What is he best known for?
The fields of study he is best known for:
His primary areas of investigation include Cell biology, Biochemistry, Phosphorylation, PI3K/AKT/mTOR pathway and Eukaryotic initiation factor.
His study in Cell biology focuses on Kinase, MAP2K7, P70-S6 Kinase 1, Signal transduction and MAP kinase kinase kinase.
His is doing research in Mitogen-activated protein kinase kinase, Amino acid, Protein biosynthesis, mTORC2 and mTORC1, both of which are found in Biochemistry.
His Phosphorylation study integrates concerns from other disciplines, such as Extracellular and Protein catabolism.
His PI3K/AKT/mTOR pathway study incorporates themes from Autophagy and Programmed cell death.
His work deals with themes such as eIF2B, Translational regulation, eIF2, EIF4E and Initiation factor, which intersect with Eukaryotic initiation factor.
His most cited work include:
- Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2 (822 citations)
- Regulation of elongation factor 2 kinase by p90RSK1 and p70 S6 kinase (649 citations)
- The mTOR pathway in the control of protein synthesis. (495 citations)
What are the main themes of his work throughout his whole career to date?
Christopher G. Proud spends much of his time researching Cell biology, Biochemistry, Phosphorylation, Protein biosynthesis and Kinase.
Christopher G. Proud frequently studies issues relating to Eukaryotic initiation factor and Cell biology.
In his work, Reticulocyte and Peptide sequence is strongly intertwined with Molecular biology, which is a subfield of Biochemistry.
His research integrates issues of Endocrinology and Internal medicine in his study of Phosphorylation.
The concepts of his Protein biosynthesis study are interwoven with issues in Translation, Translation factor, Elongation factor and Protein subunit.
Christopher G. Proud studied Kinase and EEF2 that intersect with Elongation Factor-2 Kinase and Calmodulin.
He most often published in these fields:
- Cell biology (62.50%)
- Biochemistry (46.08%)
- Phosphorylation (30.39%)
What were the highlights of his more recent work (between 2013-2021)?
- Cell biology (62.50%)
- mTORC1 (26.47%)
- Kinase (26.23%)
In recent papers he was focusing on the following fields of study:
His primary scientific interests are in Cell biology, mTORC1, Kinase, Phosphorylation and Protein biosynthesis.
His Cell biology study combines topics from a wide range of disciplines, such as Translation and EEF2.
Christopher G. Proud has begun a study into mTORC1, looking into PI3K/AKT/mTOR pathway and Biochemistry.
His biological study spans a wide range of topics, including EIF4E, Endocrinology and Adipogenesis.
Christopher G. Proud studies TOR Serine-Threonine Kinases which is a part of Phosphorylation.
His Protein biosynthesis study combines topics in areas such as eIF2B, Endoplasmic reticulum, Stable isotope labeling by amino acids in cell culture and Chinese hamster ovary cell.
Between 2013 and 2021, his most popular works were:
- mTOR inhibitors in cancer therapy. (147 citations)
- mTORC1 signaling controls multiple steps in ribosome biogenesis (118 citations)
- Eukaryotic elongation factor 2 kinase, an unusual enzyme with multiple roles. (97 citations)
In his most recent research, the most cited papers focused on:
Christopher G. Proud focuses on Cell biology, Biochemistry, mTORC1, Phosphorylation and Translation.
His study in Cell biology is interdisciplinary in nature, drawing from both EIF4E and Protein biosynthesis.
His study in Biochemistry concentrates on EEF2 and Peptide Elongation Factor 2.
His mTORC1 research incorporates themes from Cell growth and RPTOR.
Christopher G. Proud focuses mostly in the field of Phosphorylation, narrowing it down to topics relating to Amino acid and, in certain cases, Eukaryotic Initiation Factor-2 and Lysosome.
His Eukaryotic translation research includes themes of Eukaryotic initiation factor and Initiation factor.
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.
