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David P. Dixon

Researcher at Durham University

Publications -  57
Citations -  7088

David P. Dixon is an academic researcher from Durham University. The author has contributed to research in topics: Glutathione & Arabidopsis. The author has an hindex of 38, co-authored 57 publications receiving 6448 citations. Previous affiliations of David P. Dixon include GlaxoSmithKline & University of Fribourg.

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Plant glutathione S-transferases: enzymes with multiple functions in sickness and in health.

TL;DR: The role of GSTs in metabolism is unclear, although their complex regulation by environmental stimuli implies that they have important protective functions and might also have non-catalytic roles as carriers for phytochemicals.
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Plant glutathione transferases

TL;DR: The soluble glutathione transferases (GSTs) represent an excellent example of how protein families can diversify to fulfill multiple functions while conserving form and structure.
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Probing the diversity of the Arabidopsis glutathione S-transferase gene family.

TL;DR: Ten cDNAs representing all GST classes were cloned by RT-PCR and used to study AtGST expression in response to treatment with phytohormones, herbicides, oxidative stress and inoculation with virulent and avirulent strains of the downy mildew pathogen Peronospora parasitica, giving further insights into the complex regulation and enzymic functions of this plant gene super-family.
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Roles for glutathione transferases in plant secondary metabolism

TL;DR: How enzyme biochemistry and informatics are providing clues as to GST function is described, allowing for the critical evaluation of each of these hypotheses.
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Functional divergence in the glutathione transferase superfamily in plants. Identification of two classes with putative functions in redox homeostasis in Arabidopsis thaliana.

TL;DR: In this paper, the human Omega glutathione transferase (GST) superfamily was identified in Arabidopsis thaliana which differed from all other plant GSTs by containing a cysteine in place of a serine at the active site.