메뉴 건너뛰기




Volumn 100, Issue , 2014, Pages 160-166

Using isotopically-coded hydrogen peroxide as a surface modification reagent for the structural characterization of prion protein aggregates

Author keywords

Chemical surface modification; Mass spectrometry; Oxidative labeling; Prion aggregate structure; Stable isotope labeled hydrogen peroxide; Structural proteomics

Indexed keywords

BETA OLIGOMERIC PRION PROTEIN; FIBRIL PRION PROTEIN; HYDROGEN PEROXIDE; METHIONINE; PRION PROTEIN; REAGENT; TRYPTOPHAN; UNCLASSIFIED DRUG; OXYGEN; PRION;

EID: 84897038817     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2013.11.020     Document Type: Article
Times cited : (8)

References (36)
  • 2
    • 84877815476 scopus 로고    scopus 로고
    • Using multiple structural proteomics approaches for the characterization of prion proteins
    • Serpa J.J., Patterson A.P., Pan J., Han J., Wishart D.S., Petrotchenko E.V., et al. Using multiple structural proteomics approaches for the characterization of prion proteins. J Proteomics 2013, 81:31-42.
    • (2013) J Proteomics , vol.81 , pp. 31-42
    • Serpa, J.J.1    Patterson, A.P.2    Pan, J.3    Han, J.4    Wishart, D.S.5    Petrotchenko, E.V.6
  • 4
    • 0034067250 scopus 로고    scopus 로고
    • Characterization of a discontinuous epitope of the human immunodeficiency virus (HIV) core protein p24 by epitope excision and differential chemical modification followed by mass spectrometric peptide mapping analysis
    • Hochleitner E.O., Borchers C., Parker C., Bienstock R.J., Tomer K.B. Characterization of a discontinuous epitope of the human immunodeficiency virus (HIV) core protein p24 by epitope excision and differential chemical modification followed by mass spectrometric peptide mapping analysis. Protein Sci 2000, 9:487-496.
    • (2000) Protein Sci , vol.9 , pp. 487-496
    • Hochleitner, E.O.1    Borchers, C.2    Parker, C.3    Bienstock, R.J.4    Tomer, K.B.5
  • 5
    • 34548337296 scopus 로고    scopus 로고
    • Hydroxyl radical-mediated modification of proteins as probes for structural proteomics
    • Xu G., Chance M.R. Hydroxyl radical-mediated modification of proteins as probes for structural proteomics. Chem Rev 2007, 107:3514-3543.
    • (2007) Chem Rev , vol.107 , pp. 3514-3543
    • Xu, G.1    Chance, M.R.2
  • 6
    • 58149462266 scopus 로고    scopus 로고
    • Structural characterization of short-lived protein unfolding intermediates by laser-induced oxidative labeling and mass spectrometry
    • Stocks B.B., Konermann L. Structural characterization of short-lived protein unfolding intermediates by laser-induced oxidative labeling and mass spectrometry. Anal Chem 2009, 81:20-27.
    • (2009) Anal Chem , vol.81 , pp. 20-27
    • Stocks, B.B.1    Konermann, L.2
  • 7
    • 77951765288 scopus 로고    scopus 로고
    • Time-dependent changes in side chain solvent accessibility during cytochrome c folding probed by pulsed oxidative labeling and mass spectrometry
    • Stocks B.B., Konermann L. Time-dependent changes in side chain solvent accessibility during cytochrome c folding probed by pulsed oxidative labeling and mass spectrometry. J Mol Biol 2010, 398:362-373.
    • (2010) J Mol Biol , vol.398 , pp. 362-373
    • Stocks, B.B.1    Konermann, L.2
  • 8
    • 27844593258 scopus 로고    scopus 로고
    • Laser flash photolysis of hydrogen peroxide to oxidize protein solvent-accessible residues on the microsecond timescale
    • Hambly D.M., Gross M.L. Laser flash photolysis of hydrogen peroxide to oxidize protein solvent-accessible residues on the microsecond timescale. J Am Soc Mass Spectrom 2005, 16:2057-2063.
    • (2005) J Am Soc Mass Spectrom , vol.16 , pp. 2057-2063
    • Hambly, D.M.1    Gross, M.L.2
  • 9
    • 68849107091 scopus 로고    scopus 로고
    • Fast photochemical oxidation of protein footprints faster than protein unfolding
    • Gau B.C., Sharp J.S., Rempel D.L., Gross M.L. Fast photochemical oxidation of protein footprints faster than protein unfolding. Anal Chem 2009, 81:6563-6571.
    • (2009) Anal Chem , vol.81 , pp. 6563-6571
    • Gau, B.C.1    Sharp, J.S.2    Rempel, D.L.3    Gross, M.L.4
  • 10
    • 80655131110 scopus 로고    scopus 로고
    • Thermodynamic analysis of protein-ligand interactions in complex biological mixtures using a shotgun proteomics approach
    • Dearmond P.D., Xu Y., Strickland E.C., Daniels K.G., Fitzgerald M.C. Thermodynamic analysis of protein-ligand interactions in complex biological mixtures using a shotgun proteomics approach. J Proteome Res 2011, 10:4948-4958.
    • (2011) J Proteome Res , vol.10 , pp. 4948-4958
    • Dearmond, P.D.1    Xu, Y.2    Strickland, E.C.3    Daniels, K.G.4    Fitzgerald, M.C.5
  • 11
    • 7544239102 scopus 로고    scopus 로고
    • Amyloid aggregates of the prion peptide PrP106-126 are destabilised by oxidation and by the action of dendrimers
    • Heegaard P.M., Pedersen H.G., Flink J., Boas U. Amyloid aggregates of the prion peptide PrP106-126 are destabilised by oxidation and by the action of dendrimers. FEBS Lett 2004, 577:127-133.
    • (2004) FEBS Lett , vol.577 , pp. 127-133
    • Heegaard, P.M.1    Pedersen, H.G.2    Flink, J.3    Boas, U.4
  • 14
    • 0033568535 scopus 로고    scopus 로고
    • Millisecond radiolytic modification of peptides by synchrotron X-rays identified by mass spectrometry
    • Maleknia S.D., Brenowitz M., Chance M.R. Millisecond radiolytic modification of peptides by synchrotron X-rays identified by mass spectrometry. Anal Chem 1999, 71:3965-3973.
    • (1999) Anal Chem , vol.71 , pp. 3965-3973
    • Maleknia, S.D.1    Brenowitz, M.2    Chance, M.R.3
  • 16
    • 66049152925 scopus 로고    scopus 로고
    • Design of anti- and pro-aggregation variants to assess the effects of methionine oxidation in human prion protein
    • Wolschner C., Giese A., Kretzschmar H.A., Huber R., Moroder L., Budisa N. Design of anti- and pro-aggregation variants to assess the effects of methionine oxidation in human prion protein. Proc Natl Acad Sci U S A 2009, 106:7756-7761.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 7756-7761
    • Wolschner, C.1    Giese, A.2    Kretzschmar, H.A.3    Huber, R.4    Moroder, L.5    Budisa, N.6
  • 18
    • 84865234351 scopus 로고    scopus 로고
    • Methionine oxidation perturbs the structural core of the prion protein and suggests a generic misfolding pathway
    • Younan N.D., Nadal R.C., Davies P., Brown D.R., Viles J.H. Methionine oxidation perturbs the structural core of the prion protein and suggests a generic misfolding pathway. J Biol Chem 2012, 287:28263-28275.
    • (2012) J Biol Chem , vol.287 , pp. 28263-28275
    • Younan, N.D.1    Nadal, R.C.2    Davies, P.3    Brown, D.R.4    Viles, J.H.5
  • 20
    • 79951623972 scopus 로고    scopus 로고
    • Detailed biophysical characterization of the acid-induced PrP(c) to PrP(β) conversion process
    • Bjorndahl T.C., Zhou G.P., Liu X., Perez-Pineiro R., Semenchenko V., Saleem F., et al. Detailed biophysical characterization of the acid-induced PrP(c) to PrP(β) conversion process. Biochemistry 2011, 50:1162-1173.
    • (2011) Biochemistry , vol.50 , pp. 1162-1173
    • Bjorndahl, T.C.1    Zhou, G.P.2    Liu, X.3    Perez-Pineiro, R.4    Semenchenko, V.5    Saleem, F.6
  • 21
    • 84897083659 scopus 로고    scopus 로고
    • ProteinProspector [Access date]
    • ProteinProspector ProteinProspector, v 5.10.11 [Access date]. http://prospector.ucsf.edu/prospector/mshome.htm.
    • ProteinProspector, v 5.10.11
  • 22
    • 0034480310 scopus 로고    scopus 로고
    • Electrospray mass and tandem mass spectrometry identification of ozone oxidation products of amino acids and small peptides
    • Kotiaho T., Eberlin M.N., Vainiotalo P., Kostiainen R. Electrospray mass and tandem mass spectrometry identification of ozone oxidation products of amino acids and small peptides. J Am Soc Mass Spectrom 2000, 11:526-535.
    • (2000) J Am Soc Mass Spectrom , vol.11 , pp. 526-535
    • Kotiaho, T.1    Eberlin, M.N.2    Vainiotalo, P.3    Kostiainen, R.4
  • 23
    • 0038825874 scopus 로고    scopus 로고
    • Detection and characterization of methionine oxidation in peptides by collision-induced dissociation and electron capture dissociation
    • Guan Z., Yates N.A., Bakhtiar R. Detection and characterization of methionine oxidation in peptides by collision-induced dissociation and electron capture dissociation. J Am Soc Mass Spectrom 2003, 14:605-613.
    • (2003) J Am Soc Mass Spectrom , vol.14 , pp. 605-613
    • Guan, Z.1    Yates, N.A.2    Bakhtiar, R.3
  • 24
    • 0029040377 scopus 로고
    • Mass spectrometric identification of amino acid transformations during oxidation of peptides and proteins: modifications of methionine and tyrosine
    • Chowdhury S.K., Eshraghi J., Wolfe H., Forde D., Hlavac A.G., Johnston D. Mass spectrometric identification of amino acid transformations during oxidation of peptides and proteins: modifications of methionine and tyrosine. Anal Chem 1995, 67:390-398.
    • (1995) Anal Chem , vol.67 , pp. 390-398
    • Chowdhury, S.K.1    Eshraghi, J.2    Wolfe, H.3    Forde, D.4    Hlavac, A.G.5    Johnston, D.6
  • 25
    • 0027647713 scopus 로고
    • Oxidation of peptides during electrospray ionization
    • Morand K., Talbo G., Mann M. Oxidation of peptides during electrospray ionization. Rapid Commun Mass Spectrom 1993, 7:738-743.
    • (1993) Rapid Commun Mass Spectrom , vol.7 , pp. 738-743
    • Morand, K.1    Talbo, G.2    Mann, M.3
  • 26
    • 33847648434 scopus 로고    scopus 로고
    • Oxidation artifacts in the electrospray mass spectrometry of Abeta Peptide
    • Chen M., Cook K.D. Oxidation artifacts in the electrospray mass spectrometry of Abeta Peptide. Anal Chem 2007, 79:2031-2036.
    • (2007) Anal Chem , vol.79 , pp. 2031-2036
    • Chen, M.1    Cook, K.D.2
  • 27
    • 0031812471 scopus 로고    scopus 로고
    • The identification of peptide modifications derived from gel-separated proteins using electrospray triple quadrupole and ion trap analyses
    • Swiderek K.M., Davis M.T., Lee T.D. The identification of peptide modifications derived from gel-separated proteins using electrospray triple quadrupole and ion trap analyses. Electrophoresis 1998, 19:989-997.
    • (1998) Electrophoresis , vol.19 , pp. 989-997
    • Swiderek, K.M.1    Davis, M.T.2    Lee, T.D.3
  • 28
    • 2342613564 scopus 로고    scopus 로고
    • Prevention of artifactual protein oxidation generated during sodium dodecyl sulfate-gel electrophoresis
    • Sun G., Anderson V.E. Prevention of artifactual protein oxidation generated during sodium dodecyl sulfate-gel electrophoresis. Electrophoresis 2004, 25:959-965.
    • (2004) Electrophoresis , vol.25 , pp. 959-965
    • Sun, G.1    Anderson, V.E.2
  • 29
    • 28244486826 scopus 로고    scopus 로고
    • Methionine oxidation interferes with conversion of the prion protein into the fibrillar proteinase K-resistant conformation
    • Breydo L., Bocharova O.V., Makarava N., Salnikov V.V., Anderson M., Baskakov I.V. Methionine oxidation interferes with conversion of the prion protein into the fibrillar proteinase K-resistant conformation. Biochemistry 2005, 44:15534-15543.
    • (2005) Biochemistry , vol.44 , pp. 15534-15543
    • Breydo, L.1    Bocharova, O.V.2    Makarava, N.3    Salnikov, V.V.4    Anderson, M.5    Baskakov, I.V.6
  • 35
    • 84863807078 scopus 로고    scopus 로고
    • Use of proteinase K non-specific digestion for selective and comprehensive identification of interpeptide crosslinks: application to prion proteins
    • [M111.013524]
    • Petrotchenko E.V., Serpa J.J., Berjanskii M., Suriyamongkol B.P., Wishart D.S., Borchers C.H. Use of proteinase K non-specific digestion for selective and comprehensive identification of interpeptide crosslinks: application to prion proteins. Mol Cell Proteomics 2012, 11. [M111.013524].
    • (2012) Mol Cell Proteomics , vol.11
    • Petrotchenko, E.V.1    Serpa, J.J.2    Berjanskii, M.3    Suriyamongkol, B.P.4    Wishart, D.S.5    Borchers, C.H.6
  • 36
    • 34250681413 scopus 로고    scopus 로고
    • Diversity in prion protein oligomerization pathways results from domain expansion as revealed by hydrogen/deuterium exchange and disulfide linkage
    • Eghiaian F., Daubenfeld T., Quenet Y., van Audenhaege M., Bouin A.-P., van der Rest G., et al. Diversity in prion protein oligomerization pathways results from domain expansion as revealed by hydrogen/deuterium exchange and disulfide linkage. Proc Natl Acad Sci 2007, 104:7414-7419.
    • (2007) Proc Natl Acad Sci , vol.104 , pp. 7414-7419
    • Eghiaian, F.1    Daubenfeld, T.2    Quenet, Y.3    van Audenhaege, M.4    Bouin, A.-P.5    van der Rest, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.