/N-body-Information-Theory-
OR4C45 olfactory receptor family 4 subfamily C member 45 (gene/pseudogene) [Homo sapiens (human)] - Gene - NCBIOR4C45 olfactory receptor family 4 subfamily C member 45 (gene/pseudogene) [Homo sapiens (human)] - Gene - NCBI
7tm_1; 7 transmembrane receptor (rhodopsin family). cl21561. Location:26 → 296. 7tm_4; Olfactory receptor. ...
https://www.ncbi.nlm.nih.gov/gene/403257
A synthetic enzyme built from DNA flips 107 lipids per second in biological membranes | Nature CommunicationsA synthetic enzyme built from DNA flips 107 lipids per second in biological membranes | Nature Communications
Recent in vitro experiments on TMEM16 scramblases27, opsin26, and rhodopsin34 have assessed lipid flip-flop rates of , 104 s-1 ...
https://www.nature.com/articles/s41467-018-04821-5?error=cookies_not_supported
NYU Biology Faculty DirectoryNYU Biology Faculty Directory
Feedback from rhodopsin controls rhodopsin exclusion in Drosophila photoreceptors.. Nature (2011 Oct 9) PMC3208777 free full- ... Iroquois complex genes induce co-expression of rhodopsins in Drosophila.. PLoS Biol (2008 Apr 22) PMC2323304 free full-text ...
https://as.nyu.edu/departments/biology/directory.esteban-mazzoni.html
Anti-Rhodopsin [Rho 1D4], Human IgG1 kappa, Purified by Absolute Antibody, Cat. No. Ab00337-10.0 | Lucerna-Chem AGAnti-Rhodopsin [Rho 1D4], Human IgG1 kappa, Purified by Absolute Antibody, Cat. No. Ab00337-10.0 | Lucerna-Chem AG
Anti-Rhodopsin [Rho 1D4], Human IgG1 kappa, Purified. Catalog Number. Pack Size. List Price*. Quantity. ...
https://shop.lucerna-chem.ch/2810503/anti-rhodopsin-rho-1d4-human-igg1-kappa-purified
International Review of Cell and Molecular Biology, Volume 293 - 1st EditionInternational Review of Cell and Molecular Biology, Volume 293 - 1st Edition
Chapter one: Defective Trafficking of Rhodopsin and Its Role in Retinal Degenerations ...
https://www.elsevier.com/books/international-review-of-cell-and-molecular-biology/jeon/978-0-12-394304-0
BioenergeticsBioenergetics
The light-driven rhodopsin KR2 transports Na+ via the M- and O-states. However, the mechanisms by which the retinal regulates ... Identification of intermediate conformations in the photocycle of the light-driven sodium-pumping rhodopsin KR2. Journal of ... Real-time identification of two substrate-binding intermediates for the light-driven sodium pump rhodopsin. Journal of ... we report real-time identification of these intermediates for the light-driven outward current-generating Na+-pump rhodopsin. ...
https://www.jbc.org/bioenergetics?startPage=&SeriesKey=jbc
Correction: the retromer complex is required for rhodopsin recycling and its loss leads to photoreceptor degeneration<...Correction: the retromer complex is required for rhodopsin recycling and its loss leads to photoreceptor degeneration<...
Correction: the retromer complex is required for rhodopsin recycling and its loss leads to photoreceptor degeneration. PLoS ... Dive into the research topics of Correction: the retromer complex is required for rhodopsin recycling and its loss leads to ... Correction : the retromer complex is required for rhodopsin recycling and its loss leads to photoreceptor degeneration. In: ... Correction : the retromer complex is required for rhodopsin recycling and its loss leads to photoreceptor degeneration. / Wang ...
https://scholars.houstonmethodist.org/en/publications/correction-the-retromer-complex-is-required-for-rhodopsin-recycli
DeCS 2008 - Changed termsDeCS 2008 - Changed terms
Rhodopsin Kinase. G-Protein-Coupled Receptor Kinase 1. Ribonuclease H, Calf Thymus. Ribonuclease H. ...
https://decs.bvs.br/I/rep_i2008.htm
KAKEN - Research Projects | Control of cell functions at the tissue level using micro/nanotechnologies (KAKENHI-PROJECT...KAKEN - Research Projects | Control of cell functions at the tissue level using micro/nanotechnologies (KAKENHI-PROJECT...
Protective effects of transscleral sustained unoprostone delivery against retinal degeneration in S334ter rhodopsin mutant rats ...
https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-26286031/
Bovine rhodopsinPatients with retinitis pigmentosaMicrobial rhodopsinOpsinRetinitis pigmentosaTransmembraneKinaseMutationsAbsorptionPhotoreceptorsRodsFluorescentPhotoreceptor degenerationMolecularInner segmentProteinsConeSequenceCrystalMoleculeFunctionLightVisualShowFormPresentHumanOrangeFoundSpecific
Bovine rhodopsin4
  • The data suggest that 11-cis-retinal is the natural chromophore and that the protein environment of this retinal is similar to that found in bovine rhodopsin, suggesting homology with the rhodopsins of higher organisms. (nih.gov)
  • Heymann, JAW & Subramaniam, S 2000, ' Integration of deletion mutants of bovine rhodopsin into the membrane of the endoplasmic reticulum ', Molecular Membrane Biology , vol. 17, no. 3, pp. 165-174. (elsevier.com)
  • Structure of bovine rhodopsin in a trigonal crystal form. (bioseek.eu)
  • We have determined the structure of bovine rhodopsin at 2.65 A resolution using untwinned native crystals in the space group P3(1), by molecular replacement from the 2.8 A model (1F88) solved in space group P4(1). (bioseek.eu)
Patients with retinitis pigmentosa2
  • More than 100 mutations have been reported till date in the rhodopsin gene in patients with retinitis pigmentosa. (who.int)
  • Spectrum of rhodopsin mutations in Korean patients with retinitis pigmentosa. (cdc.gov)
Microbial rhodopsin2
  • Noninvasive optical inhibition with a red-shifted microbial rhodopsin. (duke.edu)
  • Here these properties are discussed in the context of color-tuning approaches of retinal chromophores, which have been extensively studied since the discovery of the first microbial rhodopsin, bacteriorhodopsin, in 1971 (Oesterhelt et al. (sfb1315.de)
Opsin3
  • Rhodopsin consists of the protein opsin linked to 11-cis retinal a prosthetic group. (3r-medical.com)
  • When exposed to light rhodopsin is split up into the yellow compound retinene and colourless protein opsin. (3r-medical.com)
  • Under the influence of light, rhodopsin is converted to orange red compound lumirhodopsin, which becomes changed to metarhodopsin, ultimately forming a yellow mixture of trans-retinene and opsin. (3r-medical.com)
Retinitis pigmentosa6
  • The P23H mutation within the rhodopsin gene (RHO) causes rhodopsin misfolding, endoplasmic reticulum (ER) stress, and activates the unfolded protein response (UPR), leading to rod photoreceptor degeneration and autosomal dominant retinitis pigmentosa (ADRP). (uab.edu)
  • IMSEAR at SEARO: Mutation analysis of codons 345 and 347 of rhodopsin gene in Indian retinitis pigmentosa patients. (who.int)
  • Dikshit M, Agarwal R. Mutation analysis of codons 345 and 347 of rhodopsin gene in Indian retinitis pigmentosa patients. (who.int)
  • The present study was undertaken to detect the reported rhodopsin gene point mutations in Indian retinitis pigmentosa patients. (who.int)
  • Prevalence of Rhodopsin mutations in autosomal dominant Retinitis Pigmentosa in Spain: clinical and analytical review in 200 families. (cdc.gov)
  • Genetic Analysis of the Rhodopsin Gene Identifies a Mosaic Dominant Retinitis Pigmentosa Mutation in a Healthy Individual. (cdc.gov)
Transmembrane3
  • Mutants containing one, three, or five N-terminal transmembrane segments of rhodopsin, as well as mutants containing only the first transmembrane segment, but with hydrophilic extensions at the C-terminus were studied. (elsevier.com)
  • The findings demonstrate that the C-terminal transmembrane segments play a crucial role in determining the final orientation of rhodopsin, and that the commitment to the correct orientation occurs only after the synthesis of at least three transmembrane segments. (elsevier.com)
  • Like many microbial rhodopsins, proteorhodopsins have seven transmembrane helices and form oligomers. (cef-mc.de)
Kinase2
  • Comparing a variety of kinases, only rhodopsin kinase and casein kinase II exhibited significant phosphorylation of the acidic peptides. (nih.gov)
  • A dark state tertiary structure in the cytoplasmic domain of rhodopsin is presumed to be the key to the restriction of binding of transducin and rhodopsin kinase to rhodopsin. (elsevier.com)
Mutations1
  • Mutations in Drosophila calnexin lead to severe defects in rhodopsin (Rh1) expression, whereas other photoreceptor cell proteins are expressed normally. (wisc.edu)
Absorption3
  • Once the 11-cis retinal is formed it automatically recombines with the scotopsin to reform rhodopsin, which then remains stable until its decomposition is again triggered by absorption of light energy. (3r-medical.com)
  • The implementation and performance of the protocol are benchmarked using different sets of rhodopsin variants whose absorption and, more relevantly, emission spectra have been experimentally measured. (bvsalud.org)
  • Rhodopsin exhibits peak absorption wavelength at about 500 nm. (bvsalud.org)
Photoreceptors2
  • A survey of the morphology and action spectra of other protists suggests that rhodopsins may be common photoreceptors of chlorophycean, prasinophycean and dinophycean algae. (nih.gov)
  • We have now overexpressed BiP to test the hypothesis that this chaperone promotes the trafficking of P23H rhodopsin to the cell membrane, reprograms the UPR favoring the survival of photoreceptors, blocks apoptosis, and, ultimately, preserves vision in ADRP rats. (uab.edu)
Rods3
  • Light falling on the retina brings about certain chemical changes in the rhodopsin and other substances present in the rods and cones. (3r-medical.com)
  • It is the metarrhodopsin II also called activated rhodopsin that excites electrical changes in the rods that then transmit the visual image into the central nervous system. (3r-medical.com)
  • These chemicals, called rhodopsin in rods and photopsins in cones, have a specific structure that enables them to absorb light of different wavelengths. (macmillan.com)
Fluorescent2
  • We present a computational protocol for the fast and automated screening of excited- state hybrid quantum mechanics /molecular mechanics (QM/MM) models of rhodopsins to be used as fluorescent probes based on the automatic rhodopsin modeling protocol (a- ARM ). (bvsalud.org)
  • We show that, despite important limitations that make unsafe to use it as a black-box tool, the protocol reproduces the observed trends in fluorescence and it is capable of selecting novel potentially fluorescent rhodopsins. (bvsalud.org)
Photoreceptor degeneration1
  • We have previously demonstrated that BiP mRNA levels are selectively reduced in animal models of ADRP arising from P23H rhodopsin expression at ages that precede photoreceptor degeneration. (uab.edu)
Molecular1
  • Here, we demonstrate a multifunctional role for calnexin as both a molecular chaperone uniquely required for rhodopsin maturation and a regulator of Ca2+ that enters photoreceptor cells during light stimulation. (wisc.edu)
Inner segment1
  • When the rhodopsin in the outer segment of the rod is exposed to light and begins to decompose, this decreases the outer segment conductance of sodium to the interior of the rod, even though the sodium ions continue to be pumped out of the inner segment. (3r-medical.com)
Proteins1
  • Now he is working on a number of important proteins in real life, including the light-gated chloride-pumping rhodopsin and the human receptor protein ACE2 in conjugation with the SARS-CoV-2 viral spike protein. (edu.hk)
Cone2
  • The rod photopigment is called rhodopsin ,cone has three photopigments, called photopsins . (wikibooks.org)
  • Light of a certain frequency reaches the right cell (the cone cell of the retina), a chemical reaction takes place in the presence of this light in a substance called rhodopsin. (consilieresicoaching.ro)
Sequence1
  • The isomerisation of retinal leads to a change of the shape of rhodopsin, which triggers a sequence of reactions, which lead to a nerve impulse. (3r-medical.com)
Crystal1
  • The observed disulfide bond formation rates correlate well with proximity of these residues found in the crystal structure of rhodopsin in the dark. (elsevier.com)
Molecule1
  • The cause of this is photo activation of electrons in the retinal portions of the rhodopsin which leads to an instantaneous change of the cis form of retinal into an all trans form, which still has the same chemical structure as the cis form but has a different physical structure- a straight molecule rather than an angulated molecule. (3r-medical.com)
Function2
  • Thus, the preservation of photoreceptor function resulting from elevated levels of BiP is due to suppression of apoptosis rather than to a promotion of rhodopsin folding. (uab.edu)
  • These findings suggest a paradigm shift regarding the way microbial rhodopsins function. (cef-mc.de)
Light3
  • When light energy is absorbed by rhodopsin, the rhodopsin begins within trillionths of a second to decompose. (3r-medical.com)
  • red light by rhodopsin and the red photopsin. (macmillan.com)
  • Purple light is absorbed by rhodopsin, blue photopsin, and red photopsin, but not green photopsin, and so on. (macmillan.com)
Visual2
  • Rhodopsin is a visual pigment ubiquitous in multicellular animals. (nih.gov)
  • If visual pigments have a common ancient origin, as is believed, then some unicellular organisms might also use a rhodopsin photoreceptor. (nih.gov)
Show2
  • We show here that the unicellular alga Chlamydomonas does indeed use a rhodopsin photoreceptor. (nih.gov)
  • The recently discovered Rhodopsin-cyclases from Chytridiomycota fungi show completely unexpected properties for microbial rhodopsins. (sfb1315.de)
Form1
  • And finally the 11-cis retinol is converted into 11-cis retinal that combines with scotopsin to form rhodopsin. (3r-medical.com)
Present1
  • Further a brief review about the concept of heterodimerization is given, which is widely present in class III cyclases but is unknown for rhodopsins. (sfb1315.de)
Human1
  • A synthetic peptide from human Rhodopsin conjugated to blue carrier protein was used as the antigen. (osenses.com)
Orange1
Found1
  • Humans cannot make Rhodopsin, instead they use and external source, b -carotene, that is found in food in order to synthesis it. (3r-medical.com)
Specific2
  • Specific for Rhodopsin. (osenses.com)
  • The experiment also wants to obtain specific data concerning whether there are changes in the conformation of a rhodopsin receptor upton exposure to microgravity. (nasa.gov)
MedlinePlus: Genes: R
MedlinePlus: Genes: R (medlineplus.gov)
Projects | Igor Pro by WaveMetrics
Projects | Igor Pro by WaveMetrics (wavemetrics.com)
PDF] N-body Information Theory (NbIT) Analysis of Rigid-Body Dynamics in Intracellular Loop 2 of the 5-HT2A Receptor | Semantic...
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Autosomal dominant congenital stationary night blindness: MedlinePlus Genetics
Autosomal dominant congenital stationary night blindness: MedlinePlus Genetics (medlineplus.gov)
Natural and Recombinant - Dog 9 ELISA - Page 1 - TELOS The Electronic Library of Life Science
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A synthetic enzyme built from DNA flips 107 lipids per second in biological membranes | Nature Communications (nature.com)
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Femtosecond-to-millisecond structural changes in a light-driven sodium pump | Nature (nature.com)
Link to Post #1
Link to Post #1 (pentaxforums.com)
ASI | Agenzia Spaziale Italiana
ASI | Agenzia Spaziale Italiana (asi.it)
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Wissenschaftliche Publikationen | Max-Planck-Gesellschaft (mpg.de)
Cryo-EM structures of the ABCA4 importer reveal mechanisms underlying substrate binding and Stargardt disease | Nature...
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Begriffe mit S | Medizin-Lexikon | gesundheit.de (gesundheit.de)
Begriffe mit R | Medizin-Lexikon | gesundheit.de
Begriffe mit R | Medizin-Lexikon | gesundheit.de (gesundheit.de)
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Begriffe mit R | Medizin-Lexikon | gesundheit.de (gesundheit.de)
Begriffe mit N | Medizin-Lexikon | gesundheit.de
Begriffe mit N | Medizin-Lexikon | gesundheit.de (gesundheit.de)
Cell Atlas of the Human Fovea and Peripheral Retina | bioRxiv
Cell Atlas of the Human Fovea and Peripheral Retina | bioRxiv (biorxiv.org)
LSM Publication List (since 2018) | NES | Paul Scherrer Institut (PSI)
LSM Publication List (since 2018) | NES | Paul Scherrer Institut (PSI) (psi.ch)
Table of Contents - November 05, 2008, 28 (45) | Journal of Neuroscience
Table of Contents - November 05, 2008, 28 (45) | Journal of Neuroscience (jneurosci.org)
Peptides
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Pharmaceuticals | Free Full-Text | Cannabinoids and Reproduction: A Lasting and Intriguing History
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A 59-Year-Old With Progressive Difficulty Seeing at Night
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Adaptive divergence in pigment composition promotes phytoplankton biodiversity | Nature
Adaptive divergence in pigment composition promotes phytoplankton biodiversity | Nature (nature.com)
NIH researchers develop gene therapy for rare ciliopathy | National Institutes of Health (NIH)
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