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Francine Casse

Researcher at Centre national de la recherche scientifique

Publications -  22
Citations -  1492

Francine Casse is an academic researcher from Centre national de la recherche scientifique. The author has contributed to research in topics: Mutant & Escherichia coli. The author has an hindex of 15, co-authored 22 publications receiving 1416 citations. Previous affiliations of Francine Casse include Institut national de la recherche agronomique.

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Functional analysis of AtHKT1 in Arabidopsis shows that Na+ recirculation by the phloem is crucial for salt tolerance

TL;DR: The whole set of data indicates that AtHKT1 is involved in Na+ recirculation from shoots to roots, probably by mediating Na+ loading into the phloem sap in shoots and unloading in roots, this recirculating removing large amounts of Na+ from the shoot and playing a crucial role in plant tolerance to salt.
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Molecular and Physiological Responses to Water Deficit in Drought-Tolerant and Drought-Sensitive Lines of Sunflower: Accumulation of Dehydrin Transcripts Correlates with Tolerance

TL;DR: HaDhn1 transcripts were similarly accumulated in the tolerant and in the sensitive plants in response to ABA, suggesting that additional factors involved in drought regulation of HaDhn 1 expression might exist in tolerant plants.
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Characterization of AtCHX17, a member of the cation/H+ exchangers, CHX family, from Arabidopsis thaliana suggests a role in K+ homeostasis

TL;DR: Using the beta-glucuronidase reporter gene strategy and in situ RT-PCR experiments, it is found that AtCHX17 was expressed preferentially in epidermal and cortical cells of the mature root zones, supporting the hypothesis that At CHX17 is involved in K(+) acquisition and homeostasis.
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A mutation leading to the total lack of nitrite reductase activity in Escherichia coli K 12

TL;DR: Mutants of E. coli, completely devoid of nitrite reductase activity with glucose or formate as donor were studied and biochemical analysis indicates that they are simultaneously affected in nitrate reductasing activities as well as in cytochrome c552 biosynthesis.