Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

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

ABSTRACT: 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.

INSTRUMENT(S):

ORGANISM(S): Pseudomonas Aeruginosa Pao1

SUBMITTER: Yunxue Guo

LAB HEAD: Yunxue Guo

PROVIDER: PXD043326 | Pride | 2024-07-20

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	EE482LPST_pfkA_1.raw	Raw
	EE482LPST_pfkA_2.raw	Raw
	EE482LPST_pfkA_3.raw	Raw
	EE482LPST_pfkB_1.raw	Raw
	EE482LPST_pfkB_2.raw	Raw

Items per page:

1 - 5 of 10

Similar Datasets

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

LC-MSMS of purified MvaU from Pseudomonass aeruginosa

Project description:To determined the phosphorylation sites of MvaU purified from MPAO1, PAO1, PAO1/pHERD20T-fpkA, PAO1/pHERD20T-fpkB, PAO1/pHERD20T-fpkA-pfkB and PAO1/pHERD20T-fpkA-pfkB-pfpC

2024-07-20 | PXD035222 | Pride

Phosphoproteomics of Pseudomonass aeruginosa with KK and KKP overproduction

Project description:To determined the effects of KK and KKP on the phosphorylation levels of proteins in PAO1, we overexpressed KK and KKP separately in PAO1 cells via pHERD20T based plasmids.

2024-07-20 | PXD035228 | 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

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

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

URI alleviates tyrosine kinase inhibitors-induced ferroptosis by reprogramming lipid metabolism in p53 wild-type liver cancers. HEK293T cells were transfected with His-URI plasmid before anti-His immunoprecipitation and gel cutting. LC-MS/MS was performed to identify URI potential binding proteins.

Project description:URI keeps low levels of p53 in a TRIM28-MDM2 dependent manner, maintains SCD1 activity and accumulation of MUFAs, and subsequently promotes resistance to TKIs in cancer cell. URI-p53-SCD1 axis mediates resistance of TKIs and may explain why p53-wild type HCC still showed intrinsic resistance to TKIs. Moreover, the combination therapy identified here may represent a promising strategy for the approximately 41% of patients with advanced HCC who have wild-type p53 and high levels of URI/SCD1.

2023-09-15 | PXD045407 | Pride

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

Proteomic Analysis of Outer Membrane Vesicles Derived from the Type A5 Strain of Mannheimia haemolytica

Project description:Mannheimia haemolytica (M. haemolytica) cause mastitis in sheep, acute sepsis in newborn lambs, and co-infections with various pathogens, leading to bovine respiratory disease syndrome (BRDS), these infections have resulted in significant economic losses to both domestic and international farming industries. An in-depth understanding of the pathogenic mechanisms of M. haemolytica is crucial for the prevention and control of this disease. Outer membrane vesicles (OMVs) play a vital role in bacterial pathogenesis, serving as key mediators of interactions between Gram-negative bacteria and their hosts. However, the specific role of OMVs in the pathogenic process of M. haemolytica remains poorly understood. To address this, we isolated OMVs from the Mannheimia haemolytica Type A5 strain (MH-5) using ultracentrifugation and subsequently characterized their secretory properties, protein composition, and immunogenicity through electron microscopy, liquid chromatography-tandem mass spectrometry (LC-MS/MS), and cellular experiments. The electron microscopy results indicated that the MH-5 strain secreted OMVs under natural growth conditions. Proteomic and bioinformatics analyses revealed that these OMVs contained 282 proteins, with significant enrichment in proteins related to immunity, iron metabolism, and catalytic activity. Cellular experiments demonstrated that, compared to the control group, the OMVs group exhibited a significant increase in the mRNA expression of IL-1β, IL-6, and TNF-α, with secretion levels increasing in a dose-dependent manner, thereby enhancing the inflammatory response. These findings lay the groundwork for further exploration of the role of OMVs in the pathogenesis of M. haemolytica and provide insights for the development of effective vaccines and antibiotics against this pathogen.

2025-06-30 | PXD064633 | 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