Aromatic lipophilic spin traps effectively inhibit RPE65 isomerohydrolase activity. - Wikidata - wikimedia - TriplyDB

Aromatic lipophilic spin traps effectively inhibit RPE65 isomerohydrolase activity.

Aromatic lipophilic spin traps effectively inhibit RPE65 isomerohydrolase activity.

http://www.wikidata.org/entity/Q35203590

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Structural basis of carotenoid cleavage: from bacteria to mammals Retinol Dehydrogenases Regulate Vitamin A Metabolism for Visual Function Chemistry of the retinoid (visual) cycle Alpha-phenyl-N-tert-butylnitrone (PBN) prevents light-induced degeneration of the retina by inhibiting RPE65 protein isomerohydrolase activity Potential implication of the chemical properties and bioactivity of nitrone spin traps for therapeutics PBN (Phenyl-N-Tert-Butylnitrone)-Derivatives Are Effective in Slowing the Visual Cycle and Rhodopsin Regeneration and in Protecting the Retina from Light-Induced Damage Aromatic residues in the substrate cleft of RPE65 protein govern retinol isomerization and modulate its progression.Inhibition of RPE65 Retinol Isomerase Activity by Inhibitors of Lipid Metabolism The Biochemical Basis of Vitamin A3 Production in Arthropod Vision Vitamin A and Vision.

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Aromatic lipophilic spin traps effectively inhibit RPE65 isomerohydrolase activity.

http://www.wikidata.org/entity/Q35203590

description

2011 nî lūn-bûn

@nan

2011 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Aromatic lipophilic spin traps effectively inhibit RPE65 isomerohydrolase activity.

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Aromatic lipophilic spin traps effectively inhibit RPE65 isomerohydrolase activity.

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Aromatic lipophilic spin traps effectively inhibit RPE65 isomerohydrolase activity.

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Aromatic lipophilic spin traps effectively inhibit RPE65 isomerohydrolase activity.

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Aromatic lipophilic spin traps effectively inhibit RPE65 isomerohydrolase activity.

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Aromatic lipophilic spin traps effectively inhibit RPE65 isomerohydrolase activity.

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Eugenia Poliakov

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Michael Ayele

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Preethi Chander

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Stephanie Kuo

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Susan Gentleman

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T Michael Redmond

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Toral Parikh

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P2860

Mutations in RPE65 cause autosomal recessive childhood-onset severe retinal dystrophy

RPE65 is the isomerohydrolase in the retinoid visual cycle

Crystal structure of native RPE65, the retinoid isomerase of the visual cycle

Mutations in the RPE65 gene in patients with autosomal recessive retinitis pigmentosa or leber congenital amaurosis

Mutations in RPE65 cause Leber's congenital amaurosis

Molecular cloning and expression of RPE65, a novel retinal pigment epithelium-specific microsomal protein that is post-transcriptionally regulated in vitro

RPE65, visual cycle retinol isomerase, is not inherently 11-cis-specific: support for a carbocation mechanism of retinol isomerization

Rpe65 is the retinoid isomerase in bovine retinal pigment epithelium

Pharmacological effects of the spin trap agents N-t-butyl-phenylnitrone (PBN) and 2,2,6, 6-tetramethylpiperidine-N-oxyl (TEMPO) in a rabbit thromboembolic stroke model: combination studies with the thrombolytic tissue plasminogen activator.

Mutation of key residues of RPE65 abolishes its enzymatic role as isomerohydrolase in the visual cycle.

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6739-6741

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10.1021/BI200532M

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32

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50

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