4.5 Review

Mass spectrometry for proteomics

Journal

CURRENT OPINION IN CHEMICAL BIOLOGY
Volume 12, Issue 5, Pages 483-490

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.cbpa.2008.07.024

Keywords

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Funding

  1. National Institutes of Health [P41 RR011823, 2R01 MH067880, U01 DE016267]
  2. American Cancer Society [PF-07-297-01-CCG]
  3. NATIONAL CENTER FOR RESEARCH RESOURCES [P41RR011823] Funding Source: NIH RePORTER
  4. NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [R01HL079442] Funding Source: NIH RePORTER
  5. NATIONAL INSTITUTE OF DENTAL &CRANIOFACIAL RESEARCH [U01DE016267] Funding Source: NIH RePORTER
  6. NATIONAL INSTITUTE OF MENTAL HEALTH [R01MH067880] Funding Source: NIH RePORTER

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Mass spectrometry has been widely used to analyze biological samples and has evolved into an indispensable tool for proteomics research. Our desire to understand the proteome has led to new technologies that push the boundary of mass spectrometry capabilities, which in return has allowed mass spectrometry to address an ever-increasing array of biological questions. The recent development of a novel mass spectrometer (Orbitrap) and new dissociation methods such as electron-transfer dissociation has made possible the exciting new areas of proteomic application. Although bottom-up proteomics (analysis of proteolytic peptide mixtures) remains the workhorse for proteomic analysis, middle-down and topdown strategies (analysis of longer peptides and intact proteins, respectively) should allow more complete characterization of protein isoforms and post-translational modifications. Finally, stable isotope labeling strategies have transformed mass spectrometry from merely descriptive to a tool for measuring dynamic changes in protein expression, interaction, and modification.

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