Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Analysis of the effect of G-alpha or GPCR mutation on the Arabidopsis Transcriptome

ABSTRACT: Analysis of the effect of G-alpha or GPCR mutation on the Arabidopsis Transcriptome Keywords: Comparitive Genome Hybridization

ORGANISM(S): Arabidopsis thaliana

PROVIDER: GSE11435 | GEO | 2010/10/01

SECONDARY ACCESSION(S): PRJNA106463

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

Analysis of the effect of G-alpha or GPCR mutation on the Arabidopsis Transcriptome

Project description:Analysis of the effect of G-alpha or GPCR mutation on the Arabidopsis Transcriptome Keywords: Comparitive Genome Hybridization The transcriptomes of wild type and mutants (G-alpha and GPCR) were compared in the current study. The study was carried out on four whole genome oligo arrays. The G-alpha mutant and its corresponding wild type variety were compared on a single array by means of a dual channel experiment (Cy3 and Cy5 labeling). The experiment was repeated on a different array as a flip-dye replicate and the data from both the sets analyzed further.

2010-09-30 | E-GEOD-11435 | biostudies-arrayexpress

Arabidopsis thaliana

Project description:Analysis of the effect of G-alpha or GPCR mutation on the Arabidopsis Transcriptome

| PRJNA106463 | ENA

GPCR expression in mouse dorsal root ganglia (DRG)

Project description:RNA of dorsal root ganglia from untreated adult mice (6-8 weeks) was tested for GPCR expression

2015-12-01 | GSE75476 | GEO

Subcellular location defines GPCR signal transduction

Project description:Subcellular location defines GPCR signal transduction

| PRJNA915973 | ENA

Arabidopsis arenosa x Arabidopsis thaliana

Project description:Interspecies hybridization between Arabidopsis thaliana and Arabidopsis arenosa

| PRJNA112519 | ENA

GPCR endocytosis confers uniformity in responses to chemically distinct ligands

Project description:This study shows that chemically and pharmacodynamically distinct agonists acting on the same GPCR can produce indistinguishable cellular responses and that this uniformity is conferred by endosomal signaling The ability of chemically distinct ligands to produce different effects on the same G protein-coupled receptor (GPCR) has interesting therapeutic implications but, if excessively propagated downstream, would introduce biological 'noise' compromising cognate ligand detection We asked if cells have the ability to limit the degree to which chemical diversity imposed at the ligand-GPCR interface is propagated to the downstream signal We carried out an unbiased analysis of the integrated cellular response elicited by two chemically and pharmacodynamically diverse β-adrenoceptor agonists, isoproterenol and salmeterol We show that both ligands generate an identical integrated response, and that this stereotyped output requires endocytosis We further demonstrate that the endosomal β2-AR signal confers uniformity on the downstream response because it is highly sensitive and saturable Based on these findings, we propose that GPCR signaling from endosomes functions as a biological noise filter to enhance reliability of cognate ligand detection

2016-11-30 | GSE87461 | GEO

Development of gene expression signatures of GPCR family.

Project description:In human HCC tumors, matching paracancerous specimens, and normal liver specimens, a targeted gene expression microanalysis was used to screen alterations in GPCR family gene expression.

2017-03-07 | GSE95698 | GEO

Genotyping of C.elegans mutants - CRISPR/Cas9 of all GPCR and neuropeptide genes

Project description:CRISPR/Cas9 genome editing was used to disrupt nearly all the GPCR and neuropeptide genes from C. elegans genome. Multiple genes were disrupted in each strain for the purpose of screening. The genotype is the list of targeted genes

2023-06-02 | E-MTAB-12983 | biostudies-arrayexpress

In vivo Brain GPCR Signaling Elucidated by Phosphoproteomics

Project description:Obtaining a systems view of G protein-coupled receptor (GPCR) signaling in its native environment is the key in development of GPCR therapeutics with fewer side effects. Using the kappa opioid receptor (KOR) as model GPCR, we employed high-throughput phosphoproteomics to investigate downstream signaling induced by structurally diverse agonists in five mouse brain-regions. Through quantification of 50,000 different phosphosites, this approach yielded a systems view of KOR in vivo signaling, revealing novel mechanisms of drug action. Pathway-selective agonists elicited differential dynamic phosphorylation of synaptic proteins, linking GPCR signaling to modulation of brain functions. We also discovered enrichment of mTOR pathway in agonists associated with aversion, a side effect. Consequently, mTOR inhibition during KOR activation abolished aversion, while preserving therapeutic analgesic and anticonvulsant effects. Our results establish high-throughput phosphoproteomics as a general strategy to investigate GPCR in vivo signaling, enabling prediction and modulation of behavioral outcomes.

2018-06-15 | PXD006637 | Pride

Exploring GPCR-arrestin interfaces with genetically encoded crosslinkers

Project description:-arrestins (arr1 and arr2) are ubiquitous regulators of G protein-coupled receptor (GPCR) signalling. Available data suggest that -arrestins dock to different receptors in different ways. However, the structural characterization of arrestin-GPCR complexes is challenging and alternative approaches to study arrestin-GPCR complexes are needed. Here, starting from the finger loop as a major site for the interaction of arrestins with GPCRs, we genetically incorporate non-canonical amino acids for photo- and chemical crosslinking into arr1 and arr2 and explore binding topologies to GPCRs forming either stable or transient complexes with arrestin: the vasopressin receptor 2 (rhodopsin-like), the corticotropin releasing factor receptor 1 and the parathyroid hormone receptor 1 (both secretin-like). We show that each receptor leaves a unique footprint on arrestin, whereas the two -arrestins yield quite similar crosslinking patterns. Furthermore, we show that the method allows defining the orientation of arrestin respect to the GPCR. Finally, we provide direct evidence for the formation of arrestin oligomers in the cell.

2020-09-21 | PXD020418 | Pride

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