메뉴 건너뛰기




Volumn 274, Issue 24, 2007, Pages 6256-6268

Top-down MS, a powerful complement to the high capabilities of proteolysis proteomics

Author keywords

Electron capture dissociation; MS; Post translational modifications; Protein characterization; Protein identification; Top down proteomics

Indexed keywords

CYSTEINE; PEPTIDE FRAGMENT;

EID: 36749004371     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2007.06147.x     Document Type: Short Survey
Times cited : (151)

References (62)
  • 1
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn JB, Mann M, Meng CK, Wong SF Whitehouse CM (1989) Electrospray ionization for mass spectrometry of large biomolecules. Science 246, 64 71.
    • (1989) Science , vol.246 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 2
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons
    • Karas M Hillenkamp F (1988) Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons. Anal Chem 60, 2299 2301.
    • (1988) Anal Chem , vol.60 , pp. 2299-2301
    • Karas, M.1    Hillenkamp, F.2
  • 4
    • 84984042980 scopus 로고
    • Protein and polymer analyses up to m/z 100,000 by laser ionization time-of-flight mass spectrometry
    • Tanaka K, Waki H, Ido Y, Akita S, Yoshida Y Yoshida T (1988) Protein and polymer analyses up to m/z 100,000 by laser ionization time-of-flight mass spectrometry. Rapid Commun Mass Spectrom 2, 151 153.
    • (1988) Rapid Commun Mass Spectrom , vol.2 , pp. 151-153
    • Tanaka, K.1    Waki, H.2    Ido, Y.3    Akita, S.4    Yoshida, Y.5    Yoshida, T.6
  • 6
    • 2642520417 scopus 로고    scopus 로고
    • Top-down proteomics
    • Kelleher NL (2004) Top-down proteomics. Anal Chem 76, 197A 203A.
    • (2004) Anal Chem , vol.76
    • Kelleher, N.L.1
  • 9
    • 0042386240 scopus 로고    scopus 로고
    • Protein identification: The origins of peptide mass fingerprinting
    • Henzel WJ, Watanabe C Stults JT (2003) Protein identification: the origins of peptide mass fingerprinting. J Am Soc Mass Spectrom 14, 931 942.
    • (2003) J Am Soc Mass Spectrom , vol.14 , pp. 931-942
    • Henzel, W.J.1    Watanabe, C.2    Stults, J.T.3
  • 10
    • 0141502007 scopus 로고    scopus 로고
    • Shotgun proteomics: Integrating technologies to answer biological questions
    • 3rd (
    • McDonald WH, Yates JR 3rd (2003) Shotgun proteomics: integrating technologies to answer biological questions. Curr Opin Mol Ther 5, 302 309.
    • (2003) Curr Opin Mol Ther , vol.5 , pp. 302-309
    • McDonald, W.H.1    Yates, J.R.2
  • 11
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold R Mann M (2003) Mass spectrometry-based proteomics. Nature 422, 198 207.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 14
    • 33749615256 scopus 로고    scopus 로고
    • Mass spectrometry: Bottom-up or top-down?
    • Chait BT (2006) Mass spectrometry: bottom-up or top-down? Science 314, 65 66.
    • (2006) Science , vol.314 , pp. 65-66
    • Chait, B.T.1
  • 15
    • 0037196338 scopus 로고    scopus 로고
    • Top down characterization of larger proteins (45 kDa) by electron capture dissociation mass spectrometry
    • Ge Y, Lawhorn BGEI, Naggar M, Strauss E, Park JH, Begley TP McLafferty FW (2002) Top down characterization of larger proteins (45 kDa) by electron capture dissociation mass spectrometry. J Am Chem Soc 124, 672 678.
    • (2002) J Am Chem Soc , vol.124 , pp. 672-678
    • Ge, Y.1    Bgei, L.2    Naggar, M.3    Strauss, E.4    Park, J.H.5    Begley, T.P.6    McLafferty, F.W.7
  • 18
    • 0034641742 scopus 로고    scopus 로고
    • Automated de novo sequencing of proteins by tandem high-resolution mass spectrometry
    • Horn DM, Zubarev RA McLafferty FW (2000) Automated de novo sequencing of proteins by tandem high-resolution mass spectrometry. Proc Natl Acad Sci USA 97, 10313 10317.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10313-10317
    • Horn, D.M.1    Zubarev, R.A.2    McLafferty, F.W.3
  • 19
    • 0037133237 scopus 로고    scopus 로고
    • Top down mass spectrometry of a 29 kDa protein for characterization of any posttranslational modification to within one residue
    • Sze SK, Ge Y, Oh HB McLafferty FW (2002) Top down mass spectrometry of a 29 kDa protein for characterization of any posttranslational modification to within one residue. Proc Natl Acad Sci USA 99, 1774 1779.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 1774-1779
    • Sze, S.K.1    Ge, Y.2    Oh, H.B.3    McLafferty, F.W.4
  • 20
    • 2642578319 scopus 로고    scopus 로고
    • A new approach for plant proteomics. Characterization of chloroplast proteins of Arabidopsis thaliana by top-down mass spectrometry
    • Zabrouskov V, Giacomelli L, van Wijk KJ McLafferty FW (2003) A new approach for plant proteomics. Characterization of chloroplast proteins of Arabidopsis thaliana by top-down mass spectrometry. Mol Cell Proteomics 2, 1253 1260.
    • (2003) Mol Cell Proteomics , vol.2 , pp. 1253-1260
    • Zabrouskov, V.1    Giacomelli, L.2    Van Wijk, K.J.3    McLafferty, F.W.4
  • 21
    • 1342283001 scopus 로고    scopus 로고
    • Characterization of two kinases involved in thiamine pyrophosphate and pyridoxal phosphate biosynthesis in Bacillus subtilis: 4-amino-5-hydroxymethyl- 2-methylpyrimidine kinase and pyridoxal kinase
    • Park JH, Burns K, Kinsland C Begley TP (2004) Characterization of two kinases involved in thiamine pyrophosphate and pyridoxal phosphate biosynthesis in Bacillus subtilis: 4-amino-5-hydroxymethyl-2-methylpyrimidine kinase and pyridoxal kinase. J Bacteriol 186, 1571 1573.
    • (2004) J Bacteriol , vol.186 , pp. 1571-1573
    • Park, J.H.1    Burns, K.2    Kinsland, C.3    Begley, T.P.4
  • 22
    • 1942541312 scopus 로고    scopus 로고
    • Simultaneous characterization of the reductive unfolding pathways of RNase B isoforms by top-down mass spectrometry
    • Xu G, Zhai H, Narayan M, McLafferty FW Scheraga HA (2004) Simultaneous characterization of the reductive unfolding pathways of RNase B isoforms by top-down mass spectrometry. Chem Biol 11, 517 524.
    • (2004) Chem Biol , vol.11 , pp. 517-524
    • Xu, G.1    Zhai, H.2    Narayan, M.3    McLafferty, F.W.4    Scheraga, H.A.5
  • 23
    • 0001804566 scopus 로고
    • Improved Fourier-transform ion-cyclotron-resonance mass spectrometry of large biomolecules
    • Beu S, Senko MW, Quinn JP McLafferty FW (1993) Improved Fourier-transform ion-cyclotron-resonance mass spectrometry of large biomolecules. J Am Soc Mass Spectrom 4, 190 192.
    • (1993) J Am Soc Mass Spectrom , vol.4 , pp. 190-192
    • Beu, S.1    Senko, M.W.2    Quinn, J.P.3    McLafferty, F.W.4
  • 25
    • 0000944563 scopus 로고    scopus 로고
    • Electron capture dissociation of multiply charged protein cations. a nonergodic process
    • Zubarev RA, Kelleher NL McLafferty FW (1998) Electron capture dissociation of multiply charged protein cations. A nonergodic process. J Am Chem Soc 120, 3265 3266.
    • (1998) J Am Chem Soc , vol.120 , pp. 3265-3266
    • Zubarev, R.A.1    Kelleher, N.L.2    McLafferty, F.W.3
  • 26
    • 0037398265 scopus 로고    scopus 로고
    • Plasma electron capture dissociation for the characterization of large proteins by top down mass spectrometry
    • Sze SK, Ge Y, Oh HB McLafferty FW (2003) Plasma electron capture dissociation for the characterization of large proteins by top down mass spectrometry. Anal Chem 75, 1599 1603.
    • (2003) Anal Chem , vol.75 , pp. 1599-1603
    • Sze, S.K.1    Ge, Y.2    Oh, H.B.3    McLafferty, F.W.4
  • 27
    • 0034667929 scopus 로고    scopus 로고
    • Activated ion electron capture dissociation for mass spectral sequencing of larger (42 kDa) proteins
    • Horn DM, Ge Y McLafferty FW (2000) Activated ion electron capture dissociation for mass spectral sequencing of larger (42 kDa) proteins. Anal Chem 72, 4778 4784.
    • (2000) Anal Chem , vol.72 , pp. 4778-4784
    • Horn, D.M.1    Ge, Y.2    McLafferty, F.W.3
  • 28
    • 0028774203 scopus 로고
    • Collisional activation of large multiply charged ions using Fourier transform mass spectrometry
    • Senko MW, Speir JP McLafferty FW (1994) Collisional activation of large multiply charged ions using Fourier transform mass spectrometry. Anal Chem 66, 2801 2808.
    • (1994) Anal Chem , vol.66 , pp. 2801-2808
    • Senko, M.W.1    Speir, J.P.2    McLafferty, F.W.3
  • 29
    • 0027997748 scopus 로고
    • Infrared multiphoton dissociation of large multiply charged ions for biomolecule sequencing
    • Little DP, Speir JP, Senko MW, O'Conner PB McLafferty FW (1994) Infrared multiphoton dissociation of large multiply charged ions for biomolecule sequencing. Anal Chem 66, 2809 2815.
    • (1994) Anal Chem , vol.66 , pp. 2809-2815
    • Little, D.P.1    Speir, J.P.2    Senko, M.W.3    O'Conner, P.B.4    McLafferty, F.W.5
  • 32
    • 26944438195 scopus 로고    scopus 로고
    • Recent developments in the ion/ion chemistry of high-mass multiply charged ions
    • Pitteri SJ McLuckey SA (2005) Recent developments in the ion/ion chemistry of high-mass multiply charged ions. Mass Spectrom Rev 24, 931 958.
    • (2005) Mass Spectrom Rev , vol.24 , pp. 931-958
    • Pitteri, S.J.1    McLuckey, S.A.2
  • 33
    • 34249022000 scopus 로고    scopus 로고
    • Implementation of electron-transfer dissociation on a hybrid linear ion trap-orbitrap mass spectrometer
    • McAlister GC, Phanstiel D, Good DM, Berggren WT Coon JJ (2007) Implementation of electron-transfer dissociation on a hybrid linear ion trap-orbitrap mass spectrometer. Anal Chem 79, 3525 3534.
    • (2007) Anal Chem , vol.79 , pp. 3525-3534
    • McAlister, G.C.1    Phanstiel, D.2    Good, D.M.3    Berggren, W.T.4    Coon, J.J.5
  • 34
    • 35848949043 scopus 로고    scopus 로고
    • Decoding protein modifications using top-down mass spectrometry
    • Siuti N Kelleher NL (2007) Decoding protein modifications using top-down mass spectrometry. Nat Methods 4, 817 821.
    • (2007) Nat Methods , vol.4 , pp. 817-821
    • Siuti, N.1    Kelleher, N.L.2
  • 36
    • 33749606981 scopus 로고    scopus 로고
    • Extending top-down mass spectrometry to proteins with masses >200 kDa
    • Han X, Jin M, Breuker K McLafferty FW (2006) Extending top-down mass spectrometry to proteins with masses >200 kDa. Science 314, 109 112.
    • (2006) Science , vol.314 , pp. 109-112
    • Han, X.1    Jin, M.2    Breuker, K.3    McLafferty, F.W.4
  • 37
    • 0032731855 scopus 로고    scopus 로고
    • Localization of O-glycosylation sites in peptides by electron capture dissociation in a Fourier transform mass spectrometer
    • Mirgorodskaya E, Roepstorff P Zubarev RA (1999) Localization of O-glycosylation sites in peptides by electron capture dissociation in a Fourier transform mass spectrometer. Anal Chem 71, 4431 4436.
    • (1999) Anal Chem , vol.71 , pp. 4431-4436
    • Mirgorodskaya, E.1    Roepstorff, P.2    Zubarev, R.A.3
  • 38
    • 0035173029 scopus 로고    scopus 로고
    • Phosphopeptide/phosphoprotein mapping by electron capture dissociation mass spectrometry
    • Shi SDH, Hemling ME, Carr SA, Horn DM, Lindh I McLafferty FW (2001) Phosphopeptide/phosphoprotein mapping by electron capture dissociation mass spectrometry. Anal Chem 73, 19 22.
    • (2001) Anal Chem , vol.73 , pp. 19-22
    • Shi, S.D.H.1    Hemling, M.E.2    Carr, S.A.3    Horn, D.M.4    Lindh, I.5    McLafferty, F.W.6
  • 42
    • 34249779529 scopus 로고    scopus 로고
    • Pervasive combinatorial modification of histone H3 in human cells
    • Garcia BA, Pesavento JJ, Mizzen CA Kelleher NL (2007) Pervasive combinatorial modification of histone H3 in human cells. Nat Methods 129, 487 489.
    • (2007) Nat Methods , vol.129 , pp. 487-489
    • Garcia, B.A.1    Pesavento, J.J.2    Mizzen, C.A.3    Kelleher, N.L.4
  • 44
    • 18744397503 scopus 로고    scopus 로고
    • Secondary and tertiary structures of gaseous protein ions characterized by electron capture dissociation mass spectrometry and photofragment spectroscopy
    • Oh HB, Breuker K, Sze SK, Ge Y, Carpenter BK McLafferty FW (2002) Secondary and tertiary structures of gaseous protein ions characterized by electron capture dissociation mass spectrometry and photofragment spectroscopy. Proc Natl Acad Sci USA 99, 15863 15868.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 15863-15868
    • Oh, H.B.1    Breuker, K.2    Sze, S.K.3    Ge, Y.4    Carpenter, B.K.5    McLafferty, F.W.6
  • 45
    • 23844466290 scopus 로고    scopus 로고
    • Multidimensional separations of ubiquitin conformers in the gas phase: Relating ion cross sections to H/D exchange measurements
    • Robinson EW Williams ER (2005) Multidimensional separations of ubiquitin conformers in the gas phase: relating ion cross sections to H/D exchange measurements. J Am Soc Mass Spectrom 16, 1427 1437.
    • (2005) J Am Soc Mass Spectrom , vol.16 , pp. 1427-1437
    • Robinson, E.W.1    Williams, E.R.2
  • 47
    • 33846444321 scopus 로고    scopus 로고
    • Resolution and structural transitions of elongated states of ubiquitin
    • Koeniger SL Clemmer DE (2007) Resolution and structural transitions of elongated states of ubiquitin. J Am Soc Mass Spectrom 18, 322 331.
    • (2007) J Am Soc Mass Spectrom , vol.18 , pp. 322-331
    • Koeniger, S.L.1    Clemmer, D.E.2
  • 48
    • 0037024186 scopus 로고    scopus 로고
    • Detailed unfolding and folding of gaseous ubiquitin ions characterized by electron capture dissociation
    • Breuker K, Oh HB, Horn DM, Cerda BA McLafferty FW (2002) Detailed unfolding and folding of gaseous ubiquitin ions characterized by electron capture dissociation. J Am Chem Soc 124, 6407 6420.
    • (2002) J Am Chem Soc , vol.124 , pp. 6407-6420
    • Breuker, K.1    Oh, H.B.2    Horn, D.M.3    Cerda, B.A.4    McLafferty, F.W.5
  • 49
    • 4744355031 scopus 로고    scopus 로고
    • Nonergodic and conformational control in electron capture dissociation of protein ions
    • Breuker K, Oh HB, Lin C, Carpenter BK McLafferty FW (2004) Nonergodic and conformational control in electron capture dissociation of protein ions. Proc Natl Acad Sci USA 101, 14011 14016.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 14011-14016
    • Breuker, K.1    Oh, H.B.2    Lin, C.3    Carpenter, B.K.4    McLafferty, F.W.5
  • 51
    • 33745303482 scopus 로고    scopus 로고
    • Investigating nonribosomal peptide and polyketide biosynthesis by direct detection of intermediates on >70 kDa polypeptides using Fourier-transform mass spectrometry
    • Hicks LM, Mazur MT, Miller LM, Dorrestein PC, Schnarr NA, Khosla C Kelleher NL (2006) Investigating nonribosomal peptide and polyketide biosynthesis by direct detection of intermediates on >70 kDa polypeptides using Fourier-transform mass spectrometry. Chembiochem 7, 904 907.
    • (2006) Chembiochem , vol.7 , pp. 904-907
    • Hicks, L.M.1    Mazur, M.T.2    Miller, L.M.3    Dorrestein, P.C.4    Schnarr, N.A.5    Khosla, C.6    Kelleher, N.L.7
  • 52
    • 24944510341 scopus 로고    scopus 로고
    • Consecutive ion activation for top down mass spectrometry: Improved protein sequencing by nozzle-skimmer dissociation
    • Zhai H, Han X, Breuker K McLafferty FW (2005) Consecutive ion activation for top down mass spectrometry: improved protein sequencing by nozzle-skimmer dissociation. Anal Chem 77, 5777 5784.
    • (2005) Anal Chem , vol.77 , pp. 5777-5784
    • Zhai, H.1    Han, X.2    Breuker, K.3    McLafferty, F.W.4
  • 53
    • 23744495939 scopus 로고    scopus 로고
    • The thermal unfolding of native cytochrome c in the transition from solution to gas phase probed by native electron capture dissociation
    • Breuker K McLafferty FW (2005) The thermal unfolding of native cytochrome c in the transition from solution to gas phase probed by native electron capture dissociation. Angew Chem Int Ed 44, 4911 4914.
    • (2005) Angew Chem Int Ed , vol.44 , pp. 4911-4914
    • Breuker, K.1    McLafferty, F.W.2
  • 54
    • 4043055054 scopus 로고    scopus 로고
    • Domain organization of Salmonella typhimurium formylglycinamide ribonucleotide amidotransferase revealed by X-ray crystallography
    • Anand R, Hoskins AA, Stubbe J Ealick SE (2004) Domain organization of Salmonella typhimurium formylglycinamide ribonucleotide amidotransferase revealed by X-ray crystallography. Biochemistry 43, 10328 10342.
    • (2004) Biochemistry , vol.43 , pp. 10328-10342
    • Anand, R.1    Hoskins, A.A.2    Stubbe, J.3    Ealick, S.E.4
  • 55
    • 0022615457 scopus 로고
    • Location of the interchain disulfide bonds of the fourth component of human complement (C4): Evidence based on the liberation of fragments secondary to thiol-disulfide interchange reactions
    • Seya T, Nagasawa S Atkinson JP (1986) Location of the interchain disulfide bonds of the fourth component of human complement (C4): evidence based on the liberation of fragments secondary to thiol-disulfide interchange reactions. J Immunol 136, 4152 4156.
    • (1986) J Immunol , vol.136 , pp. 4152-4156
    • Seya, T.1    Nagasawa, S.2    Atkinson, J.P.3
  • 57
    • 32444436985 scopus 로고    scopus 로고
    • Top down approaches for measuring expression ratios of intact yeast proteins using Fourier-transform mass spectrometry
    • Du Y, Parks BA, Sohn S, Kwast KE Kelleher NL (2006) Top down approaches for measuring expression ratios of intact yeast proteins using Fourier-transform mass spectrometry. Anal Chem 78, 686 694.
    • (2006) Anal Chem , vol.78 , pp. 686-694
    • Du, Y.1    Parks, B.A.2    Sohn, S.3    Kwast, K.E.4    Kelleher, N.L.5
  • 60
    • 32344453899 scopus 로고    scopus 로고
    • Mass spectrometric characterization of human histone H3: A bird's eye view
    • Thomas CE, Mizzen CA Kelleher NL (2006) Mass spectrometric characterization of human histone H3: a bird's eye view. J Proteome Res 5, 240 247.
    • (2006) J Proteome Res , vol.5 , pp. 240-247
    • Thomas, C.E.1    Mizzen, C.A.2    Kelleher, N.L.3
  • 61
    • 34948821302 scopus 로고    scopus 로고
    • Global assessment of combinatorial post-translational modification of core histones in yeast using contemporary mass spectrometry. LYS4 trimethylation correlates with degree of acetylation on the same H3 tail
    • Jiang L, Smith JN, Anderson SL, Ma P, Mizzen CA Kelleher NL (2007) Global assessment of combinatorial post-translational modification of core histones in yeast using contemporary mass spectrometry. LYS4 trimethylation correlates with degree of acetylation on the same H3 tail. J Biol Chem 21, 27923 27934.
    • (2007) J Biol Chem , vol.21 , pp. 27923-27934
    • Jiang, L.1    Smith, J.N.2    Anderson, S.L.3    Ma, P.4    Mizzen, C.A.5    Kelleher, N.L.6
  • 62
    • 34447535180 scopus 로고    scopus 로고
    • Incorporation of nonmethyl branches by isoprenoid-like logic: Multiple beta-alkylation events in the biosynthesis of myxovirescin A1
    • Calderone CT, Iwig DF, Dorrestein PC, Kelleher NL Walsh CT (2007) Incorporation of nonmethyl branches by isoprenoid-like logic: multiple beta-alkylation events in the biosynthesis of myxovirescin A1. Chem Biol 14, 835 846.
    • (2007) Chem Biol , vol.14 , pp. 835-846
    • Calderone, C.T.1    Iwig, D.F.2    Dorrestein, P.C.3    Kelleher, N.L.4    Walsh, C.T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.