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Maria Giulia Egidi

Publications -  6
Citations -  716

Maria Giulia Egidi is an academic researcher. The author has contributed to research in topics: Energy source & Proteomics. The author has an hindex of 6, co-authored 6 publications receiving 632 citations.

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Proteomics applied on plant abiotic stresses: Role of heat shock proteins (HSP)☆

TL;DR: A relationship between ROS and HSP also seems to exist, corroborating the hypothesis that during the course of evolution, plants were able to achieve a high degree of control over ROS toxicity and are now using ROS as signalling molecules to induce HSPs.
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Proteomic analysis of a spring wheat cultivar in response to prolonged cold stress

TL;DR: Physiological and biochemical parameters sustained proteomics findings allowing the present research to contribute to the current knowledge on these long‐term responses, which may be crucial to stress adaptation under field conditions.
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The influence of temperature on plant development in a vernalization-requiring winter wheat: A 2-DE based proteomic investigation.

TL;DR: Proteomics was used to study the influence of both optimal and low temperatures on growth and development in a vernalization-requiring winter wheat after prolonged times of treatment and observed a marked increase of wrab17, wcor18 and glycine-rich RNA-binding proteins.
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Proteomics and transcriptomics investigation on longissimus muscles in Large White and Casertana pig breeds

TL;DR: Casertana and Large White pig breeds are characterized by a different tendency toward fat accumulation as they exhibit opposite genetic and physiological traits with respect to the energy metabolism, and physiological differences were investigated in longissimus lumborum muscles through proteomics and microarray approaches.
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Troubleshooting in platelet storage temperature and new perspectives through proteomics.

TL;DR: The initial events which trigger morphological and physiological changes upon cold activation, partially distinguishable from physiological activation are discussed, which compromise viability of cold stored platelets, as they exert their physiological role through their ability to change shape and activate under various conditions.