Characterization and analysis of frog photoreceptor membranes. - Wikidata - awgldk - TriplyDB

Characterization and analysis of frog photoreceptor membranes.

Characterization and analysis of frog photoreceptor membranes.

http://www.wikidata.org/entity/Q36428494

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Proteomic identification of unique photoreceptor disc components reveals the presence of PRCD, a protein linked to retinal degeneration The GTPase activating factor for transducin in rod photoreceptors is the complex between RGS9 and type 5 G protein beta subunit cGMP binding sites on photoreceptor phosphodiesterase: role in feedback regulation of visual transduction.Probing the catalytic sites and activation mechanism of photoreceptor phosphodiesterase using radiolabeled phosphodiesterase inhibitors The glutamic acid-rich protein-2 (GARP2) is a high affinity rod photoreceptor phosphodiesterase (PDE6)-binding protein that modulates its catalytic properties.Efficacy and selectivity of phosphodiesterase-targeted drugs in inhibiting photoreceptor phosphodiesterase (PDE6) in retinal photoreceptors.Molecular aspects of photoreceptor function.Micropinocytic ingestion of glycosylated albumin by isolated microvessels: possible role in pathogenesis of diabetic microangiopathy Membrane attachment is key to protecting transducin GTPase-activating complex from intracellular proteolysis in photoreceptors Onset of feedback reactions underlying vertebrate rod photoreceptor light adaptation Changes in cGMP concentration correlate with some, but not all, aspects of the light-regulated conductance of frog rod photoreceptors Evaluation of the 17-kDa prenyl-binding protein as a regulatory protein for phototransduction in retinal photoreceptors Turnover of rod photoreceptor outer segments. II. Membrane addition and loss in relationship to light Turnover of rod photoreceptor outer segments. I. Membrane addition and loss in relationship to temperature.Membrane assembly in retinal photoreceptors I. Freeze-fracture analysis of cytoplasmic vesicles in relationship to disc assembly The ultrastructure of lipid-depleted rod photoreceptor membranes Freeze-fracture evidence for the presence of cholesterol in particle-free patches of basal disks and the plasma membrane of retinal rod outer segments of mice and frogs Influence of calcium on guanosine 3',5'-cyclic monophosphate levels in frog rod outer segments Calcium and cyclic GMP regulation of light-sensitive protein phosphorylation in frog photoreceptor membranes.Frog rod outer segments with attached inner segment ellipsoids as an in vitro model for photoreceptors on the retina.Transduction persists in rod photoreceptors after depletion of intracellular calcium Regulation of intracellular cyclic GMP concentration by light and calcium in electropermeabilized rod photoreceptors.Rod outer segment structure influences the apparent kinetic parameters of cyclic GMP phosphodiesterase.Renewal of opsin in the photoreceptor cells of the mosquito Two temporal phases of light adaptation in retinal rods.Structure and function of the visual arrestin oligomer.Use of Ca--EGTA buffers for transposing Ca2+ efflux into pH changes. Application to rod outer segment membrane vesicles.Light-sensitive swelling of isolated frog rod outer segments as an in vitro assay for visual transduction and dark adaptation.Microspectrophotometry of visual pigments.Loss of mTOR signaling affects cone function, cone structure and expression of cone specific proteins without affecting cone survival.The accessibility of bovine rhodopsin in photoreceptor membranes.Light-induced changes in GTP and ATP in frog rod photoreceptors. Comparison with recovery of dark current and light sensitivity during dark adaptation.Regulation of photoreceptor phosphodiesterase catalysis by its non-catalytic cGMP-binding sites.Regulation of photoreceptor phosphodiesterase (PDE6) by phosphorylation of its inhibitory gamma subunit re-evaluated.Specific binding of RGS9-Gbeta 5L to protein anchor in photoreceptor membranes greatly enhances its catalytic activity.Phosducin facilitates light-driven transducin translocation in rod photoreceptors. Evidence from the phosducin knockout mouse.Compartment-specific phosphorylation of phosducin in rods underlies adaptation to various levels of illumination.An effector site that stimulates G-protein GTPase in photoreceptors.Recoverin undergoes light-dependent intracellular translocation in rod photoreceptors.A rhodopsin-lipid-water lamellar system: its characterisation by x-ray diffraction and electron microscopy.

P2860

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P2860

Characterization and analysis of frog photoreceptor membranes.

http://www.wikidata.org/entity/Q36428494

description

1971 nî lūn-bûn

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1971年の論文

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1971年学术文章

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1971年学术文章

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1971年学术文章

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1971年学术文章

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1971年学术文章

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1971年學術文章

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1971年學術文章

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1971年學術文章

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name

Characterization and analysis of frog photoreceptor membranes.

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Characterization and analysis of frog photoreceptor membranes.

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type

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Characterization and analysis of frog photoreceptor membranes.

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Characterization and analysis of frog photoreceptor membranes.

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Characterization and analysis of frog photoreceptor membranes.

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Characterization and analysis of frog photoreceptor membranes.

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The Journal of General Physiology

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Characterization and analysis of frog photoreceptor membranes.

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Bownds D

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Gaide-Huguenin AC

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Gordon-Walker A

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Robinson W

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P2860

The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis

Isolation of the fundamental polypeptide subunits of biological membranes.

The isolation of retinal outer segment fragments.

Calcium and adenosine triphosphate binding to renal membranes.

The molecular weight of rhodopsin and the nature of the rhodopsin-digitonin complex.

On the mechanism of the relaxing effect of fragmented sarcoplasmic reticulum.

Molecular weight analysis of oligopeptides by electrophoresis in polyacrylamide gel with sodium dodecyl sulfate.

The molecular weight of the undegraded polypeptide chain of yeast hexokinase.

Structure of visual pigments. I. Purification, molecular weight, and composition of bovine visual pigment500.

Metabolism of glucose and reduction of retinaldehyde in retinal photoreceptors.

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Photoreceptor protein

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