Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

LC-MSMS of purified MvaU from Pseudomonass aeruginosa

ABSTRACT: 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

INSTRUMENT(S):

ORGANISM(S): Pseudomonas Aeruginosa Pao1

SUBMITTER: Yunxue Guo

LAB HEAD: Yunxue Guo

PROVIDER: PXD035222 | Pride | 2024-07-20

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	YD032GP_MvaU_in_MPAO1.rar	Other
	YD032GP_MvaU_in_MPAO1.raw	Raw
	YD148GP_DT_MvaU_in_PAO1.rar	Other
	YD148GP_DT_MvaU_in_PAO1.raw	Raw
	YE006GP_mvaU_from_PAO1-pHERD20T-PfkA.rar	Other

Items per page:

1 - 5 of 13

Similar Datasets

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

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

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

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

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

mouse embryonic stem cells heterochromatin-associated protein and Nat10 IP-MS

Project description:The sonication-resistant heterochromatin (srHC) fragments of mESCs were isolated by sucrose gradient ultracentrifugation, and the heterochromatin-associated proteins were enriched by Co-IP combined with mass spectrometry (Co-IP/MS) using anti-H3K9me3, IgG was used as a negative control. The Nat10 interacted proteins in mESCs were isolated by 3×Flag-Nat10 fusion protein overexpression and performed IP-MS using anti-Flag, IgG antibody was used as a negative control.

2025-06-23 | PXD056153 | Pride

DYRK1B phosphorylates FOXO1 to promote hepatic gluconeogenesis

Project description:Dual-specificity tyrosine phosphorylation-regulated kinase 1B (DYRK1B), a member of the CMGC group of kinase, is associated with metabolic syndrome. However, the molecular mechanisms involved remain elusive. In this study, we demonstrate that Dyrk1b expression is induced in liver by fasting and in diabetic mice. Using both in vivo and in vitro studies, we show that DYRK1B promotes hepatic gluconeogenesis and glucose intolerance. Liver-specific Dyrk1b conditional knockout mice were protected from diet-induced hyperglycemia. Mechanistically, DYRK1B interacts with and phosphorylates FOXO1, primarily at Thr467/Ser468, which is essential for its nuclear localization. Additionally, DYRK1B inhibits AKT mediated FOXO1 phosphorylation at Thr24 and Ser256, thereby enhancing its nuclear retention. DYRK1B mediated phosphorylation enhances the expression of gluconeogenic genes and promotes gluconeogenesis. Further, a pharmacological inhibitor of DYRK1B significantly reduced blood glucose levels in diabetic mice. Collectively, these findings offer new insights into DYRK1B’s role in the glucose metabolism and identify it as a new therapeutic target for treating diabetes.

2025-05-07 | PXD052214 | 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