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Volumn 32, Issue 4, 2013, Pages 257-268

Mass spectrometry-based strategies for protein disulfide bond identification

Author keywords

Disulfide bond; Mass spectrometry; Protein pharmaceuticals

Indexed keywords


EID: 84888273200     PISSN: 07930135     EISSN: None     Source Type: Journal    
DOI: 10.1515/revac-2013-0011     Document Type: Article
Times cited : (38)

References (93)
  • 1
    • 0029890570 scopus 로고    scopus 로고
    • Electrospray ionization and matrix assisted laser desorption/ionization mass spectrometry: Powerful analytical tools in recombinant protein chemistry
    • Andersen, J. S.; Svensson, B.; Roepstorff, P. Electrospray ionization and matrix assisted laser desorption/ionization mass spectrometry: powerful analytical tools in recombinant protein chemistry. Nat. Biotechnol. 1996, 14, 449-457.
    • (1996) Nat. Biotechnol. , vol.14 , pp. 449-457
    • Andersen, J.S.1    Svensson, B.2    Roepstorff, P.3
  • 2
    • 33745684811 scopus 로고    scopus 로고
    • Electron capture dissociation mass spectrometry in characterization of peptides and proteins
    • Bakhtiar, R.; Guan, Z. Electron capture dissociation mass spectrometry in characterization of peptides and proteins. Biotechnol. Lett. 2006, 28, 1047-1059.
    • (2006) Biotechnol. Lett. , vol.28 , pp. 1047-1059
    • Bakhtiar, R.1    Guan, Z.2
  • 3
    • 0035416831 scopus 로고    scopus 로고
    • Overalkylation of a protein digest with iodoacetamide
    • Boja, E. S.; Fales, H. M. Overalkylation of a protein digest with iodoacetamide. Anal. Chem. 2001, 73, 3576-3582.
    • (2001) Anal. Chem. , vol.73 , pp. 3576-3582
    • Boja, E.S.1    Fales, H.M.2
  • 4
    • 67650754060 scopus 로고    scopus 로고
    • Mass measurement and top-down hplc/ms analysis of intact monoclonal antibodies on a hybrid linear quadrupole ion trap-orbitrap mass spectrometer
    • Bondarenko, P. V.; Second, T. P.; Zabrouskov, V.; Makarov, A. A.; Zhang, Z. Mass measurement and top-down HPLC/MS analysis of intact monoclonal antibodies on a hybrid linear quadrupole ion trap-orbitrap mass spectrometer. J. Am. Soc. Mass. Spectrom. 2009, 20, 1415-1424.
    • (2009) J. Am. Soc. Mass. Spectrom. , vol.20 , pp. 1415-1424
    • Bondarenko, P.V.1    Second, T.P.2    Zabrouskov, V.3    Makarov, A.A.4    Zhang, Z.5
  • 5
    • 0000836690 scopus 로고
    • Evidence for possible nonspecific reactions between n-ethylmaleimide and proteins
    • Brewer, C. F.; Riehm, J. P. Evidence for possible nonspecific reactions between n-ethylmaleimide and proteins. Anal. Biochem. 1967, 18, 248-255.
    • (1967) Anal. Biochem. , vol.18 , pp. 248-255
    • Brewer, C.F.1    Riehm, J.P.2
  • 7
    • 33750313493 scopus 로고    scopus 로고
    • Reversed-phase liquid chromatography in-line with negative ionization electrospray mass spectrometry for the characterization of the disulfide-linkages of an immunoglobulin gamma antibody
    • Chelius, D.; Wimer, M. E. H.; Bondareriko, P. V. Reversed-phase liquid chromatography in-line with negative ionization electrospray mass spectrometry for the characterization of the disulfide-linkages of an immunoglobulin gamma antibody. J. Am. Soc. Mass. Spectrom. 2006, 17, 1590-1598.
    • (2006) J. Am. Soc. Mass. Spectrom. , vol.17 , pp. 1590-1598
    • Chelius, D.1    Wimer, M.E.H.2    Bondareriko, P.V.3
  • 8
    • 73649112404 scopus 로고    scopus 로고
    • New algorithm for the identification of intact disulfide linkages based on fragmentation characteristics in tandem mass spectra
    • Choi, S.; Jeong, J.; Na, S.; Lee, H. S.; Kim, H. Y.; Lee, K. J.; Paek, E. New algorithm for the identification of intact disulfide linkages based on fragmentation characteristics in tandem mass spectra. J. Proteome Res. 2010, 9, 626-635.
    • (2010) J. Proteome Res. , vol.9 , pp. 626-635
    • Choi, S.1    Jeong, J.2    Na, S.3    Lee, H.S.4    Kim, H.Y.5    Lee, K.J.6    Paek, E.7
  • 9
    • 0037085393 scopus 로고    scopus 로고
    • Disulfide bond assignments of secreted frizzled-related protein-1 provide insights about frizzled homology and netrin modules
    • Chong, J. M.; Uren, A.; Rubin, J. S.; Speicher, D. W. Disulfide bond assignments of secreted frizzled-related protein-1 provide insights about frizzled homology and netrin modules. J. Biol. Chem. 2002, 277, 5134-5144.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5134-5144
    • Chong, J.M.1    Uren, A.2    Rubin, J.S.3    Speicher, D.W.4
  • 10
    • 0036874397 scopus 로고    scopus 로고
    • Dissociations of disulfide-linked gaseous polypeptide/protein anions: Ion chemistry with implications for protein identification and characterization
    • Chrisman, P. A.; McLuckey, S. A. Dissociations of disulfide-linked gaseous polypeptide/protein anions: Ion chemistry with implications for protein identification and characterization. J. Proteome Res. 2002, 1, 549-557.
    • (2002) J. Proteome Res. , vol.1 , pp. 549-557
    • Chrisman, P.A.1    McLuckey, S.A.2
  • 11
    • 20444465142 scopus 로고    scopus 로고
    • So2 - Electron transfer ion/ion reactions with disulfide linked polypeptide ions
    • Chrisman, P. A.; Pitteri, S. J.; Hogan, J. M.; McLuckey, S. A. So2 - electron transfer ion/ion reactions with disulfide linked polypeptide ions. J. Am. Soc. Mass. Spectrom. 2005, 16, 1020-1030.
    • (2005) J. Am. Soc. Mass. Spectrom. , vol.16 , pp. 1020-1030
    • Chrisman, P.A.1    Pitteri, S.J.2    Hogan, J.M.3    McLuckey, S.A.4
  • 12
    • 79955757738 scopus 로고    scopus 로고
    • Collision induced dissociation products of disulfide-bonded peptides: Ions result from the cleavage of more than one bond
    • Clark, D. F.; Go, E. P.; Toumi, M. L.; Desaire, H. Collision induced dissociation products of disulfide-bonded peptides: ions result from the cleavage of more than one bond. J. Am. Soc. Mass. Spectrom. 2011, 22, 492-498.
    • (2011) J. Am. Soc. Mass. Spectrom. , vol.22 , pp. 492-498
    • Clark, D.F.1    Go, E.P.2    Toumi, M.L.3    Desaire, H.4
  • 13
    • 84863072274 scopus 로고    scopus 로고
    • Electron transfer dissociation (etd) of peptides containing intrachain disulfide bonds
    • Cole, S. R.; Ma, X. X.; Zhang, X. R.; Xia, Y. Electron transfer dissociation (ETD) of peptides containing intrachain disulfide bonds. J. Am. Soc. Mass. Spectrom. 2012, 23, 310-320.
    • (2012) J. Am. Soc. Mass. Spectrom. , vol.23 , pp. 310-320
    • Cole, S.R.1    Ma, X.X.2    Zhang, X.R.3    Xia, Y.4
  • 14
    • 0028906033 scopus 로고
    • Facile, in-situ matrix-assisted laser-desorption ionization mass-spectrometry analysis and assignment of disulfide pairings in heteropeptide molecules
    • Crimmins, D. L.; Saylor, M.; Rush, J.; Thoma, R. S. Facile, in-situ matrix-assisted laser-desorption ionization mass-spectrometry analysis and assignment of disulfide pairings in heteropeptide molecules. Anal. Biochem. 1995, 226, 355-361.
    • (1995) Anal. Biochem. , vol.226 , pp. 355-361
    • Crimmins, D.L.1    Saylor, M.2    Rush, J.3    Thoma, R.S.4
  • 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
  • 17
    • 0027562690 scopus 로고
    • In situ reduction suitable for matrix-assisted laser desorption ionization and liquid secondary ionization using tris(2-carboxyethyl)phosphine
    • Fischer, W. H.; Rivier, J. E.; Craig, A. G. In situ reduction suitable for matrix-assisted laser desorption ionization and liquid secondary ionization using tris(2-carboxyethyl)phosphine. Rapid Commun. Mass Spectrom. 1993, 7, 225-228.
    • (1993) Rapid Commun. Mass Spectrom. , vol.7 , pp. 225-228
    • Fischer, W.H.1    Rivier, J.E.2    Craig, A.G.3
  • 18
    • 42649119769 scopus 로고    scopus 로고
    • Picomole-level mapping of protein disulfides by mass spectrometry following partial reduction and alkylation
    • Foley, S. F.; Sun, Y.; Zheng, T. S.; Wen, D. Picomole-level mapping of protein disulfides by mass spectrometry following partial reduction and alkylation. Anal. Biochem. 2008, 377, 95-104.
    • (2008) Anal. Biochem. , vol.377 , pp. 95-104
    • Foley, S.F.1    Sun, Y.2    Zheng, T.S.3    Wen, D.4
  • 19
    • 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
  • 20
    • 0034946628 scopus 로고    scopus 로고
    • Alkylation kinetics of proteins in preparation for two-dimensional maps: A matrix assisted laser desorption/ionization-mass spectrometry investigation
    • Galvani, M.; Hamdan, M.; Herbert, B.; Righetti, P. G. Alkylation kinetics of proteins in preparation for two-dimensional maps: A matrix assisted laser desorption/ionization-mass spectrometry investigation. Electrophoresis 2001, 22, 2058-2065.
    • (2001) Electrophoresis , vol.22 , pp. 2058-2065
    • Galvani, M.1    Hamdan, M.2    Herbert, B.3    Righetti, P.G.4
  • 21
    • 33645682750 scopus 로고    scopus 로고
    • Pro-crosslink, Software tool for protein crosslinking and mass spectrometry
    • Gao, Q. X.; Xue, S.; Doneanu, C. E.; Shaffer, S. A.; Goodlett, D. R.; Nelson, S. D. Pro-crosslink. Software tool for protein crosslinking and mass spectrometry. Anal. Chem. 2006, 78, 2145-2149.
    • (2006) Anal. Chem. , vol.78 , pp. 2145-2149
    • Gao, Q.X.1    Xue, S.2    Doneanu, C.E.3    Shaffer, S.A.4    Goodlett, D.R.5    Nelson, S.D.6
  • 22
    • 79955403717 scopus 로고    scopus 로고
    • Analysis of the disulfide bond arrangement of the hiv-1 envelope protein con-s gp140 delta cfi shows variability in the v1 and v2 regions
    • Go, E. P.; Zhang, Y.; Menon, S.; Desaire, H. Analysis of the disulfide bond arrangement of the HIV-1 envelope protein CON-S gp140 delta CFI shows variability in the V1 and V2 regions. J. Proteome Res. 2011, 10, 578-591.
    • (2011) J. Proteome Res. , vol.10 , pp. 578-591
    • Go, E.P.1    Zhang, Y.2    Menon, S.3    Desaire, H.4
  • 23
    • 0036882287 scopus 로고    scopus 로고
    • Protein disulfide bond determination by mass spectrometry
    • Gorman, J. J.; Wallis, T. P.; Pitt, J. J. Protein disulfide bond determination by mass spectrometry. Mass Spectrom. Rev. 2002, 21, 183-216.
    • (2002) Mass Spectrom. Rev. , vol.21 , pp. 183-216
    • Gorman, J.J.1    Wallis, T.P.2    Pitt, J.J.3
  • 24
    • 0027448780 scopus 로고
    • Disulfide structures of highly bridged peptides - A new strategy for analysis
    • Gray, W. R. Disulfide structures of highly bridged peptides - A new strategy for analysis. Protein Sci. 1993, 2, 1732-1748.
    • (1993) Protein Sci , vol.2 , pp. 1732-1748
    • Gray, W.R.1
  • 25
    • 0000498985 scopus 로고
    • Nature of the amino acid residues involved in the inactivation of ribonuclease by iodoacetate
    • Gundlach, H. G.; Stein, W. H.; Moore, S. Nature of the amino acid residues involved in the inactivation of ribonuclease by iodoacetate. J. Biol. Chem. 1959, 234, 1754-1760.
    • (1959) J. Biol. Chem. , vol.234 , pp. 1754-1760
    • Gundlach, H.G.1    Stein, W.H.2    Moore, S.3
  • 26
    • 0027977003 scopus 로고
    • Direct assignment of disulfide bonds by edman degradation of selected peptidefragments
    • Haniu, M.; Acklin, C.; Kenney, W. C.; Rohde, M. F. Direct assignment of disulfide bonds by edman degradation of selected peptidefragments. Int. J. Pept. Protein Res. 1994, 43, 81-86.
    • (1994) Int. J. Pept. Protein Res. , vol.43 , pp. 81-86
    • Haniu, M.1    Acklin, C.2    Kenney, W.C.3    Rohde, M.F.4
  • 27
    • 69949093360 scopus 로고    scopus 로고
    • An introduction to methods for analyzing thiols and disulfides: Reactions, reagents, and practical considerations
    • Hansen, R. E.; Winther, J. R. An introduction to methods for analyzing thiols and disulfides: reactions, reagents, and practical considerations. Anal. Biochem. 2009, 394, 147-158.
    • (2009) Anal. Biochem. , vol.394 , pp. 147-158
    • Hansen, R.E.1    Winther, J.R.2
  • 28
    • 0031279764 scopus 로고    scopus 로고
    • The reduction of disulfide bonds in proteins at mercury electrodes
    • Honeychurch, M. J. The reduction of disulfide bonds in proteins at mercury electrodes. Bioelectrochem. Bioenerg. 1997, 44, 13-21.
    • (1997) Bioelectrochem. Bioenerg. , vol.44 , pp. 13-21
    • Honeychurch, M.J.1
  • 29
    • 0348014635 scopus 로고    scopus 로고
    • Stable-isotope dimethyl labeling for quantitative proteomics
    • Hsu, J. L.; Huang, S. Y.; Chow, N. H.; Chen, S. H. Stable-isotope dimethyl labeling for quantitative proteomics. Anal. Chem. 2003, 75, 6843-6852.
    • (2003) Anal. Chem. , vol.75 , pp. 6843-6852
    • Hsu, J.L.1    Huang, S.Y.2    Chow, N.H.3    Chen, S.H.4
  • 30
    • 14844331822 scopus 로고    scopus 로고
    • Beyond quantitative proteomics: Signal enhancement of the a(1) ion as a mass tag for peptide sequencing using dimethyl labeling
    • Hsu, J. L.; Huang, S. Y.; Shiea, J. T.; Huang, W. Y.; Chen, S. H. Beyond quantitative proteomics: signal enhancement of the a(1) ion as a mass tag for peptide sequencing using dimethyl labeling. J. Proteome Res. 2005, 4, 101-108.
    • (2005) J. Proteome Res. , vol.4 , pp. 101-108
    • Hsu, J.L.1    Huang, S.Y.2    Shiea, J.T.3    Huang, W.Y.4    Chen, S.H.5
  • 31
    • 57449086157 scopus 로고    scopus 로고
    • Assignment of disulfide-linked peptides using automatic a(1) ion recognition
    • Huang, S. Y.; Wen, C. H.; Li, D. T.; Hsu, J. L.; Chen, C.; Shi, F. K.; Lin, Y. Y. Assignment of disulfide-linked peptides using automatic a(1) ion recognition. Anal. Chem. 2008, 80, 9135-9140.
    • (2008) Anal. Chem. , vol.80 , pp. 9135-9140
    • Huang, S.Y.1    Wen, C.H.2    Li, D.T.3    Hsu, J.L.4    Chen, C.5    Shi, F.K.6    Lin, Y.Y.7
  • 32
    • 84861862180 scopus 로고    scopus 로고
    • Automatic disulfide bond assignment using a(1) ion screening by mass spectrometry for structural characterization of protein pharmaceuticals
    • Huang, S.-Y.; Hsieh, Y.-T.; Chen, C.-H.; Chen, C.-C.; Sung, W.-C.; Chou, M.-Y.; Chen, S.-F. Automatic disulfide bond assignment using a(1) ion screening by mass spectrometry for structural characterization of protein pharmaceuticals. Anal. Chem. 2012, 84, 4900-4906.
    • (2012) Anal. Chem. , vol.84 , pp. 4900-4906
    • Huang, S.-Y.1    Hsieh, Y.-T.2    Chen, C.-H.3    Chen, C.-C.4    Sung, W.-C.5    Chou, M.-Y.6    Chen, S.-F.7
  • 33
    • 84855545271 scopus 로고    scopus 로고
    • Application of maldi tof/tof mass spectrometry and collision-induced dissociation for the identification of disulfide-bonded peptides
    • Janecki, D. J.; Nemeth, J. F. Application of MALDI TOF/TOF mass spectrometry and collision-induced dissociation for the identification of disulfide-bonded peptides. J. Mass Spectrom. 2011, 46, 677-688.
    • (2011) J. Mass Spectrom. , vol.46 , pp. 677-688
    • Janecki, D.J.1    Nemeth, J.F.2
  • 34
    • 0034925355 scopus 로고    scopus 로고
    • Determination of the disulfide bond pattern of the endogenous and recombinant angiogenesis inhibitor endostatin by mass spectrometry
    • John, H.; Forssmann, W. G. Determination of the disulfide bond pattern of the endogenous and recombinant angiogenesis inhibitor endostatin by mass spectrometry. Rapid Commun. Mass Spectrom. 2001, 15, 1222-1228.
    • (2001) Rapid Commun. Mass Spectrom. , vol.15 , pp. 1222-1228
    • John, H.1    Forssmann, W.G.2
  • 35
    • 0030809823 scopus 로고    scopus 로고
    • Determination of tumor necrosis factor binding protein disulfide structure: Deviation of the fourth domain structure from the tnfr/ngfr family cysteine-rich region signature
    • Jones, M. D.; Hunt, J.; Liu, J. L.; Patterson, S. D.; Kohno, T.; Lu, H. S. Determination of tumor necrosis factor binding protein disulfide structure: deviation of the fourth domain structure from the TNFR/NGFR family cysteine-rich region signature. Biochemistry (Mosc). 1997, 36, 14914-14923.
    • (1997) Biochemistry (Mosc) , vol.36 , pp. 14914-14923
    • Jones, M.D.1    Hunt, J.2    Liu, J.L.3    Patterson, S.D.4    Kohno, T.5    Lu, H.S.6
  • 36
    • 2642520417 scopus 로고    scopus 로고
    • Top-down proteomics
    • Kelleher, N. L. Top-down proteomics. Anal. Chem. 2004, 76, 196A-203A.
    • (2004) Anal. Chem. , vol.76
    • Kelleher, N.L.1
  • 37
    • 0036401454 scopus 로고    scopus 로고
    • Identification of s-glutathionylated cellular proteins during oxidative stress and constitutive metabolism by affinity purification and proteomic analysis
    • Lind, C.; Gerdes, R.; Hamnell, Y.; Schuppe-Koistinen, I.; von Lowenhielm, H. B.; Holmgren, A.; Cotgreave, I. A. Identification of S-glutathionylated cellular proteins during oxidative stress and constitutive metabolism by affinity purification and proteomic analysis. Arch. Biochem. Biophys. 2002, 406, 229-240.
    • (2002) Arch. Biochem. Biophys. , vol.406 , pp. 229-240
    • Lind, C.1    Gerdes, R.2    Hamnell, Y.3    Schuppe-Koistinen, I.4    Von Lowenhielm, H.B.5    Holmgren, A.6    Cotgreave, I.A.7
  • 38
    • 0033081236 scopus 로고    scopus 로고
    • Carbamylation of cysteine: A potential artifact in peptide mapping of hemoglobins in the presence of urea
    • Lippincott, J.; Apostol, I. Carbamylation of cysteine: A potential artifact in peptide mapping of hemoglobins in the presence of urea. Anal. Biochem. 1999, 267, 57-64.
    • (1999) Anal. Biochem. , vol.267 , pp. 57-64
    • Lippincott, J.1    Apostol, I.2
  • 39
    • 77953603827 scopus 로고    scopus 로고
    • Ranking the susceptibility of disulfide bonds in human iggs1 antibodies by reduction, differential alkylation, and lc-ms analysis
    • Liu, H.; Chumsae, C.; Gaza-Bulseco, G.; Hurkmans, K.; Radziejewski, C. H. Ranking the susceptibility of disulfide bonds in human IgGs1 antibodies by reduction, differential alkylation, and LC-MS analysis. Anal. Chem. 2010, 82, 5219-5226.
    • (2010) Anal. Chem. , vol.82 , pp. 5219-5226
    • Liu, H.1    Chumsae, C.2    Gaza-Bulseco, G.3    Hurkmans, K.4    Radziejewski, C.H.5
  • 40
    • 14344257790 scopus 로고    scopus 로고
    • Detection and localization of protein modifications by high resolution tandem mass spectrometry
    • Meng, F. Y.; Forbes, A. J.; Miller, L. M.; Kelleher, N. L. Detection and localization of protein modifications by high resolution tandem mass spectrometry. Mass Spectrom. Rev. 2005, 24, 126-134.
    • (2005) Mass Spectrom. Rev. , vol.24 , pp. 126-134
    • Meng, F.Y.1    Forbes, A.J.2    Miller, L.M.3    Kelleher, N.L.4
  • 41
    • 80053052717 scopus 로고    scopus 로고
    • Cleavage of multiple disulfide bonds in insulin via gold cationization and collision-induced dissociation
    • Mentinova, M.; McLuckey, S. A. Cleavage of multiple disulfide bonds in insulin via gold cationization and collision-induced dissociation. Int. J. Mass Spectrom. 2011, 308, 133-136.
    • (2011) Int. J. Mass Spectrom. , vol.308 , pp. 133-136
    • Mentinova, M.1    McLuckey, S.A.2
  • 42
    • 0032763687 scopus 로고    scopus 로고
    • Strategies for locating disulfide bonds in a monoclonal antibody via mass spectrometry
    • Mhatre, R.; Woodard, J.; Zeng, C. H. Strategies for locating disulfide bonds in a monoclonal antibody via mass spectrometry. Rapid Commun. Mass Spectrom. 1999, 13, 2503-2510.
    • (1999) Rapid Commun. Mass Spectrom. , vol.13 , pp. 2503-2510
    • Mhatre, R.1    Woodard, J.2    Zeng, C.H.3
  • 43
    • 51649130184 scopus 로고    scopus 로고
    • O-18 labeling over a coffee break: A rapid strategy for quantitative proteomics
    • Mirza, S. P.; Greene, A. S.; Olivier, M. O-18 labeling over a coffee break: A rapid strategy for quantitative proteomics. J. Proteome Res. 2008, 7, 3042-3048.
    • (2008) J. Proteome Res. , vol.7 , pp. 3042-3048
    • Mirza, S.P.1    Greene, A.S.2    Olivier, M.3
  • 44
    • 0035896603 scopus 로고    scopus 로고
    • Determination of the disulfide structure and n-glycosylation sites of the extracellular domain of the human signal transducer gp130
    • Moritz, R. L.; Hall, N. E.; Connolly, L. M.; Simpson, R. J. Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130. J. Biol. Chem. 2001, 276, 8244-8253.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8244-8253
    • Moritz, R.L.1    Hall, N.E.2    Connolly, L.M.3    Simpson, R.J.4
  • 45
    • 79951542333 scopus 로고    scopus 로고
    • An efficient algorithmic approach for mass spectrometry-based disulfide connectivity determination using multi-ion analysis
    • Murad, W.; Singh, R.; Yen, T.-Y. An efficient algorithmic approach for mass spectrometry-based disulfide connectivity determination using multi-ion analysis. BMC Bioinformatics 2011, 12(Suppl 1), S12.
    • (2011) BMC Bioinformatics , vol.12 , Issue.SUPPL. 1
    • Murad, W.1    Singh, R.2    Yen, T.-Y.3
  • 46
    • 0028544044 scopus 로고
    • Prompt fragmentation of disulfide-linked peptides during matrix-assisted laser-desorption ionization mass-spectrometry
    • Patterson, S. D.; Katta, V. Prompt fragmentation of disulfide-linked peptides during matrix-assisted laser-desorption ionization mass-spectrometry. Anal. Chem. 1994, 66, 3727-3732.
    • (1994) Anal. Chem. , vol.66 , pp. 3727-3732
    • Patterson, S.D.1    Katta, V.2
  • 47
    • 84859402594 scopus 로고    scopus 로고
    • Purification and high-resolution top-down mass spectrometric characterization of human salivary alpha-amylase
    • Peng, Y.; Chen, X.; Sato, T.; Rankin, S. A.; Tsuji, R. F.; Ge, Y. Purification and high-resolution top-down mass spectrometric characterization of human salivary alpha-amylase. Anal. Chem. 2012, 84, 3339-3346.
    • (2012) Anal. Chem. , vol.84 , pp. 3339-3346
    • Peng, Y.1    Chen, X.2    Sato, T.3    Rankin, S.A.4    Tsuji, R.F.5    Ge, Y.6
  • 48
    • 0030451064 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry of sialylated glycopeptides and proteins using 2, 6-dihydroxyacetophenone as a matrix
    • Pitt, J. J.; Gorman, J. J. Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry of sialylated glycopeptides and proteins using 2, 6-dihydroxyacetophenone as a matrix. Rapid Commun. Mass Spectrom. 1996, 10, 1786-1788.
    • (1996) Rapid Commun. Mass Spectrom. , vol.10 , pp. 1786-1788
    • Pitt, J.J.1    Gorman, J.J.2
  • 49
    • 0034050542 scopus 로고    scopus 로고
    • Determination of the disulfide bond arrangement of newcastle disease virus hemagglutinin neuraminidase - correlation with a beta-sheet propeller structural fold predicted for paramyxoviridae attachment proteins
    • Pitt, J. J.; Da Silva, E.; Gorman, J. J. Determination of the disulfide bond arrangement of Newcastle disease virus hemagglutinin neuraminidase - correlation with a beta-sheet propeller structural fold predicted for paramyxoviridae attachment proteins. J. Biol. Chem. 2000, 275, 6469-6478.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6469-6478
    • Pitt, J.J.1    Da Silva, E.2    Gorman, J.J.3
  • 50
    • 0041884862 scopus 로고    scopus 로고
    • Automated data interpretation based on the concept of "negative signature mass" for mass-mapping disulfide structures of cystinyl proteins
    • Qi, J. F.; Wu, W.; Borges, C. R.; Hang, D. H.; Rupp, M.; Torng, E.; Watson, J. T. Automated data interpretation based on the concept of "negative signature mass" for mass-mapping disulfide structures of cystinyl proteins. J. Am. Soc. Mass. Spectrom. 2003, 14, 1032-1038.
    • (2003) J. Am. Soc. Mass. Spectrom. , vol.14 , pp. 1032-1038
    • Qi, J.F.1    Wu, W.2    Borges, C.R.3    Hang, D.H.4    Rupp, M.5    Torng, E.6    Watson, J.T.7
  • 51
    • 35648959317 scopus 로고    scopus 로고
    • Prompt disulfide fragmentations of disulfide-containing proteins in a matrix-assisted laser desorption/ionization source
    • Qiu, X.; Cui, M.; Lil, H.; Liu, Z.; Liu, S. Prompt disulfide fragmentations of disulfide-containing proteins in a matrix-assisted laser desorption/ionization source. Rapid Commun. Mass Spectrom. 2007, 21, 3520-3525.
    • (2007) Rapid Commun. Mass Spectrom. , vol.21 , pp. 3520-3525
    • Qiu, X.1    Cui, M.2    Lil, H.3    Liu, Z.4    Liu, S.5
  • 52
    • 34548167855 scopus 로고    scopus 로고
    • New method for characterizing highly disulfidebridged 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 disulfidebridged 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
  • 53
    • 0036315870 scopus 로고    scopus 로고
    • 'Top down' protein characterization via tandem mass spectrometry
    • Reid, G. E.; McLuckey, S. A. 'Top down' protein characterization via tandem mass spectrometry. J. Mass Spectrom. 2002, 37, 663-675.
    • (2002) J. Mass Spectrom. , vol.37 , pp. 663-675
    • Reid, G.E.1    McLuckey, S.A.2
  • 54
    • 33750030779 scopus 로고    scopus 로고
    • Detection of reversible protein thiol modifications in tissues
    • Rogers, L. K.; Leinweber, B. L.; Smith, C. V. Detection of reversible protein thiol modifications in tissues. Anal. Biochem. 2006, 358, 171-184.
    • (2006) Anal. Biochem. , vol.358 , pp. 171-184
    • Rogers, L.K.1    Leinweber, B.L.2    Smith, C.V.3
  • 55
    • 0021058414 scopus 로고
    • A new mass-spectrometric c-terminal sequencing technique finds a similarity between gammainterferon and alpha-2-interferon and identifies a proteolytically clipped gamma-interferon that retains full antiviral activity
    • Rose, K.; Simona, M. G.; Offord, R. E.; Prior, C. P.; Otto, B.; Thatcher, D. R. A new mass-spectrometric c-terminal sequencing technique finds a similarity between gammainterferon and alpha-2-interferon and identifies a proteolytically clipped gamma-interferon that retains full antiviral activity. Biochem. J 1983, 215, 273-277.
    • (1983) Biochem. J , vol.215 , pp. 273-277
    • Rose, K.1    Simona, M.G.2    Offord, R.E.3    Prior, C.P.4    Otto, B.5    Thatcher, D.R.6
  • 56
    • 0001047886 scopus 로고
    • Disulphide interchange reactions
    • Ryle, A. P.; Sanger, F. Disulphide interchange reactions. Biochem. J 1955, 60, 535-540.
    • (1955) Biochem. J , vol.60 , pp. 535-540
    • Ryle, A.P.1    Sanger, F.2
  • 57
    • 0000658944 scopus 로고
    • A disulphide interchange reaction
    • Sanger, F. A disulphide interchange reaction. Nature 1953, 171, 1025-1026.
    • (1953) Nature , vol.171 , pp. 1025-1026
    • Sanger, F.1
  • 58
    • 0037093139 scopus 로고    scopus 로고
    • Partial reduction and two-step modification of proteins for identification of disulfide bonds
    • Schnaible, V.; Wefing, S.; Bucker, A.; Wolf-Kummeth, S.; Hoffmann, D. Partial reduction and two-step modification of proteins for identification of disulfide bonds. Anal. Chem. 2002a, 74, 2386-2393.
    • (2002) Anal. Chem. , vol.74 , pp. 2386-2393
    • Schnaible, V.1    Wefing, S.2    Bucker, A.3    Wolf-Kummeth, S.4    Hoffmann, D.5
  • 60
    • 0033626528 scopus 로고    scopus 로고
    • 13C nmr chemical shifts can predict disulfide bond formation
    • Sharma, D.; Rajarathnam, K. 13C NMR chemical shifts can predict disulfide bond formation. J. Biomol. NMR 2000, 18, 165-171.
    • (2000) J. Biomol. NMR , vol.18 , pp. 165-171
    • Sharma, D.1    Rajarathnam, K.2
  • 61
    • 34248545257 scopus 로고    scopus 로고
    • Applications of mass spectrometry for the structural characterization of recombinant protein pharmaceuticals
    • Srebalus Barnes, C. A.; Lim, A. Applications of mass spectrometry for the structural characterization of recombinant protein pharmaceuticals. Mass Spectrom. Rev. 2007, 26, 370-388.
    • (2007) Mass Spectrom. Rev. , vol.26 , pp. 370-388
    • Srebalus Barnes, C.A.1    Lim, A.2
  • 62
    • 0001582001 scopus 로고
    • Reactions of cyanate present in aqueous urea with amino acids and proteins
    • Stark, G. R.; Stein, W. H.; Moore, S. Reactions of cyanate present in aqueous urea with amino acids and proteins. J. Biol. Chem. 1960, 235, 3177-3181.
    • (1960) J. Biol. Chem. , vol.235 , pp. 3177-3181
    • Stark, G.R.1    Stein, W.H.2    Moore, S.3
  • 64
    • 82555170557 scopus 로고    scopus 로고
    • Structural analysis of intact monoclonal antibodies by electron transfer dissociation mass spectrometry
    • Tsybin, Y. O.; Fornelli, L.; Stoermer, C.; Luebeck, M.; Parra, J.; Nallet, S.; Wurm, F. M.; Hartmer, R. Structural analysis of intact monoclonal antibodies by electron transfer dissociation mass spectrometry. Anal. Chem. 2011, 83, 8919-8927.
    • (2011) Anal. Chem. , vol.83 , pp. 8919-8927
    • Tsybin, Y.O.1    Fornelli, L.2    Stoermer, C.3    Luebeck, M.4    Parra, J.5    Nallet, S.6    Wurm, F.M.7    Hartmer, R.8
  • 67
    • 0034774524 scopus 로고    scopus 로고
    • Identification of disulfide-linked peptides by isotope profiles produced by peptic digestion of proteins in 50% (18)o water
    • Wallis, T. P.; PittWallis, T. P.; Pitt, J. J.; Gorman, J. J. Identification of disulfide-linked peptides by isotope profiles produced by peptic digestion of proteins in 50% (18)O water. Protein Sci. 2001, 10, 2251-2271.
    • (2001) Protein Sci , vol.10 , pp. 2251-2271
    • Wallis, T.P.1    PittWallis, T.P.2    Pitt, J.J.3    Gorman, J.J.4
  • 68
    • 79954492422 scopus 로고    scopus 로고
    • Characterization and comparison of disulfide linkages and scrambling patterns in therapeutic monoclonal antibodies: Using lc-ms with electron transfer dissociation
    • Wang, Y.; Lu, Q. Z.; Wu, S. L.; Karger, B. L.; Hancock, W. S. Characterization and comparison of disulfide linkages and scrambling patterns in therapeutic monoclonal antibodies: using LC-MS with electron transfer dissociation. Anal. Chem. 2011, 83, 3133-3140.
    • (2011) Anal. Chem. , vol.83 , pp. 3133-3140
    • Wang, Y.1    Lu, Q.Z.2    Wu, S.L.3    Karger, B.L.4    Hancock, W.S.5
  • 69
    • 33144457109 scopus 로고    scopus 로고
    • A program for the identification of disulfide bonds in proteins from mass spectra
    • Wefing, S.; Schnaible, V.; Hoffmann, D. Searchxlinks. A program for the identification of disulfide bonds in proteins from mass spectra. Anal. Chem. 2006, 78, 1235-1241.
    • (2006) Anal. Chem. , vol.78 , pp. 1235-1241
    • Wefing, S.1    Schnaible, V.2    Hoffmann, D.S.3
  • 70
    • 0026139976 scopus 로고
    • Identification of nearest-neighbor peptides in protease digests by mass-spectrometry for construction of sequence-ordered tryptic maps
    • Whaley, B.; Caprioli, R. M. Identification of nearest-neighbor peptides in protease digests by mass-spectrometry for construction of sequence-ordered tryptic maps. Biol. Mass Spectrom. 1991, 20, 210-214.
    • (1991) Biol. Mass Spectrom. , vol.20 , pp. 210-214
    • Whaley, B.1    Caprioli, R.M.2
  • 71
    • 67650388719 scopus 로고    scopus 로고
    • Global quantitative proteomic profiling through 18o-labeling in combination with ms/ms spectra analysis
    • White, C. A.; Oey, N.; Emili, A. Global quantitative proteomic profiling through 18O-labeling in combination with MS/MS spectra analysis. J. Proteome Res. 2009, 8, 3653-3665.
    • (2009) J. Proteome Res. , vol.8 , pp. 3653-3665
    • White, C.A.1    Oey, N.2    Emili, A.3
  • 72
    • 55849104839 scopus 로고    scopus 로고
    • Application of electron transfer dissociation (etd) for the analysis of posttranslational modifications
    • Wiesner, J.; Premsler, T.; Sickmann, A. Application of electron transfer dissociation (ETD) for the analysis of posttranslational modifications. Proteomics 2008, 8, 4466-4483.
    • (2008) Proteomics , vol.8 , pp. 4466-4483
    • Wiesner, J.1    Premsler, T.2    Sickmann, A.3
  • 73
    • 0031173707 scopus 로고    scopus 로고
    • Mass spectrometry as a readout of protein structure and function
    • Winston, R. L.; Fitzgerald, M. C. Mass spectrometry as a readout of protein structure and function. Mass Spectrom. Rev. 1997, 16, 165-179.
    • (1997) Mass Spectrom. Rev. , vol.16 , pp. 165-179
    • Winston, R.L.1    Fitzgerald, M.C.2
  • 74
    • 0031050298 scopus 로고    scopus 로고
    • A novel methodology for assignment of disulfide bond pairings in proteins
    • Wu, J.; Watson, J. T. A novel methodology for assignment of disulfide bond pairings in proteins. Protein Sci. 1997, 6, 391-398.
    • (1997) Protein Sci , vol.6 , pp. 391-398
    • Wu, J.1    Watson, J.T.2
  • 75
    • 4444324208 scopus 로고    scopus 로고
    • 'Signature sets', minimal fragment sets for identifying protein disulfide structures with cyanylation-based mass mapping methodology
    • Wu, W.; Huang, W.; Qi, R. F.; Chou, Y. T.; Torng, E.; Watson, J. T. 'Signature sets', minimal fragment sets for identifying protein disulfide structures with cyanylation-based mass mapping methodology. J. Proteome Res. 2004, 3, 770-777.
    • (2004) J. Proteome Res. , vol.3 , pp. 770-777
    • Wu, W.1    Huang, W.2    Qi, R.F.3    Chou, Y.T.4    Torng, E.5    Watson, J.T.6
  • 76
    • 58149510241 scopus 로고    scopus 로고
    • Mass spectrometric determination of disulfide linkages in recombinant therapeutic proteins using online lc-ms with electron-transfer dissociation
    • Wu, S. L.; Jiang, H. T.; Lu, Q. Z.; Dai, S. J.; Hancock, W. S.; Karger, B. L. Mass spectrometric determination of disulfide linkages in recombinant therapeutic proteins using online LC-MS with electron-transfer dissociation. Anal. Chem. 2009, 81, 112-122.
    • (2009) Anal. Chem. , vol.81 , pp. 112-122
    • Wu, S.L.1    Jiang, H.T.2    Lu, Q.Z.3    Dai, S.J.4    Hancock, W.S.5    Karger, B.L.6
  • 77
    • 34249094851 scopus 로고    scopus 로고
    • A mass accuracy sensitive probability based scoring algorithm for database searching of tandem mass spectrometry data
    • Xu, H.; Freitas, M. A. A mass accuracy sensitive probability based scoring algorithm for database searching of tandem mass spectrometry data. BMC Bioinformatics 2007, 8, 133.
    • (2007) BMC Bioinformatics , vol.8 , pp. 133
    • Xu, H.1    Freitas, M.A.2
  • 78
    • 38649131282 scopus 로고    scopus 로고
    • Identification and characterization of disulfide bonds in proteins and peptides from tandem ms data by use of the massmatrix ms/ms search engine
    • Xu, H.; Zhang, L. W.; Freitas, M. A. Identification and characterization of disulfide bonds in proteins and peptides from tandem MS data by use of the MassMatrix MS/MS search engine. J Proteome Res. 2008, 7, 138-144.
    • (2008) J Proteome Res. , vol.7 , pp. 138-144
    • Xu, H.1    Zhang, L.W.2    Freitas, M.A.3
  • 80
    • 0032540696 scopus 로고    scopus 로고
    • Disulfide mass mapping in proteins containing adjacent cysteines is possible with cyanylation/cleavage methodology
    • Yang, Y.; Wu, J.; Watson, J. T. Disulfide mass mapping in proteins containing adjacent cysteines is possible with cyanylation/cleavage methodology. J. Am. Chem. Soc. 1998, 120, 5834-5835.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 5834-5835
    • Yang, Y.1    Wu, J.2    Watson, J.T.3
  • 81
    • 70449502844 scopus 로고    scopus 로고
    • A new method for analysis of disulfide-containing proteins by matrix-assisted laser desorption ionization (maldi) mass spectrometry
    • Yang, H. M.; Liu, N.; Qiu, X. Y.; Liu, S. Y. A new method for analysis of disulfide-containing proteins by matrix-assisted laser desorption ionization (MALDI) mass spectrometry. J. Am. Soc. Mass. Spectrom. 2009, 20, 2284-2293.
    • (2009) J. Am. Soc. Mass. Spectrom. , vol.20 , pp. 2284-2293
    • Yang, H.M.1    Liu, N.2    Qiu, X.Y.3    Liu, S.Y.4
  • 82
    • 0036744350 scopus 로고    scopus 로고
    • Disulfide proteome in the analysis of protein function and structure
    • Yano, H.; Kuroda, S.; Buchanan, B. B. Disulfide proteome in the analysis of protein function and structure. Proteomics 2002, 2, 1090-1096.
    • (2002) Proteomics , vol.2 , pp. 1090-1096
    • Yano, H.1    Kuroda, S.2    Buchanan, B.B.3
  • 83
    • 0033863181 scopus 로고    scopus 로고
    • Characterization of cysteine residues and disulfide bonds in proteins by liquid chromatography/electrospray ionization tandem mass spectrometry
    • Yen, T. Y.; Joshi, R. K.; Yan, H.; Seto, N. O. L.; Palcic, M. M.; Macher, B. A. Characterization of cysteine residues and disulfide bonds in proteins by liquid chromatography/electrospray ionization tandem mass spectrometry. J. Mass Spectrom. 2000, 35, 990-1002.
    • (2000) J. Mass Spectrom. , vol.35 , pp. 990-1002
    • Yen, T.Y.1    Joshi, R.K.2    Yan, H.3    Seto, N.O.L.4    Palcic, M.M.5    Macher, B.A.6
  • 84
    • 0036161645 scopus 로고    scopus 로고
    • Characterizing closely spaced, complex disulfide bond patterns in peptides and proteins by liquid chromatography/electrospray ionization tandem mass spectrometry
    • Yen, T. Y.; Yan, H.; Macher, B. A. Characterizing closely spaced, complex disulfide bond patterns in peptides and proteins by liquid chromatography/ electrospray ionization tandem mass spectrometry. J. Mass Spectrom. 2002, 37, 15-30.
    • (2002) J. Mass Spectrom. , vol.37 , pp. 15-30
    • Yen, T.Y.1    Yan, H.2    Macher, B.A.3
  • 85
    • 69749098499 scopus 로고    scopus 로고
    • Methodology for determining disulfide linkage patterns of closely spaced cysteine residues
    • Zhang, B.; Cockrill, S. L. Methodology for determining disulfide linkage patterns of closely spaced cysteine residues. Anal. Chem. 2009, 81, 7314-7320.
    • (2009) Anal. Chem. , vol.81 , pp. 7314-7320
    • Zhang, B.1    Cockrill, S.L.2
  • 86
    • 84859393607 scopus 로고    scopus 로고
    • Comprehensive analysis of protein modifications by top-down mass spectrometry
    • Zhang, H.; Ge, Y. Comprehensive analysis of protein modifications by top-down mass spectrometry. Circ. Cardiovasc. Genet. 2011, 4, 711.
    • (2011) Circ. Cardiovasc. Genet. , vol.4 , pp. 711
    • Zhang, H.1    Ge, Y.2
  • 87
    • 33746260415 scopus 로고    scopus 로고
    • Mapping of protein disulfide bonds using negative ion fragmentation with a broadband precursor selection
    • Zhang, M.; Kaltashov, I. A. Mapping of protein disulfide bonds using negative ion fragmentation with a broadband precursor selection. Anal. Chem. 2006, 78, 4820-4829.
    • (2006) Anal. Chem. , vol.78 , pp. 4820-4829
    • Zhang, M.1    Kaltashov, I.A.2
  • 88
    • 0036901746 scopus 로고    scopus 로고
    • Complete disulfide bond assignment of a recombinant immunoglobulin g4 monoclonal antibody
    • Zhang, W.; Marzilli, L. A.; Rouse, J. C.; Czupryn, M. J. Complete disulfide bond assignment of a recombinant immunoglobulin G4 monoclonal antibody. Anal. Biochem. 2002, 311, 1-9.
    • (2002) Anal. Biochem. , vol.311 , pp. 1-9
    • Zhang, W.1    Marzilli, L.A.2    Rouse, J.C.3    Czupryn, M.J.4
  • 89
    • 76149108167 scopus 로고    scopus 로고
    • Determination of fab-hinge disulfide connectivity in structural isoforms of a recombinant human immunoglobulin g2 antibody
    • Zhang, B.; Harder, A. G.; Connelly, H. M.; Maheu, L. L.; Cockrill, S. L. Determination of Fab-hinge disulfide connectivity in structural isoforms of a recombinant human immunoglobulin G2 antibody. Anal. Chem. 2010, 82, 1090-1099.
    • (2010) Anal. Chem. , vol.82 , pp. 1090-1099
    • Zhang, B.1    Harder, A.G.2    Connelly, H.M.3    Maheu, L.L.4    Cockrill, S.L.5
  • 90
    • 79952411402 scopus 로고    scopus 로고
    • Online mass spectrometric analysis of proteins/peptides following electrolytic cleavage of disulfide bonds
    • Zhang, Y.; Dewald, H. D.; Chen, H. Online mass spectrometric analysis of proteins/peptides following electrolytic cleavage of disulfide bonds. J. Proteome Res. 2011, 10, 1293-1304.
    • (2011) J. Proteome Res. , vol.10 , pp. 1293-1304
    • Zhang, Y.1    Dewald, H.D.2    Chen, H.3
  • 91
    • 84859882824 scopus 로고    scopus 로고
    • Electrochemistryassisted top-down characterization of disulfide-containing proteins
    • Zhang, Y.; Cui, W.; Zhang, H.; Dewald, H. D.; Chen, H. Electrochemistryassisted top-down characterization of disulfide-containing proteins. Anal. Chem. 2012, 84, 3838-3842.
    • (2012) Anal. Chem. , vol.84 , pp. 3838-3842
    • Zhang, Y.1    Cui, W.2    Zhang, H.3    Dewald, H.D.4    Chen, H.5
  • 92
    • 80053533242 scopus 로고    scopus 로고
    • Electron transfer dissociation of modified peptides and proteins
    • Zhou, Y.; Dong, J.; Vachet, R. W. Electron transfer dissociation of modified peptides and proteins. Curr. Pharm. Biotechnol. 2011, 12, 1558-1567.
    • (2011) Curr. Pharm. Biotechnol. , vol.12 , pp. 1558-1567
    • Zhou, Y.1    Dong, J.2    Vachet, R.W.3
  • 93
    • 0033620364 scopus 로고    scopus 로고
    • Electron capture dissociation of gaseous multiply-charged proteins is favored at disulfide bonds and other sites of high hydrogen atom affinity
    • Zubarev, R. A.; Kruger, N. A.; Fridriksson, E. K.; Lewis, M. A.; Horn, D. M.; Carpenter, B. K.; McLafferty, F. W. Electron capture dissociation of gaseous multiply-charged proteins is favored at disulfide bonds and other sites of high hydrogen atom affinity. J. Am. Chem. Soc. 1999, 121, 2857-2862.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 2857-2862
    • Zubarev, R.A.1    Kruger, N.A.2    Fridriksson, E.K.3    Lewis, M.A.4    Horn, D.M.5    Carpenter, B.K.6    McLafferty, F.W.7


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