标题
Tuning the signalling output of protein kinase C
作者
关键词
-
出版物
BIOCHEMICAL SOCIETY TRANSACTIONS
Volume 42, Issue 6, Pages 1477-1483
出版商
Portland Press Ltd.
发表日期
2014-11-24
DOI
10.1042/bst20140172
参考文献
相关参考文献
注意:仅列出部分参考文献,下载原文获取全部文献信息。- Intramolecular Conformational Changes Optimize Protein Kinase C Signaling
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- Heat Shock Proteins Regulate Activation-induced Proteasomal Degradation of the Mature Phosphorylated Form of Protein Kinase C
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- Agonist-induced Down-regulation of Endogenous Protein Kinase C α through an Endolysosomal Mechanism
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- Scaffold State Switching Amplifies, Accelerates, and Insulates Protein Kinase C Signaling
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- Electrostatic and Hydrophobic Interactions Differentially Tune Membrane Binding Kinetics of the C2 Domain of Protein Kinase Cα
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- Regulated Binding of Importin-α to Protein Kinase Cδ in Response to Apoptotic Signals Facilitates Nuclear Import
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- Rb-dependent cellular senescence, multinucleation and susceptibility to oncogenic transformation through PKC scaffolding by SSeCKS/AKAP12
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- Interaction with AKAP79 Modifies the Cellular Pharmacology of PKC
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- Recognition of an intra-chain tandem 14-3-3 binding site within PKCɛ
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- NMR Structure/Function Relationships of Peptides Corresponding to the C1B1 Region of PKCγ
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- Essential function of TORC2 in PKC and Akt turn motif phosphorylation, maturation and signalling
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- The mammalian target of rapamycin complex 2 controls folding and stability of Akt and protein kinase C
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