Effects on ligand interaction and membrane translocation of the positively charged arginine residues situated along the C1 domain binding cleft in the atypical protein kinase C isoforms.
about
The Novel PKCθ from Benchtop to ClinicIdentification of the activator-binding residues in the second cysteine-rich regulatory domain of protein kinase Cθ (PKCθ)Protein kinase C: poised to signalp23/Tmp21 associates with protein kinase Cdelta (PKCdelta) and modulates its apoptotic function.Charge density influences C1 domain ligand affinity and membrane interactionsStructural basis of protein kinase C isoform functionHomology modeling of mosquito cytochrome P450 enzymes involved in pyrethroid metabolism: insights into differences in substrate selectivity.Requirements for pseudosubstrate arginine residues during autoinhibition and phosphatidylinositol 3,4,5-(PO₄)₃-dependent activation of atypical PKC.Characterization of the interaction of phorbol esters with the C1 domain of MRCK (myotonic dystrophy kinase-related Cdc42 binding kinase) alpha/beta.Diacylglycerol lactones targeting the structural features that distinguish the atypical C1 domains of protein kinase C ζ and ι from typical C1 domains.Molecular basis for failure of "atypical" C1 domain of Vav1 to bind diacylglycerol/phorbol ester.Partitioning-defective protein 6 (Par-6) activates atypical protein kinase C (aPKC) by pseudosubstrate displacement.Zeta Inhibitory Peptide Disrupts Electrostatic Interactions That Maintain Atypical Protein Kinase C in Its Active Conformation on the Scaffold p62.The human biliverdin reductase-based peptide fragments and biliverdin regulate protein kinase Cδ activity: the peptides are inhibitors or substrate for the protein kinase C.Functional comparison of protein domains within aPKCs involved in nucleocytoplasmic shuttling.Protein kinase Cζ exhibits constitutive phosphorylation and phosphatidylinositol-3,4,5-triphosphate-independent regulationProtein Scaffolds Control Localized Protein Kinase Cζ Activity.Metabolic functions of atypical protein kinase C: "good" and "bad" as defined by nutritional status.The Multifunctional Protein Kinase C-ε in Cancer Development and Progression.Protein kinase C as a tumor suppressor.A single residue in the C1 domain sensitizes novel protein kinase C isoforms to cellular diacylglycerol production.Kinases of eIF2a Switch Translation of mRNA Subset during Neuronal Plasticity.Kinetic analysis of the interaction of the C1 domain of protein kinase C with lipid membranes by stopped-flow spectroscopy.HIF and HOIL-1L-mediated PKCζ degradation stabilizes plasma membrane Na,K-ATPase to protect against hypoxia-induced lung injury.Modeling studies on the structural determinants for the DAG/phorbol ester binding to C1 domain.The C1 domain of Vav3, a novel potential therapeutic target.Protein kinase C: perfectly balanced.Refining a steroidogenic model: an analysis of RNA-seq datasets from insect prothoracic glands.
P2860
Q27024068-675394F4-F32D-4955-81BE-61DE5DAFC6BEQ27683701-A2B931F7-F5BB-4E35-A700-306FC0CDFBBEQ28265620-3A0C5E71-107C-4B34-A86F-24F07C7C669EQ30500170-307B8F9E-E499-425E-B9FB-7D0259E8F8C8Q33959125-BCB6E159-A51A-49F4-AF16-944CBF78EDE4Q33973406-A85EFB5F-8054-4553-A065-8C4B6EF51C5BQ34011288-6191EC56-3C29-4725-A578-6AA127DFB4FEQ34139024-5376E3DB-E1B9-489A-B6A1-2D8596AEC7D9Q34748568-BC14C172-6386-4482-9EDB-2B2ED844078CQ35027203-9585394C-0A2C-444A-83BD-0318E280A8A2Q35921737-0D04A5AD-68A8-4CCC-B274-F9F60BC0996CQ36033174-2DD77316-5BF9-48CE-899E-1DD53105E00CQ36065198-AF60E6B4-F8EE-4F43-A0FF-D6C8853EC19AQ36098076-9FC3B086-95C3-493A-BC41-469EAC9A7857Q36425605-67414400-4547-4955-9B96-CA847C267BBFQ36954156-09C3C025-F2FF-42B4-ADF4-2C231DBA6ABFQ37034450-99132821-29B6-4948-9581-5FFC69CE4F25Q37174783-9511FE1E-07BD-4B20-B7DD-2ABD28D8A24EQ38204165-24CD7393-5895-4269-8F5A-0E647B10F7E7Q39286734-4D2E9697-F43F-4ED0-A952-A35E64F1DAACQ42503419-D8813D4C-C300-40F9-99A8-B6F7B9862E73Q43476509-ACDE705B-AACF-4AE2-A6C4-013CF8796FC8Q45953801-05C75864-BBBE-4229-BA30-842D0002CF51Q46133539-99902D22-D38E-4471-87DD-5A4B035092A4Q46231206-CC730DC0-73B7-45A6-8079-EBF2AF414E4BQ47777161-77BD5159-3D56-414E-B203-58385D83E39AQ52669759-CB622E10-795E-4A58-8BE8-C87F1634CB3FQ55645537-869CFC01-C437-4726-801B-AEC0C168B963
P2860
Effects on ligand interaction and membrane translocation of the positively charged arginine residues situated along the C1 domain binding cleft in the atypical protein kinase C isoforms.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
Effects on ligand interaction ...... cal protein kinase C isoforms.
@en
type
label
Effects on ligand interaction ...... cal protein kinase C isoforms.
@en
prefLabel
Effects on ligand interaction ...... cal protein kinase C isoforms.
@en
P2093
P2860
P356
P1476
Effects on ligand interaction ...... cal protein kinase C isoforms.
@en
P2093
Megan L Peach
Peter M Blumberg
Stephen Wincovitch
Susan H Garfield
Victor E Marquez
Yongmei Pu
P2860
P304
33773-33788
P356
10.1074/JBC.M606560200
P407
P577
2006-09-01T00:00:00Z