Mark H. Rider mainly investigates Biochemistry, Protein kinase A, Cell biology, Phosphorylation and AMPK. His study in Protein kinase A is interdisciplinary in nature, drawing from both Glycogen synthase, P70-S6 Kinase 1 and Spliceosome. Mark H. Rider studies Cell biology, focusing on MAP2K7 in particular.
His work investigates the relationship between MAP2K7 and topics such as Mitogen-activated protein kinase kinase that intersect with problems in Cyclin-dependent kinase 2. His work in Phosphorylation addresses issues such as Kinase, which are connected to fields such as Adenylate kinase, Adenine nucleotide and Signal transduction. His Glycolysis research is multidisciplinary, incorporating perspectives in Fructose, Oxidative phosphorylation and Phosphofructokinase 2.
His scientific interests lie mostly in Biochemistry, Protein kinase A, Cell biology, Phosphorylation and AMPK. He regularly ties together related areas like Molecular biology in his Biochemistry studies. When carried out as part of a general Protein kinase A research project, his work on Mitogen-activated protein kinase kinase is frequently linked to work in EEF2, therefore connecting diverse disciplines of study.
His Cell biology research incorporates themes from GLUT4 and GRB10. His work on Protein kinase B, P70-S6 Kinase 1 and Protein phosphorylation as part of general Phosphorylation study is frequently connected to Ribosomal protein s6, therefore bridging the gap between diverse disciplines of science and establishing a new relationship between them. His biological study spans a wide range of topics, including Glucose transporter, Endocrinology, Glucose uptake and Internal medicine.
Mark H. Rider spends much of his time researching AMPK, Cell biology, Biochemistry, Protein kinase A and Internal medicine. His research in AMPK intersects with topics in Glucose uptake, Activator, Insulin resistance and Skeletal muscle. His Cell biology research is multidisciplinary, incorporating elements of Phosphofructokinase 2, PFKFB4, Na+/K+-ATPase and Cell growth.
His work in the fields of Biochemistry, such as Enzyme, Metabolite and Intracellular, overlaps with other areas such as Tau isoforms and Absolute quantification. His work in Protein kinase A covers topics such as Adenine nucleotide which are related to areas like Adenylate kinase, Signal transduction, Catabolism and Anabolism. His studies deal with areas such as Nuclear receptor and Endocrinology as well as Internal medicine.
His primary areas of investigation include Biochemistry, Cell biology, AMPK, Pentose phosphate pathway and Phosphorylation. The various areas that he examines in his Biochemistry study include Internal medicine and Muscle contraction. His Cell biology research is multidisciplinary, incorporating perspectives in PFKFB4, Phosphofructokinase 2, Allosteric regulation and Cancer research.
AMPK is a subfield of Protein kinase A that Mark H. Rider investigates. The concepts of his Pentose phosphate pathway study are interwoven with issues in Metabolite, Phosphatase, Pyruvate kinase and Metabolic pathway. His Phosphorylation study combines topics from a wide range of disciplines, such as Signal transduction, Adenylate kinase, Kinase and Adenine nucleotide.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
Role of PFKFB3-Driven Glycolysis in Vessel Sprouting
Katrien De Bock;Maria Georgiadou;Sandra Schoors;Anna Kuchnio.
Cell (2013)
Phosphorylation and activation of heart PFK-2 by AMPK has a role in the stimulation of glycolysis during ischaemia.
A S Marsin;L Bertrand;M H Rider;J Deprez.
Current Biology (2000)
Phosphorylation and activation of heart 6-phosphofructo-2-kinase by protein kinase B and other protein kinases of the insulin signaling cascades
Johan Deprez;Didier Vertommen;Dario R. Alessi;Louis Hue.
Journal of Biological Chemistry (1997)
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;Jigna V. Patel.
Current Biology (2002)
Role of fructose 2,6-bisphosphate in the control of glycolysis in mammalian tissues.
Louis Hue;Mark Rider.
Biochemical Journal (1987)
6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase: head-to-head with a bifunctional enzyme that controls glycolysis
Mark H. Rider;Luc Bertrand;Didier Vertommen;Paul A. Michels.
Biochemical Journal (2004)
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.
Journal of Biological Chemistry (2006)
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.
Journal of Biological Chemistry (2003)
A Cluster of Mutations in the UMOD Gene Causes Familial Juvenile Hyperuricemic Nephropathy with Abnormal Expression of Uromodulin
Karin Dahan;Olivier Devuyst;Michèle Smaers;Didier Vertommen.
Journal of The American Society of Nephrology (2003)
Sustained activation of AMP-activated protein kinase induces c-Jun N-terminal kinase activation and apoptosis in liver cells.
Delphine Meisse;Mark Van de Casteele;Christophe Beauloye;Isabelle Hainault.
FEBS Letters (2002)
If you think any of the details on this page are incorrect, let us know.
We appreciate your kind effort to assist us to improve this page, it would be helpful providing us with as much detail as possible in the text box below:
Université Catholique de Louvain
Université Catholique de Louvain
Institut Cochin
Université Paris Cité
University of Adelaide
Université Catholique de Louvain
University of Edinburgh
Australian Catholic University
Université Catholique de Louvain
Grenoble Alpes University
Hong Kong University of Science and Technology
University of Minnesota
University of Toronto
University of Murcia
Graz University of Technology
University of Lapland
Stanford University
Imperial College London
University of California, Los Angeles
Centre national de la recherche scientifique, CNRS
Burnet Institute
Australian Catholic University
Cornell University
Northwestern University
Harvard University
Indiana University