Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

MRNA changes induced by Unfolded protein response

ABSTRACT: mRNA changes induced by Unfolded protein response

PROVIDER: PRJNA532892 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR8899060.fastq.gz	Fastqsanger.gz
	SRR8899061.fastq.gz	Fastqsanger.gz
	SRR8899062.fastq.gz	Fastqsanger.gz
	SRR8899063.fastq.gz	Fastqsanger.gz
	SRR8899064.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 9

Similar Datasets

miRNA changes induced by Unfolded protein response

Project description:miRNA changes induced by Unfolded protein response

| PRJNA482755 | ENA

mRNA changes induced by Unfolded protein response

Project description:We report the results NGS based of mRNA profiling in human bronchial epithelial cells (16HBE14o-) up on ER stress induction with Tunicamycin (2.5ug/ml) and ALLN (100uM)

2019-12-31 | GSE129813 | GEO

mRNA-seq of worms and the mitochondrial unfolded protein response (UPRmt)

Project description:mRNA-seq of worms and the mitochondrial unfolded protein response (UPRmt)

| PRJNA591855 | ENA

The Toxoplasma unfolded protein response

2013-05-24 | GSE43722 | GEO

mRNA-seq of worms and the mitochondrial unfolded protein response (UPRmt)

Project description:To cope with a challenging and unpredictable environment, living systems have evolved several organelle-specific stress responses, e.g. the cytosolic heat shock response (HSR), the endoplasmic reticulum unfolded protein response (UPRER) and the mitochondrial unfolded protein response (UPRmt). UPRmt monitors mitochondrial function and homeostasis in general. However, the mechanism of UPRmt remains largely unexplored. Here we identified that histone deacetylase HDA-1 is associated with homeobox domain-containing protein DVE-1 in UPRmt activation in Caenorhabditis elegans. Knocking down ATP synthase subunit atp-2 generates mitochondrial stress and induces UPRmt. After analyzing the mRNA profiles of worms on L4440 RNAi, hda-1 RNAi or dve-1 RNAi and untreated or treated with atp-2 RNAi, we found that 283 hda-1_dependent genes and 218 dve-1_dependent genes were upregulated in response to atp-2 RNAi.

2020-07-19 | GSE141041 | GEO

The Toxoplasma unfolded protein response

Project description:To characterize the nature of the unfolded protein response in this Toxoplasma, we carried out microarray analyses to measure the changes in the transcriptome and in translational control during ER stress. Total RNA or RNA fractionated into monosomes or polysomes were purified from parasites treated with DMSO or tunicamycin for 1 hour. RNA was processed for microarray analysis using a ToxoGeneChip.

2013-05-24 | E-GEOD-43722 | biostudies-arrayexpress

Ribosomal mistranslation leads to silencing of the unfolded protein response and increased mitochondrial biogenesis

Project description:Translation fidelity is the limiting factor in the accuracy of gene expression. With an estimated frequency of 10-4, errors in mRNA decoding occur in a mostly stochastic manner. Little is known about the response of higher eukaryotes to chronic loss of ribosomal accuracy as per an increase in the random error rate of mRNA decoding. Here, we present a global and comprehensive picture of the cellular changes in response to translational accuracy in mammalian ribosomes impaired by genetic manipulation. In addition to affecting established protein quality control pathways, such as elevated transcript levels for cytosolic chaperones, activation of the ubiquitin-proteasome system, and translational slowdown, ribosomal mistranslation led to unexpected responses. In particular, we observed increased mitochondrial biogenesis associated with import of misfolded proteins into the mitochondria and silencing of the unfolded protein response in the endoplasmic reticulum. This study describes the metabolomic analysis of HEK293 cells lines expressing mutant ribosomal protein RPS2 (human A226Y). RPS2 A226Y mutation has been shown to cause misreading and readthrough. Results provide insight into the response to chronic mistranslation in mammalian cells.

2019-09-17 | MTBLS106 | MetaboLights

Hepatic unfolded protein response in liver transplant patients

Project description:Hepatic unfolded protein response in liver transplant patients

| PRJNA840895 | ENA

Translational profiling in the unfolded protein response

Project description:The unfolded protein response (UPR) couples cellular translation rates and gene expression to the protein folding status of the endoplasmic reticulum (ER). Upon activation, the UPR machinery elicits a general suppression of protein synthesis and activation of stress gene expression, which act coordinately to restore protein folding homeostasis. We report here that UPR activation promotes the release of signal sequence-encoding mRNAs from the ER to the cytosol as a mechanism to decrease protein influx into the ER. This release of mRNA begins rapidly, then gradually recovers with ongoing stress. Upon release into the cytosol, these mRNAs have divergent fates: some synthesize full-length proteins, while others are translationally inactive and retain nascent protein chains. Together, these findings identify the dynamic subcellular localization of mRNAs and translation as a regulatory feature of the cellular response to protein folding stress. Cells were treated with a timecourse of Thapsigargin or DTT, then fractionated and analyzed by mRNA-seq or ribosome profiling

2014-08-28 | E-GEOD-53743 | biostudies-arrayexpress

Unfolded Protein Response

Project description:To dissect the requirements of membrane protein degradation from the ER, we expressed the mouse major histocompatibility complex class I heavy chain H-2K(b) in yeast. Like other proteins degraded from the ER, unassembled H-2K(b) heavy chains are not transported to the Golgi but are degraded in a proteasome-dependent manner. The overexpression of H-2K(b) heavy chains induces the unfolded protein response (UPR). In yeast mutants unable to mount the UPR, H-2K(b) heavy chains are greatly stabilized. This defect in degradation is suppressed by the expression of the active form of Hac1p, the transcription factor that upregulates UPR-induced genes. These results indicate that induction of the UPR is required for the degradation of protein substrates from the ER. Set of arrays organized by shared biological context, such as organism, tumors types, processes, etc. Computed

2005-08-16 | E-GEOD-3130 | biostudies-arrayexpress

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