MassIVE MSV000093899

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The development of a high-throughput kinase activity platform using nanoLC-MS/MS with DIA approach for studying the anticancer mechanism of Taxol in ovarian cancer

Description

Protein phosphorylation, a process mediated by protein kinases, plays a pivotal role in increasing protein diversity, thereby influencing various cellular functions. Peptide substrates have been employed for in vitro phosphorylation experiments using purified kinases or cell lysates. In this study, we have developed a quantitative, high-throughput platform for assessing multikinase activity, based on nanoLC-MS/MS with data-independent acquisition (DIA) approach. This platform was evaluated by studying the kinase activity of Taxol- treated SKOV3 cells. A library containing 38 peptide substrates was designed and analyzed to indicate the activity of major kinases in cancer development. [doi:10.25345/C59Z90P5R] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: Kinase assay ; Mass spectrometry ; Data independent acquisition ; Taxol

Contact

Principal Investigators:
(in alphabetical order)
Chao-Jung Chen, Proteomics Core Laboratory, Department of Medical Research, China Medical University Hospital, Taichung 40402, Taiwan, Taiwan
Submitting User: cjchen_01
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Number of distinct peptide sequences (including modified variants or peptidoforms) reported across all analyses (original submission and reanalyses) associated with this dataset.

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Number of distinct proteins found to be differentially abundant in at least one comparison across all analyses (original submission and reanalyses) associated with this dataset.

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Distinct protein accessions are counted across all files submitted in the "Statistical Analysis of Quantified Analytes" category having a "Protein" column in this dataset.

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