title: Decoding protein modifications using top-down mass spectrometry.
abstract: 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.
authors: Department of Chemistry, University of Illinois at Urbana-Champaign, 53 Roger Adams Laboratory, 600 South Matthews Avenue, Urbana, Illinois 61801, USA.
authors: Nertila
authors: N
authors: Siuti
authors: Neil L
authors: NL
authors: Kelleher
mesh_terms: D002843:Chromatin / Q000737:chemistry; D013058:Mass Spectrometry / Q000379:methods*; D008565:Membrane Proteins / Q000737:chemistry; D020033:Protein Isoforms / Q000737:chemistry; D011499:Protein Processing, Post-Translational; D040901:Proteomics / Q000379:methods*; D053719:Tandem Mass Spectrometry / Q000379:methods
chemical_list: D002843:Chromatin; D008565:Membrane Proteins; D020033:Protein Isoforms