Schiff-base deprotonation is mandatory for light-dependent rhodopsin phosphorylation.

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The kinetics and thermodynamics of bleaching of rhodopsin in dimyristoylphosphatidylcholine. Identification of meta-I, meta-II, and meta-III intermediates

P2860

Q42584319-FAA90628-0F30-486D-BCF3-B90CF7E13768

P2860

Schiff-base deprotonation is mandatory for light-dependent rhodopsin phosphorylation.

Item

http://www.wikidata.org/entity/Q42804918

description

1989 nî lūn-bûn

@nan

1989年の論文

@ja

1989年論文

@yue

1989年論文

@zh-hant

1989年論文

@zh-hk

1989年論文

@zh-mo

1989年論文

@zh-tw

1989年论文

@wuu

1989年论文

@zh

1989年论文

@zh-cn

name

Schiff-base deprotonation is mandatory for light-dependent rhodopsin phosphorylation.

@en

Schiff-base deprotonation is mandatory for light-dependent rhodopsin phosphorylation.

@nl

type

Item

label

Schiff-base deprotonation is mandatory for light-dependent rhodopsin phosphorylation.

@en

Schiff-base deprotonation is mandatory for light-dependent rhodopsin phosphorylation.

@nl

prefLabel

Schiff-base deprotonation is mandatory for light-dependent rhodopsin phosphorylation.

@en

Schiff-base deprotonation is mandatory for light-dependent rhodopsin phosphorylation.

@nl

P1476

Schiff-base deprotonation is mandatory for light-dependent rhodopsin phosphorylation.

@en

P2093

B Seckler

http://www.w3.org/2001/XMLSchema#string

R R Rando

http://www.w3.org/2001/XMLSchema#string

P2860

Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48-kDa protein of rod outer segments

Light-dependent phosphorylation of rhodopsin. Purification and properties of rhodopsin kinase

Complex formation between metarhodopsin II and GTP-binding protein in bovine photoreceptor membranes leads to a shift of the photoproduct equilibrium

A simplification of the protein assay method of Lowry et al. which is more generally applicable

Deprotonation of the Schiff base of rhodopsin is obligate in the activation of the G protein.

Cyclic GMP cascade of vision.

Energetics of primary processes in visula escitation: photocalorimetry of rhodopsin in rod outer segment membranes.

A rapid, sensitive, and versatile assay for protein using Coomassie brilliant blue G250.

Removing unbound detergent from hydrophobic proteins.

Photophysics of light transduction in rhodopsin and bacteriorhodopsin.

P304

489-493

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P31

scholarly article

P356

10.1042/BJ2640489

http://www.w3.org/2001/XMLSchema#string

P407

English

P433

http://www.w3.org/2001/XMLSchema#string

P478

264

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P577

1989-12-01T00:00:00Z

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P5875

20550943

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P698

2604728

http://www.w3.org/2001/XMLSchema#string

P921

phosphorylation

P932

1133606

http://www.w3.org/2001/XMLSchema#string

Schiff-base deprotonation is mandatory for light-dependent rhodopsin phosphorylation.

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P2860

P2860

Schiff-base deprotonation is mandatory for light-dependent rhodopsin phosphorylation.

description

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type

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prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698

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P356

P407

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P478

P577

P5875

P698

P921

P932