D
Didier Vertommen
Researcher at Université catholique de Louvain
Publications - 191
Citations - 8341
Didier Vertommen is an academic researcher from Université catholique de Louvain. The author has contributed to research in topics: Phosphorylation & Protein kinase A. The author has an hindex of 47, co-authored 165 publications receiving 7144 citations. Previous affiliations of Didier Vertommen include Katholieke Universiteit Leuven & Catholic University of Leuven.
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Journal ArticleDOI
Activation of AMP-Activated Protein Kinase Leads to the Phosphorylation of Elongation Factor 2 and an Inhibition of Protein Synthesis
Sandrine Horman,Gareth J. Browne,Ulrike Krause,J. V. Patel,Didier Vertommen,Luc Bertrand,A. Lavoinne,Louis Hue,Christopher G. Proud,Mark H. Rider +9 more
TL;DR: The activation of e EF2 kinase by AMPK, resulting in the phosphorylation and inactivation of eEF2, provides a novel mechanism for the inhibition of protein synthesis.
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Phosphorylation and activation of heart 6-phosphofructo-2-kinase by protein kinase B and other protein kinases of the insulin signaling cascades
TL;DR: It is proposed that PKB is part of the insulin signaling cascade for PFK-2 activation in heart and phosphorylated Ser-466 and Ser-483 in the BH1 isoform, but to different extents.
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6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase: head-to-head with a bifunctional enzyme that controls glycolysis
TL;DR: A PFK-2/FBPase-2 sequence in the genome of one prokaryote could be the result of horizontal gene transfer from a eukaryote distantly related to all other organisms, possibly a protist.
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Insulin Antagonizes Ischemia-induced Thr172 Phosphorylation of AMP-activated Protein Kinase α-Subunits in Heart via Hierarchical Phosphorylation of Ser485/491
Sandrine Horman,Didier Vertommen,Richard Heath,Dietbert Neumann,Véronique Mouton,Aangela Woods,Uwe Schlattner,Theo Wallimann,David Carling,Louis Hue,Mark H. Rider +10 more
TL;DR: It is proposed that the effect of insulin to antagonize AMP-activatedprotein kinase activation involves a hierarchical mechanism whereby Ser485/Ser491 phosphorylation by protein kinase B reduces subsequent phosphorylated of Thr172 by LKB1 and the resulting activation of AMp-activated protein Kinase.
Journal ArticleDOI
Identification of phosphorylation sites in AMP-activated protein kinase (AMPK) for upstream AMPK kinases and study of their roles by site-directed mutagenesis.
Angela Woods,Didier Vertommen,Dietbert Neumann,Roland Türk,J.D. Bayliss,Uwe Schlattner,Theo Wallimann,David Carling,Mark H. Rider +8 more
TL;DR: The identification of two new phosphorylation sites in the α-subunit, viz.