Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Down/up regulation of nad biosynthesis in arabidopsis and role of l-aspartate oxidase-Down/up regulation of NAD biosynthesis in Arabidopsis : role of L-Aspartate oxidase

ABSTRACT: down/up regulation of nad biosynthesis in arabidopsis and role of l-aspartate oxidase-Down/up regulation of NAD biosynthesis in Arabidopsis : role of L-Aspartate oxidase

PROVIDER: PRJNA493580 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Similar Datasets

down/up regulation of nad biosynthesis in arabidopsis and role of l-aspartate oxidase-Down/up regulation of NAD biosynthesis in Arabidopsis : role of L-Aspartate oxidase

Project description:rs13_01_lao - down/up regulation of nad biosynthesis in arabidopsis and role of l-aspartate oxidase - Study of the biosynthesis of NAD in Arabidopsis. Involvment of L-Aspartate oxidase gene using T-DNA mutant (SAIL1145_B10) and overexpressor lines (promotor 35S, vector PCW162) at the same developmental stage (12 leaves) - Study of the biosynthesis of NAD in Arabidopsis. Involvment of L-Aspartate oxidase gene using T-DNA mutant (SAIL1145_B10) and overexpressor lines (promotor 35S, vector PCW162) at the same developmental stage (12 leaves)

2018-10-01 | GSE120564 | GEO

Down regulation of qptgene in arabidopsis-Regulation of NAD biosynthesis in Arabidopsis : role of quinolinate phosphoribosyltransferase.

Project description:rs11-08_nad2 - down regulation of qptgene in arabidopsis - Study of the biosynthesis of NAD in Arabidopsis. Involvment of QPTgene using the knock out Salk mutant N575260. - Study of the biosynthesis of NAD in Arabidopsis. Involvment of QPTgene using the knock out Salk mutant N575260. 2 dye-swap - normal vs transgenic comparison

2013-08-01 | E-GEOD-49034 | biostudies-arrayexpress

quinolinate-Deregulation of NAD biosynthesis

Project description:rs09-02_quinolinate - quinolinate - Study of the impact of an inductible increase in the NAD concentration in arabidopsis - Comparison between the mutant or the control after a quinolinate treatment Keywords: treated vs untreated comparison,wt vs mutant comparison 6 dye-swap - CATMA arrays

2010-07-01 | E-GEOD-19084 | biostudies-arrayexpress

Effects of nitrate-induced promotion of de novo NAD synthesis in Arabidopsis thaliana

Project description:In higher plants, NAD synthesis starts with the oxidation of aspartate. This oxidation is catalyzed by aspartate oxidase (AO) encoded by a nitrate-inducible gene. To assess the effects of this upregulation of AO gene in response to a nitrate supply, a transgenic line was generated by introduction of AO gene under the control of a mutated AO promoter into the ao knockout mutant. Since, unlike the wild-type AO promoter, this mutated AO promoter was not activated by a nitrate supply, gene expression in this transgenic line was compared with that in another transgenic line that was generated by introduction of AO gene under the regulation of the wild-type AO promoter into the ao knockout mutant. Changes in gene expression in response to a nitrate supply were analyzed in these transgenic lines.

2022-05-18 | GSE136542 | GEO

NAD Salvage Supports Serine Biosynthesis

Project description:Maintenance of NAD+ levels by mitochondrial complex I, the NAD+ salvage pathway, and other routes is an important factor in of neurodegenerative disease and cancer. Both the production of NAD+ and the metabolic enzymes that require it as a redox cofactor or substrate differ widely in abundance across cell types and conditions. Disruption in the NAD+ supply thus exerts different effects depending on the cellular NAD+ requirements existing in the cell. Pharmacological depletion of NAD+ is actively being pursued in cancer and other diseases but these effects are not fully understood. Here, we combine quantitative proteomics and metabolomics to understand the consequences of disrupting cellular NAD+ levels and find that inhibiting the NAD+ salvage pathway depletes serine biosynthesis from glucose by impeding the NAD+-dependent protein 3-phosphoglycerate dehydrogenase (PHGDH). Importantly, breast cancers that depend on PHGDH are exquisitely sensitive to blocking the NAD+ salvage pathway. PHGDH, and the rate-limiting enzyme of NAD+ salvage are also correlated in public tumor proteome and transcript datasets. These findings are immediately translatable to the pharmacological inhibition of NAMPT in PHGDH-dependent cancers.

2018-08-14 | PXD007790 | Pride

Down regulation of qptgene in arabidopsis-Regulation of NAD biosynthesis in Arabidopsis : role of quinolinate phosphoribosyltransferase.

2013-08-01 | GSE49034 | GEO

quinolinate-Deregulation of NAD biosynthesis

2010-07-01 | GSE19084 | GEO

Nicotinamide Starvation of Mycobacteria Defective for de novo NAD Biosynthesis

Project description:Mycobacteria can synthesize NAD+ using either the de novo biosynthesis pathway or the salvage pathway. The deletion of the three genes involved specifically in the NAD+ de novo biosynthesis pathway in the human pathogen Mycobacterium tuberculosis had no effect on the growth of the strain in vivo. In contrast, the same deletion in the bovine pathogen Mycobacterium bovis resulted in a strain that could not grow in vivo and could only grow in vitro with substantial nicotinamide supplmentation. This striking difference was attributed to the known defect in the nicotinamidase PncA of M. bovis, since introducing the M. tuberculosis pncA gene into the M. bovis strain defective for de novo NAD+ biosynthesis restored growth in vitro and in vivo. This study demonstrates that NAD+ starvation is a cidal event in mycobacteria and confirms that enzymes common to the de novo and salvage pathways may be good drug targets. We also propose that simultaneously targeting both the salvage and the de novo NAD+ biosynthesis pathways represents a potentially effective way to treat infection with tubercle bacilli. To characterize the lethality induced by nicotinamide starvation transcriptional profiling of the auxotrophs was performed. Triplicate 50 mL cultures of M. tuberculosis and M. bovis Delta nadABC mutants were grown in 7H9 OADC glycerol 0.05% tween broth in 500 mL roller bottles to an OD600nm= 0.1 in a roller incubator at 37Â°C. The cells were washed 1x in PBS and resuspended in 50 mL 7H9 OADC glycerol 0.05% tween broth with or without 20mg/L nicotinamide and returned to the incubator. After 7 days, cultures were harvested. Three biological replicates of each of two species with one dye-flip each

2010-05-14 | E-GEOD-18909 | biostudies-arrayexpress

knock out mutant n575260-NAD biosynthesis in Arabidopsis : role of quinolinate phosphoribosyltransferase

Project description:rs11-01_nad - knock out mutant n575260 - Study of the impact of a deregulation in the NAD concentration in arabidopsis - Study of the biosynthesis of NAD in Arabidopsis. Involvment of QPRTgene using the knock out mutant N575260 from Salk. 2 dye-swap - gene knock out

2012-02-03 | E-GEOD-30976 | biostudies-arrayexpress

IFNg Regulates NAD+ Metabolism in Human Monocytes

Project description:IFNg is an essential and pleiotropic activator of monocytes, but little is known about the changes in cellular metabolism required for IFNg-induced activation. We sought to characterize and elucidate the mechanisms by which IFNg reprograms monocyte metabolism to support its immunologic activities. Monocytes from healthy controls and patients with gain-of-function mutations in STAT1 (STAT1 GOF), or loss-of-function mutations in mitochondrial complex I (Leigh syndrome) and NADPH oxidase (chronic granulomatous disease, CGD) were metabolically phenotyped. We found that IFNg increased oxygen consumption rates (OCR), indicative of reactive oxygen species generation by both mitochondria and NADPH oxidase. Transcriptional profiling of human monocyte derived macrophages revealed that this oxidative phenotype was driven by an IFNg-induced reprogramming of NAD+ metabolism, which is dependent on nicotinamide phosphoribosyltransferase (NAMPT)-mediated NAD+ salvage to generate NADH and NADPH for oxidation by mitochondrial complex I and NADPH oxidase, respectively. Monocytes from patients with STAT1 GOF demonstrated higher than normal OCR, while monocytes from Leigh syndrome and CGD patients demonstrated reduced OCR. Chemical inhibition of NAMPT completely abrogated the IFNg-induced oxygen consumption, comparable to levels observed in CGD patients. These data identify an IFNg-induced, NAMPT-dependent, NAD+ salvage pathway that is critical for IFNg activation of human monocytes.

2021-12-31 | GSE176562 | GEO

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data