Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


Sci. Signal., 27 March 2012
Vol. 5, Issue 217, p. rs2
[DOI: 10.1126/scisignal.2002548]


Editor's Summary

Improving Throughput
Mass spectrometry is a powerful tool for monitoring changes in protein abundance and posttranslational modifications. Dephoure and Gygi describe a mass spectrometry approach that enables the analysis of samples from multiple conditions simultaneously by combining two different labeling methods, which they call "hyperplexing." Using this method, the authors monitored changes in protein abundance in yeast in response to the drug rapamycin, an inhibitor of the kinase TOR, that has been clinically used as an immunosuppressant and anticancer agent. Rapamycin-induced changes in the abundance of proteins in a six-point time course with biological triplicates were monitored in a single experiment. Statistical analysis provided a high-confidence set of proteins that increased or decreased in abundance in response to this drug. This technique should facilitate the application of quantitative mass spectrometry to the analysis of dynamic cellular events.

Citation: N. Dephoure, S. P. Gygi, Hyperplexing: A Method for Higher-Order Multiplexed Quantitative Proteomics Provides a Map of the Dynamic Response to Rapamycin in Yeast. Sci. Signal. 5, rs2 (2012).

Read the Full Text

Targeted proteomics reveals strain-specific changes in the mouse insulin and central metabolic pathways after a sustained high-fat diet.
E. Sabido, Y. Wu, L. Bautista, T. Porstmann, C.-Y. Chang, O. Vitek, M. Stoffel, and R. Aebersold (2014)
Mol Syst Biol 9, 681
   Abstract »    Full Text »    PDF »
Development of a 5-plex SILAC Method Tuned for the Quantitation of Tyrosine Phosphorylation Dynamics.
M. Tzouros, S. Golling, D. Avila, J. Lamerz, M. Berrera, M. Ebeling, H. Langen, and A. Augustin (2013)
Mol. Cell. Proteomics 12, 3339-3349
   Abstract »    Full Text »    PDF »
Native SILAC: Metabolic Labeling of Proteins in Prototroph Microorganisms Based on Lysine Synthesis Regulation.
F. Frohlich, R. Christiano, and T. C. Walther (2013)
Mol. Cell. Proteomics 12, 1995-2005
   Abstract »    Full Text »    PDF »
Latency-Associated Degradation of the MRP1 Drug Transporter During Latent Human Cytomegalovirus Infection.
M. P. Weekes, S. Y. L. Tan, E. Poole, S. Talbot, R. Antrobus, D. L. Smith, C. Montag, S. P. Gygi, J. H. Sinclair, and P. J. Lehner (2013)
Science 340, 199-202
   Abstract »    Full Text »    PDF »
Protein Complex-Based Analysis Framework for High-Throughput Data Sets.
A. Vinayagam, Y. Hu, M. Kulkarni, C. Roesel, R. Sopko, S. E. Mohr, and N. Perrimon (2013)
Science Signaling 6, rs5
   Abstract »    Full Text »    PDF »

To Advertise     Find Products

Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882