Ras genes are among the most frequently mutated oncogenes in human malignancies. To date, there are no successful anti-cancer drugs in the clinic that target Ras proteins or their pathways. Therefore, it is imperative to identify and characterize new components that regulate Ras activity or mediate its downstream signaling. The data set is an affinity purification followed by mass spectrometry (AP-MS) experiment to identify new molecular components that physically interact with Ras. HRasV12 was ectopically expressed with the Flag moiety. A number of candidate binding partners have been identified in the AP-MS. Radil was among the top-enriched proteins. The data set contains the raw files for the AP-MS experiment.
[doi:10.25345/C5J163]
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: KRas ; Radil ; affinity purification
Principal Investigators: (in alphabetical order) |
Beatrix Ueberheide, NYU School of Medicine, USA |
Submitting User: | Trixi |
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Owner | Reanalyses | |
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Experimental Design | ||
Conditions:
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Identification Results | ||
Proteins (Human, Remapped):
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Proteins (Reported):
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PSMs:
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Quantification Results | ||
Differential Proteins:
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Quantified Proteins:
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