The C2 Domain and Altered ATP-Binding Loop Phosphorylation at Ser³⁵⁹ Mediate the Redox-Dependent Increase in Protein Kinase C-δ Activity
about
Protein kinase C mechanisms that contribute to cardiac remodellingA novel phosphorylation site at Ser130 adjacent to the pseudosubstrate domain contributes to the activation of protein kinase C-δ.Mechanisms for redox-regulation of protein kinase C.Protein kinase C delta phosphorylates ecdysone receptor B1 to promote gene expression and apoptosis under 20-hydroxyecdysone regulation.Multifunctional roles of PKCδ: Opportunities for targeted therapy in human diseasePhos-tag SDS-PAGE resolves agonist- and isoform-specific activation patterns for PKD2 and PKD3 in cardiomyocytes and cardiac fibroblasts.CLEAVAGE ALTERS THE MOLECULAR DETERMINANTS OF PROTEIN KINASE C-δ CATALYTIC ACTIVITY.Homing in: Mechanisms of Substrate Targeting by Protein Kinases.
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P2860
The C2 Domain and Altered ATP-Binding Loop Phosphorylation at Ser³⁵⁹ Mediate the Redox-Dependent Increase in Protein Kinase C-δ Activity
description
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2015 թուականի Մարտին հրատարակուած գիտական յօդուած
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2015年の論文
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2015年論文
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2015年論文
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2015年論文
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2015年論文
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2015年论文
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name
The C2 Domain and Altered ATP- ...... in Protein Kinase C-δ Activity
@ast
The C2 Domain and Altered ATP- ...... in Protein Kinase C-δ Activity
@en
type
label
The C2 Domain and Altered ATP- ...... in Protein Kinase C-δ Activity
@ast
The C2 Domain and Altered ATP- ...... in Protein Kinase C-δ Activity
@en
prefLabel
The C2 Domain and Altered ATP- ...... in Protein Kinase C-δ Activity
@ast
The C2 Domain and Altered ATP- ...... in Protein Kinase C-δ Activity
@en
P2093
P2860
P356
P1476
The C2 Domain and Altered ATP- ...... in Protein Kinase C-δ Activity
@en
P2093
Jennifer E Van Eyk
Jianli Gong
Pingbo Zhang
Sivaraj Sivaramakrishnan
Susan F Steinberg
Yongneng Yao
P2860
P304
P356
10.1128/MCB.01436-14
P407
P577
2015-03-09T00:00:00Z