Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Analysis of cellular responsive nuclear/cytoplasmic mRNA distribution to viral virulence factor and dihydroorotate dehydrogenase (DHODH) inhibition

ABSTRACT: This SuperSeries is composed of the SubSeries listed below.

ORGANISM(S): Homo sapiens

PROVIDER: GSE35117 | GEO | 2012/01/17

SECONDARY ACCESSION(S): PRJNA150733

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Similar Datasets

Analysis of cellular responsive nuclear/cytoplasmic mRNA distribution to viral virulence factor and dihydroorotate dehydrogenase (DHODH) inhibition

Project description:This SuperSeries is composed of the following subset Series: GSE35112: Genome-wide analysis of gene expression and nuclear/cytoplasmic distribution by compound 1 treatment [293T-M] GSE35113: Genome-wide analysis of gene expression and nuclear/cytoplasmic distribution by compound 1 treatment [293T_NS1-1] GSE35114: Genome-wide analysis of gene expression and nuclear/cytoplasmic distribution by compound 1 treatment [293T_NS1-2] GSE35115: Genome-wide analysis of gene expression by compound 1 treatment [HBEC_3h] GSE35116: Genome-wide analysis of gene expression by compound 1 treatment [HBEC_6_12hr] Refer to individual Series

2012-01-17 | E-GEOD-35117 | biostudies-arrayexpress

Functional expression of human dihydroorotate dehydrogenase (DHODH) in pyr4 mutants of ustilago maydis allows target validation of DHODH inhibitors in vivo.

Project description: Not available

| S-EPMC1907109 | biostudies-literature

Original 2-(3-Alkoxy-1H-pyrazol-1-yl)azines Inhibitors of Human Dihydroorotate Dehydrogenase (DHODH).

Project description: Not available

| S-EPMC4516315 | biostudies-literature

Exploitation of dihydroorotate dehydrogenase (DHODH) and p53 activation as therapeutic targets: A case study in polypharmacology.

Project description: Not available

| S-EPMC7939445 | biostudies-literature

Efficacy and safety of dihydroorotate dehydrogenase (DHODH) inhibitors "leflunomide" and "teriflunomide" in Covid-19: A narrative review.

Project description: Not available

| S-EPMC8180448 | biostudies-literature

Proteomic analysis of U2OS cells treated with the dihydroorotate dehydrogenase (DHODH) inhibitor Brequinar

Project description:The mitochondrial respiratory chain assembles into higher order complexes termed supercomplexes (SCs) under certain physiological or metabolic stimuli. A small molecule screen developed by the lab identified DHODH inhibitors as potent activators of SC assembly in cancer cells. To investigate the proteomic regulation of SCs under nucleotide deficiency, we treated U2OS cells for 48 hours with Brequinar (500 nM). Proteomic analysis highlighted strong signatures of respiratory chain subunit abundance and peroxisomal-derived ether phospholipid synthesis enzymes. Bypassing DHODH inhibition through uridine supplementation prevented these alterations. These findings establish a coordinated cellular response to reduced nucleotide pools that stimulates ether phospholipid synthesis and respiratory chain supra-assembly.

2022-02-16 | PXD023882 | Pride

Changes in nuclear and cytoplasmic microRNA distribution following hypoxic stress

Project description:Purpose: MicroRNAs have well characterized roles in cytoplasmic gene regulation by binding mRNA and inhibiting translation. However, besides this post-transcriptional gene silencing, miRNAs have also been implicated in transcriptional gene regulation and alternative splicing, events that are restricted to the cell nucleus. The nuclear functions of miRNAs are currently not understood, and there is a paucity of systematic studies of miRNA nuclear-cytoplasmic distribution and fewer still which have investigated this in the context of physiological conditions. Methods: Here we performed nuclear-cytoplasmic fractionation in a mouse endothelial cell line in hypoxia and characterized the localization of miRNAs using small RNA sequencing. Results: We show here that there is a broad population of mature miRNAs in the cell nucleus and that it is also altered upon exposure to hypoxia. Conclusions: Our results strongly imply that miRNAs have extensive regulatory functions in the nucleus and expand potential therapeutic use of small RNA molecules.

2019-07-17 | GSE125390 | GEO

Nuclear LSm8 affects number of cytoplasmic processing bodies via controlling cellular distribution of Like-Sm proteins.

Project description: Not available

| S-EPMC3459855 | biostudies-other

Ubiquitination on Lysine 247 of Newcastle Disease Virus Matrix Protein Enhances Viral Replication and Virulence by Driving Nuclear-Cytoplasmic Trafficking.

Project description: Not available

| S-EPMC8791254 | biostudies-literature

Dihydroorotate dehydrogenase inhibition reveals metabolic vulnerability in chronic myeloid leukemia

Project description:The development of different generations of BCR-ABL1 tyrosine kinases inhibitors (TKIs) has led the overall survival (OS) of the chronic myeloid leukemia (CML) patients to become almost similar to that of a control population without leukemia, but the TKI therapy can be successfully discontinued only in half of those who are achieving a deep molecular response, that eans in approximately 15-20% of the entire population. In addition, although few, there are CML patients who show resistance to TKI therapy, are prone to progress to more advanced phases of the disease and die of CML related causes. Therefore, implementing an alternative approach for targeting TKI resistant leukemic cells would be of the essence in trying to solve these problems. Dihydroorotate dehydrogenase (DHODH) is a druggable enzyme in the de novo pyrimidine biosynthesis pathway that is located in the inner membrane of mitochondria. Here, we found that CML CD34+ cells and CML cell lines are vulnerable to DHODH inhibition mediated by Meds433, a new and potent DHODH inhibitor recently developed by our group. Meds433 significantly activated the apoptotic pathway and suppressed cell growth of CML cells in vitro and in vivo in a xenograft mice model. Moreover, inhibition of DHODH led to the reduction of amino acids and induction of huge metabolic stress in CML CD34+. Altogether, our study shows that targeting pyrimidine synthesis is a promising approach for targeting CML stem/progenitor cells, helping more patients to achieve good molecular response and possibly successful treatment discontinuation.

2022-07-06 | GSE177485 | GEO

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

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