期刊
JOURNAL OF PROTEOME RESEARCH
卷 4, 期 6, 页码 1952-1960出版社
AMER CHEMICAL SOC
DOI: 10.1021/pr0501315
关键词
post-translational modifications; breast cancer; proteome; mass spectrometry; membrane proteins; high throughput; subcellular; multidimensional liquid chromatography; functional genomics; pathways
资金
- NCI NIH HHS [CA86135] Funding Source: Medline
- NCRR NIH HHS [RR18522] Funding Source: Medline
Normal and cancer cell line proteomes were profiled using high throughput mass spectrometry techniques. Application of protein-level and peptide-level sample fractionation combined with LCMS/MS analysis enabled identification of 2235 unmodified proteins representing a broad range of functional and compartmental classes. An iterative multistep search strategy was used to identify post-translational modifications, revealing several proteins that are preferentially modified in cancer cells. Information regarding both unmodified and modified protein forms was combined with publicly available gene expression and protein-protein interaction data. The resulting integrated dataset revealed several functionally related proteins that are differentially regulated between normal and cancer cell lines.
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