Dataset Information

Yagpm2_2

ABSTRACT: enrichment for specialized purple membrane proteins, cell culture #2 Goo et al., unpublished data.

INSTRUMENT(S): Unknown

ORGANISM(S): Halobacterium Nrc-1 (halobacterium)

SUBMITTER: Y. A. Goo, E. C. Yi, N. S. Baliga, W. A. Tao, M. Pan, R. Aebersold, D. R. Goodlett, L. Hood and W. V. Ng

PROVIDER: PAe000252 | PeptideAtlas | 2011-12-31

REPOSITORIES: PeptideAtlas

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			Action	DRS
	PAe000252_250_search.params.tar.gz	Other
	PAe000252_250_sequest.params	Other
	PAe000252_RAW.tar	Raw
	PAe000252_README	Other
	PAe000252_Search_Results_250_201104181134.properties	Other

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Publications

Quantitative proteomics reveals that Hsp90 inhibition preferentially targets kinases and the DNA damage response.

Sharma Kirti K Vabulas R Martin RM Macek Boris B Pinkert Stefan S Cox Jürgen J Mann Matthias M Hartl F Ulrich FU

Molecular & cellular proteomics : MCP 20111213 3

Despite the increasing importance of heat shock protein 90 (Hsp90) inhibitors as chemotherapeutic agents in diseases such as cancer, their global effects on the proteome remain largely unknown. Here we use high resolution, quantitative mass spectrometry to map protein expression changes associated with the application of the Hsp90 inhibitor, 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG). In depth data obtained from five replicate SILAC experiments enabled accurate quantificatio ...[more]

PMID: 22167270

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