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The Plant Cell|August 2, 2005
The critical role of Arabidopsis electron-transfer flavoprotein:ubiquinone oxidoreductase during dark-induced starvationKimitsune Ishizaki, Tony R Larson, Nicolas Schauer, et al.
The Plant Journal : for Cell and Molecular Biology|August 23, 2006
The mitochondrial electron transfer flavoprotein complex is essential for survival of Arabidopsis in extended darknessKimitsune Ishizaki, Nicolas Schauer, Tony R Larson, et al.
The Plant Cell|September 4, 2003
Enzymes of glycolysis are functionally associated with the mitochondrion in Arabidopsis cellsPhilippe Giegé, Joshua L Heazlewood, Ute Roessner-Tunali, et al.
The Plant Cell|June 24, 2005
A Rab-E GTPase mutant acts downstream of the Rab-D subclass in biosynthetic membrane traffic to the plasma membrane in tobacco leaf epidermisHuanquan Zheng, Luísa Camacho, Edmund Wee, et al.
Biochemical and Biophysical Research Communications|June 21, 2011
Sphingolipid long chain base phosphates can regulate apoptotic-like programmed cell death in plantsKeith P Alden, Sandrine Dhondt-Cordelier, Kerrie L McDonald, et al.
The Plant Journal : for Cell and Molecular Biology|April 30, 2005
Comparative transcriptome analysis reveals significant differences in gene expression and signalling pathways between developmental and dark/starvation-induced senescence in ArabidopsisVicky Buchanan-Wollaston, Tania Page, Elizabeth Harrison, et al.
The Plant Cell|May 27, 2010
Identification of the 2-hydroxyglutarate and isovaleryl-CoA dehydrogenases as alternative electron donors linking lysine catabolism to the electron transport chain of Arabidopsis mitochondriaWagner L Araújo, Kimitsune Ishizaki, Adriano Nunes-Nesi, et al.
Plant Physiology|July 27, 2011
Analysis of a range of catabolic mutants provides evidence that phytanoyl-coenzyme A does not act as a substrate of the electron-transfer flavoprotein/electron-transfer flavoprotein:ubiquinone oxidoreductase complex in Arabidopsis during dark-induced senescenceWagner L Araújo, Kimitsune Ishizaki, Adriano Nunes-Nesi, et al.
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