Dephosphorylation of PKCdelta by protein phosphatase 2Ac and its inhibition by nucleotides
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Protein kinase C delta negatively regulates tyrosine hydroxylase activity and dopamine synthesis by enhancing protein phosphatase-2A activity in dopaminergic neuronsProtein kinase C-dependent dephosphorylation of tyrosine hydroxylase requires the B56δ heterotrimeric form of protein phosphatase 2AActive site inhibitors protect protein kinase C from dephosphorylation and stabilize its mature form.Resistance of Akt kinases to dephosphorylation through ATP-dependent conformational plasticity.Formation of ternary complex of human biliverdin reductase-protein kinase Cδ-ERK2 protein is essential for ERK2-mediated activation of Elk1 protein, nuclear factor-κB, and inducible nitric-oxidase synthase (iNOS).Protein kinase Cδ oxidation contributes to ERK inactivation in lupus T cellsRegulation of smooth muscle by inducible nitric oxide synthase and NADPH oxidase in vascular proliferative diseasesHeat shock proteins regulate activation-induced proteasomal degradation of the mature phosphorylated form of protein kinase C.Occupational hazards: allosteric regulation of protein kinases through the nucleotide-binding pocket.Protein kinase C: the "masters" of calcium and lipid.Autoregulation of kinase dephosphorylation by ATP binding in AGC protein kinases.Biliverdin reductase: a target for cancer therapy?Novel phosphorylation site markers of protein kinase C delta activation.Identification of two distinct pathways of protein kinase Calpha down-regulation in intestinal epithelial cells.Vitamin E (alpha-tocopherol) attenuates cyclo-oxygenase 2 transcription and synthesis in immortalized murine BV-2 microgliaProtein kinase d inhibitors uncouple phosphorylation from activity by promoting agonist-dependent activation loop phosphorylation.Calmodulin and ATP support activity of the Cav1.2 channel through dynamic interactions with the channel.The Role of Regulatory Domains in Maintaining Autoinhibition in the Multidomain Kinase PKCα.Biliverdin reductase: more than a namesake - the reductase, its Peptide fragments, and biliverdin regulate activity of the three classes of protein kinase CAllosteric regulation of PKCθ: understanding multistep phosphorylation and priming by ligands in AGC kinases.PKC maturation is promoted by nucleotide pocket occupation independently of intrinsic kinase activity.The siRNA-mediated knockdown of GluN3A in 46C-derived neural stem cells affects mRNA expression levels of neural genes, including known iGluR interactors.
P2860
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P2860
Dephosphorylation of PKCdelta by protein phosphatase 2Ac and its inhibition by nucleotides
description
2002 nî lūn-bûn
@nan
2002 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Dephosphorylation of PKCdelta ...... its inhibition by nucleotides
@ast
Dephosphorylation of PKCdelta ...... its inhibition by nucleotides
@en
Dephosphorylation of PKCdelta ...... its inhibition by nucleotides
@nl
type
label
Dephosphorylation of PKCdelta ...... its inhibition by nucleotides
@ast
Dephosphorylation of PKCdelta ...... its inhibition by nucleotides
@en
Dephosphorylation of PKCdelta ...... its inhibition by nucleotides
@nl
prefLabel
Dephosphorylation of PKCdelta ...... its inhibition by nucleotides
@ast
Dephosphorylation of PKCdelta ...... its inhibition by nucleotides
@en
Dephosphorylation of PKCdelta ...... its inhibition by nucleotides
@nl
P2093
P2860
P1433
P1476
Dephosphorylation of PKCdelta ...... its inhibition by nucleotides
@en
P2093
Jozef Goris
Jyoti Srivastava
Stephen M Dilworth
P2860
P304
P356
10.1016/S0014-5793(02)02500-0
P407
P50
P577
2002-04-01T00:00:00Z