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Cited by 1,110

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Protein Kinase C Isotypes Controlled by Phosphoinositide 3-Kinase Through the Protein Kinase PDK1

Le Good, J. Ann, Ziegler, Wolfgang H., Parekh, Davey B., Alessi, Dario R., Cohen, Philip, Parker, Peter J.·1998·Science

Abstract

Phosphorylation sites in members of the protein kinase A (PKA), PKG, and PKC kinase subfamily are conserved. Thus, the PKB kinase PDK1 may be responsible for the phosphorylation of PKC isotypes. PDK1 phosphorylated the activation loop sites of PKCζ and PKCδ in vitro and in a phosphoinositide 3-kinase (PI 3-kinase)–dependent manner in vivo in human embryonic kidney (293) cells. All members of the PKC family tested formed complexes with PDK1. PDK1-dependent phosphorylation of PKCδ in vitro was stimulated by combined PKC and PDK1 activators. The activation loop phosphorylation of PKCδ in response to serum stimulation of cells was PI 3-kinase–dependent and was enhanced by PDK1 coexpression.

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Metadata

Authors
Le Good, J. A., Ziegler, W. H., Parekh, D. B., Alessi, D. R., Cohen, P., & Parker, P. J.
Venue
Science
Published
1998-09-25
Volume
281
Issue
5385
Pages
2042-2045
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2146989813
Cited by
1,110
References
2
FWCI
28.25
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Protein Kinase C Isotypes Controlled by Phosphoinositide 3-Kinase Through the Protein Kinase PDK1. https://app.cochat.ai/papers/10.1126/science.281.5385.2042
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Le Good, J. A., Ziegler, W. H., Parekh, D. B., Alessi, D. R., Cohen, P., & Parker, P. J. (1998). Protein Kinase C Isotypes Controlled by Phosphoinositide 3-Kinase Through the Protein Kinase PDK1. Science. https://doi.org/10.1126/science.281.5385.2042

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