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ProteomicsPP2A inhibition is a druggable MEK inhibitor resistance mechanism in KRAS-mutant lung cancer cells
TiO2-enriched and non-enriched samples and a pooled TiO2-enriched alkaline phosphatase treated sample from subconfluent A549 lung adenocarcinoma cells line. Cells were subjected to on of the 6 different treatments: Control sample, RNAi mediated depletion of PPP2R1A, CIP2A, or PME-1, and treatment w...
ORGANISM(S): Homo sapiens (Human) 
2018-10-11 | PXD009900 | Pride
Phosphoproteomics Pp2a A549 Lung cancer 
ProteomicsPME1 interactome - Relevance Rank Platform (RRP) for Functional Filtering of High Content Protein-Protein Interaction Data
For a single step AP-MS identification of PME1 interactome was established a cell line stably expressing either Strep-tag alone or Strep_PME-1 fusion protein. After Strep-tag affinity purification, proteins were separated on SDS-PAGE gel, silver stained and protein bands that showed visually...
ORGANISM(S): Homo sapiens (Human) 
2015-12-08 | PXD002637 | Pride
Human 
ProteomicsMDAMB-231 Fusion Lumos, LC-MSMS
The protein phosphatase 2A (PP2A) heterotrimer PP2A-B56A is a human tumor suppressor. However, the molecular mechanisms inhibiting PP2A-B56A in cancer are poorly understood. Here, we report Phosphoproteomics study of single point mutation of CIP2A(K21A) in triple negative breast cancer cell line (MD...
ORGANISM(S): Homo sapiens (Human) 
2022-10-21 | PXD035179 | Pride
Human Triple negative breast cancer cell line Tmt Massspectrometry 
ProteomicsStructural mechanism for inhibition of PP2A-B56 and oncogenicity by CIP2A
Abstract The protein phosphatase 2A (PP2A) heterotrimer PP2A-B56 is a human tumor suppressor. However, the molecular mechanisms inhibiting PP2A-B56in cancer are poorly understood. Here, we report molecular level details and structural mechanism of PP2A-B56inhibition by an oncoprotein CIP2A. Upon di...
ORGANISM(S): Mus musculus (Mouse) 
2023-03-11 | PXD030297 | Pride
Ap-ms Protein phosphatase Mouse Oncogene Interactome 
ProteomicsLabel-free quantitative phosphoproteomics with novel pairwise abundance normalization reveals synergistic RAS and CIP2A signaling
Label-free quantification is a powerful method for studying cellular protein phosphorylation dynamics. However, whether current data normalization methods achieve sufficient accuracy has not been examined systematically. Here, we demonstrate that a large uni-directional shift in the phosphopeptide ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080775 | MassIVE
UnknownDUSP6 inhibition overcomes Neuregulin/HER3-driven therapy tolerance in HER2+ breast cancer
Not available
S-SCDT-10_1038-S44321-024-00088-0 | biostudies-other
ProteomicsHeLa phosphoproteome regulated by PP2A related proteins
HeLa cells were treated with siRNAs of PP2A related proteins or with okadaic acid, in triplicates. Tryptic digests of extracted proteins were analyzed using a Q Exactive mass spectrometer, before and after TiO2 phosphopeptide enrichment. Data were searched with Mascot via Proteome Discoverer. For ph...
ORGANISM(S): Homo Sapiens (human) 
2020-02-19 | PXD016102 | JPOST Repository
UnknownLIMA1-alpha staining predicts curative intent surgery response in HPV negative head and neck cancer
Not available
S-SCDT-10_1038-S44321-025-00266-8 | biostudies-other
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