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

Data up to Jan 2025

Published1998
Citations383
References32

Total Citations Per Year

Abstract

References (32)

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1998 • 612 citations

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1998 • 579 citations

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

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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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Three protein kinase structures define a common motif

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Requirement for negative charge on “activation loop” of protein kinase C.

1994 • 153 citations

Phosphorylation at Conserved Carboxyl-terminal Hydrophobic Motif Regulates the Catalytic and Regulatory Domains of Protein Kinase C

1997 • 151 citations

Autophosphorylation of Protein Kinase C at Three Separated Regions of Its Primary Sequence

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1994 • 139 citations

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

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Determination of in Vivo Phosphorylation Sites in Protein Kinase C

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Identification of the phosphorylated region responsible for the permissive activation of protein kinase C

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Protein kinase C autophosphorylates by an intrapeptide reaction.

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1998 • 57 citations

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Regulation of conventional protein kinase C isozymes by phosphoinositide-dependent kinase… (1998) – Current Biology | Metascience Observatory Explorer