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Volumn 9, Issue 8, 2010, Pages 4053-4060

Identification of disulfide bonds in protein proteolytic degradation products using de novo -protein unique sequence tags approach

Author keywords

de novo sequencing; disulfide bonds; peptides; Peptidome; plasma; tandem mass spectrometry; unique sequence tags

Indexed keywords

ANTITHROMBIN III; CERULOPLASMIN; CYSTEINE; FIBRINOGEN; PEPTIDE; PROTEIN TAG; PROTHROMBIN; VITRONECTIN;

EID: 77955441004     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr1002559     Document Type: Article
Times cited : (7)

References (25)
  • 1
    • 51749114237 scopus 로고    scopus 로고
    • Protein folding includes oligomerization - Examples from the endoplasmic reticulum and cytosol
    • Christis, C.; Lubsen, N. H.; Braakman, I. Protein folding includes oligomerization-examples from the endoplasmic reticulum and cytosol FEBS J. 2008, 275, 4700-4727
    • (2008) FEBS J. , vol.275 , pp. 4700-4727
    • Christis, C.1    Lubsen, N.H.2    Braakman, I.3
  • 2
    • 66749163678 scopus 로고    scopus 로고
    • Disulfide formation in the ER and mitochondria: Two solutions to a common process
    • Riemer, J.; Bulleid, N.; Herrmann, J. M. Disulfide formation in the ER and mitochondria: two solutions to a common process Science 2009, 324, 1284-1287
    • (2009) Science , vol.324 , pp. 1284-1287
    • Riemer, J.1    Bulleid, N.2    Herrmann, J.M.3
  • 3
    • 70350504578 scopus 로고    scopus 로고
    • Targets of protective tumor immunity
    • Dranoff, G. Targets of protective tumor immunity Ann. N.Y. Acad. Sci. 2009, 1174, 74-80
    • (2009) Ann. N.Y. Acad. Sci. , vol.1174 , pp. 74-80
    • Dranoff, G.1
  • 4
    • 67849095440 scopus 로고    scopus 로고
    • Contribution of allosteric disulfide bonds to regulation of hemostasis
    • Hogg, P. J. Contribution of allosteric disulfide bonds to regulation of hemostasis J. Thromb. Haemost. 2009, 7, 12-16
    • (2009) J. Thromb. Haemost. , vol.7 , pp. 12-16
    • Hogg, P.J.1
  • 5
    • 62449244004 scopus 로고    scopus 로고
    • Cell death: Protein misfolding and neurodegenerative diseases
    • Nakamura, T.; Lipton, S. A. Cell death: protein misfolding and neurodegenerative diseases Apoptosis 2009, 14, 455-468
    • (2009) Apoptosis , vol.14 , pp. 455-468
    • Nakamura, T.1    Lipton, S.A.2
  • 6
    • 73149099387 scopus 로고    scopus 로고
    • Molecular basis for the recognition and cleavages of IGF-II, TGF-α, and amylin by human insulin-degrading enzyme
    • doi:10.1016/j.jmb.2009.10.072
    • Guo, Q.; Manolopoulou, M.; Bian, Y.; Schilling, A. B.; Tang, W-.J. Molecular basis for the recognition and cleavages of IGF-II, TGF-α, and amylin by human insulin-degrading enzyme J. Mol. Biol. 2009, doi:10.1016/j.jmb.2009.10.072
    • (2009) J. Mol. Biol.
    • Guo, Q.1    Manolopoulou, M.2    Bian, Y.3    Schilling, A.B.4    Tang -., W.J.5
  • 8
    • 0030841587 scopus 로고    scopus 로고
    • Electron-density map interpretation
    • Jones, T. A.; Kjeldgaard, M. Electron-density map interpretation Methods Enzymol. 1997, 277, 173-208
    • (1997) Methods Enzymol. , vol.277 , pp. 173-208
    • Jones, T.A.1    Kjeldgaard, M.2
  • 9
    • 0027236599 scopus 로고
    • Determination of the disulphide bonding pattern in proteins by local and global analysis of nuclear magnetic resonance data. Application to flavoridin
    • Klaus, W.; Broger, C.; Gerber, P.; Senn, H. Determination of the disulphide bonding pattern in proteins by local and global analysis of nuclear magnetic resonance data. Application to flavoridin J. Mol. Biol. 1993, 232, 897-906
    • (1993) J. Mol. Biol. , vol.232 , pp. 897-906
    • Klaus, W.1    Broger, C.2    Gerber, P.3    Senn, H.4
  • 10
    • 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
  • 11
    • 33845316805 scopus 로고    scopus 로고
    • De Novo sequencing and disulfide mapping of a bromotryptophan-containing conotoxin by Fourier transform ion cyclotron resonance mass spectrometry
    • Nair, S. S.; Nilsson, C. L.; Emmett, M. R.; Schaub, T. M.; Gowd, K. H.; Thakur, S. S.; Krishnan, K. S.; Balaram, P.; Marshall, A. G. De Novo sequencing and disulfide mapping of a bromotryptophan-containing conotoxin by Fourier transform ion cyclotron resonance mass spectrometry Anal. Chem. 2006, 78, 8082-8088
    • (2006) Anal. Chem. , vol.78 , pp. 8082-8088
    • Nair, S.S.1    Nilsson, C.L.2    Emmett, M.R.3    Schaub, T.M.4    Gowd, K.H.5    Thakur, S.S.6    Krishnan, K.S.7    Balaram, P.8    Marshall, A.G.9
  • 12
    • 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.; 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.2    Freitas, M.A.3
  • 13
    • 70349286679 scopus 로고    scopus 로고
    • Sequential proteolysis and high-field FTICR MS to determine disulfide connectivity and 4-maleimide TEMPO spin-label location in L126C GM2 activator protein
    • Tipton, J. D.; Carter, J. D.; Mathias, J. D.; Emmett, M. R.; Franucci, G. E.; Marshall, A. G. Sequential proteolysis and high-field FTICR MS to determine disulfide connectivity and 4-maleimide TEMPO spin-label location in L126C GM2 activator protein Anal. Chem. 2009, 81, 7611-7617
    • (2009) Anal. Chem. , vol.81 , pp. 7611-7617
    • Tipton, J.D.1    Carter, J.D.2    Mathias, J.D.3    Emmett, M.R.4    Franucci, G.E.5    Marshall, A.G.6
  • 15
    • 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
  • 17
    • 54349083037 scopus 로고    scopus 로고
    • De novo sequencing of unique sequence tags for discovery of post-translational modifications of proteins
    • Shen, Y.; Tolić, N.; Hixson, K. K.; Purvine, S. O.; Anderson, G. A.; Smith, R. D. De novo sequencing of unique sequence tags for discovery of post-translational modifications of proteins Anal. Chem. 2008, 80, 7742-7754
    • (2008) Anal. Chem. , vol.80 , pp. 7742-7754
    • Shen, Y.1    Tolić, N.2    Hixson, K.K.3    Purvine, S.O.4    Anderson, G.A.5    Smith, R.D.6
  • 19
    • 0022898222 scopus 로고
    • Prothrombin fragment 1•2•3, a major product of prothrombin activation in human plasma
    • Rabiet, M. J.; Blashill, A.; Furie, B.; Furie, B. C. Prothrombin fragment 1•2•3, a major product of prothrombin activation in human plasma J. Biol. Chem. 1986, 261, 13210-13215
    • (1986) J. Biol. Chem. , vol.261 , pp. 13210-13215
    • Rabiet, M.J.1    Blashill, A.2    Furie, B.3    Furie, B.C.4
  • 20
    • 0022257124 scopus 로고
    • Characterization of human S protein, an inhibitor of the membrane attack complex of complement. Demonstration of a free reactive thiol group
    • Dahlbäck, B.; Podack, E. R. Characterization of human S protein, an inhibitor of the membrane attack complex of complement. Demonstration of a free reactive thiol group Biochemistry 1985, 24, 2368-2374
    • (1985) Biochemistry , vol.24 , pp. 2368-2374
    • Dahlbäck, B.1    Podack, E.R.2
  • 21
    • 0018571889 scopus 로고
    • The thrombin cleavage site in bovine antithrombin
    • Jörnvall, H.; Fish, W. W.; Björk, I. The thrombin cleavage site in bovine antithrombin FEBS Lett. 1979, 106, 358-362
    • (1979) FEBS Lett. , vol.106 , pp. 358-362
    • Jörnvall, H.1    Fish, W.W.2    Björk, I.3
  • 22
    • 0015909639 scopus 로고
    • Primary structure of peptides released during activation of human plasminogen by urokinase
    • Wiman, B. Primary structure of peptides released during activation of human plasminogen by urokinase Eur. J. Biochem. 1973, 39, 109
    • (1973) Eur. J. Biochem. , vol.39 , pp. 109
    • Wiman, B.1
  • 23
    • 0022652530 scopus 로고
    • Detection of disulfide bonds and localization of interchain linkages in the their (C3) and the forth (C4) components of human complement
    • Janatova, J. Detection of disulfide bonds and localization of interchain linkages in the their (C3) and the forth (C4) components of human complement Biochem. J. 1986, 233, 819-825
    • (1986) Biochem. J. , vol.233 , pp. 819-825
    • Janatova, J.1
  • 25
    • 16644386648 scopus 로고    scopus 로고
    • The importance of disulfide bridging
    • Swaisgood, H. E. The importance of disulfide bridging Biotechnol. Adv. 2005, 23, 71-73
    • (2005) Biotechnol. Adv. , vol.23 , pp. 71-73
    • Swaisgood, H.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.