Phosphorylation at conserved carboxyl-terminal hydrophobic motif regulates the catalytic and regulatory domains of protein kinase C
about
The phosphatase PHLPP controls the cellular levels of protein kinase CThe extended protein kinase C superfamilyRegulation of protein kinase C inactivation by Fas-associated protein with death domainPKA, PKC, and AKAP localization in and around the neuromuscular junctionDynamics and Membrane Interactions of Protein Kinase CShort linear motifs - ex nihilo evolution of protein regulationThe Novel PKCθ from Benchtop to ClinicHigh resolution crystal structure of the human PDK1 catalytic domain defines the regulatory phosphopeptide docking site.Regulation of protein kinase D by multisite phosphorylation. Identification of phosphorylation sites by mass spectrometry and characterization by site-directed mutagenesisAssociation of immature hypophosphorylated protein kinase cepsilon with an anchoring protein CG-NAPPhosphorylation of the protein kinase C-theta activation loop and hydrophobic motif regulates its kinase activity, but only activation loop phosphorylation is critical to in vivo nuclear-factor-kappaB inductionThe C-terminal V5 domain of Protein Kinase Cα is intrinsically disordered, with propensity to associate with a membrane mimeticActivation-dependent degradation of protein kinase C eta.DUSP3/VHR is a pro-angiogenic atypical dual-specificity phosphatase.Phosphorylation of seminal vesicle protein IV on Ser58 enhances its peroxidase-stimulating activity.Acute ethanol administration rapidly increases phosphorylation of conventional protein kinase C in specific mammalian brain regions in vivoMultiple pathways control protein kinase C phosphorylation.Structural basis of protein kinase C isoform functionThe turn motif is a phosphorylation switch that regulates the binding of Hsp70 to protein kinase C.BART inhibits pancreatic cancer cell invasion by PKCα inactivation through binding to ANX7.Protein kinase C isoforms as specific targets for modulation of vascular smooth muscle function in hypertension.Regulation of the ABC kinases by phosphorylation: protein kinase C as a paradigmPeptidyl-prolyl isomerase Pin1 controls down-regulation of conventional protein kinase C isozymesPKC isozymes and diacylglycerol-regulated proteins as effectors of growth factor receptors.A comprehensive map of the toll-like receptor signaling network.Protein Kinase C Inhibitors as Modulators of Vascular Function and their Application in Vascular DiseaseInsight into intra- and inter-molecular interactions of PKC: design of specific modulators of kinase function.Protein kinase Cζ exhibits constitutive phosphorylation and phosphatidylinositol-3,4,5-triphosphate-independent regulationThe chaperones Hsp90 and Cdc37 mediate the maturation and stabilization of protein kinase C through a conserved PXXP motif in the C-terminal tail.The life and death of protein kinase C.Distinct enzyme combinations in AKAP signalling complexes permit functional diversity.Proliferating or differentiating stimuli act on different lipid-dependent signaling pathways in nuclei of human leukemia cells.Autophosphorylation suppresses whereas kinase inhibition augments the translocation of protein kinase Calpha in response to diacylglycerol.Molecular mechanisms regulating protein kinase Czeta turnover and cellular transformation.Intramolecular C2 Domain-Mediated Autoinhibition of Protein Kinase C βII.Interplay between calcium, diacylglycerol, and phosphorylation in the spatial and temporal regulation of PKCalpha-GFP.The carboxyl terminus of protein kinase c provides a switch to regulate its interaction with the phosphoinositide-dependent kinase, PDK-1.CD45 negatively regulates monocytic cell differentiation by inhibiting phorbol 12-myristate 13-acetate-dependent activation and tyrosine phosphorylation of protein kinase Cdelta.Mammalian TOR controls one of two kinase pathways acting upon nPKCdelta and nPKCepsilon.Multisite dephosphorylation and desensitization of conventional protein kinase C isotypes
P2860
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P2860
Phosphorylation at conserved carboxyl-terminal hydrophobic motif regulates the catalytic and regulatory domains of protein kinase C
description
1997 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 1997
@ast
im Juli 1997 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1997/07/18)
@sk
vědecký článek publikovaný v roce 1997
@cs
wetenschappelijk artikel (gepubliceerd op 1997/07/18)
@nl
наукова стаття, опублікована в липні 1997
@uk
name
Phosphorylation at conserved c ...... ry domains of protein kinase C
@ast
Phosphorylation at conserved c ...... ry domains of protein kinase C
@en
Phosphorylation at conserved c ...... ry domains of protein kinase C
@nl
type
label
Phosphorylation at conserved c ...... ry domains of protein kinase C
@ast
Phosphorylation at conserved c ...... ry domains of protein kinase C
@en
Phosphorylation at conserved c ...... ry domains of protein kinase C
@nl
prefLabel
Phosphorylation at conserved c ...... ry domains of protein kinase C
@ast
Phosphorylation at conserved c ...... ry domains of protein kinase C
@en
Phosphorylation at conserved c ...... ry domains of protein kinase C
@nl
P2860
P356
P1476
Phosphorylation at conserved c ...... ry domains of protein kinase C
@en
P2093
A. C. Newton
A. S. Edwards
P2860
P304
18382–18390
P356
10.1074/JBC.272.29.18382
P407
P577
1997-07-18T00:00:00Z