Topography of the rhodopsin molecule. Identification of the domain phosphorylated.
about
Labelling of the cytoplasmic domains of ovine rhodopsin with hydrophilic chemical probesThe opsin family of proteins.The molecular aspects of visual photoreceptors.Protein phosphorylation in the brain.Rhodopsin phosphorylation suggests biochemical heterogeneities of retinal rod disks.Mechanistic studies on rhodopsin kinase. Light-dependent phosphorylation of C-terminal peptides of rhodopsin.Structural studies on membrane-bound bovine rhodopsin.Phosphorylation of ovine rhodopsin. Identification of the phosphorylated sites.On the disulphide bonds of rhodopsinsRegulation of retinal transducin by C-terminal peptides of rhodopsin.Phosphorylation of solubilised dark-adapted rhodopsin. Insights into the activation of rhodopsin kinase.A segment corresponding to amino acids Val170-Arg182 of bovine arrestin is capable of binding to phosphorylated rhodopsin.
P2860
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P2860
Topography of the rhodopsin molecule. Identification of the domain phosphorylated.
description
1978 nî lūn-bûn
@nan
1978年の論文
@ja
1978年論文
@yue
1978年論文
@zh-hant
1978年論文
@zh-hk
1978年論文
@zh-mo
1978年論文
@zh-tw
1978年论文
@wuu
1978年论文
@zh
1978年论文
@zh-cn
name
Topography of the rhodopsin molecule. Identification of the domain phosphorylated.
@en
Topography of the rhodopsin molecule. Identification of the domain phosphorylated.
@nl
type
label
Topography of the rhodopsin molecule. Identification of the domain phosphorylated.
@en
Topography of the rhodopsin molecule. Identification of the domain phosphorylated.
@nl
prefLabel
Topography of the rhodopsin molecule. Identification of the domain phosphorylated.
@en
Topography of the rhodopsin molecule. Identification of the domain phosphorylated.
@nl
P2093
P2860
P356
P1433
P1476
Topography of the rhodopsin molecule. Identification of the domain phosphorylated.
@en
P2093
P2860
P304
P356
10.1042/BJ1750421
P407
P577
1978-11-01T00:00:00Z