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Volumn 28, Issue 14, 2006, Pages 1047-1059

Electron capture dissociation mass spectrometry in characterization of peptides and proteins

Author keywords

Electron capture dissociation; Electron transfer dissociation; Electrospray ionization; Fourier transform mass spectrometry; Post translational modifications

Indexed keywords

ELECTRON CAPTURE DISSOCIATION; ELECTRON TRANSFER DISSOCIATION (ETD); ELECTROSPRAY IONIZATION; FOURIER TRANSFORM MASS SPECTROMETRY; POST-TRANSLATIONAL MODIFICATIONS;

EID: 33745684811     PISSN: 01415492     EISSN: 15736776     Source Type: Journal    
DOI: 10.1007/s10529-006-9065-z     Document Type: Review
Times cited : (67)

References (82)
  • 1
    • 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
  • 2
    • 0001310867 scopus 로고
    • Fourier-transform electrospray instrumentation for tandem high-resolution mass spectrometry of large molecules
    • Beu SC, Senko MW, Quinn JP, Wampler FM III, McLafferty FW (1993) Fourier-transform electrospray instrumentation for tandem high-resolution mass spectrometry of large molecules. J Am Soc Mass Spectrom 4:557-565
    • (1993) J Am Soc Mass Spectrom , vol.4 , pp. 557-565
    • Beu, S.C.1    Senko, M.W.2    Quinn, J.P.3    Wampler III, F.M.4    McLafferty, F.W.5
  • 3
    • 33644783669 scopus 로고    scopus 로고
    • Combined top-down and bottom-up proteomics identifies a phsophorylation site in stem-loop-binding proteins that contributes to high-affinity RNA binding
    • USA
    • Borchers CH, Thapar R, Petrotchenko EV, Torres MP, Speir JP, Easterling M, Dominski Z, Marzluff WF (2006) Combined top-down and bottom-up proteomics identifies a phsophorylation site in stem-loop-binding proteins that contributes to high-affinity RNA binding. Proc Natl Acad Sci USA 103:3094-3099
    • (2006) Proc Natl Acad Sci , vol.103 , pp. 3094-3099
    • Borchers, C.H.1    Thapar, R.2    Petrotchenko, E.V.3    Torres, M.P.4    Speir, J.P.5    Easterling, M.6    Dominski, Z.7    Marzluff, W.F.8
  • 4
    • 4744355031 scopus 로고    scopus 로고
    • Nonergodic and conformational control of the electron capture dissociation of protein molecules
    • USA
    • Breuker K, Oh H-B, Lin C, Carpenter BK, McLafferty FW (2004) Nonergodic and conformational control of the electron capture dissociation of protein molecules. Proc Natl Acad Sci USA 101:14011-14016
    • (2004) Proc Natl Acad Sci , vol.101 , pp. 14011-14016
    • Breuker, K.1    Oh, H.-B.2    Lin, C.3    Carpenter, B.K.4    McLafferty, F.W.5
  • 6
    • 10644230156 scopus 로고    scopus 로고
    • A comprehensive picture of non-site specific oxidation of methionine residues by peroxides in protein pharmaceuticals
    • Chu J-W, Yin J, Brooks BR, Wang DIC, Ricci MS, Brems DN, Trout BL (2004) A comprehensive picture of non-site specific oxidation of methionine residues by peroxides in protein pharmaceuticals. J Pharm Sci 93:3096-3102
    • (2004) J Pharm Sci , vol.93 , pp. 3096-3102
    • Chu, J.-W.1    Yin, J.2    Brooks, B.R.3    Wang, D.I.C.4    Ricci, M.S.5    Brems, D.N.6    Trout, B.L.7
  • 8
    • 10044289273 scopus 로고    scopus 로고
    • Identification of sites of ubiquitination in proteins: A Fourier transform ion cyclotron resonance mass spectrometry approach
    • Cooper HJ, Heath JK, Jaffray E, Hay RT, Lam TT, Marshall AG (2004) Identification of sites of ubiquitination in proteins: a Fourier transform ion cyclotron resonance mass spectrometry approach. Anal Chem 76:6982-6988
    • (2004) Anal Chem , vol.76 , pp. 6982-6988
    • Cooper, H.J.1    Heath, J.K.2    Jaffray, E.3    Hay, R.T.4    Lam, T.T.5    Marshall, A.G.6
  • 9
    • 14744299376 scopus 로고    scopus 로고
    • The role of electron capture dissociation in biomolecular analysis
    • Cooper HJ, Hakansson K, Marshall AG (2005) The role of electron capture dissociation in biomolecular analysis. Mass Spectrom Rev 24:201-222
    • (2005) Mass Spectrom Rev , vol.24 , pp. 201-222
    • Cooper, H.J.1    Hakansson, K.2    Marshall, A.G.3
  • 12
    • 0032872359 scopus 로고    scopus 로고
    • Dermal and transdermal delivery of protein pharmaceuticals: Lipid-based delivery systems for interferon alpha
    • Foldvari M, Baca-Estrada ME, He Z, Hu J, Attah-Poku S, King M (1999) Dermal and transdermal delivery of protein pharmaceuticals: lipid-based delivery systems for interferon alpha. Biotechnol Appl Biochem 30:129-137
    • (1999) Biotechnol Appl Biochem , vol.30 , pp. 129-137
    • Foldvari, M.1    Baca-Estrada, M.E.2    He, Z.3    Hu, J.4    Attah-Poku, S.5    King, M.6
  • 13
    • 18244365849 scopus 로고    scopus 로고
    • Protein drug stability: A formulation challenge
    • Frokjaer S, Otzen DE (2005) Protein drug stability: a formulation challenge. Nature Rev Drug Discov 4:298-306
    • (2005) Nature Rev Drug Discov , vol.4 , pp. 298-306
    • Frokjaer, S.1    Otzen, D.E.2
  • 14
    • 0036881230 scopus 로고    scopus 로고
    • Quality control of biotechnology-derived vaccines: Technical and regulatory considerations
    • Fuchs F (2002) Quality control of biotechnology-derived vaccines: technical and regulatory considerations. Biochimie 84:1173-1179
    • (2002) Biochimie , vol.84 , pp. 1173-1179
    • Fuchs, F.1
  • 18
    • 0036884614 scopus 로고    scopus 로고
    • Identification and localization of the fatty acid modification in ghrelin by electron capture dissociation
    • Guan Z (2002) Identification and localization of the fatty acid modification in ghrelin by electron capture dissociation. J Am Soc Mass Spectrom 13:1443-1447
    • (2002) J Am Soc Mass Spectrom , vol.13 , pp. 1443-1447
    • Guan, Z.1
  • 20
    • 0038825874 scopus 로고    scopus 로고
    • Detection and characterization of methionine oxidation in peptides by collision-induced dissociation and electron capture dissociation
    • Guan Z, Yates NA, Bakhtiar R (2003) Detection and characterization of methionine oxidation in peptides by collision-induced dissociation and electron capture dissociation. J Am Soc Mass Spectrom 14:605-613
    • (2003) J Am Soc Mass Spectrom , vol.14 , pp. 605-613
    • Guan, Z.1    Yates, N.A.2    Bakhtiar, R.3
  • 21
    • 33745703563 scopus 로고    scopus 로고
    • Polymer therapeutics: Concepts and applications
    • Haag R, Kratz F (2006) Polymer therapeutics: concepts and applications. Angew Chem Int Ed Engl 45:1198-1215
    • (2006) Angew Chem Int Ed Engl , vol.45 , pp. 1198-1215
    • Haag, R.1    Kratz, F.2
  • 24
    • 0028725629 scopus 로고
    • Analytical strategies for the determination of protein modifications
    • Janis LJ, Davis GC (1994) Analytical strategies for the determination of protein modifications. Dev Biol Stand 83:135-142
    • (1994) Dev Biol Stand , vol.83 , pp. 135-142
    • Janis, L.J.1    Davis, G.C.2
  • 25
    • 22844436226 scopus 로고    scopus 로고
    • Recent advances in tumor-targeting anticancer drug conjugates
    • Jaracz S, Chen J, Kuznetsova LV, Ojima I (2005) Recent advances in tumor-targeting anticancer drug conjugates. Bioorg Med Chem 13:5043-5054
    • (2005) Bioorg Med Chem , vol.13 , pp. 5043-5054
    • Jaracz, S.1    Chen, J.2    Kuznetsova, L.V.3    Ojima, I.4
  • 26
    • 13544276336 scopus 로고    scopus 로고
    • Glycosylation of recombinant antibody therapeutics
    • Jefferis R (2005) Glycosylation of recombinant antibody therapeutics. Biotechnol Prog 21:11-16
    • (2005) Biotechnol Prog , vol.21 , pp. 11-16
    • Jefferis, R.1
  • 28
    • 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
  • 30
    • 0038154088 scopus 로고    scopus 로고
    • Localization of intramolecular monosulfide bridges in lantibiotics determined with electron capture induced dissociation
    • Kleinnijenhuis AJ, Duursma MC, Breukink E, Heeren RMA, Heck AJR (2003) Localization of intramolecular monosulfide bridges in lantibiotics determined with electron capture induced dissociation. Anal Chem 75:3219-3225
    • (2003) Anal Chem , vol.75 , pp. 3219-3225
    • Kleinnijenhuis, A.J.1    Duursma, M.C.2    Breukink, E.3    Heeren, R.M.A.4    Heck, A.J.R.5
  • 31
    • 0025411841 scopus 로고
    • Effect of reducing disulfide-containing proteins on electrospray Ionization mass spectra
    • Loo JA, Edmonds CG, Udseth HR, Smith RD (1990) Effect of reducing disulfide-containing proteins on electrospray Ionization mass spectra. Anal Chem 62:693-698
    • (1990) Anal Chem , vol.62 , pp. 693-698
    • Loo, J.A.1    Edmonds, C.G.2    Udseth, H.R.3    Smith, R.D.4
  • 32
    • 0030733229 scopus 로고    scopus 로고
    • Applications of site-specific chemical modification in the manufacture of biopharmaceuticals: I. An overview
    • Lundblad RL, Bradshaw RA (1997) Applications of site-specific chemical modification in the manufacture of biopharmaceuticals: I. An overview. Biotechnol Appl Biochem 26:143-151
    • (1997) Biotechnol Appl Biochem , vol.26 , pp. 143-151
    • Lundblad, R.L.1    Bradshaw, R.A.2
  • 33
    • 0031623267 scopus 로고    scopus 로고
    • Fourier transform ion cyclotron resonance mass spectrometry: A primer
    • Marshall AG, Hendrickson CL, Jackson GS (1998) Fourier transform ion cyclotron resonance mass spectrometry: a primer. Mass Spectrom Rev 17:1-35
    • (1998) Mass Spectrom Rev , vol.17 , pp. 1-35
    • Marshall, A.G.1    Hendrickson, C.L.2    Jackson, G.S.3
  • 34
  • 36
    • 0005387475 scopus 로고
    • Principles of collisional activation in analytical mass spectrometry
    • McLuckey SA (1992) Principles of collisional activation in analytical mass spectrometry. J Am Soc Mass Spectrom 3:599-614
    • (1992) J Am Soc Mass Spectrom , vol.3 , pp. 599-614
    • McLuckey, S.A.1
  • 38
    • 14344257790 scopus 로고    scopus 로고
    • Detection and localization of protein modifications by high resolution tandem mass spectrometry
    • Meng F, Forbes AJ, Miller LM, Kelleher NL (2005) Detection and localization of protein modifications by high resolution tandem mass spectrometry. Mass Spectrom Rev 24:126-134
    • (2005) Mass Spectrom Rev , vol.24 , pp. 126-134
    • Meng, F.1    Forbes, A.J.2    Miller, L.M.3    Kelleher, N.L.4
  • 39
    • 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
  • 40
    • 0043261498 scopus 로고    scopus 로고
    • Pegylation: Engineering improved biopharmaceuticals for oncology
    • Molineux G (2003) Pegylation: engineering improved biopharmaceuticals for oncology. Pharmacotherapy 23:3S-8S
    • (2003) Pharmacotherapy , vol.23
    • Molineux, G.1
  • 41
    • 1842535270 scopus 로고    scopus 로고
    • The design and development of pegfilgrastim (PEG-rmetHuG-CSF, Neulasta®)
    • Molineux G (2004) The design and development of pegfilgrastim (PEG-rmetHuG-CSF, Neulasta®). Curr Pharm Design 10:1235-1244
    • (2004) Curr Pharm Design , vol.10 , pp. 1235-1244
    • Molineux, G.1
  • 42
    • 0031308296 scopus 로고    scopus 로고
    • FDA perspective on specifications for biotechnology products: From IND to PLA
    • Murano G (1997) FDA perspective on specifications for biotechnology products: from IND to PLA. Dev Biol Stand 91:3-13
    • (1997) Dev Biol Stand , vol.91 , pp. 3-13
    • Murano, G.1
  • 43
    • 0242569357 scopus 로고    scopus 로고
    • "Top down" characterization is a complementary technique to peptide sequencing for identifying protein species in complex mixtures
    • Nemeth-Cawley JF, Tangarone BS, Rouse JC (2003) "Top down" characterization is a complementary technique to peptide sequencing for identifying protein species in complex mixtures. J Proteomics 2:495-505
    • (2003) J Proteomics , vol.2 , pp. 495-505
    • Nemeth-Cawley, J.F.1    Tangarone, B.S.2    Rouse, J.C.3
  • 45
    • 0034659815 scopus 로고    scopus 로고
    • Proteomics to study genes and genomes
    • Pandey A, Mann M (2000) Proteomics to study genes and genomes. Nature 405:837-846
    • (2000) Nature , vol.405 , pp. 837-846
    • Pandey, A.1    Mann, M.2
  • 46
    • 1642272372 scopus 로고    scopus 로고
    • Shotgun annotation of histone modifications: A new approach for streamlined characterization of proteins by top down mass spectrometry
    • Pesavento JJ, Kim Y-B, Taylor GK, Kelleher NL (2004) Shotgun annotation of histone modifications: a new approach for streamlined characterization of proteins by top down mass spectrometry. J Am Chem Soc 126:3386-3387
    • (2004) J Am Chem Soc , vol.126 , pp. 3386-3387
    • Pesavento, J.J.1    Kim, Y.-B.2    Taylor, G.K.3    Kelleher, N.L.4
  • 47
    • 30544433136 scopus 로고    scopus 로고
    • Methods in enzymology: O-glycosylation of proteins
    • Peter-Katalinic J (2005) Methods in enzymology: O-glycosylation of proteins. Meth Enzymol 405:139-171
    • (2005) Meth Enzymol , vol.405 , pp. 139-171
    • Peter-Katalinic, J.1
  • 48
    • 33645506491 scopus 로고    scopus 로고
    • The use of a hybrid linear trap/FT-ICR mass spectrometer for on-line high resolution/high mass accuracy bottom-up sequencing
    • Peterman SM, Dufresne CP, Horning S (2005) The use of a hybrid linear trap/FT-ICR mass spectrometer for on-line high resolution/high mass accuracy bottom-up sequencing. J Biomol Tech 16:112-124
    • (2005) J Biomol Tech , vol.16 , pp. 112-124
    • Peterman, S.M.1    Dufresne, C.P.2    Horning, S.3
  • 49
    • 0036315870 scopus 로고    scopus 로고
    • "Top down" protein characterization via tandem mass spectrometry
    • Reid GE, McLuckey SA (2002) "Top down" protein characterization via tandem mass spectrometry. J Mass Spectrom 37:663-675
    • (2002) J Mass Spectrom , vol.37 , pp. 663-675
    • Reid, G.E.1    McLuckey, S.A.2
  • 50
    • 7444255626 scopus 로고    scopus 로고
    • Membrane targeting of lipid modified signal transduction proteins
    • Resh MD (2004) Membrane targeting of lipid modified signal transduction proteins. Subcell Biochem 37:217-232
    • (2004) Subcell Biochem , vol.37 , pp. 217-232
    • Resh, M.D.1
  • 52
    • 24344456043 scopus 로고    scopus 로고
    • Top-down characterization of protein pharmaceuticals by liquid chromatography/mass spectrometry: Application to recombinant factor IX comparability-a case study
    • Rouse JC, McClellan JE, Patel HK, Jankowski MA, Porter TJ (2005) Top-down characterization of protein pharmaceuticals by liquid chromatography/mass spectrometry: application to recombinant factor IX comparability-a case study. Methods Mol Biol 308:435-460
    • (2005) Methods Mol Biol , vol.308 , pp. 435-460
    • Rouse, J.C.1    McClellan, J.E.2    Patel, H.K.3    Jankowski, M.A.4    Porter, T.J.5
  • 53
    • 1942472616 scopus 로고    scopus 로고
    • Freeze-drying of proteins: Some emerging concerns
    • Roy I, Gupta MN (2004) Freeze-drying of proteins: some emerging concerns. Biotechnol Appl Biochem 39:165-177
    • (2004) Biotechnol Appl Biochem , vol.39 , pp. 165-177
    • Roy, I.1    Gupta, M.N.2
  • 54
    • 0038282916 scopus 로고    scopus 로고
    • Proteomics: Drug target discovery on an industrial scale
    • Ryan TE, Patterson SD (2002) Proteomics: drug target discovery on an industrial scale. Trends Biotechnol 20:S45-S51
    • (2002) Trends Biotechnol , vol.20
    • Ryan, T.E.1    Patterson, S.D.2
  • 55
    • 24044508863 scopus 로고    scopus 로고
    • New data base-independent, sequence tag-based scoring of peptide MS/MS data validates Mowse score, recovers below threshold data, singles out modified peptides, and assesses the quality of MS/MS techniques
    • Savitski MM, Nielsen ML, Zubarev RA (2005) New data base-independent, sequence tag-based scoring of peptide MS/MS data validates Mowse score, recovers below threshold data, singles out modified peptides, and assesses the quality of MS/MS techniques. Mol Cell Proteomics 4:1180-1188
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1180-1188
    • Savitski, M.M.1    Nielsen, M.L.2    Zubarev, R.A.3
  • 56
    • 32944459736 scopus 로고    scopus 로고
    • Factors influencing the immunogenicity of therapeutic proteins
    • Schellekens H (2005) Factors influencing the immunogenicity of therapeutic proteins. Nephrol. Dial. Transplant 20 Suppl. 6:vi3-vi9
    • (2005) Nephrol. Dial. Transplant , vol.20 , Issue.6 SUPPL.
    • Schellekens, H.1
  • 57
    • 0034033915 scopus 로고    scopus 로고
    • Identification of peptide oxidation by tandem mass spectrometry
    • Schey KL, Finley EL (2000) Identification of peptide oxidation by tandem mass spectrometry. Acc Chem Res 33:299-306
    • (2000) Acc Chem Res , vol.33 , pp. 299-306
    • Schey, K.L.1    Finley, E.L.2
  • 58
    • 26844489700 scopus 로고    scopus 로고
    • Methods for the detection of paxillin posttranslational modifications and interacting proteins by mass spectrometry
    • Schroeder MJ, Webb DJ, Shabanowitz J, Horwitz AF, Hunt DF (2005) Methods for the detection of paxillin posttranslational modifications and interacting proteins by mass spectrometry. J Proteome Res 4:1831-1841
    • (2005) J Proteome Res , vol.4 , pp. 1831-1841
    • Schroeder, M.J.1    Webb, D.J.2    Shabanowitz, J.3    Horwitz, A.F.4    Hunt, D.F.5
  • 59
    • 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
  • 60
    • 0043269180 scopus 로고    scopus 로고
    • Modification of clearance of therapeutic and potentially therapeutic proteins
    • Sheffield WP (2001) Modification of clearance of therapeutic and potentially therapeutic proteins. Current Drug Targets: Cardiovas Hemat Dis 1:1-22
    • (2001) Current Drug Targets: Cardiovas Hemat Dis , vol.1 , pp. 1-22
    • Sheffield, W.P.1
  • 61
  • 62
    • 25444435396 scopus 로고    scopus 로고
    • Glycoengineering: The effect of glycosylation on the properties of therapeutic proteins
    • Sinclair AM, Elliott S (2005) Glycoengineering: the effect of glycosylation on the properties of therapeutic proteins. J Pharm Sci 94:1626-1635
    • (2005) J Pharm Sci , vol.94 , pp. 1626-1635
    • Sinclair, A.M.1    Elliott, S.2
  • 63
    • 6944233454 scopus 로고    scopus 로고
    • Ion activation methods for tandem mass spectrometry
    • Sleno L, Volmer DA (2004) Ion activation methods for tandem mass spectrometry. J Mass Spectrom 39:1091-1112
    • (2004) J Mass Spectrom , vol.39 , pp. 1091-1112
    • Sleno, L.1    Volmer, D.A.2
  • 65
    • 27144468685 scopus 로고    scopus 로고
    • Developments in ghrelin biology and potential clinical relevance
    • Smith RG, Jiang H, Sun Y (2005) Developments in ghrelin biology and potential clinical relevance. Trends Endocrinol Metab 16:436-442
    • (2005) Trends Endocrinol Metab , vol.16 , pp. 436-442
    • Smith, R.G.1    Jiang, H.2    Sun, Y.3
  • 67
    • 30644469415 scopus 로고    scopus 로고
    • Molecular weight determination of peptides and proteins by ESI and MALDI
    • Strupat K (2005) Molecular weight determination of peptides and proteins by ESI and MALDI. Meth Enzymol 405:1-36
    • (2005) Meth Enzymol , vol.405 , pp. 1-36
    • Strupat, K.1
  • 68
    • 3042789073 scopus 로고    scopus 로고
    • Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry
    • USA
    • Syka JEP, Coon JJ, Schroeder MJ, Shabanowitz J, Hunt DF (2004) Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry. Proc Natl Acad Sci USA 101:9528-9533
    • (2004) Proc Natl Acad Sci , vol.101 , pp. 9528-9533
    • Syka, J.E.P.1    Coon, J.J.2    Schroeder, M.J.3    Shabanowitz, J.4    Hunt, D.F.5
  • 69
    • 0037133237 scopus 로고    scopus 로고
    • Top-down mass spectrometry of a 29-kDa protein for characterization of any posttranslational modification to within one residue
    • USA
    • Sze S-K, Ge Y, Oh H-B, 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 , vol.99 , pp. 1774-1779
    • Sze, S.-K.1    Ge, Y.2    Oh, H.-B.3    McLafferty, F.W.4
  • 70
    • 4344634877 scopus 로고    scopus 로고
    • Pharmacokinetic aspects of biotechnology products
    • Tang L, Persky AM, Hochhaus G, Meibohm B (2004) Pharmacokinetic aspects of biotechnology products. J Pharm Sci 93:2184-2204
    • (2004) J Pharm Sci , vol.93 , pp. 2184-2204
    • Tang, L.1    Persky, A.M.2    Hochhaus, G.3    Meibohm, B.4
  • 72
    • 28044433451 scopus 로고    scopus 로고
    • Protein posttranslational modifications: The chemistry of proteome diversifications
    • Walsh CT, Garneau-Tsodikova S, Gatto GJ (2005) Protein posttranslational modifications: the chemistry of proteome diversifications. Angew Chem Int Ed 44:7342-7372
    • (2005) Angew Chem Int Ed , vol.44 , pp. 7342-7372
    • Walsh, C.T.1    Garneau-Tsodikova, S.2    Gatto, G.J.3
  • 73
    • 0032782071 scopus 로고    scopus 로고
    • Instability, stabilization, and formulation of liquid protein pharmaceuticals
    • Wang W (1999) Instability, stabilization, and formulation of liquid protein pharmaceuticals. Int J Pharm 185:129-188
    • (1999) Int J Pharm , vol.185 , pp. 129-188
    • Wang, W.1
  • 74
    • 27144550160 scopus 로고    scopus 로고
    • Arming antibodies: Prospects and challenges for immunoconjugates
    • Wu AM, Senter PD (2005) Arming antibodies: prospects and challenges for immunoconjugates. Nat Biotechnol 23:1137-1146
    • (2005) Nat Biotechnol , vol.23 , pp. 1137-1146
    • Wu, A.M.1    Senter, P.D.2
  • 75
    • 8344271026 scopus 로고    scopus 로고
    • Production of recombinant protein therapeutics in cultivated mammalian cells
    • Wurn FM (2004) Production of recombinant protein therapeutics in cultivated mammalian cells. Nat Biotechnol 22:1393-1398
    • (2004) Nat Biotechnol , vol.22 , pp. 1393-1398
    • Wurn, F.M.1
  • 77
    • 3042689578 scopus 로고    scopus 로고
    • Mass spectral analysis in proteomics
    • Yates JR (2004) Mass spectral analysis in proteomics. Annu Rev Biophys Struct 33:297-316
    • (2004) Annu Rev Biophys Struct , vol.33 , pp. 297-316
    • Yates, J.R.1
  • 79
    • 0038610834 scopus 로고    scopus 로고
    • Reactions of polypeptide ions with electrons in the gas phase
    • Zubarev RA (2003) Reactions of polypeptide ions with electrons in the gas phase. Mass Spectrom Rev 22:57-77
    • (2003) Mass Spectrom Rev , vol.22 , pp. 57-77
    • Zubarev, R.A.1
  • 80
    • 1242351309 scopus 로고    scopus 로고
    • Electron capture dissociation mass spectrometry
    • Zubarev RA (2004) Electron capture dissociation mass spectrometry. Curr Opin Biotechnol 15:12-16
    • (2004) Curr Opin Biotechnol , vol.15 , pp. 12-16
    • Zubarev, R.A.1
  • 81
    • 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
  • 82
    • 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 RA, Kruger NA, Fridriksson EK, Lewis MA, Horn DM, Carpenter BK, McLafferty FW (1999) 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 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.