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ORGANISM(S): Homo sapiens 
Malate dehydrogenases (MDHs) catalyze a reversible NAD(P)-dependent-oxidoreductase reaction that plays an important role in central metabolism and redox homeostasis of plant cells. Recent studies suggest a moonlighting function of plastidial NAD-dependent MDH (plNAD-MDH) in plastid biogenesis, indep...
ORGANISM(S): Escherichia Coli 
This experiment was performed to challenge E. coli response to acetate when switched from N-Acetyl Glucosamine (NAG) to malate as the main substrate. Here, E. coli BW25113 strain was grown in M9 medium complemented with 15 mM NAG, The cells were grown to mid-exponential phase in shake flasks at 37...
ORGANISM(S): Escherichia coli K-12 
Exogenous supply of citrate and malate to Arabidopsis leaves to monitor transcriptional changes resulting from these treatments.
ORGANISM(S): Arabidopsis thaliana 
In plant cells, the ALMTs are key plasma and vacuolar membranes anion channels regulating plant responses to the environment. Vacuolar ALMTs control stomata aperture and anion accumulation in guard cells. The activation of vacuolar ALMTs is voltage and malate dependent, but the underlying mechanisms...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2025-03-04 | PXD059651 | Pride
Arabidopsis thaliana mutants in mitochondria malate metabolism
The purple sulfur bacterium Allochromatium vinosum DSM 180T is one of the best studied sulfur-oxidizing anoxygenic phototrophic bacteria and has been developed into a model organism for laboratory-based studies of oxidative sulfur metabolism. Here, we took advantage of the organismM-bM-^@M-^Ys high ...
ORGANISM(S): Allochromatium vinosum DSM 180 
The purple sulfur bacterium Allochromatium vinosum DSM 180T is one of the best studied sulfur-oxidizing anoxygenic phototrophic bacteria and has been developed into a model organism for laboratory-based studies of oxidative sulfur metabolism. Here, we took advantage of the organismM-bM-^@M-^Ys high ...
ORGANISM(S): Allochromatium vinosum DSM 180 
L.hongkongensis transcriptomes grown in media supplemented with or without malate
Investigating the RNAs bound by Malate Dehydrgenase 2
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