3-Hydroxy-3-methylglutaryl-coenzyme A reductase from Arabidopsis thaliana is structurally distinct from the yeast and animal enzymes.
about
Regulation of HMG-CoA reductase: identification of the site phosphorylated by the AMP-activated protein kinase in vitro and in intact rat liverCloning, expression, and characterization of cDNAs encoding Arabidopsis thaliana squalene synthaseImmunological evidence for eight spans in the membrane domain of 3-hydroxy-3-methylglutaryl coenzyme A reductase: implications for enzyme degradation in the endoplasmic reticulumRegulation of squalene synthase, a key enzyme of sterol biosynthesis, in tobacco.Expression of 3-hydroxy-3-methylglutaryl-CoA reductase, p-hydroxybenzoate-m-geranyltransferase and genes of phenylpropanoid pathway exhibits positive correlation with shikonins content in arnebia [Arnebia euchroma (Royle) Johnston].Molecular cloning and sequence analysis of 3-hydroxy-3-methylglutaryl-coenzyme A reductase from the human parasite Schistosoma mansoniSpecies-specific expansion and molecular evolution of the 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGR) gene family in plants.Terpene Specialized Metabolism in Arabidopsis thalianaIsoprenoid biosynthesis is required for miRNA function and affects membrane association of ARGONAUTE 1 in Arabidopsis.Genetic and biochemical evaluation of eucaryotic membrane protein topology: multiple transmembrane domains of Saccharomyces cerevisiae 3-hydroxy-3-methylglutaryl coenzyme A reductaseComplete blockage of the mevalonate pathway results in male gametophyte lethalityArabidopsis thaliana contains two differentially expressed 3-hydroxy-3-methylglutaryl-CoA reductase genes, which encode microsomal forms of the enzyme.Targeting and topology in the membrane of plant 3-hydroxy-3-methylglutaryl coenzyme A reductase.Sterol metabolism.Differential activation of potato 3-hydroxy-3-methylglutaryl coenzyme A reductase genes by wounding and pathogen challenge.The N-terminal domain of tomato 3-hydroxy-3-methylglutaryl-CoA reductases. Sequence, microsomal targeting, and glycosylation.Molecular dissection of the role of the membrane domain in the regulated degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase.
P2860
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P2860
3-Hydroxy-3-methylglutaryl-coenzyme A reductase from Arabidopsis thaliana is structurally distinct from the yeast and animal enzymes.
description
1989 nî lūn-bûn
@nan
1989 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի ապրիլին 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
3-Hydroxy-3-methylglutaryl-coe ...... the yeast and animal enzymes.
@ast
3-Hydroxy-3-methylglutaryl-coe ...... the yeast and animal enzymes.
@en
type
label
3-Hydroxy-3-methylglutaryl-coe ...... the yeast and animal enzymes.
@ast
3-Hydroxy-3-methylglutaryl-coe ...... the yeast and animal enzymes.
@en
prefLabel
3-Hydroxy-3-methylglutaryl-coe ...... the yeast and animal enzymes.
@ast
3-Hydroxy-3-methylglutaryl-coe ...... the yeast and animal enzymes.
@en
P2860
P356
P1476
3-Hydroxy-3-methylglutaryl-coe ...... the yeast and animal enzymes.
@en
P2093
P2860
P304
P356
10.1073/PNAS.86.8.2779
P407
P577
1989-04-01T00:00:00Z