(Q28616439)

3 February 2017

title

Regulation of conventional protein kinase C isozymes by phosphoinositide-dependent kinase 1 (PDK-1) (English)

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3 February 2017

E. M. Dutil

1

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3 February 2017

A. Toker

series ordinal

2

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3 February 2017

A. C. Newton

series ordinal

3

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3 February 2017

language of work or name

English

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publication date

17 December 2016

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3 February 2017

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3 February 2017

volume

8

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3 February 2017

issue

25

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3 February 2017

page(s)

1366–1375

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Three protein kinase structures define a common motif

3 February 2017

cites work

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Active and inactive protein kinases: structural basis for regulation

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Phosphorylation and activation of cAMP-dependent protein kinase by phosphoinositide-dependent protein kinase

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Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex

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Activity of the MAP kinase ERK2 is controlled by a flexible surface loop

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Protein kinase C and lipid signaling for sustained cellular responses

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Regulation of protein kinase C.

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Determination of in Vivo Phosphorylation Sites in Protein Kinase C

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Protein kinase C is regulated in vivo by three functionally distinct phosphorylations

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7 January 2021

Autophosphorylation of protein kinase C at three separated regions of its primary sequence

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7 January 2021

Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Balpha

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7 January 2021

Phosphorylation and activation of p70s6k by PDK1

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3-Phosphoinositide-dependent protein kinase 1 (PDK1) phosphorylates and activates the p70 S6 kinase in vivo and in vitro

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3-Phosphoinositide-dependent protein kinase-1 (PDK1): structural and functional homology with the Drosophila DSTPK61 kinase

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Dual role of phosphatidylinositol-3,4,5-trisphosphate in the activation of protein kinase B

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Translocation of PDK-1 to the plasma membrane is important in allowing PDK-1 to activate protein kinase B

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7 January 2021

Regulation of protein kinase C zeta by PI 3-kinase and PDK-1

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7 January 2021

Phosphorylation at conserved carboxyl-terminal hydrophobic motif regulates the catalytic and regulatory domains of protein kinase C

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7 January 2021

Protected-Site Phosphorylation of Protein Kinase C in Hippocampal Long-Term Potentiation

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Threonine-497 is a critical site for permissive activation of protein kinase C alpha

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Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1

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The direct measurement of protein kinase C (PKC) activity in isolated membranes using a selective peptide substrate

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Cloning and expression of multiple protein kinase C cDNAs

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Phosphorylation of protein kinase C-alpha on serine 657 controls the accumulation of active enzyme and contributes to its phosphatase-resistant state

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7 January 2021

10.1016/S0960-9822(98)00017-7

Identifiers

DOI

0 references

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