References of "Rojas-Beltran, J"
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See detailChanges In Oxylipin Synthesis After Phytophthora Infestans Infection Of Potato Leaves Do Not Correlate With Resistance
Fauconnier, Marie-Laure ULg; Rojas-Beltran, J.; Dupuis, B. et al

in Plant Physiology and Biochemistry (2008), 46(8-9), 823-831

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See detailOxylipin Profile And Antioxidant Status Of Potato Tubers During Extended Storage At Room Temperature
Delaplace, Pierre ULg; Rojas-Beltran, J.; Frettinger, P. et al

in Plant Physiology and Biochemistry (2008), 46(12), 1077-1084

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See detailOptimisation de la transformation génétique de la pomme de terre par Agrobacterium tumefaciens. Utilisation de la résistance à l'hygromycine comme marqueur sélectif.
M'Hamdi, M.; Rouvière, C.; Rojas-Beltran J et al

in Biotechnologie, Agronomie, Société et Environnement = Biotechnology, Agronomy, Society and Environment [=BASE] (2003), 7

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See detailInduction of potato (Solanum tuberosum L.) tuber sprouting by hydrogen peroxide.
Bajji, M.; M'Hamdi, M.; Gastiny, F. et al

in Free Radical Research (2003), 37

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See detailSymposium « Les lipides de Plantes »
Fauconnier, Marie-Laure ULg; Rojas-Beltran, J.; Hoyaux, P. et al

Poster (2001, July 10)

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See detailStudy of lipoxygenase activity during storage of potato tubers (Solanum tuberosum L.) in relation with membrane integrity.
Fauconnier, Marie-Laure ULg; Rojas-Beltran, J.; Hoyaux, P. et al

Poster (2001, June 06)

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See detail- Evolution of lipoxygenase activity during storage of potato tubers (Solanum tuberosum L. cv. Bintje)
Fauconnier, Marie-Laure ULg; Koto, N.; Hoyaux, P. et al

in Bulletin de la Société des Sciences de Liège (1999), 68(5-6), 319

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See detailMolecular cloning and characterization of a soluble inorganic pyrophosphatase in potato.
du Jardin, Patrick ULg; Rojas-Beltran, J.; Gebhardt, C. et al

in Plant Physiology (1995), 109(3), 853-60

A cDNA clone encoding a soluble inorganic pyrophosphatase (EC 3.6.1.1) of potato (Solanum tuberosum L.) was isolated by screening a developing tuber library with a heterologous probe. The central domain ... [more ▼]

A cDNA clone encoding a soluble inorganic pyrophosphatase (EC 3.6.1.1) of potato (Solanum tuberosum L.) was isolated by screening a developing tuber library with a heterologous probe. The central domain of the encoded polypeptide is nearly identical at the sequence level with its Arabidopsis homolog (J.J. Kieber and E.R. Signer [1991] Plant Mol Biol 16: 345-348). Computer-assisted analysis of the potato, Arabidopsis, and Escherichia coli soluble pyrophosphatases indicated a remarkably conserved organization of the hydrophobic protein domains. The enzymatic function of the potato protein could be deduced from the presence of amino acid residues highly conserved in soluble pyrophosphatases and was confirmed by its capacity to complement a thermosensitive pyrophosphatase mutation in E. coli. The potato polypeptide was purified from complemented bacterial cells and its pyrophosphatase activity was shown to be strictly dependent on Mg2+ and strongly inhibited by Ca2+. The subcellular location of the potato pyrophosphatase is unknown. Structure analysis of the N-terminal protein domain failed to recognize typical transit peptides and the calculated molecular mass of the polypeptide (24 kD) is significantly inferior to the values reported for the plastidic (alkaline) or mitochondrial pyrophosphatases in plants (28-42 kD). Two unlinked loci could be mapped by restriction fragment length polymorphism analysis in the potato genome using the full-length cDNA as probe. [less ▲]

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