Mass spectrometry-based proteomics

Brian L. Hood, Timothy D. Veenstra, Thomas P. Conrads*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

Advances in genomic analysis, including improvements in DNA sequencing, bioinformatics and the routine application of microarray technology to characterize gene expression profiles, have set the stage for understanding how genes are organized and regulated. However, the genetic blueprint cannot accurately predict which proteins are expressed, where they are localized in a cell, and in what quantity and form they are present. Proteomics is a field of study that addresses these important and varied issues. Rapid innovations in core technologies such as separations and mass spectrometry (MS) required to characterize proteins on a global scale are poised to bring about a comprehensive understanding of how changes in protein expression and function affect complex signaling and regulatory networks. These advances have significant implications for understanding how the myriad activities carried out in a cell are regulated in health and disease. This review discusses basic proteomics advances including specific examples that utilize such methodologies as two-dimensional polyacrylamide gel electrophoresis (2D PAGE), solution-based “shotgun” proteomics utilizing multidimensional separations of complex mixtures and the use of stable-isotope labeling for conducting global protein abundance profiles.

Original languageEnglish
Pages (from-to)375-380
Number of pages6
JournalInternational Congress Series
Volume1266
Issue numberC
DOIs
StatePublished - 1 Apr 2004
Externally publishedYes

Keywords

  • 2D PAGE
  • ICAT
  • Mass spectrometry
  • Multidimensional separation
  • Proteomics

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