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Volumn 46, Issue 7, 2014, Pages 1625-1634

Recent developments and applications of electron transfer dissociation mass spectrometry in proteomics

Author keywords

Electron transfer dissociation; Glycosylation; Mass spectrometry; Phosphorylation; Top down proteomics

Indexed keywords

GLYCOPEPTIDE; PHOSPHOPROTEIN;

EID: 84903636844     PISSN: 09394451     EISSN: 14382199     Source Type: Journal    
DOI: 10.1007/s00726-014-1726-y     Document Type: Short Survey
Times cited : (37)

References (65)
  • 2
    • 60149111900 scopus 로고    scopus 로고
    • Characterization of glycopeptides by combining collision-induced dissociation and electron-transfer dissociation mass spectrometry data
    • Alley WR Jr, Mechref Y, Novotny MV (2009) Characterization of glycopeptides by combining collision-induced dissociation and electron-transfer dissociation mass spectrometry data. Rapid Commun Mass Spectrom 23:161-170
    • (2009) Rapid Commun Mass Spectrom , vol.23 , pp. 161-170
    • Alley Jr., W.R.1    Mechref, Y.2    Novotny, M.V.3
  • 4
    • 84856841046 scopus 로고    scopus 로고
    • 2-deoxy D-glucose prevents cell surface expression of NKG2D ligands through inhibition of N-linked glycosylation
    • Andresen L, Skovbakke SL, Persson G, Hagemann-Jensen M, Hansen KA, Jensen H, Skov S (2012) 2-deoxy D-glucose prevents cell surface expression of NKG2D ligands through inhibition of N-linked glycosylation. J Immunol 188:1847-1855
    • (2012) J Immunol , vol.188 , pp. 1847-1855
    • Andresen, L.1    Skovbakke, S.L.2    Persson, G.3    Hagemann-Jensen, M.4    Hansen, K.A.5    Jensen, H.6    Skov, S.7
  • 6
    • 33947204534 scopus 로고    scopus 로고
    • Electron transfer dissociation of N-glycopeptides: Loss of the entire N-glycosylated asparagine side chain
    • DOI 10.1002/rcm.2929
    • Catalina MI, Koeleman CA, Deelder AM, Wuhrer M (2007) Electron transfer dissociation of N-glycopeptides: loss of the entire N-glycosylated asparagine side chain. Rapid Commun Mass Spectrom 21:1053-1061 (Pubitemid 46426828)
    • (2007) Rapid Communications in Mass Spectrometry , vol.21 , Issue.6 , pp. 1053-1061
    • Catalina, M.I.1    Koeleman, C.A.M.2    Deelder, A.M.3    Wuhrer, M.4
  • 8
    • 84862786913 scopus 로고    scopus 로고
    • Development of a combined chemical and enzymatic approach for the mass spectrometric identification and quantification of aberrant N-glycosylation
    • Chen R, Wang F, Tan Y, Sun Z, Song C, Ye M, Wang H, Zou H (2012) Development of a combined chemical and enzymatic approach for the mass spectrometric identification and quantification of aberrant N-glycosylation. J Proteomics 75:1666-1674
    • (2012) J Proteomics , vol.75 , pp. 1666-1674
    • Chen, R.1    Wang, F.2    Tan, Y.3    Sun, Z.4    Song, C.5    Ye, M.6    Wang, H.7    Zou, H.8
  • 9
    • 84881201651 scopus 로고    scopus 로고
    • A 40-50 kDa glycoprotein associated with mucus is identified as a-1-acid glycoprotein in carcinoma of the stomach
    • Chirwa N, Govender D, Ndimba B, Lotz Z, Tyler M, Panieri E, Kahn D, Mall AS (2012) A 40-50 kDa glycoprotein associated with mucus is identified as a-1-acid glycoprotein in carcinoma of the stomach. J Cancer 3:83-92
    • (2012) J Cancer , vol.3 , pp. 83-92
    • Chirwa, N.1    Govender, D.2    Ndimba, B.3    Lotz, Z.4    Tyler, M.5    Panieri, E.6    Kahn, D.7    Mall, A.S.8
  • 11
    • 79960210781 scopus 로고    scopus 로고
    • Improved identification of O-linked glycopeptides from ETD data with optimized scoring for different charge states and cleavage specificities
    • Darula Z, Chalkley RJ, Lynn A, Baker PR, Medzihradszky KF (2011) Improved identification of O-linked glycopeptides from ETD data with optimized scoring for different charge states and cleavage specificities. Amino Acids 1:321-328
    • (2011) Amino Acids , vol.1 , pp. 321-328
    • Darula, Z.1    Chalkley, R.J.2    Lynn, A.3    Baker, P.R.4    Medzihradszky, K.F.5
  • 12
    • 72149102185 scopus 로고    scopus 로고
    • Affinity enrichment and characterization of mucin core-1 type glycopeptides from bovine serum
    • Darula Z, Medzihradszky KF (2009) Affinity enrichment and characterization of mucin core-1 type glycopeptides from bovine serum. Mol Cell Proteomics 8:2515-2526
    • (2009) Mol Cell Proteomics , vol.8 , pp. 2515-2526
    • Darula, Z.1    Medzihradszky, K.F.2
  • 13
    • 33847347565 scopus 로고    scopus 로고
    • Structural analysis of O-glycopeptides employing negative- and positive-ion multi-stage mass spectra obtained by collision-induced and electron-capture dissociations in linear ion trap time-of-flight mass spectrometry
    • DOI 10.1002/rcm.2885
    • Deguchi K, Ito H, Baba T, Hirabayashi A, Nakagawa H, Fumoto M, Hinou H, Nishimura S (2007) Structural analysis of O-glycopeptides employing negative- and positive-ion multi-stage mass spectra obtained by collision-induced and electron-capture dissociations in linear ion trap time-of-flight mass spectrometry. Rapid Commun Mass Spectrom 21:691-698 (Pubitemid 46340313)
    • (2007) Rapid Communications in Mass Spectrometry , vol.21 , Issue.5 , pp. 691-698
    • Deguchi, K.1    Ito, H.2    Baba, T.3    Hirabayashi, A.4    Nakagawa, H.5    Fumoto, M.6    Hinou, H.7    Nishimura, S.-I.8
  • 14
    • 33748310730 scopus 로고    scopus 로고
    • Protein analysis: From proteins to proteomes
    • Delom F, Chevet E (2006) Protein analysis: from proteins to proteomes. Proteome Sci 4:15
    • (2006) Proteome Sci , vol.4 , pp. 15
    • Delom, F.1    Chevet, E.2
  • 15
    • 84867576799 scopus 로고    scopus 로고
    • Gas-phase dissociation of glycosylated peptide ions
    • Dodds ED (2012) Gas-phase dissociation of glycosylated peptide ions. Mass Spectrom Rev 31:666-682
    • (2012) Mass Spectrom Rev , vol.31 , pp. 666-682
    • Dodds, E.D.1
  • 16
    • 84867009703 scopus 로고    scopus 로고
    • Application of the ETD/PTR reactions in top-down proteomics as a faster alternative to bottom-up nanoLC-MS/MS protein identification
    • Drabik A, Bodzon-Kulakowska A, Suder P (2012) Application of the ETD/PTR reactions in top-down proteomics as a faster alternative to bottom-up nanoLC-MS/MS protein identification. J Mass Spectrom 47:1347-1352
    • (2012) J Mass Spectrom , vol.47 , pp. 1347-1352
    • Drabik, A.1    Bodzon-Kulakowska, A.2    Suder, P.3
  • 17
    • 79551503762 scopus 로고    scopus 로고
    • Catch me if you can: Mass spectrometry-based phosphoproteomics and quantification strategies
    • Eyrich B, Sickmann A, Zahedi RP (2011) Catch me if you can: mass spectrometry-based phosphoproteomics and quantification strategies. Proteomics 11:554-570
    • (2011) Proteomics , vol.11 , pp. 554-570
    • Eyrich, B.1    Sickmann, A.2    Zahedi, R.P.3
  • 18
    • 84861389555 scopus 로고    scopus 로고
    • Herpes B virus utilizes human nectin-1 but not HVEM or PILRα for cell-cell fusion and virus entry
    • Fan Q, Amen M, Harden M, Severini A, Griffiths A, Longnecker R (2012) Herpes B virus utilizes human nectin-1 but not HVEM or PILRα for cell-cell fusion and virus entry. J Virol 86:4468-4476
    • (2012) J Virol , vol.86 , pp. 4468-4476
    • Fan, Q.1    Amen, M.2    Harden, M.3    Severini, A.4    Griffiths, A.5    Longnecker, R.6
  • 19
    • 84868535848 scopus 로고    scopus 로고
    • Fully automated chip-based nanoelectrospray combined with electron transfer dissociation for high throughput top-down proteomics
    • Flangea C, Schiopu C, Capitan F, Mosoarca C, Manea M, Sisu E, Zamfir AD (2013) Fully automated chip-based nanoelectrospray combined with electron transfer dissociation for high throughput top-down proteomics. Cent Eur J Chem 11:25-34
    • (2013) Cent Eur J Chem , vol.11 , pp. 25-34
    • Flangea, C.1    Schiopu, C.2    Capitan, F.3    Mosoarca, C.4    Manea, M.5    Sisu, E.6    Zamfir, A.D.7
  • 21
    • 79751504755 scopus 로고    scopus 로고
    • Phosphorylation mechanism and structure of serine-arginine protein kinases
    • Ghosh G, Adams JA (2011) Phosphorylation mechanism and structure of serine-arginine protein kinases. FEBS J 278:587-597
    • (2011) FEBS J , vol.278 , pp. 587-597
    • Ghosh, G.1    Adams, J.A.2
  • 22
    • 84865737357 scopus 로고    scopus 로고
    • Peptide identification by tandem mass spectrometry with alternate fragmentation modes
    • Guthals A, Bandeira N (2012) Peptide identification by tandem mass spectrometry with alternate fragmentation modes. Mol Cell Proteomics 9:550-557
    • (2012) Mol Cell Proteomics , vol.9 , pp. 550-557
    • Guthals, A.1    Bandeira, N.2
  • 23
    • 84873401358 scopus 로고    scopus 로고
    • LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins
    • Halim A, Rüetschi U, Larson G, Nilsson J (2013) LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins. J Proteome Res 12:573-584
    • (2013) J Proteome Res , vol.12 , pp. 573-584
    • Halim, A.1    Rüetschi, U.2    Larson, G.3    Nilsson, J.4
  • 24
    • 42949096464 scopus 로고    scopus 로고
    • Rapidly alternating transmission mode electron-transfer dissociation and collisional activation for the characterization of polypeptide ions
    • DOI 10.1021/ac7022734
    • Han H, Xia Y, Yang M, McLuckey SA (2008) Rapidly alternating transmission mode electron-transfer dissociation and collisional activation for the characterization of polypeptide ions. Anal Chem 80:3492-3497 (Pubitemid 351620739)
    • (2008) Analytical Chemistry , vol.80 , Issue.9 , pp. 3492-3497
    • Han, H.1    Xia, Y.2    Yang, M.3    McLuckey, S.A.4
  • 25
    • 84856330250 scopus 로고    scopus 로고
    • O-glycoproteomics: Site-specific O-glycoprotein analysis by CID/ETD electrospray ionization tandem mass spectrometry and top-down glycoprotein sequencing by insource decay MALDI mass spectrometry
    • Hanisch FG (2012) O-glycoproteomics: site-specific O-glycoprotein analysis by CID/ETD electrospray ionization tandem mass spectrometry and top-down glycoprotein sequencing by insource decay MALDI mass spectrometry. Methods Mol Biol 842:179-189
    • (2012) Methods Mol Biol , vol.842 , pp. 179-189
    • Hanisch, F.G.1
  • 26
    • 84869476043 scopus 로고    scopus 로고
    • Automated and high confidence protein phosphorylation site localization using complementary collision-activated dissociation and electron transfer dissociation tandem mass spectrometry
    • Hansen TA, Sylvester M, Jensen ON, Kjeldsen F (2012) Automated and high confidence protein phosphorylation site localization using complementary collision-activated dissociation and electron transfer dissociation tandem mass spectrometry. Anal Chem 84:9694-9699
    • (2012) Anal Chem , vol.84 , pp. 9694-9699
    • Hansen, T.A.1    Sylvester, M.2    Jensen, O.N.3    Kjeldsen, F.4
  • 27
    • 79955555659 scopus 로고    scopus 로고
    • Targeting the phosphatidylinositol 3-kinase signaling pathway in breast cancer
    • Hernandez-Aya LF, Gonzalez-Angulo AM (2011) Targeting the phosphatidylinositol 3-kinase signaling pathway in breast cancer. Oncologist 16:404-414
    • (2011) Oncologist , vol.16 , pp. 404-414
    • Hernandez-Aya, L.F.1    Gonzalez-Angulo, A.M.2
  • 28
    • 17444375706 scopus 로고    scopus 로고
    • Complementary structural information from a tryptic N-linked glycopeptide via electron transfer ion/ion reactions and collision-induced dissociation
    • DOI 10.1021/pr049770q
    • Hogan JM, Pitteri SJ, Chrisman PA, McLuckey SA (2005) Complementary structural information from a tryptic N-linked glycopeptide via electron transfer ion/ion reactions and collision-induced dissociation. J Proteome Res 4:628-632 (Pubitemid 40548173)
    • (2005) Journal of Proteome Research , vol.4 , Issue.2 , pp. 628-632
    • Hogan, J.M.1    Pitteri, S.J.2    Chrisman, P.A.3    McLuckey, S.A.4
  • 29
    • 84855405436 scopus 로고    scopus 로고
    • Tandem mass tag protein labeling for top-down identification and quantification
    • Hung CW, Tholey A (2012) Tandem mass tag protein labeling for top-down identification and quantification. Anal Chem 84:161-170
    • (2012) Anal Chem , vol.84 , pp. 161-170
    • Hung, C.W.1    Tholey, A.2
  • 30
    • 80051624221 scopus 로고    scopus 로고
    • Dissociation techniques in mass spectrometry-based proteomics
    • Jones AW, Cooper HJ (2011) Dissociation techniques in mass spectrometry-based proteomics. Analyst 136:3419-3429
    • (2011) Analyst , vol.136 , pp. 3419-3429
    • Jones, A.W.1    Cooper, H.J.2
  • 32
    • 84859222468 scopus 로고    scopus 로고
    • Electron transfer dissociation mass spectrometry in proteomics
    • Kim MS, Pandey A (2012) Electron transfer dissociation mass spectrometry in proteomics. Proteomics 12:530-542
    • (2012) Proteomics , vol.12 , pp. 530-542
    • Kim, M.S.1    Pandey, A.2
  • 33
    • 80051672948 scopus 로고    scopus 로고
    • Tools for analyzing the phosphoproteome and other phosphorylated biomolecules: A review
    • Leitner A, Sturm M, Lindner W (2011) Tools for analyzing the phosphoproteome and other phosphorylated biomolecules: a review. Anal Chim Acta 703:19-30
    • (2011) Anal Chim Acta , vol.703 , pp. 19-30
    • Leitner, A.1    Sturm, M.2    Lindner, W.3
  • 34
    • 79952690543 scopus 로고    scopus 로고
    • How phosphorylation controls p53
    • MacLaine NJ, Hupp TR (2011) How phosphorylation controls p53. Cell Cycle 10:916-921
    • (2011) Cell Cycle , vol.10 , pp. 916-921
    • MacLaine, N.J.1    Hupp, T.R.2
  • 35
    • 84874103116 scopus 로고    scopus 로고
    • Glycopeptide identification using liquid-chromatography-compatible hot electron capture dissociation in a radiofrequency-quadrupole ion trap
    • Manri N, Satake H, Kaneko A, Hirabayashi A, Baba T, Sakamoto T (2013) Glycopeptide identification using liquid-chromatography-compatible hot electron capture dissociation in a radiofrequency-quadrupole ion trap. Anal Chem 85:2056-2063
    • (2013) Anal Chem , vol.85 , pp. 2056-2063
    • Manri, N.1    Satake, H.2    Kaneko, A.3    Hirabayashi, A.4    Baba, T.5    Sakamoto, T.6
  • 36
    • 84877328542 scopus 로고    scopus 로고
    • Top-down structural analysis of an intact monoclonal antibody by electron capture dissociation-Fourier transform ion cyclotron resonance-mass spectrometry
    • Mao Y, Valeja SG, Rouse JC, Hendrickson CL, Marshall AG (2013) Top-down structural analysis of an intact monoclonal antibody by electron capture dissociation-Fourier transform ion cyclotron resonance-mass spectrometry. Anal Chem 85:4239-4246
    • (2013) Anal Chem , vol.85 , pp. 4239-4246
    • Mao, Y.1    Valeja, S.G.2    Rouse, J.C.3    Hendrickson, C.L.4    Marshall, A.G.5
  • 37
    • 84903644538 scopus 로고    scopus 로고
    • Practical aspects of trapped ion mass spectrometry
    • CRC Press, USA
    • McAlister GC, Coon JJ (2010) Practical aspects of trapped ion mass spectrometry, Applications of ion trapping devices, vol V. CRC Press, USA, pp 59-73
    • (2010) Applications of Ion Trapping Devices , vol.5 , pp. 59-73
    • McAlister, G.C.1    Coon, J.J.2
  • 40
    • 84862596522 scopus 로고    scopus 로고
    • Impact of phosphoproteomics on studies of bacterial physiology
    • Mijakovic I, Macek B (2012) Impact of phosphoproteomics on studies of bacterial physiology. FEMS Microbiol Rev 36:877-892
    • (2012) FEMS Microbiol Rev , vol.36 , pp. 877-892
    • Mijakovic, I.1    Macek, B.2
  • 43
    • 84874978868 scopus 로고    scopus 로고
    • Top-down structural analysis of posttranslationally modified proteins by Fourier transform ion cyclotron resonance-MS with hydrogen/deuterium exchange and electron capture dissociation
    • Pan J, Borchers CH (2013) Top-down structural analysis of posttranslationally modified proteins by Fourier transform ion cyclotron resonance-MS with hydrogen/deuterium exchange and electron capture dissociation. Proteomics 13:974-981
    • (2013) Proteomics , vol.13 , pp. 974-981
    • Pan, J.1    Borchers, C.H.2
  • 44
    • 61849088987 scopus 로고    scopus 로고
    • Elucidation of O-glycosylation structures of the beta-amyloid precursor protein by liquid chromatography-mass spectrometry using electron transfer dissociation and collision induced dissociation
    • Perdivara I, Petrovich R, Allinquant B, Deterding LJ, Tomer KB, Przybylski M (2009) Elucidation of O-glycosylation structures of the beta-amyloid precursor protein by liquid chromatography-mass spectrometry using electron transfer dissociation and collision induced dissociation. J Proteome Res 8:631-642
    • (2009) J Proteome Res , vol.8 , pp. 631-642
    • Perdivara, I.1    Petrovich, R.2    Allinquant, B.3    Deterding, L.J.4    Tomer, K.B.5    Przybylski, M.6
  • 46
    • 79953174969 scopus 로고    scopus 로고
    • Simultaneous glycan-peptide characterization using hydrophilic interaction chromatography and parallel fragmentation by CID, higher energy collisional dissociation, and electron transfer dissociation MS applied to the N-linked glycoproteome of Campylobacter jejuni
    • Scott NE, Parker BL, Connolly AM, Paulech J, Edwards AV, Crossett B, Falconer L, Kolarich D, Djordjevic SP, Højrup P, Packer NH, Larsen MR, Cordwell SJ (2011) Simultaneous glycan-peptide characterization using hydrophilic interaction chromatography and parallel fragmentation by CID, higher energy collisional dissociation, and electron transfer dissociation MS applied to the N-linked glycoproteome of Campylobacter jejuni. Mol Cell Proteomics 10(2):M000031-MCP201
    • (2011) Mol Cell Proteomics , vol.10 , Issue.2
    • Scott, N.E.1    Parker, B.L.2    Connolly, A.M.3    Paulech, J.4    Edwards, A.V.5    Crossett, B.6    Falconer, L.7    Kolarich, D.8    Djordjevic, S.P.9    Højrup, P.10    Packer, N.H.11    Larsen, M.R.12    Cordwell, S.J.13
  • 47
    • 84866084330 scopus 로고    scopus 로고
    • Higher energy collision dissociation (HCD) product ion-triggered electron transfer dissociation (ETD) mass spectrometry for the analysis of N-linked glycoproteins
    • Singh C, Zampronio CG, Creese AJ, Cooper HJ (2012) Higher energy collision dissociation (HCD) product ion-triggered electron transfer dissociation (ETD) mass spectrometry for the analysis of N-linked glycoproteins. J Proteome Res 11:4517-4525
    • (2012) J Proteome Res , vol.11 , pp. 4517-4525
    • Singh, C.1    Zampronio, C.G.2    Creese, A.J.3    Cooper, H.J.4
  • 48
    • 77949569318 scopus 로고    scopus 로고
    • A simple cellulose column procedure for selective enrichment of glycopeptides and characterization by nano LC coupled with electrontransfer and high-energy collisional-dissociation tandem mass spectrometry
    • Snovida SI, Bodnar ED, Viner R, Saba J, Perreault H (2010) A simple cellulose column procedure for selective enrichment of glycopeptides and characterization by nano LC coupled with electrontransfer and high-energy collisional-dissociation tandem mass spectrometry. Carbohydr Res 345:792-801
    • (2010) Carbohydr Res , vol.345 , pp. 792-801
    • Snovida, S.I.1    Bodnar, E.D.2    Viner, R.3    Saba, J.4    Perreault, H.5
  • 49
    • 59049086847 scopus 로고    scopus 로고
    • Human embryonic stem cell phosphoproteome revealed by electron transfer dissociation tandem mass spectrometry
    • Swaney DL, Wenger CD, Thomson JA, Coon JJ (2009) Human embryonic stem cell phosphoproteome revealed by electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci USA 106:995-1000
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 995-1000
    • Swaney, D.L.1    Wenger, C.D.2    Thomson, J.A.3    Coon, J.J.4
  • 51
    • 83755220066 scopus 로고    scopus 로고
    • Site-specific characterisation of densely O-glycosylated mucin-type peptides using electron transfer dissociation ESI-MS/MS
    • Thaysen-Andersen M, Wilkinson BL, Payne RJ, Packer NH (2011) Site-specific characterisation of densely O-glycosylated mucin-type peptides using electron transfer dissociation ESI-MS/MS. Electrophoresis 32:3536-3545
    • (2011) Electrophoresis , vol.32 , pp. 3536-3545
    • Thaysen-Andersen, M.1    Wilkinson, B.L.2    Payne, R.J.3    Packer, N.H.4
  • 52
    • 84876194893 scopus 로고    scopus 로고
    • Structure of the non-catalytic domain of the protein disulfide isomerase-related protein (PDIR) reveals function in protein binding
    • Vinaik R, Kozlov G, Gehring K (2013) Structure of the non-catalytic domain of the protein disulfide isomerase-related protein (PDIR) reveals function in protein binding. PLoS One 8(4):e62021
    • (2013) PLoS One , vol.8 , Issue.4
    • Vinaik, R.1    Kozlov, G.2    Gehring, K.3
  • 53
    • 79954616758 scopus 로고    scopus 로고
    • Ultrasensitive characterization of site-specific glycosylation of affinity-purified haptoglobin from lung cancer patient plasma using 10 μm i.D. Porous layer open tubular liquid chromatography-linear ion trap collision-induced dissociation/electron transfer dissociation mass spectrometry
    • Wang D, Hincapie M, Rejtar T, Karger BL (2011) Ultrasensitive characterization of site-specific glycosylation of affinity-purified haptoglobin from lung cancer patient plasma using 10 μm i.d. porous layer open tubular liquid chromatography-linear ion trap collision-induced dissociation/electron transfer dissociation mass spectrometry. Anal Chem 83:2029-2037
    • (2011) Anal Chem , vol.83 , pp. 2029-2037
    • Wang, D.1    Hincapie, M.2    Rejtar, T.3    Karger, B.L.4
  • 54
    • 30144438909 scopus 로고    scopus 로고
    • Methods in enzymology
    • Elsevier Academic Press, USA
    • Wells JM, McLuckey SA (2005) Methods in enzymology, Biological mass spectrometry, vol 402. Elsevier Academic Press, USA, pp 148-186
    • (2005) Biological Mass Spectrometry , vol.402 , pp. 148-186
    • Wells, J.M.1    McLuckey, S.A.2
  • 55
    • 36349016738 scopus 로고    scopus 로고
    • On-line LC-MS approach combining collision-induced dissociation (CID), electron-transfer dissociation (ETD), and CID of an isolated charge-reduced species for the trace-level characterization of proteins with post-translational modifications
    • DOI 10.1021/pr070313u
    • Wu SL, Hühmer AF, Hao Z, Karger BL (2007) On-line LC-MS approach combining collision-induced dissociation (CID), electron-transfer dissociation (ETD), and CID of an isolated charge-reduced species for the trace-level characterization of proteins with post-translational modifications. J Proteome Res 6:4230-4244 (Pubitemid 350158501)
    • (2007) Journal of Proteome Research , vol.6 , Issue.11 , pp. 4230-4244
    • Wu, S.-L.1    Huhmer, A.F.R.2    Hao, Z.3    Karger, B.L.4
  • 56
    • 84856238781 scopus 로고    scopus 로고
    • Elucidation of the sugar recognition ability of the lectin domain of UDP-GalNAc:Polypeptide N-acetylgalactosaminyltransferase 3 by using unnatural glycopeptide substrates
    • Yoshimura Y, Nudelman AS, Levery SB, Wandall HH, Bennett EP, Hindsgaul O, Clausen H, Nishimura S (2012) Elucidation of the sugar recognition ability of the lectin domain of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3 by using unnatural glycopeptide substrates. Glycobiology 22:429-438
    • (2012) Glycobiology , vol.22 , pp. 429-438
    • Yoshimura, Y.1    Nudelman, A.S.2    Levery, S.B.3    Wandall, H.H.4    Bennett, E.P.5    Hindsgaul, O.6    Clausen, H.7    Nishimura, S.8
  • 57
    • 79951996840 scopus 로고    scopus 로고
    • Comprehensive characterization of the site-specific N-glycosylation of wild-type and recombinant human lactoferrin expressed in the milk of transgenic cloned cattle
    • Yu T, Guo C, Wang J, Hao P, Sui S, Chen X, Zhang R, Wang P, Yu G, Zhang L, Dai Y, Li N (2011) Comprehensive characterization of the site-specific N-glycosylation of wild-type and recombinant human lactoferrin expressed in the milk of transgenic cloned cattle. Glycobiology 21:206-224
    • (2011) Glycobiology , vol.21 , pp. 206-224
    • Yu, T.1    Guo, C.2    Wang, J.3    Hao, P.4    Sui, S.5    Chen, X.6    Zhang, R.7    Wang, P.8    Yu, G.9    Zhang, L.10    Dai, Y.11    Li, N.12
  • 60
    • 34250797997 scopus 로고    scopus 로고
    • Enrichment and analysis of nonenzymatically glycated peptides: Boronate affinity chromatography coupled with electron-transfer dissociation mass spectrometry
    • DOI 10.1021/pr070112q
    • Zhang Q, Tang N, Brock JW, Mottaz HM, Ames JM, Baynes JW, Smith RD, Metz TO (2007) Enrichment and analysis of nonenzymatically glycated peptides: boronate affinity chromatography coupled with electron-transfer dissociation mass spectrometry. J Proteome Res 6:2323-2330 (Pubitemid 46985120)
    • (2007) Journal of Proteome Research , vol.6 , Issue.6 , pp. 2323-2330
    • Zhang, Q.1    Tang, N.2    Brock, J.W.C.3    Mottaz, H.M.4    Ames, J.M.5    Baynes, J.W.6    Smith, R.D.7    Metz, T.O.8
  • 61
    • 80053533242 scopus 로고    scopus 로고
    • Electron transfer dissociation of modified peptides and proteins
    • Zhou Y, Dong J, Vachet RW (2011) Electron transfer dissociation of modified peptides and proteins. Curr Pharm Biotechnol 12:1558-1567
    • (2011) Curr Pharm Biotechnol , vol.12 , pp. 1558-1567
    • Zhou, Y.1    Dong, J.2    Vachet, R.W.3
  • 62
    • 84877780038 scopus 로고    scopus 로고
    • Principles of electron capture and transfer dissociation mass spectrometry applied to peptide and protein structure analysis
    • Zhurov KO, Fornelli L, Wodrich MD, Laskay UA, Tsybin YO (2013) Principles of electron capture and transfer dissociation mass spectrometry applied to peptide and protein structure analysis. Chem Soc Rev 42(12):5014-5030
    • (2013) Chem Soc Rev , vol.42 , Issue.12 , pp. 5014-5030
    • Zhurov, K.O.1    Fornelli, L.2    Wodrich, M.D.3    Laskay, U.A.4    Tsybin, Y.O.5
  • 63
    • 33745616790 scopus 로고    scopus 로고
    • Protein primary structure using orthogonal fragmentation techniques in Fourier transform mass spectrometry
    • Zubarev R (2006) Protein primary structure using orthogonal fragmentation techniques in Fourier transform mass spectrometry. Expert Rev Proteomics 3:251-261
    • (2006) Expert Rev Proteomics , vol.3 , pp. 251-261
    • Zubarev, R.1
  • 64
    • 1242351309 scopus 로고    scopus 로고
    • Electron-capture dissociation tandem mass spectrometry
    • Zubarev RA (2004) Electron-capture dissociation tandem mass spectrometry. Curr Opin Biotechnol 15:12-16
    • (2004) Curr Opin Biotechnol , vol.15 , pp. 12-16
    • Zubarev, R.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.