J
Jenny Bain
Researcher at University of Dundee
Publications - 19
Citations - 7717
Jenny Bain is an academic researcher from University of Dundee. The author has contributed to research in topics: Kinase & MAP2K7. The author has an hindex of 18, co-authored 19 publications receiving 7318 citations. Previous affiliations of Jenny Bain include University of Padua.
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Journal ArticleDOI
The selectivity of protein kinase inhibitors: a further update.
Jenny Bain,Lorna Plater,Matthew Elliott,Natalia Shpiro,C. James Hastie,Hilary McLauchlan,Iva V. Klevernic,J. Simon C. Arthur,Dario R. Alessi,Philip Cohen +9 more
TL;DR: Harmine has been identified as a potent and specific inhibitor of DYRK1A (dual-specificity tyrosine-phosphorylated and -regulated kinase 1A) in vitro and the results have further emphasized the need for considerable caution in using small-molecule inhibitors of protein kinases to assess the physiological roles of these enzymes.
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Calmodulin-dependent protein kinase kinase-β is an alternative upstream kinase for AMP-activated protein kinase
Simon A. Hawley,David A. Pan,Kirsty J. Mustard,Louise Ross,Jenny Bain,Arthur M. Edelman,Bruno G. Frenguelli,D. Grahame Hardie +7 more
TL;DR: It is reported that there is a significant basal activity and phosphorylation of AMPK in LKB1-deficient cells that can be stimulated by Ca2+ ionophores, and studies using the CaMKK inhibitor STO-609 and isoform-specific siRNAs show thatCaMKKbeta is required for this effect.
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The specificities of protein kinase inhibitors: an update.
TL;DR: The results suggest that the combined use of Roscovitine and Kenpaullone may be useful for identifying substrates and physiological roles of cyclin-dependent protein kinases, whereas the combineduse of Kenp Paullone and LiCl may be Useful for identifying substrateates and physiology roles of glycogen synthase kinase 3.
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Exploitation of KESTREL to identify NDRG family members as physiological substrates for SGK1 and GSK3
James Murray,David G. Campbell,Nicholas A. Morrice,Gillian C. Auld,Natalia Shpiro,Rodolpho Marquez,Mark Peggie,Jenny Bain,Graham B. Bloomberg,Florian Grahammer,Florian Lang,Peer Wulff,Dietmar Kuhl,Philip Cohen +13 more
TL;DR: NDRG1 and NDRG2 are identified as physiological substrates for SGK1, and it is demonstrated that phosphorylation of N DRG1 by SGK 1 primes it for phosphorylated by GSK3.
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BIRB796 inhibits all p38 MAPK isoforms in vitro and in vivo.
TL;DR: The compound BIRB796 also inhibits the activity and activation of SAPK3/p38γ as discussed by the authors, which is a physiological substrate of p38α and p38β.