Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Proteomics of truncated APC in CRC cell

ABSTRACT: Trunc-APC immunoprecipitation (IP) and protein mass spectrometry (MS) analysis to identify potential partners.

ORGANISM(S): Homo Sapiens

SUBMITTER: Dan Xie

PROVIDER: PXD040800 | iProX | Mon Mar 13 00:00:00 GMT 2023

REPOSITORIES: iProX

ACCESS DATA

Json Xml

Similar Datasets

Project description:To further illustrate the mechanism of HEXB mediated YAP1 activation in GBM cells, immunoprecipitation-mass spectrometry (IP-MS) was employed to identify potential binding partners of HEXB.

2024-08-22 | PXD045019 | Pride

Homo sapiens

Project description:IP-MS

| PRJNA951272 | ENA

Hepa1-6 cell line overexpressing Flag-LTA4H LC-MS/MS

Project description:To explore potential proteins binding with LTA4H, co-immunoprecipitation (co-IP) and LC-MS/MS analysis were performed using Hepa1-6 cells overexpressing Flag-LTA4H. Anti-Flag and anti-IgG antibodies were used for immunoprecipitation to identify the interacting proteins.

2025-05-07 | PXD060326 | Pride

Potential proteins interated with CHRONO in human U2OS cells

Project description:We screened the protein partners that associate with CHRONO using immunoprecipitation followed with mass spectrometry (IP-MS). IP-MS identified proteins involved in multiple protein-protein interaction networks that are functional in multiple pathways and cellular functions.

2025-05-06 | PXD046945 | Pride

Adult mouse choroid plexus OTX2 Co-IP

Project description:To analyze OTX2 function in adult choroid plexus, we performed several OTX2 co-immunoprecipitation (co-IP) experiments with mass spectrometry analysis to identify potential protein partners. We previously discovered that OTX2 protein also accumulates non-cell autonomously in subventricular zone (SVZ) and rostral migratory stream (RMS) astrocytes and in visual cortex (VCx) parvalbumin cells. The identification of alternate protein partners in cell-autonomous and non-cell-autonomous contexts would suggest OTX2 takes on specific roles after transferring between cells. In order to test this hypothesis, and to reinforce choroid plexus analysis, we also performed OTX2 co-IP on lysates from adult mouse SVZ, RMS and VCx.

2021-08-23 | PXD021244 | Pride

Mass spectrometry (MS) to identify potential binding partners of UNC5B protein

Project description:Immunoprecipitation samples were collected using anti-Flag antibody from control vector and Flag-UNC5B-overexpressing HEK293T cells and subjected to mass spectrometry (MS) to identify potential binding partners of UNC5B protein.

2023-02-22 | PXD040319 |

Chromatin proteomics reveals novel combinatorial histone modification signatures that mark distinct subpopulations of macrophage enhancers [RNA-seq]

Project description:The activity of enhancers and promoters fine-tunes the transcriptional program of mammalian cells through the recruitment and interplay between cell type-specific and ubiquitous transcription factors. Despite their key role in modulating transcription, the identification of enhancers is challenged by their limited sequence conservation and highly variable distance from target genes. Although enhancers are characterised by the strong enrichment of mono-methylation at lysine 4 of histone H3, mirrored by low tri-methylation at the same residue, a comprehensive list of enhancers-associated histone post-translational modifications (PTMs) is still lacking. We undertook a proteomics investigation, based on chromatin immunoprecipitation combined with mass spectrometry (MS), to identify histone marks specifically associated to cis-regulatory elements in macrophages, focusing on enhancers. We also profiled their plasticity during the transcriptional activation induced by an inflammatory stimulus. The proteomic analysis suggested novel PTM associations, which were validated by analysis of ChIP- and RNA-seq data, whose intersection revealed the existence of novel sub-populations of enhancers marked by specific signatures: the dual mark H3K4me1/K36me2 labels transcription at enhancers, whereas H3K4me1/K36me3 and H3K4me1/K79me2 tag distinct intronic enhancers. While demonstrating that analyzing restricted genomic regions can disclose the combinatorial language of histone modifications, this study highlights the potential of MS-based proteomics in addressing fundamental questions in epigenetics.

2017-09-05 | GSE91008 | GEO

Chromatin proteomics reveals novel combinatorial histone modification signatures that mark distinct subpopulations of macrophage enhancers [ChIP-seq]

2017-09-05 | GSE91007 | GEO

A translational regulator MHZ9 modulates ethylene signaling in rice

Project description:In this project, we identified a novel RNA-binding protein, MHZ9. And we analyzed the potential proteins interacted with MHZ9 through immunoprecipitation-mass spectrometry (IP-MS). The N-terminal domain of MHZ9 (MHZ9-N) contains a putative RNA splicing and modification domain PRP4. To identify RNA binding sites in the MHZ9-N. We performed XRNAX-IP-MS assay.

2023-07-20 | PXD041240 | Pride

HCC cell lines LC-MS/MS to identify PRMT3 interaction

Project description:we performed immunoprecipitation-mass spectrometry (IP-MS) analysis using the syngenetic Hepa1-6 cells to identify novel PRMT3 substrates that may be the key downstream effectors regulating the T cell-mediated anti-tumor immunity.

2024-05-29 | PXD047693 | 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