Proteomics

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Chemical phosphoproteomics reveals kinase network topologies associated to genotypes and phenotypes of cancer cells.


ABSTRACT: We compare the in vitro specificity profiles of several kinase inhibitors with their effects on cellular phosphoproteomes. For this aim, we developed an algorithm which utilizes information on kinase inhibitor selectivity to determine the most probable kinase(s) acting upstream of phosphorylation sites present in phosphoproteomics data obtained from cancer cells treated with kinase inhibitors.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Pedro Cutillas  

PROVIDER: MSV000090571 | MassIVE | Sat Oct 22 21:47:00 BST 2022

SECONDARY ACCESSION(S): PXD015943

REPOSITORIES: MassIVE

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Publications

Reconstructing kinase network topologies from phosphoproteomics data reveals cancer-associated rewiring.

Hijazi Maruan M   Smith Ryan R   Rajeeve Vinothini V   Bessant Conrad C   Cutillas Pedro R PR  

Nature biotechnology 20200120 4


Understanding how oncogenic mutations rewire regulatory-protein networks is important for rationalizing the mechanisms of oncogenesis and for individualizing anticancer treatments. We report a chemical phosphoproteomics method to elucidate the topology of kinase-signaling networks in mammalian cells. We identified >6,000 protein phosphorylation sites that can be used to infer >1,500 kinase-kinase interactions and devised algorithms that can reconstruct kinase network topologies from these phosph  ...[more]

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