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lipoprotein
identification of nineteen N-myristoylation sites and three characteristic sites
proteolytic modification
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proteolysis releases a soluble, active fragment of 52-56 kDa
glycoprotein
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glycoprotein
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the enzyme sequence contains a glycosylation site
glycoprotein
identification of five N-glycosylation sites
phosphoprotein
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phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
isoform HMGR1S is inactivated through phosphorylation at Ser577 by the AKIN10-GRIK1 kinase cascade system in vitro
phosphoprotein
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phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
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phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
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phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
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phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
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activity is regulated by phosphorylation and dephosphorylation
phosphoprotein
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phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
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phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
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phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
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phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
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phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
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phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
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phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
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phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
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phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
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activity is regulated by phosphorylation and dephosphorylation
phosphoprotein
the enzyme is phosphorylated at Ser872 by AMP-activated protein kinase and reversibly dephosphorylated by phosphatase 2A
phosphoprotein
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phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
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regulation of the plant enzyme by phosphorylation/dephosphorylation
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
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phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
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phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
Ochromonas malhamensis
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phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
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phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
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phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
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the enzyme sequence contains a phosphorylation site
phosphoprotein
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phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
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phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
activity is regulated by phosphorylation and dephosphorylation
phosphoprotein
-
activity is regulated by phosphorylation and dephosphorylation
-
phosphoprotein
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phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
regulation of the plant enzyme by phosphorylation/dephosphorylation
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
regulation of the plant enzyme by phosphorylation/dephosphorylation
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
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phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
identification of a cAMP-and cGMP-dependent protein kinase phosphorylation site, thirteen Protein kinase C phosphorylation sites, and eleven Casein kinase II phosphorylation sites
phosphoprotein
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phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
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phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
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phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
additional information
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protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
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protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
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protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
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protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
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protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
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protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
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protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
the isozyme is not regulated by phosphorylation
additional information
the isozyme is not regulated by phosphorylation
additional information
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the isozyme is not regulated by phosphorylation
additional information
the isozyme is probably not regulated by phosphorylation
additional information
the isozyme is probably not regulated by phosphorylation
additional information
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the isozyme is probably not regulated by phosphorylation
additional information
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genistein, eicosapentaenoic acid and docosahexaenoic acid down-regulate reductase activity, primarily through posttranscriptional effects
additional information
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protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
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ubiquitination and proteasomal degradation of microsomal, but not mitochondrial, HMGR isozymes depends on environmental salinity, overview
additional information
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protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
Ochromonas malhamensis
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated