Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

CEBPbeta interacting partners identification.

ABSTRACT: 293T cells were transfected with pCMV CEBPbeta LAP2 isoform. Two days post transfection, nuclear extracts were subjected to Co immunoprecipitation with mouse anti-CEBPbeta (clone H-7) or mouse control IgG using Protein G Dynabeads. After washing with RIPA buffer, beads were subjected to Mass spectrometry based protein identification to find interacting partners of CEBPbeta.

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Dr. Prabha Sampath

PROVIDER: PXD006565 | JPOST Repository | Tue May 23 00:00:00 BST 2017

REPOSITORIES: jPOST

ACCESS DATA

Json Xml

Similar Datasets

DIAPH1 interaction partner identification using BioID.

Project description:293T cells were transfected with p TRIPZ BirA tagged DIAPH1. Two days post transfection, cells were treated with puromycin to select transfectants. The entire BirA-DIAPH1 cassette is under the control of Tet inducible promoter. Induction of DIAPH1 was achieved by treating cells with Doxycycline (10ug/ml) for 24hrs followed by 50uM of Biotin treatment, overnight, to induce biotinylation of interacting partners. Cells treated with Biotin alone (no Dox) were used as a control for IP. Cytoplasmic extracts were prepared and subjected to immunoprecipitation using Streptavidin magnetic beads. Beads were washed with RIPA buffer and subjected to Mass spectrometry based protein identification to find interacting partners of DIAPH1.

2017-05-23 | PXD006564 | JPOST Repository

Identification of the proteins that are associated with ALKBH5 by an affinity purification and mass spectrometry (MS) analysis in human 293T cells.

Project description:Our proteomics analysis is for characterization of ALKBH5 protein interactions in 293T cells. We expressed HA-tagged ALKBH5 in 293T cells, prepared nuclear extracts, and subjected them to affinity purification using an anti-HA antibody, followed by mass spectrometry analysis of the purified protein.

2023-07-26 | PXD042183 | Pride

NHLBI TOPMed: Partners HealthCare Biobank

Project description:NHLBI TOPMed: Partners HealthCare Biobank

| PRJNA300701 | ENA

A Critical Role of Nuclear m6A Reader YTHDC1 in Leukemogenesis by Regulating MCM Complex-Mediated DNA Replication

Project description:PLKO.1 lentiviral vectors contained scramble shRNA, YTHDC1 shRNA 1# and YTHDC1 shRNA 2# were transfected into 293T cells together with package plasmids pMDG.2 and Δ8.91. The supernatant medium contained virus was collected and subjected to infect MOLM-13 cells by spinoculation, MOLM-13 cell is an AML cell line. The positive cells were collected 3 days after viral infection and subjected to RNA-seq.

2021-06-25 | GSE178859 | GEO

DAI Senses Influenza A Virus Genomic RNA and Activates RIPK3-Dependent Cell Death

Project description:293T were transfected with plasmids expressing DNA-dependent activator of IFN-regulatory factors (DAI) or retinoic acid-inducible gene 1 (RIG-I). Transfected cells were subsequently infected with influenza A/Puerto Rico/8/34 virus for 12 hours. Cell extract was subjected to FLAG Ab beads, washed, and retained. RNA was sequenced using the Illumina TruSeq Stranded Total RNA Library kit. The input sample represents total RNA from vector-infected cells.

2016-09-27 | GSE87372 | GEO

Over-expression of truncated FMRP with 295 amino acid residues: HEK293T cells

Project description:We used microarrays to detail the global gene expression in stably transfected HEK 293T cells of the over-expression of truncated FMRP containing 295 amino acid residues, which were compared with control (stably transfected HEK 293T cells of empty lentiviral vector (pLEX-MCS).

2015-05-08 | GSE68668 | GEO

Genome-wide analysis of gene expression and nuclear/cytoplasmic distribution by compound 1 treatment [293T-M]

Project description:Analysis of cellular response to DHODH inhibition at gene expression and nuclear/cytoplasmic distribution level. The NS1 protein of influenza virus is a major virulence factor essential for virus replication as it re-directs the host cell to promote viral protein expression. NS1 inhibits cellular mRNA processing and export, down-regulating host gene expression and enhancing viral gene expression. We report here the identification of a non-toxic quinoline carboxylic acid that reverts the inhibition of mRNA nuclear export by NS1, in the absence or presence of virus. This quinoline carboxylic acid directly inhibited dihydroorotate dehydrogenase (DHODH), a host enzyme required for *de novo* pyrimidine biosynthesis, and partially reduced pyrimidine levels. This effect induced NXF1 expression, which promoted mRNA nuclear export in the presence of NS1. The release of NS1-mediated mRNA export block by DHODH inhibition also occurred in the presence of VSV M protein, another viral inhibitor of mRNA export. This reversal of mRNA export block allowed expression of antiviral factors. Thus, pyrimidines play a necessary role in the inhibition of mRNA nuclear export by virulence factors. Five million 293T cells were non-transfected or transfected with 6ug of pEGFPN3-M-GFP for 16h. Then, cells were untreated or treated with compound 1(5uM) for 24h. RNA from total cell extracts or from nuclear or cytoplasmic fractions were obtained

2012-01-17 | E-GEOD-35112 | biostudies-arrayexpress

Genome-wide analysis of gene expression and nuclear/cytoplasmic distribution by compound 1 treatment [293T_NS1-1]

Project description:Analysis of cellular response to DHODH inhibition at gene expression and nuclear/cytoplasmic distribution level. The NS1 protein of influenza virus is a major virulence factor essential for virus replication as it re-directs the host cell to promote viral protein expression. NS1 inhibits cellular mRNA processing and export, down-regulating host gene expression and enhancing viral gene expression. We report here the identification of a non-toxic quinoline carboxylic acid that reverts the inhibition of mRNA nuclear export by NS1, in the absence or presence of virus. This quinoline carboxylic acid directly inhibited dihydroorotate dehydrogenase (DHODH), a host enzyme required for *de novo* pyrimidine biosynthesis, and partially reduced pyrimidine levels. This effect induced NXF1 expression, which promoted mRNA nuclear export in the presence of NS1. The release of NS1-mediated mRNA export block by DHODH inhibition also occurred in the presence of VSV M protein, another viral inhibitor of mRNA export. This reversal of mRNA export block allowed expression of antiviral factors. Thus, pyrimidines play a necessary role in the inhibition of mRNA nuclear export by virulence factors. Five million 293T cells were non-transfected or transfected with 6ug of pCAGGS-NS1 for 16h. Then, cells were untreated or treated with compound 1(5uM) for 24h. RNA from total cell extracts or from nuclear or cytoplasmic fractions were obtained

2012-01-17 | E-GEOD-35113 | biostudies-arrayexpress

Genome-wide analysis of gene expression and nuclear/cytoplasmic distribution by compound 1 treatment [293T_NS1-2]

Project description:Analysis of cellular response to DHODH inhibition at gene expression and nuclear/cytoplasmic distribution level. The NS1 protein of influenza virus is a major virulence factor essential for virus replication as it re-directs the host cell to promote viral protein expression. NS1 inhibits cellular mRNA processing and export, down-regulating host gene expression and enhancing viral gene expression. We report here the identification of a non-toxic quinoline carboxylic acid that reverts the inhibition of mRNA nuclear export by NS1, in the absence or presence of virus. This quinoline carboxylic acid directly inhibited dihydroorotate dehydrogenase (DHODH), a host enzyme required for *de novo* pyrimidine biosynthesis, and partially reduced pyrimidine levels. This effect induced NXF1 expression, which promoted mRNA nuclear export in the presence of NS1. The release of NS1-mediated mRNA export block by DHODH inhibition also occurred in the presence of VSV M protein, another viral inhibitor of mRNA export. This reversal of mRNA export block allowed expression of antiviral factors. Thus, pyrimidines play a necessary role in the inhibition of mRNA nuclear export by virulence factors. Five million 293T cells were non-transfected or transfected with 6ug of pCAGGS-NS1 for 16h. Then, cells were untreated or treated with compound 1(5uM) for 24h. RNA from total cell extracts or from nuclear or cytoplasmic fractions were obtained

2012-01-17 | E-GEOD-35114 | biostudies-arrayexpress

Gene expression data from HEK-293T cells transfected with miR-194 mimics

Project description:Nuclear factor κB (NF-κB) pathway plays an important role in hepatocellular carcinoma (HCC) progression. miR-194 was previously shown to reduce the induction of NF-κB activity upon addition of tumor necrosis factor α (TNFα). To clarify the molecular mechanism responsible for the effect of miR-194 on NF-κB pathway, mRNA microarray assays were performed to identify the genes that were suppressed by miR-194. HEK-293T cells transfected with miR-194 mimics were cultured for RNA extraction and hybridization on Affymetrix mRNA microarrays. These were compared against the control, which were HEK-293T cells transfected with negative control mimics.

2015-07-01 | E-GEOD-70434 | biostudies-arrayexpress

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