(Q42825096)

English

The phosphoinositide-dependent kinase, PDK-1, phosphorylates conventional protein kinase C isozymes by a mechanism that is independent of phosphoinositide 3-kinase

scientific article published on 28 September 2001

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

8 November 2017

The phosphoinositide-dependent kinase, PDK-1, phosphorylates conventional protein kinase C isozymes by a mechanism that is independent of phosphoinositide 3-kinase (English)

1 reference

Europe PubMed Central

PubMed publication ID

8 November 2017

phosphorylation

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author name string

E D Sonnenburg

1

1 reference

Europe PubMed Central

PubMed publication ID

8 November 2017

T Gao

2

1 reference

Europe PubMed Central

PubMed publication ID

8 November 2017

A C Newton

3

1 reference

Europe PubMed Central

PubMed publication ID

8 November 2017

language of work or name

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publication date

28 September 2001

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Europe PubMed Central

PubMed publication ID

8 November 2017

number of pages

9

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based on heuristic

inferred from page(s)

Journal of Biological Chemistry

1 reference

Europe PubMed Central

PubMed publication ID

8 November 2017

276

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Europe PubMed Central

PubMed publication ID

8 November 2017

48

1 reference

Europe PubMed Central

PubMed publication ID

8 November 2017

45289-45297

1 reference

Europe PubMed Central

PubMed publication ID

8 November 2017

Cellular signaling: pivoting around PDK-1.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107416200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107416200

21 January 2018

Studies and perspectives of protein kinase C.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107416200

21 January 2018

Multiple pathways control protein kinase C phosphorylation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107416200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107416200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107416200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107416200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107416200

21 January 2018

Protein kinase C: structural and spatial regulation by phosphorylation, cofactors, and macromolecular interactions

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107416200

21 January 2018

The hydrophobic phosphorylation motif of conventional protein kinase C is regulated by autophosphorylation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107416200

21 January 2018

Protein kinase B kinases that mediate phosphatidylinositol 3,4,5-trisphosphate-dependent activation of protein kinase B

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107416200

21 January 2018

Role of phosphatidylinositol 3,4,5-trisphosphate in regulating the activity and localization of 3-phosphoinositide-dependent protein kinase-1

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107416200

21 January 2018

Role of translocation in the activation and function of protein kinase B

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107416200

21 January 2018

Domain swapping used to investigate the mechanism of protein kinase B regulation by 3-phosphoinositide-dependent protein kinase 1 and Ser473 kinase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107416200

21 January 2018

Effect of phosphoinositide-dependent kinase 1 on protein kinase B translocation and its subsequent activation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107416200

21 January 2018

Dual role of pseudosubstrate in the coordinated regulation of protein kinase C by phosphorylation and diacylglycerol

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107416200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107416200

21 January 2018

Carboxyl-terminal phosphorylation regulates the function and subcellular localization of protein kinase C betaII.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107416200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107416200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107416200

21 January 2018

The carboxyl terminus of protein kinase c provides a switch to regulate its interaction with the phosphoinositide-dependent kinase, PDK-1.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107416200

21 January 2018

Association of methionyl-tRNA synthetase with detergent-insoluble components of the rough endoplasmic reticulum

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107416200

21 January 2018

Protein kinase C V3 domain mutants with differential sensitivities to m-calpain are not resistant to phorbol-ester-induced down-regulation.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107416200

21 January 2018

Phosphorylation of threonine 638 critically controls the dephosphorylation and inactivation of protein kinase Calpha.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107416200

21 January 2018

A 3-phosphoinositide-dependent protein kinase-1 (PDK1) docking site is required for the phosphorylation of protein kinase Czeta (PKCzeta ) and PKC-related kinase 2 by PDK1

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107416200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107416200

21 January 2018

Insulin and PIP3 activate PKC-zeta by mechanisms that are both dependent and independent of phosphorylation of activation loop (T410) and autophosphorylation (T560) sites

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107416200

21 January 2018

Caenorhabditis elegans PIAK, a phospholipid-independent kinase that activates the AKT/PKB survival kinase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107416200

21 January 2018

Further evidence that 3-phosphoinositide-dependent protein kinase-1 (PDK1) is required for the stability and phosphorylation of protein kinase C (PKC) isoforms.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107416200

21 January 2018

Rapamycin-sensitive phosphorylation of PKC on a carboxy-terminal site by an atypical PKC complex

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107416200

21 January 2018

Signalling pathways regulating the dephosphorylation of Ser729 in the hydrophobic domain of protein kinase Cepsilon upon cell passage

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107416200

21 January 2018

Identifiers

10.1074/JBC.M107416200

1 reference

Europe PubMed Central

PubMed publication ID

8 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

8 November 2017

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