Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Identification of NUP153 protein complex

ABSTRACT: Protein complex were collected by immunoprecipitation.

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Masaharu Hazawa

PROVIDER: PXD032875 | JPOST Repository | Tue Oct 24 00:00:00 BST 2023

REPOSITORIES: jPOST

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	TE5_IP_NUP153.xlsx	Xlsx
	TE5_IP_NUP153_20210630_Aur120_20210702.mgf	Mgf
	TE5_IP_NUP153_20210630_Aur120_20210702.raw	Raw
	TE5_IgG_IP.xlsx	Xlsx
	TE5_IgG_IP_20210630_Aur120_20210702.mgf	Mgf

Items per page:

1 - 5 of 12

Similar Datasets

Identification of circulating protein biomarkers for pancreatic cancer cachexia

Project description:Over 80% of patients with pancreatic ductal adenocarcinoma (PDAC) suffer from cachexia, characterized by severe muscle and fat loss and yet, there are no biomarkers identified for this debilitating condition. Our objective was to identify circulating protein biomarkers using serum for human PDAC cachexia and understand their biological functions. Serum from 30 patients with PDAC was collected and protein profiles were generated using SOMAscan. The protein profiles were correlated with clinical variables such as Cancer associated weight loss (CAWL), body composition measurements of skeletal muscle index (SMI), skeletal muscle density (SMD), total adipose index (TAI) using Spearman’s correlation. Overall, 110 proteins of 1294 correlated with these clinical measures - 47 proteins for CAWL, 19 for SMI, 14 for SMD, and 30 for TAI (r-value 0.5, p<0.05). LYVE1, a homolog of CD44 implicated in tumor metastasis, was the top CAWL-associated protein (r= 0.67, p=0.0001). Protein co-expression network analysis identified immune system related pathways such as B-cell signaling, natural killer cell signaling, IL6 signaling in addition to identifying other known pathways in cachexia. Taken together, these data identify both immune system molecules and additional secreted factors and pathways not previously associated with PDAC and confirm the activation of previously identified pathways.

2020-12-31 | GSE119483 | GEO

Identification of RNA bound to the TDP-43 ribonucleoprotein complex

Project description:In total 3 mice brain tissues were used for this experiment. Tissue from each mouse brain was divided for immunoprecipitation with 5ug of either rabbit anti-TDP-43 antibody (Abcam) or normal rabbit IgG (Sigma) .The antibodies were first incubated with the lysate overnight at 4 degrees C, after which 50 uL of protein G Dynabeads(tm) (Invitrogen(tm)) added and the solution incubated for 1 hour at 4 degrees C with rotation. Following several washing with washing buffer (Invitrogen(tm)), the protein-RNA complex was eluted from 20 uL of bead-protein complex using 10 uL of elution buffer (Invitrogen(tm)) and seperated on a 10% NuPage(tm) Bis-Tris gel (Invitrogen(tm)). RNA was isolated from the remaining 30 uL of protein-bead complex using TRIzol reagent (Invitrogen) followed by DNaseI treatment (Ambion). The TDP-43 immunoprecipitated RNA was converted to cDNA, fragmented and biotin labelled using WT cDNA synthesis & amplification kit and Terminal Labeling Kit (Affymetrix(tm)) for Affymetrix(tm) GeneChip(tm) Mouse Gene 1.0 ST and 3'-IVT expression analysis kit (Affymetrix(tm)) for GeneChip(tm) Mouse 430_2 arrays according to the standard protocol. Labelled RNA was hybridised to arrays in a hybridization oven (Affymetrix(tm)) at 45 degrees C rotating at 60 rpm for 17 hours and scanned using the Affymetrix(tm) GeneChip Scanner. Successful hybridisation to the microarray was checked using Expression Console software (Affymetrix(tm)) and the data (.CEL files) transferred to Partek Genomics Suite for statistical analysis. TDP-43 and IgG immunoprecipitated RNA samples were each hybridised to 3 GeneChip Mouse Gene 1.0 ST and 3 GeneChip Mouse 430 (n = 6 for each group).

2012-02-06 | E-MEXP-3500 | biostudies-arrayexpress

Protein import motor complex reacts to mitochondrial misfolding by reducing protein import and activating mitophagy

Project description:Protein import motor complex reacts to mitochondrial misfolding by reducing protein import and activating mitophagy

| PRJNA854161 | ENA

The KMT2 complex protein ASH2L controls meiosis through silencing transposon

Project description:The KMT2 complex protein ASH2L controls meiosis through silencing transposon

| PRJNA1032460 | ENA

Identification of mRNAs associated with the protein complex ZC3H41/Z41AP (Tb927.11.1980/Tb927.7.7460) in Trypanosoma brucei

Project description:Identification of mRNAs associated with the protein complex ZC3H41/Z41AP (Tb927.11.1980/Tb927.7.7460) in Trypanosoma brucei

| PRJNA878470 | ENA

RNA-binding protein immunoprecipitation (RIP)and RNA sequencing

Project description:RNA-binding protein immunoprecipitation (RIP)and RNA sequencing

| PRJNA555809 | ENA

TheRole of Rad23/Rad4 protein complex in transcription and DNA repair in yeast

Project description:The Rad23/Rad4 protein complex plays a major role in DNA damage recognition during nucleotide excision repair (NER) in yeast. We recently showed that two distinct pathways contribute to efficient NER in yeast. The first operates independently of de novo protein synthesis and requires a nonproteolytic function of the 19S regulatory complex of the 26S proteasome and Rad23. The second pathway requires de novo protein synthesis, and relies on the activity of a newly identified E3 ubiquitin ligase that ubiquitinates Rad4 in response to UV. Surprisingly, we found that cells deleted of either Rad23 or Rad4 caused reduced Rad4 and Rad23 mRNA levels respectively. We considered the possibility of an unexpected role of Rad23 and Rad4 in regulating the expression of genes involved in the transcriptional response to DNA damage. Gene expression profiling has suggested that Rad23 and Rad4 may function as a complex to affect transcription of a small subset of genes in response to UV damage. To determine how Rad4 and Rad23 contribute to the regulation of these genes, we have examined the occupancy of Rad4/Rad23 in their promoter regions by chromatin immunoprecipitation (ChIP), both in the presence and absence of UV damage. Our preliminary ChIP data suggests that the Rad4/Rad23 complex regulates a set of genes in response to UV light.

2009-06-01 | GSE11871 | GEO

Identification of an eight-protein biosignature for the diagnosis of tuberculosis

Project description:Mycobacterium tuberculosis (Mtb) antigen-specific cellular response is promising for detectionof Mtb infection, but not efficient for diagnosis of TB. We firstly identified 16 TB disease-specific protein markers measured in the culture supernatant of Mtb-stimulated whole blood using a 640 human proteins array, the highest throughput antibody-based protein array available at the time when we did this study. Potential TB-related proteins were then analyzed across three different patient cohorts comprised of healthy controls, LTBI, non-TB pneumonia, and TB patients to evaluate how the biomarkers performed in diagnosing TB in the real clinical setting. The data finally reveal an eight-protein biosignature of TB.

2019-06-25 | GSE133249 | GEO

An mRNA cap-binding complex in giant viruses controls protein synthesis

Project description:An mRNA cap-binding complex in giant viruses controls protein synthesis

| PRJNA1225729 | ENA

The Integrator complex terminates promoter-proximal transcription at protein-coding genes

Project description:The Integrator complex terminates promoter-proximal transcription at protein-coding genes

| PRJNA471515 | ENA