Functional and quantitative proteomics using SILAC
Top Cited Papers
- 1 December 2006
- journal article
- research article
- Published by Springer Nature in Nature Reviews Molecular Cell Biology
- Vol. 7 (12) , 952-958
- https://doi.org/10.1038/nrm2067
Abstract
Stable-isotope labelling by amino acids in cell culture (SILAC) has emerged as a simple and powerful format for quantitative proteomics. What are the current applications for SILAC? And, how will this technology be used in the future? Researchers in many biological areas now routinely characterize proteins by mass spectrometry. Among the many formats for quantitative proteomics, stable-isotope labelling by amino acids in cell culture (SILAC) has emerged as a simple and powerful one. SILAC removes false positives in protein-interaction studies, reveals large-scale kinetics of proteomes and — as a quantitative phosphoproteomics technology — directly uncovers important points in the signalling pathways that control cellular decisions.Keywords
This publication has 62 references indexed in Scilit:
- Condensin and Repo-Man–PP1 co-operate in the regulation of chromosome architecture during mitosisNature Cell Biology, 2006
- Phosphoproteomic analysis of Her2/neu signaling and inhibitionProceedings of the National Academy of Sciences, 2006
- Scoring proteomes with proteotypic peptide probesNature Reviews Molecular Cell Biology, 2005
- Nucleolar proteome dynamicsNature, 2005
- Phosphotyrosine interactome of the ErbB‐receptor kinase familyMolecular Systems Biology, 2005
- Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factorsProceedings of the National Academy of Sciences, 2003
- Mass spectrometry-based proteomicsNature, 2003
- Comparative assessment of large-scale data sets of protein–protein interactionsNature, 2002
- Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometryNature, 2002
- Functional organization of the yeast proteome by systematic analysis of protein complexesNature, 2002