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ProteomicsDUSP2 dephosphorylates STAT3 at Y705 and S727 residues
In the related study, to determine whether DUSP2 definitively served as a phosphatase for STAT3, an in vitro phosphatase assay was used. Using S-tag beads, p-STAT3 was pulled down from IL-6 stimulated HEK293T cells transfected with STAT3-S-Tag. DUSP2 or control protein, which was purified from HEK29...
ORGANISM(S): Homo sapiens (Human) 
2015-10-13 | PXD002743 | Pride
Dusp2 Phosphorylation Stat3 
UnknownInfluence of Macrocyclization Strategies on DNA-Encoded Cyclic Peptide Libraries.
Not available
S-EPMC12308377 | biostudies-literature
UnknownDesign, Construction, and Screening of Diversified Pyrimidine-Focused DNA-Encoded Libraries.
Not available
S-EPMC10424316 | biostudies-literature
UnknownDistinct trajectories of perinatal depression in Chinese women: application of latent growth mixture modelling.
Not available
S-EPMC8751241 | biostudies-literature
ProteomicsIdentification of PAC1 interactome in activated T cells
To examine the molecular mechanisms by which PAC1 suppresses T cell response to antigen, we conducted immunoprecipitation followed by mass spectrometry to characterize PAC1-associated proteins in activated T cells
ORGANISM(S): Homo sapiens (Human) 
2020-01-07 | PXD012201 | Pride
Pac1 T cells Interactome 
UnknownCovalent DNA-Encoded Library Workflow Drives Discovery of SARS-CoV-2 Nonstructural Protein Inhibitors.
Not available
S-EPMC11673110 | biostudies-literature
ProteomicsSTN1 facilitates metastasis by promoting transcription of EMT-activator ZEB1 in pancreatic cancer
As pancreatic ductal adenocarcinoma (PDAC) poses a formidable clinical challenge, demanding further exploration of its pathogenesis and drugs targeted for metastasis-the main cause of mortality. Here, we identified STN1, a CST complex member crucial for maintaining telomere lengths and genome stabil...
ORGANISM(S): Homo sapiens (Human) 
2025-08-05 | PXD062518 | Pride
Pancreatic cancer  stn1  stat3 
ProteomicsIdentification of proteins affected by PTENα under stress conditions by mass spectrometry
Stress granules are known to be related with selective translation. To determine which proteins are regulated by stress granules assembly in Ptenα─/─ MEFs, we performed a mass spectrometry analysis of Ptenα+/+ and Ptenα─/─ MEFs under oxidative stress.
ORGANISM(S): Mus Musculus 
PXD021840 |
ProteomicsIdentification of PTENα associated proteins under stress condictions in B16 cells by mass spectrometry
PTENα is the first isoform of tumor suppressor PTEN. To investigate the molecular mechanism by which PTENα modulates cell response to inflammation, we performed pull-down assays with FLAG-tagged proteins coupled with mass spectrometry under condition of H2O2 treatment in B16 cells.
ORGANISM(S): Mus Musculus 
2021-07-13 | PXD040709 |
ProteomicsDeepFLR Facilitates False Localization Rate Control in Phosphoproteomics
Site-specific phosphorylation events affect nearly all the cellular processes and correct phosphosite localization plays an important role in biological or medical health studies. However, direct false localization rate (FLR) control remains challenging in phosphoproteomics. Here, we propose DeepFLR...
ORGANISM(S): Homo Sapiens 
2023-04-04 | PXD037580 |
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