Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

TLNRD1-GFP pulldown in HEK cells

ABSTRACT: In this study, we pull-down human TLNRD1-GFP and GFP from HEK cells. Binding partners were then analysed using mass-spectrometry.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Guillaume Jacquemet

LAB HEAD: Guillaume Jacquemet

PROVIDER: PXD045258 | Pride | 2024-01-27

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	160518_Heks_GFPR1.dat	Other
	160518_Heks_GFPR1.msf	Msf
	160518_Heks_TLNRD1_R1.dat	Other
	160518_Heks_TLNRD1_R1.msf	Msf
	180515_GFP_R1_111.raw	Raw

Items per page:

1 - 5 of 42

Similar Datasets

A m6A methyltransferase fine-tune m6A modification and ubiquitination to balance antiviral immunity and yield

Project description:Posttranscriptional and posttranslational modifications play crucial roles in plant immunity. However, how plant fine-tune these two modifications to activate antiviral immunity remains unknown. Here, we report that the m6A methyltransferase TaHAKAI is utilized by wheat yellow mosaic virus (WYMV) to increase viral genomic m6A modification and promotes viral replication. However, TaHAKAI also functions as an E3 ligase that targets the viral RNA silencing suppressor P2 for degradation and inhibits viral infection. A major allele of TaHAKAI in susceptible cultivar reduced the E3 ligase activity but not m6A methyltransferase activity, promoting viral infection. Interestingly, TaHAKAIR attenuates the mRNA stability of TaWPS1, the negative regulator of spike development, to increase panicle length and spikelet number by modulating its m6A modification. Our study reveals a new mechanisms of balancing disease resistance and yield by fine-tuning m6A modification and ubiquitination.

2024-10-09 | PXD056650 | Pride

The LC-MSMS technique identifies the difference in modification levels between two proteins

Project description:Mass spectrometry has been used as a useful tool to determine the degree of protein modification. In this study, the degree of phosphorylation between two materials, TaHAKAIR and TaHAKAIS, was identified by technique. There is a key amino acid variation in TaHAKAIR and TaHAKAIS. The phosphorylation level of TaHAKAIR and TaHAKAIS at this amino acid site was significantly changed by mass spectrometry, and the phosphorylation level of TaHAKAIR was the highest.

2025-04-06 | PXD062647 | Pride

Development of a multiplexed platform to study laccases and cellulase activities using nanostructure-initiator mass spectrometry (NIMS)

Project description:Lignocellulosic biomass is composed of three major biopolymers: cellulose, hemicellulose and lignin. Although lignin has long been considered a waste product in biomass conversion efforts, its utilization has since been identified as critical to the economic viability of second-generation biofuel production. There is thus increasing interest in finding enzymes and enzyme cocktails which can efficiently deconstruct both the cellulose/hemicellulose and lignin components of lignocellulosic biomass. Analytical tools capable of quickly detecting both glycan and lignin deconstruction could are needed to support the development and characterization of efficient enzymes/enzyme cocktails.

2021-09-09 | PXD020215 | Pride

Proteomic study of low-birth-weight nephropathy molecular pathogenesis in rats

Project description:We investigated the molecular pathogenesis of LBW rats obtained by intraperitoneal injection of dexamethasone into pregnant animals. Normal-birth-weight (NBW) rats were used as controls with seven animals per group. When the rats were four weeks old, the left kidneys were removed and used for comprehensive label-free proteomic studies

2022-02-15 | PXD018948 | Pride

YBX1-IP in mouse bone marrw myeloma cells

Project description:The total protein of bone marrw myeloma cells was extracted with cell lysis buffer for IP. YBX1 antibody was used to perform Immunoprecipitation.

2023-04-19 | PXD039386 | Pride

Phosphoproteomics analysis of Pseudomonas aeruginosa with PfkA overproduction

Project description:To determined the phosphorylation sites of proteins after overproduction of PfkA in MPAO1 via pHERD20T-fpkA, and cells without overproduciton of this protein was used as a control.

2024-07-20 | PXD035424 | Pride

Protein mass Protein mass spectrometry was used to detect the degree of biotinylation of V5-APEX2-HBC-NES after adding H2O2, and to search for host factors that interact with HBV core protein.spectrometry was used to detect the degree of biotinylation of V5-APEX2-HBC-NES after adding H2O2, and to search for host factors that interact with HBV core protein.

Project description:Chronic hepatitis B virus (HBV) infection is a leading cause of liver cirrhosis and liver cancer, representing a global health problem for which a functional cure is difficult to achieve. The HBV core protein (HBc) is essential for multiple steps in the viral life cycle; it is the building block of the nucleocapsid in which viral DNA reverse transcription occurs, and it mediates viral–host cell interactions critical to HBV infection persistence. However, systematic studies targeting HBc-interacting proteins remain lacking. An engineered ascorbate peroxidase called APEX2, is genetically targeted to a cellular region of interest and biochemically labeled neighboring proteins within living cells. Cells are then lysed, and biotinylated proteins are enriched with streptavidin beads and identified by mass spectrometry.Here, we combined HBc with the engineered ascorbate peroxidase 2 (APEX2) to systematically identify HBc-related proteins in living cells.

2025-05-06 | PXD036510 | Pride

ENKD1 binding partners with high scores were identified by mass spectrometry.

Project description:In this study, proteomics was utilized to screen proteins interacting with ENKD1. affinity purification coupled with mass spectrometry (AP-MS) was employed to systematically identify ENKD1-interacting proteins. Following immunoprecipitation and SDS-PAGE separation, the co-purified proteins were analyzed by liquid chromatography-tandem mass spectrometry (LC-MS/MS). This process helps uncover ENKD1's function, its role in cellular pathways.

2025-02-12 | PXD060678 | Pride

LC-MSMS of native MvaU-His purified from Pseudomonass aeruginosa

Project description:To determined the phosphorylation sites of MvaU-His purified from MPAO1::mvaU-His with overexpression of KKP components

2024-07-20 | PXD044529 | Pride

Phosphoproteomics analysis of Pseudomonas aeruginosa with PfkA, PfkB and PfpC overproduction

Project description:To determined the phosphorylation sites of proteins after overproduction of PfkA, PfkB and PfpC individually in PAO1 via pHERD20T-pfkA, pHERD20T-pfkB and pHERD20T-pfpC.

2024-07-20 | PXD043326 | 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