M. Rider

Publications171
h-index46
Citations8,815
Highly Influential Citations414
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Phosphorylation and activation of heart PFK-2 by AMPK has a role in the stimulation of glycolysis during ischaemia
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Role of PFKFB3-Driven Glycolysis in Vessel Sprouting
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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*
TLDR
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.
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6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: head-to-head with a bifunctional enzyme that controls glycolysis.
TLDR
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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Activation of AMP-Activated Protein Kinase Leads to the Phosphorylation of Elongation Factor 2 and an 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*
TLDR
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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Role of fructose 2,6-bisphosphate in the control of glycolysis in mammalian tissues.
TLDR
The purpose of this article is to specify the conditions under which Fru-2,6-P2 plays a role in the control of glycolysis, and to review recent studies dealing with Fru’s metabolism in mammalian tissues other than liver.
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Identification of Phosphorylation Sites in AMP-activated Protein Kinase (AMPK) for Upstream AMPK Kinases and Study of Their Roles by Site-directed Mutagenesis*
TLDR
The identification of two new phosphorylation sites in the α-subunit, viz.
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Cloning, sequencing and expression of rat liver 3-phosphoglycerate dehydrogenase.
TLDR
Rat liver d-3-phosphoglycerate dehydrogenase was purified to homogeneity and digested with trypsin, and the sequences of two peptides were determined, indicating that this enzyme is not involved in human D- or L-hydroxyglutaric aciduria.
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Mechanisms of control of heart glycolysis.
TLDR
The kinetic properties and the biochemical characteristics of control steps (glucose transporters, hexokinase, glycogen phosphorylase and phosphofructokinases) in the heart are considered together to explain the control of glycolysis by substrate supply and availability, energy demand, oxygen deprivation and hormones.
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