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Richard A. Currie
Researcher at University of Dundee
Publications - 20
Citations - 2670
Richard A. Currie is an academic researcher from University of Dundee. The author has contributed to research in topics: Medicine & Biology. The author has an hindex of 12, co-authored 13 publications receiving 2579 citations.
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Journal ArticleDOI
Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities.
Simon Dowler,Richard A. Currie,David G. Campbell,Maria Deak,Gursant S Kular,C P Downes,Dario R. Alessi +6 more
TL;DR: This study lays the foundation for future work to establish the phospholipid-binding specificities of these proteins in vivo, and their physiological role(s).
Journal ArticleDOI
PDK1 acquires PDK2 activity in the presence of a synthetic peptide derived from the carboxyl terminus of PRK2
Anudharan Balendran,Antonio Casamayor,Maria Deak,Andrew D. Paterson,Piers R. J. Gaffney,Richard A. Currie,C. Peter Downes,Dario R. Alessi +7 more
TL;DR: PDK1 and PDK2 might be the same enzyme, the substrate specificity and activity of PDK1 being regulated through its interaction with another protein(s), and PRK2 is a probable substrate for PDK 1.
Journal ArticleDOI
Role of phosphatidylinositol 3,4,5-trisphosphate in regulating the activity and localization of 3-phosphoinositide-dependent protein kinase-1.
Richard A. Currie,Kay S. Walker,Alexander Gray,Maria Deak,Antonio Casamayor,C P Downes,Philip Cohen,Dario R. Alessi,John M. Lucocq +8 more
TL;DR: Results indicate that PtdIns(3,4,5)P3 plays several roles in the PDK1-induced activation of P KBalpha, and binds to the PH domain of PKB, altering its conformation so that it can be activated by PDK 1.
Journal ArticleDOI
The PIF-binding pocket in PDK1 is essential for activation of S6K and SGK, but not PKB.
TL;DR: It is demonstrated that a pocket in the kinase domain of PDK1, termed the ‘PIF‐binding pocket’, plays a key role in mediating the interaction and phosphorylation of S6K1 and SGK1 at their T‐loop motif byPDK1.
Journal ArticleDOI
Identification of a pocket in the PDK1 kinase domain that interacts with PIF and the C‐terminal residues of PKA
Ricardo M. Biondi,Peter C. F. Cheung,Antonio Casamayor,Maria Deak,Richard A. Currie,Dario R. Alessi +5 more
TL;DR: The results suggest that the PIF‐binding pocket on the kinase domain of PDK1 acts as a ‘docking site’, enabling it to interact with and enhance the phosphorylation of its substrates.