The membrane binding domain of rod cGMP phosphodiesterase is posttranslationally modified by methyl esterification at a C-terminal cysteine.
about
Identification and characterization of all-trans-retinol dehydrogenase from photoreceptor outer segments, the visual cycle enzyme that reduces all-trans-retinal to all-trans-retinolBrain G protein gamma subunits contain an all-trans-geranylgeranylcysteine methyl ester at their carboxyl termini.RAS-converting enzyme 1-mediated endoproteolysis is required for trafficking of rod phosphodiesterase 6 to photoreceptor outer segmentsGreasing the protein biosynthesis machinery of photoreceptor neurons: Role for postprenylation processing of proteins.Isoprenylation masks a conformational epitope and enhances trans-dominant inhibitory function of the large hepatitis delta antigen.Farnesyl cysteine C-terminal methyltransferase activity is dependent upon the STE14 gene product in Saccharomyces cerevisiae.Deficiency of Isoprenylcysteine Carboxyl Methyltransferase (ICMT) Leads to Progressive Loss of Photoreceptor FunctionSignal transducing membrane complexes of photoreceptor outer segments.Membrane-binding domain of the small G protein G25K contains an S-(all-trans-geranylgeranyl)cysteine methyl ester at its carboxyl terminus.Retinol dehydrogenases: membrane-bound enzymes for the visual function.Complete cDNA sequences of mouse rod photoreceptor cGMP phosphodiesterase alpha- and beta-subunits, and identification of beta'-, a putative beta-subunit isozyme produced by alternative splicing of the beta-subunit gene.The gamma subunit of brain G-proteins is methyl esterified at a C-terminal cysteine.Solubilization of membrane-bound rod phosphodiesterase by the rod phosphodiesterase recombinant delta subunit.Modulation of insulin secretion from normal rat islets by inhibitors of the post-translational modifications of GTP-binding proteinsPhosphorylation of bovine rod photoreceptor cyclic GMP phosphodiesterase.Characterization of prenylated protein methyltransferase in Leishmania.Light- and guanosine 5'-3-O-(thio)triphosphate-sensitive localization of a G protein and its effector on detergent-resistant membrane rafts in rod photoreceptor outer segments.Mechanistic insights into the role of prenyl-binding protein PrBP/δ in membrane dissociation of phosphodiesterase 6.Affinities of bovine photoreceptor cGMP phosphodiesterases for rod and cone inhibitory subunits.
P2860
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P2860
The membrane binding domain of rod cGMP phosphodiesterase is posttranslationally modified by methyl esterification at a C-terminal cysteine.
description
1989 nî lūn-bûn
@nan
1989 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
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
name
The membrane binding domain of ...... tion at a C-terminal cysteine.
@ast
The membrane binding domain of ...... tion at a C-terminal cysteine.
@en
The membrane binding domain of ...... tion at a C-terminal cysteine.
@nl
type
label
The membrane binding domain of ...... tion at a C-terminal cysteine.
@ast
The membrane binding domain of ...... tion at a C-terminal cysteine.
@en
The membrane binding domain of ...... tion at a C-terminal cysteine.
@nl
prefLabel
The membrane binding domain of ...... tion at a C-terminal cysteine.
@ast
The membrane binding domain of ...... tion at a C-terminal cysteine.
@en
The membrane binding domain of ...... tion at a C-terminal cysteine.
@nl
P2093
P2860
P356
P1476
The membrane binding domain of ...... tion at a C-terminal cysteine.
@en
P2093
P2860
P304
P356
10.1073/PNAS.86.23.9238
P407
P577
1989-12-01T00:00:00Z