| Literature DB >> 27453469 |
Ulrike Kusebauch1, David S Campbell1, Eric W Deutsch1, Caroline S Chu1, Douglas A Spicer1, Mi-Youn Brusniak1, Joseph Slagel1, Zhi Sun1, Jeffrey Stevens1, Barbara Grimes1, David Shteynberg1, Michael R Hoopmann1, Peter Blattmann2, Alexander V Ratushny3, Oliver Rinner4, Paola Picotti2, Christine Carapito2, Chung-Ying Huang1, Meghan Kapousouz1, Henry Lam5, Tommy Tran1, Emek Demir6, John D Aitchison3, Chris Sander6, Leroy Hood1, Ruedi Aebersold7, Robert L Moritz8.
Abstract
The ability to reliably and reproducibly measure any protein of the human proteome in any tissue or cell type would be transformative for understanding systems-level properties as well as specific pathways in physiology and disease. Here, we describe the generation and verification of a compendium of highly specific assays that enable quantification of 99.7% of the 20,277 annotated human proteins by the widely accessible, sensitive, and robust targeted mass spectrometric method selected reaction monitoring, SRM. This human SRMAtlas provides definitive coordinates that conclusively identify the respective peptide in biological samples. We report data on 166,174 proteotypic peptides providing multiple, independent assays to quantify any human protein and numerous spliced variants, non-synonymous mutations, and post-translational modifications. The data are freely accessible as a resource at http://www.srmatlas.org/, and we demonstrate its utility by examining the network response to inhibition of cholesterol synthesis in liver cells and to docetaxel in prostate cancer lines.Entities:
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Year: 2016 PMID: 27453469 PMCID: PMC5245710 DOI: 10.1016/j.cell.2016.06.041
Source DB: PubMed Journal: Cell ISSN: 0092-8674 Impact factor: 41.582