Dataset Information

Alkylation Damage by Lipid Electrophiles Targets Functional Protein Systems

ABSTRACT: These data correspond to "Alkylation Damage by Lipid Electrophiles Targets Functional Protein Systems," a paper from Codreanu, Liebler, et al, published at the journal _Molecular and Cellular Proteomics_ in 2013. Modifications also include: 4-hydroxynonenal (HNE) (UniMod #53), H(16) C(9) O(2), Monoisotopic mass 156.115030 4-Oxononenal (ONE) (UniMod #721), H(14) C(9) O(2), Monoisotopic mass 154.099380 Modifications may be observed in both reduced and oxidized forms (a mass shift of two Da).

INSTRUMENT(S): LTQ

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

SUBMITTER: Daniel C. Liebler

PROVIDER: MSV000078490 | MassIVE | Mon Nov 18 14:22:00 GMT 2013

REPOSITORIES: MassIVE

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Alkylation damage by lipid electrophiles targets functional protein systems.

Codreanu Simona G SG Ullery Jody C JC Zhu Jing J Tallman Keri A KA Beavers William N WN Porter Ned A NA Marnett Lawrence J LJ Zhang Bing B Liebler Daniel C DC

Molecular & cellular proteomics : MCP 20140115 3

Protein alkylation by reactive electrophiles contributes to chemical toxicities and oxidative stress, but the functional impact of alkylation damage across proteomes is poorly understood. We used Click chemistry and shotgun proteomics to profile the accumulation of proteome damage in human cells treated with lipid electrophile probes. Protein target profiles revealed three damage susceptibility classes, as well as proteins that were highly resistant to alkylation. Damage occurred selectively acr ...[more]

PMID: 24429493

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