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Volumn 85, Issue 16, 2013, Pages 7809-7817

In-source decay during matrix-assisted laser desorption/ionization combined with the collisional process in an FTICR mass spectrometer

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID RESIDUES; COLLISIONAL PROCESS; FOURIER TRANSFORM ION CYCLOTRON RESONANCE; IMAGING EXPERIMENTS; INTERMEDIATE PRESSURES; LONG RESIDENCE TIME; MATRIX ASSISTED LASER DESORPTION/IONIZATION; SEQUENCING OF PEPTIDES;

EID: 84882699306     PISSN: 00032700     EISSN: 15206882     Source Type: Journal    
DOI: 10.1021/ac401234q     Document Type: Article
Times cited : (26)

References (43)
  • 1
    • 0029397704 scopus 로고
    • Sequence-specific fragmentation of matrix-assisted laser-desorbed protein/peptide ions
    • Brown, R. S.; Lennon, J. J. Sequence-specific fragmentation of matrix-assisted laser-desorbed protein/peptide ions Anal. Chem. 1995, 67, 3990-3999
    • (1995) Anal. Chem. , vol.67 , pp. 3990-3999
    • Brown, R.S.1    Lennon, J.J.2
  • 2
    • 34548014772 scopus 로고    scopus 로고
    • Protein sequence information by matrix-assisted laser desorption/ionization in-source decay mass spectrometry
    • Hardouin, J. Protein sequence information by matrix-assisted laser desorption/ionization in-source decay mass spectrometry Mass Spectrom. Rev. 2007, 26, 672-682
    • (2007) Mass Spectrom. Rev. , vol.26 , pp. 672-682
    • Hardouin, J.1
  • 3
    • 0032519109 scopus 로고    scopus 로고
    • Identifying proteins using matrix-assisted laser desorption/ionization in-source fragmentation data combined with database searching
    • Reiber, D. C.; Grover, T. A.; Brown, R. S. Identifying proteins using matrix-assisted laser desorption/ionization in-source fragmentation data combined with database searching Anal. Chem. 1998, 70, 673-683
    • (1998) Anal. Chem. , vol.70 , pp. 673-683
    • Reiber, D.C.1    Grover, T.A.2    Brown, R.S.3
  • 4
    • 0032531567 scopus 로고    scopus 로고
    • Applications of in-source fragmentation of protein ions for direct sequence analysis by delayed extraction MALDI-TOF mass spectrometry
    • Katta, V.; Chow, D. T.; Rohde, M. F. Applications of in-source fragmentation of protein ions for direct sequence analysis by delayed extraction MALDI-TOF mass spectrometry Anal. Chem. 1998, 70, 4410-4416
    • (1998) Anal. Chem. , vol.70 , pp. 4410-4416
    • Katta, V.1    Chow, D.T.2    Rohde, M.F.3
  • 5
    • 0030704702 scopus 로고    scopus 로고
    • Direct sequence analysis of proteins by in-source fragmentation during delayed ion extraction
    • Lennon, J. J.; Walsh, K. A. Direct sequence analysis of proteins by in-source fragmentation during delayed ion extraction Protein Sci. 1997, 6, 2446-2453
    • (1997) Protein Sci. , vol.6 , pp. 2446-2453
    • Lennon, J.J.1    Walsh, K.A.2
  • 6
    • 77952503261 scopus 로고    scopus 로고
    • MALDI-in source decay applied to mass spectrometry imaging: A new tool for protein identification
    • Debois, D.; Bertrand, V.; Quinton, L.; De Pauw-Gillet, M.-C.; De Pauw, E. MALDI-in source decay applied to mass spectrometry imaging: A new tool for protein identification Anal. Chem. 2010, 82, 4036-4045
    • (2010) Anal. Chem. , vol.82 , pp. 4036-4045
    • Debois, D.1    Bertrand, V.2    Quinton, L.3    De Pauw-Gillet, M.-C.4    De Pauw, E.5
  • 9
    • 0035563598 scopus 로고    scopus 로고
    • α bond cleavage of the peptide backbone via hydrogen abstraction
    • α bond cleavage of the peptide backbone via hydrogen abstraction J. Am. Soc. Mass Spectrom. 2001, 12, 1044-1049
    • (2001) J. Am. Soc. Mass Spectrom. , vol.12 , pp. 1044-1049
    • Takayama, M.1
  • 10
    • 11844304974 scopus 로고    scopus 로고
    • Fragmentation of peptides in MALDI in-source decay mediated by hydrogen radicals
    • Köcher, T.; Engström, Å.; Zubarev, R. A. Fragmentation of peptides in MALDI in-source decay mediated by hydrogen radicals Anal. Chem. 2005, 77, 172-177
    • (2005) Anal. Chem. , vol.77 , pp. 172-177
    • Köcher, T.1    Engström, Å.2    Zubarev, R.A.3
  • 11
    • 84874589400 scopus 로고    scopus 로고
    • Ultraviolet laser induced hydrogen transfer reaction: Study of the first step of MALDI in-source decay mass spectrometry
    • Asakawa, D.; Calligaris, D.; Smargiasso, N.; De Pauw, E. Ultraviolet laser induced hydrogen transfer reaction: Study of the first step of MALDI in-source decay mass spectrometry J. Phys. Chem. B 2013, 117, 2321-2327
    • (2013) J. Phys. Chem. B , vol.117 , pp. 2321-2327
    • Asakawa, D.1    Calligaris, D.2    Smargiasso, N.3    De Pauw, E.4
  • 12
    • 0035566768 scopus 로고    scopus 로고
    • In-source decay characteristics of peptides in matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Takayama, M. In-source decay characteristics of peptides in matrix-assisted laser desorption/ionization time-of-flight mass spectrometry J. Am. Soc. Mass Spectrom. 2001, 12, 420-427
    • (2001) J. Am. Soc. Mass Spectrom. , vol.12 , pp. 420-427
    • Takayama, M.1
  • 13
    • 84860569521 scopus 로고    scopus 로고
    • 2-Aminobenzamide and 2-aminobenzoic acid as new MALDI matrices inducing radical mediated in-source decay of peptides and proteins
    • Smargiasso, N.; Quinton, L.; De Pauw, E. 2-Aminobenzamide and 2-aminobenzoic acid as new MALDI matrices inducing radical mediated in-source decay of peptides and proteins J. Am. Soc. Mass Spectrom. 2012, 23, 469-474
    • (2012) J. Am. Soc. Mass Spectrom. , vol.23 , pp. 469-474
    • Smargiasso, N.1    Quinton, L.2    De Pauw, E.3
  • 14
    • 32944469447 scopus 로고    scopus 로고
    • Rapid sequencing and disulfide mapping of peptides containing disulfide bonds by using 1,5-diaminonaphthalene as a reductive matrix
    • Fukuyama, Y.; Iwamoto, S.; Tanaka, K. Rapid sequencing and disulfide mapping of peptides containing disulfide bonds by using 1,5-diaminonaphthalene as a reductive matrix J. Mass Spectrom. 2006, 41, 191-201
    • (2006) J. Mass Spectrom. , vol.41 , pp. 191-201
    • Fukuyama, Y.1    Iwamoto, S.2    Tanaka, K.3
  • 15
    • 36448947243 scopus 로고    scopus 로고
    • Rational selection of the optimum MALDI matrix for top-down proteomics by in-source decay
    • Demeure, K.; Quinton, L.; Gabelica, V.; De Pauw, E. Rational selection of the optimum MALDI matrix for top-down proteomics by in-source decay Anal. Chem. 2007, 79, 8678-8685
    • (2007) Anal. Chem. , vol.79 , pp. 8678-8685
    • Demeure, K.1    Quinton, L.2    Gabelica, V.3    De Pauw, E.4
  • 16
    • 34548167855 scopus 로고    scopus 로고
    • New method for characterizing highly disulfide-bridged peptides in complex mixtures: Application to toxin identification from crude venoms
    • Quinton, L.; Demeure, K.; Dobson, R.; Gilles, N.; Gabelica, V.; De Pauw, E. New method for characterizing highly disulfide-bridged peptides in complex mixtures: Application to toxin identification from crude venoms J. Proteome Res. 2007, 6, 3216-3223
    • (2007) J. Proteome Res. , vol.6 , pp. 3216-3223
    • Quinton, L.1    Demeure, K.2    Dobson, R.3    Gilles, N.4    Gabelica, V.5    De Pauw, E.6
  • 17
    • 84874612107 scopus 로고    scopus 로고
    • Discrimination of isobaric Leu/Ile residues by MALDI in-source decay mass spectrometry
    • Asakawa, D.; Smargiasso, N.; De Pauw, E. Discrimination of isobaric Leu/Ile residues by MALDI in-source decay mass spectrometry J. Am. Soc. Mass Spectrom. 2013, 24, 197-200
    • (2013) J. Am. Soc. Mass Spectrom. , vol.24 , pp. 197-200
    • Asakawa, D.1    Smargiasso, N.2    De Pauw, E.3
  • 18
    • 0037445356 scopus 로고    scopus 로고
    • On the formation of initial ion velocities in matrix-assisted laser desorption ionization: Virtual desorption time as an additional parameter describing ion ejection dynamics
    • Spengler, B.; Kirsch, D. On the formation of initial ion velocities in matrix-assisted laser desorption ionization: Virtual desorption time as an additional parameter describing ion ejection dynamics Int. J. Mass Spectrom. 2003, 226, 71-83
    • (2003) Int. J. Mass Spectrom. , vol.226 , pp. 71-83
    • Spengler, B.1    Kirsch, D.2
  • 19
    • 0042478301 scopus 로고    scopus 로고
    • The initial ion velocity and its dependence on matrix, analyte and preparation method in ultraviolet matrix-assisted laser desorption / ionization
    • Glückmann, M.; Karas, M. The initial ion velocity and its dependence on matrix, analyte and preparation method in ultraviolet matrix-assisted laser desorption / ionization J. Mass Spectrom. 1999, 34, 467-477
    • (1999) J. Mass Spectrom. , vol.34 , pp. 467-477
    • Glückmann, M.1    Karas, M.2
  • 20
    • 0037445412 scopus 로고    scopus 로고
    • The initial-ion velocity as a marker for different desorption-ionization mechanisms in MALDI
    • Karas, M.; Bahr, U.; Fournier, I.; Glückmann, M.; Pfenninger, A. The initial-ion velocity as a marker for different desorption-ionization mechanisms in MALDI Int. J. Mass Spectrom. 2003, 226, 239-248
    • (2003) Int. J. Mass Spectrom. , vol.226 , pp. 239-248
    • Karas, M.1    Bahr, U.2    Fournier, I.3    Glückmann, M.4    Pfenninger, A.5
  • 21
    • 84875125078 scopus 로고    scopus 로고
    • Peptide backbone fragmentation initiated by side-chain loss at cysteine residue in matrix-assisted laser desorption/ionization in-source decay mass spectrometry
    • Asakawa, D.; Smargiasso, N.; Quinton, L.; De Pauw, E. Peptide backbone fragmentation initiated by side-chain loss at cysteine residue in matrix-assisted laser desorption/ionization in-source decay mass spectrometry J. Mass Spectrom. 2013, 48, 352-360
    • (2013) J. Mass Spectrom. , vol.48 , pp. 352-360
    • Asakawa, D.1    Smargiasso, N.2    Quinton, L.3    De Pauw, E.4
  • 22
    • 0032531567 scopus 로고    scopus 로고
    • Applications of in-source fragmentation of protein ions for direct sequence analysis by delayed extraction MALDI-TOF mass spectrometry
    • Katta, V.; Chow, D. T.; Rohde, M. F. Applications of in-source fragmentation of protein ions for direct sequence analysis by delayed extraction MALDI-TOF mass spectrometry Anal. Chem. 1998, 70, 4410-4416
    • (1998) Anal. Chem. , vol.70 , pp. 4410-4416
    • Katta, V.1    Chow, D.T.2    Rohde, M.F.3
  • 23
    • 70350639277 scopus 로고    scopus 로고
    • In-source fragmentation of very labile peptides in matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Sachon, E.; Clodic, G.; Blasco, T.; Jacquot, Y.; Bolbach, G. In-source fragmentation of very labile peptides in matrix-assisted laser desorption/ionization time-of-flight mass spectrometry Anal. Chem. 2009, 81, 8986-8992
    • (2009) Anal. Chem. , vol.81 , pp. 8986-8992
    • Sachon, E.1    Clodic, G.2    Blasco, T.3    Jacquot, Y.4    Bolbach, G.5
  • 24
    • 73249149948 scopus 로고    scopus 로고
    • Ammonium sulfate and MALDI in-source decay: A winning combination for sequencing peptides
    • Delvolve, A.; Woods, A. S. Ammonium sulfate and MALDI in-source decay: A winning combination for sequencing peptides Anal. Chem. 2009, 81, 9585-9589
    • (2009) Anal. Chem. , vol.81 , pp. 9585-9589
    • Delvolve, A.1    Woods, A.S.2
  • 25
    • 84876212031 scopus 로고    scopus 로고
    • Comparison between enhanced MALDI in-source decay by ammonium persulfate and N-or C-terminal derivatization methods for detailed peptide structure determination
    • Horvatic, A.; Dodig, I.; Vuletic, T.; Pavokovic, D.; Hamersak, Z.; Butorac, A.; Cindric, M. Comparison between enhanced MALDI in-source decay by ammonium persulfate and N-or C-terminal derivatization methods for detailed peptide structure determination Anal. Chem. 2013, 85, 3940-3947
    • (2013) Anal. Chem. , vol.85 , pp. 3940-3947
    • Horvatic, A.1    Dodig, I.2    Vuletic, T.3    Pavokovic, D.4    Hamersak, Z.5    Butorac, A.6    Cindric, M.7
  • 26
    • 65249140527 scopus 로고    scopus 로고
    • Effect of gas pressure and gas type on the fragmentation of peptide and oligosaccharide ions generated in an elevated pressure UV/IR-MALDI ion source coupled to an orthogonal time-of-flight mass spectrometer
    • Soltwisch, J.; Souady, J.; Berkenkamp, S.; Dreisewerd, K. Effect of gas pressure and gas type on the fragmentation of peptide and oligosaccharide ions generated in an elevated pressure UV/IR-MALDI ion source coupled to an orthogonal time-of-flight mass spectrometer Anal. Chem. 2009, 81, 2921-2934
    • (2009) Anal. Chem. , vol.81 , pp. 2921-2934
    • Soltwisch, J.1    Souady, J.2    Berkenkamp, S.3    Dreisewerd, K.4
  • 27
    • 77954182561 scopus 로고    scopus 로고
    • Discrimination of isobaric leucine and isoleucine residues and analysis of post-translational modifications in peptides by MALDI in-source decay mass spectrometry combined with collisional cooling
    • Soltwisch, J.; Dreisewerd, K. Discrimination of isobaric leucine and isoleucine residues and analysis of post-translational modifications in peptides by MALDI in-source decay mass spectrometry combined with collisional cooling Anal. Chem. 2010, 82, 5628-5635
    • (2010) Anal. Chem. , vol.82 , pp. 5628-5635
    • Soltwisch, J.1    Dreisewerd, K.2
  • 28
    • 0031623267 scopus 로고    scopus 로고
    • Fourier transform ion cyclotron resonance mass spectrometry: A primer
    • Marshall, A. G.; Hendrickson, C. L.; Jackson, G. S. Fourier transform ion cyclotron resonance mass spectrometry: A primer Mass.Spectrom. Rev. 1998, 17, 1-35
    • (1998) Mass.Spectrom. Rev. , vol.17 , pp. 1-35
    • Marshall, A.G.1    Hendrickson, C.L.2    Jackson, G.S.3
  • 30
    • 79960367713 scopus 로고    scopus 로고
    • Matrix sublimation/recrystallization for imaging proteins by mass spectrometry at high spatial resolution
    • Yang, J.; Caprioli, R. M. Matrix sublimation/recrystallization for imaging proteins by mass spectrometry at high spatial resolution Anal. Chem. 2011, 83, 5728-5734
    • (2011) Anal. Chem. , vol.83 , pp. 5728-5734
    • Yang, J.1    Caprioli, R.M.2
  • 31
    • 0038610834 scopus 로고    scopus 로고
    • Reactions of polypeptide ions with electrons in the gas phase
    • Zubarev, R. A. Reactions of polypeptide ions with electrons in the gas phase Mass Spectrom. Rev. 2003, 22, 57-77
    • (2003) Mass Spectrom. Rev. , vol.22 , pp. 57-77
    • Zubarev, R.A.1
  • 32
    • 77958159767 scopus 로고    scopus 로고
    • New advances in the understanding of the in-source decay fragmentation of peptides in MALDI-TOF-MS
    • Demeure, K.; Gabelica, V.; De Pauw, E. New advances in the understanding of the in-source decay fragmentation of peptides in MALDI-TOF-MS J. Am. Soc. Mass Spectrom. 2010, 21, 1906-1917
    • (2010) J. Am. Soc. Mass Spectrom. , vol.21 , pp. 1906-1917
    • Demeure, K.1    Gabelica, V.2    De Pauw, E.3
  • 33
    • 32044464509 scopus 로고    scopus 로고
    • Cooperative effect of factors governing molecular ion yields in desorption/ionization mass spectrometry
    • Nishikaze, T.; Takayama, M. Cooperative effect of factors governing molecular ion yields in desorption/ionization mass spectrometry Rapid Commun. Mass Spectrom. 2006, 20, 376-382
    • (2006) Rapid Commun. Mass Spectrom. , vol.20 , pp. 376-382
    • Nishikaze, T.1    Takayama, M.2
  • 34
    • 0029810698 scopus 로고    scopus 로고
    • Influence of peptide composition, gas-phase basicity, and chemical modification on fragmentation efficiency: Evidence for the mobile proton model
    • Dongré, A. R.; Jones, J. L.; Somogyi, á.; Wysocki, V. H. Influence of peptide composition, gas-phase basicity, and chemical modification on fragmentation efficiency: Evidence for the mobile proton model J. Am. Chem. Soc. 1996, 118, 8365-8374
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 8365-8374
    • Dongré, A.R.1    Jones, J.L.2    Somogyi, Á.3    Wysocki, V.H.4
  • 35
    • 21844457685 scopus 로고    scopus 로고
    • Fragmentation pathways of protonated peptides
    • Paizs, B.; Suhai, S. Fragmentation pathways of protonated peptides Mass Spectrom. Rev. 2005, 24, 508-548
    • (2005) Mass Spectrom. Rev. , vol.24 , pp. 508-548
    • Paizs, B.1    Suhai, S.2
  • 36
    • 0001595008 scopus 로고
    • The effect of protonation site on bond strengths in simple peptides: Application of ab initio and modified neglect of differential overlap bond orders and modified neglect of differential overlap energy partitioning
    • Somogyi, á.; Wysocki, V. H.; Mayer, I. The effect of protonation site on bond strengths in simple peptides: Application of ab initio and modified neglect of differential overlap bond orders and modified neglect of differential overlap energy partitioning J. Am. Soc. Mass Spectrom. 1994, 5, 704-717
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 704-717
    • Somogyi, Á.1    Wysocki, V.H.2    Mayer, I.3
  • 37
    • 0028555378 scopus 로고
    • Ab initio studies of neutral and protonated triglycines: Comparison of calculated and experimental gas-phase basicity
    • Zhang, K.; Cassady, C. J.; Chung-Phillips, A. Ab initio studies of neutral and protonated triglycines: Comparison of calculated and experimental gas-phase basicity J. Am. Chem. Soc. 1994, 116, 11512-11521
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 11512-11521
    • Zhang, K.1    Cassady, C.J.2    Chung-Phillips, A.3
  • 38
    • 79959919729 scopus 로고    scopus 로고
    • α-C bond cleavage of the peptide backbone in maldi in-source decay using salicylic acid derivative matrices
    • α-C bond cleavage of the peptide backbone in maldi in-source decay using salicylic acid derivative matrices J. Am. Soc. Mass Spectrom. 2011, 22, 1224-1233
    • (2011) J. Am. Soc. Mass Spectrom. , vol.22 , pp. 1224-1233
    • Asakawa, D.1    Takayama, M.2
  • 39
    • 84859576031 scopus 로고    scopus 로고
    • Fragmentation processes of hydrogen-deficient peptide radicals in matrix-assisted laser desorption/ionization in-source decay mass spectrometry
    • Asakawa, D.; Takayama, M. Fragmentation processes of hydrogen-deficient peptide radicals in matrix-assisted laser desorption/ionization in-source decay mass spectrometry J. Phys. Chem. B 2012, 116, 4016-4023
    • (2012) J. Phys. Chem. B , vol.116 , pp. 4016-4023
    • Asakawa, D.1    Takayama, M.2
  • 40
    • 0032725664 scopus 로고    scopus 로고
    • Locating and identifying posttranslational modifications by in-source decay during MALDI-TOF mass spectrometry
    • Lennon, J. J.; Walsh, K. A. Locating and identifying posttranslational modifications by in-source decay during MALDI-TOF mass spectrometry Protein Sci. 1999, 8, 2487-2493
    • (1999) Protein Sci. , vol.8 , pp. 2487-2493
    • Lennon, J.J.1    Walsh, K.A.2
  • 41
    • 79959242453 scopus 로고    scopus 로고
    • Top-down sequencing of O-glycoproteins by in-source decay matrix-assisted laser desorption ionization mass spectrometry for glycosylation site analysis
    • Hanisch., F.-G. Top-down sequencing of O-glycoproteins by in-source decay matrix-assisted laser desorption ionization mass spectrometry for glycosylation site analysis Anal. Chem. 2011, 83, 4829-4837
    • (2011) Anal. Chem. , vol.83 , pp. 4829-4837
    • Hanisch, F.-G.1
  • 42
    • 67649213067 scopus 로고    scopus 로고
    • Phosphopeptide fragmentation and analysis by mass spectrometry
    • Boersema, P. J.; Mohammed, S.; Heck, A. J. R. Phosphopeptide fragmentation and analysis by mass spectrometry J. Mass Spectrom. 2009, 44, 861-878
    • (2009) J. Mass Spectrom. , vol.44 , pp. 861-878
    • Boersema, P.J.1    Mohammed, S.2    Heck, A.J.R.3


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