Nature Methods
- 4, 817 - 821 (2007)
Published online: 27 September 2007; | doi:10.1038/nmeth1097
Decoding protein modifications using top-down mass spectrometryNertila Siuti & Neil L Kelleher
Nertila Siuti and Neil L. Kelleher are in the Departments of Chemistry and Biochemistry, and the Institute for Genomic Biology, University of Illinois at Urbana-Champaign, 53 Roger Adams Laboratory, 600 South Matthews Avenue, Urbana, Illinois 61801, USA. kelleher@scs.uiuc.edu
Top-down mass spectrometry is an emerging technology which strives to preserve the post-translationally modified forms of proteins present in vivo by measuring them intact, rather than measuring peptides produced from them by proteolysis. The top-down technology is beginning to capture the interest of biologists and mass spectrometrists alike, with a main goal of deciphering interaction networks operative in cellular pathways. Here we outline recent approaches and applications of top-down mass spectrometry as well as an outlook for its future.
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