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Christine H. Foyer

Researcher at University of Birmingham

Publications -  517
Citations -  68406

Christine H. Foyer is an academic researcher from University of Birmingham. The author has contributed to research in topics: Photosynthesis & Glutathione. The author has an hindex of 116, co-authored 490 publications receiving 61381 citations. Previous affiliations of Christine H. Foyer include Rothamsted Research & Newcastle University.

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Field Phenotyping of Soybean Roots for Drought Stress Tolerance

TL;DR: It is demonstrated that root system phenotyping using markers that are easy-to-apply under field conditions can be used to determine genotypic differences in drought tolerance in soybean.
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Effect of Chilling on Carbon Assimilation, Enzyme Activation, and Photosynthetic Electron Transport in the Absence of Photoinhibition in Maize Leaves

TL;DR: It is concluded that chilling produces a decrease in photosynthetic capacity without changing the internal operational, regulatory or stoichiometric relationships between photoynthetic electron transport and carbon assimilation.
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The transcription factor ABI4 is required for the ascorbic acid-dependent regulation of growth and regulation of jasmonate-dependent defense signaling pathways in Arabidopsis.

TL;DR: It is demonstrated that low ascorbate triggers ABA- and jasmonate-dependent signaling pathways in leaves that together regulate growth through ABI4, and cellular redox homeostasis exerts a strong influence on sugar-dependent growth regulation.
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Persulfidation-based Modification of Cysteine Desulfhydrase and the NADPH Oxidase RBOHD Controls Guard Cell Abscisic Acid Signaling.

TL;DR: It is shown that ABA stimulates the persulfidation of l-CYSTEINE DESULFHYDRASE1, an important endogenous H2S enzyme, at Cys44 and Cys205 in a redox-dependent manner, and s-persulfidation-induced RBOHD activity is relevant to ABA-induced stomatal closure.
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Subcellular Localisation and Identification of Superoxide Dismutase in the Leaves of Higher Plants

TL;DR: Investigation of the subcellular location of superoxide dismutase in the leaves of spinach and other C3 plants found most activity appeared to be located within chloroplasts, but there is more than can be accounted for by contamination withchloroplasts.