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Volumn 8, Issue 1, 2014, Pages

Applying the tools of chemistry (mass spectrometry and covalent modification by small molecule reagents) to the detection of prions and the study of their structure

Author keywords

Covalent modification; Lysine; Mass spectrometry; Monoclonal antibody; Prion; Western blot

Indexed keywords

AMINO ACID; ASPARAGINE; DISULFIDE; EPITOPE; LYSINE; METHIONINE; POLYMER; PRION PROTEIN; PROTEINASE K; REAGENT;

EID: 84896906381     PISSN: 19336896     EISSN: 1933690X     Source Type: Journal    
DOI: 10.4161/pri.27891     Document Type: Review
Times cited : (9)

References (120)
  • 1
    • 0022476747 scopus 로고
    • Scrapie and cellular PrP isoforms are encoded by the same chromosomal gene
    • Basler K, Oesch B, Scott M, Westaway D, Wälchli M, Groth DF, McKinley MP, Prusiner SB, Weissmann C. Scrapie and cellular PrP isoforms are encoded by the same chromosomal gene. Cell 1986; 46:417-28; PMID:2873895; http://dx.doi. org/10.1016/0092-8674(86)90662-8 (Pubitemid 16031678)
    • (1986) Cell , vol.46 , Issue.3 , pp. 417-428
    • Basler, K.1    Oesch, B.2    Scott, M.3
  • 2
    • 0022802258 scopus 로고
    • The major polypeptide of scrapie-associated fibrils (SAF) has the same size, charge distribution and N-terminal protein sequence as predicted for the normal brain protein (PrP)
    • PMID:3096712
    • Hope J, Morton LJ, Farquhar CF, Multhaup G, Beyreuther K, Kimberlin RH. The major polypeptide of scrapie-associated fibrils (SAF) has the same size, charge distribution and N-terminal protein sequence as predicted for the normal brain protein (PrP). EMBO J 1986; 5:2591-7; PMID:3096712
    • (1986) EMBO J , vol.5 , pp. 2591-2597
    • Hope, J.1    Morton, L.J.2    Farquhar, C.F.3    Multhaup, G.4    Beyreuther, K.5    Kimberlin, R.H.6
  • 3
    • 0027534612 scopus 로고
    • Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencing
    • Stahl N, Baldwin MA, Teplow DB, Hood L, Gibson BW, Burlingame AL, Prusiner SB. Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencing. Biochemistry 1993; 32:1991-2002; PMID:8448158; http://dx.doi. org/10.1021/bi00059a016 (Pubitemid 23086050)
    • (1993) Biochemistry , vol.32 , Issue.8 , pp. 1991-2002
    • Stahl, N.1    Baldwin, M.A.2    Teplow, D.B.3    Hood, L.4    Gibson, B.W.5    Burlingame, A.L.6    Prusiner, S.B.7
  • 4
    • 0021752457 scopus 로고
    • Purification and structural studies of a major scrapie prion protein
    • Prusiner SB, Groth DF, Bolton DC, Kent SB, Hood LE. Purification and structural studies of a major scrapie prion protein. Cell 1984; 38:127-34; PMID:6432339; http://dx.doi. org/10.1016/0092-8674(84)90533-6 (Pubitemid 15216542)
    • (1984) Cell , vol.38 , Issue.1 , pp. 127-134
    • Prusiner, S.B.1    Groth, D.F.2    Bolton, D.C.3
  • 5
    • 0023676109 scopus 로고
    • Purification and properties of the cellular and scrapie hamster prion proteins
    • PMID:3138115
    • Turk E, Teplow DB, Hood LE, Prusiner SB. Purification and properties of the cellular and scrapie hamster prion proteins. Eur J Biochem 1988; 176:21-30; PMID:3138115; http://dx.doi. org/10.1111/j.1432-1033.1988.tb14246.x
    • (1988) Eur J Biochem , vol.176 , pp. 21-30
    • Turk, E.1    Teplow, D.B.2    Hood, L.E.3    Prusiner, S.B.4
  • 6
    • 0022000573 scopus 로고
    • Scrapie PrP 27-30 is a sialoglycoprotein
    • Bolton DC, Meyer RK, Prusiner SB. Scrapie PrP 27-30 is a sialoglycoprotein. J Virol 1985; 53:596-606; PMID:3918176 (Pubitemid 15162162)
    • (1985) Journal of Virology , vol.53 , Issue.2 , pp. 596-606
    • Bolton, D.C.1    Meyer, R.K.2    Prusiner, S.B.3
  • 7
    • 0034932318 scopus 로고    scopus 로고
    • Mass spectrometric analysis of prion proteins
    • DOI 10.1016/S0065-3233(01)57017-5
    • Baldwin MA. Mass spectrometric analysis of prion proteins. Adv Protein Chem 2001; 57:29-54; PMID:11447694; http://dx.doi.org/10.1016/ S0065-3233(01)57017-5 (Pubitemid 32622679)
    • (2001) Advances in Protein Chemistry , vol.57 , pp. 29-54
    • Baldwin, M.A.1
  • 8
    • 0023663071 scopus 로고
    • Scrapie prion protein contains a phosphatidylinositol glycolipid
    • PMID:2444340
    • Stahl N, Borchelt DR, Hsiao K, Prusiner SB. Scrapie prion protein contains a phosphatidylinositol glycolipid. Cell 1987; 51:229-40; PMID:2444340; http://dx.doi.org/10.1016/0092-8674(87)90150-4
    • (1987) Cell , vol.51 , pp. 229-240
    • Stahl, N.1    Borchelt, D.R.2    Hsiao, K.3    Prusiner, S.B.4
  • 10
    • 0024434503 scopus 로고
    • Diversity of oligosaccharide structures linked to asparagines of the scrapie prion protein
    • Endo T, Groth D, Prusiner SB, Kobata A. Diversity of oligosaccharide structures linked to asparagines of the scrapie prion protein. Biochemistry 1989; 28:8380-8; PMID:2574992; http://dx.doi.org/10.1021/ bi00447a017 (Pubitemid 19269028)
    • (1989) Biochemistry , vol.28 , Issue.21 , pp. 8380-8388
    • Endo, T.1    Groth, D.2    Prusiner, S.B.3    Kobata, A.4
  • 12
    • 0033551196 scopus 로고    scopus 로고
    • Sitespecific characterization of the N-linked glycans of murine prion protein by high-performance liquid chromatography/electrospray mass spectrometry and exoglycosidase digestions
    • PMID:10200178
    • Stimson E, Hope J, Chong A, Burlingame AL. Sitespecific characterization of the N-linked glycans of murine prion protein by high-performance liquid chromatography/electrospray mass spectrometry and exoglycosidase digestions. Biochemistry 1999; 38:4885-95; PMID:10200178; http://dx.doi. org/10.1021/bi982330q
    • (1999) Biochemistry , vol.38 , pp. 4885-4895
    • Stimson, E.1    Hope, J.2    Chong, A.3    Burlingame, A.L.4
  • 13
    • 0026094450 scopus 로고
    • Electrospray mass spectrometry of the glycosylinositol phospholipid of the scrapie prion protein
    • PMID:1686992
    • Stahl N, Baldwin MA, Prusiner SB. Electrospray mass spectrometry of the glycosylinositol phospholipid of the scrapie prion protein. Cell Biol Int Rep 1991; 15:853-62; PMID:1686992; http://dx.doi. org/10.1016/0309-1651(91)90037-J.
    • (1991) Cell Biol Int Rep , vol.15 , pp. 853-862
    • Stahl, N.1    Baldwin, M.A.2    Prusiner, S.B.3
  • 14
    • 0026780714 scopus 로고
    • Glycosylinositol phospholipid anchors of the scrapie and cellular prion proteins contain sialic acid
    • PMID:1350920
    • Stahl N, Baldwin MA, Hecker R, Pan KM, Burlingame AL, Prusiner SB. Glycosylinositol phospholipid anchors of the scrapie and cellular prion proteins contain sialic acid. Biochemistry 1992; 31:5043-53; PMID:1350920; http://dx.doi. org/10.1021/bi00136a600
    • (1992) Biochemistry , vol.31 , pp. 5043-5053
    • Stahl, N.1    Baldwin, M.A.2    Hecker, R.3    Pan, K.M.4    Burlingame, A.L.5    Prusiner, S.B.6
  • 16
    • 84897038817 scopus 로고    scopus 로고
    • Using isotopicallycoded hydrogen peroxide as a surface modification reagent for the structural characterization of prion protein aggregates
    • (Forthcoming); PMID:24316355
    • Serpa JJ, Makepeace KA, Borchers TH, Wishart DS, Petrotchenko EV, Borchers CH. Using isotopicallycoded hydrogen peroxide as a surface modification reagent for the structural characterization of prion protein aggregates. J Proteomics 2013; (Forthcoming); PMID:24316355; http://dx.doi. org/10.1016/j.jprot.2013.11.020
    • (2013) J Proteomics
    • Serpa, J.J.1    Makepeace, K.A.2    Borchers, T.H.3    Wishart, D.S.4    Petrotchenko, E.V.5    Borchers, C.H.6
  • 19
    • 69949142350 scopus 로고    scopus 로고
    • Distinct structures of scrapie prion protein (PrPSc)-seeded versus spontaneous recombinant prion protein fibrils revealed by hydrogen/deuterium exchange
    • PMID:19596861
    • Smirnovas V, Kim JI, Lu X, Atarashi R, Caughey B, Surewicz WK. Distinct structures of scrapie prion protein (PrPSc)-seeded versus spontaneous recombinant prion protein fibrils revealed by hydrogen/deuterium exchange. J Biol Chem 2009; 284:24233-41; PMID:19596861; http://dx.doi. org/10.1074/jbc. M109.036558
    • (2009) J Biol Chem , vol.284 , pp. 24233-24241
    • Smirnovas, V.1    Kim, J.I.2    Lu, X.3    Atarashi, R.4    Caughey, B.5    Surewicz, W.K.6
  • 20
    • 23044458520 scopus 로고    scopus 로고
    • Sc structure using chemical cross-linking and mass spectrometry: Evidence of the proximity of Gly90 amino termini in the PrP 27-30 aggregate
    • DOI 10.1021/bi0501582
    • Onisko B, Fernández EG, Freire ML, Schwarz A, Baier M, Camiña F, García JR, Rodríguez-Segade Villamarín S, Requena JR. Probing PrPSc structure using chemical cross-linking and mass spectrometry: evidence of the proximity of Gly90 amino termini in the PrP 27-30 aggregate. Biochemistry 2005; 44:10100-9; PMID:16042387; http://dx.doi. org/10.1021/bi0501582 (Pubitemid 41076805)
    • (2005) Biochemistry , vol.44 , Issue.30 , pp. 10100-10109
    • Onisko, B.1    Fernandez, E.G.2    Freire, M.L.3    Schwarz, A.4    Baier, M.5    Camina, F.6    Garcia, J.R.7    Villamarin, S.R.-S.8    Requena, J.R.9
  • 21
    • 84863807078 scopus 로고    scopus 로고
    • Use of proteinase K nonspecific digestion for selective and comprehensive identification of interpeptide cross-links: Application to prion proteins
    • PMID:22438564
    • Petrotchenko EV, Serpa JJ, Hardie DB, Berjanskii M, Suriyamongkol BP, Wishart DS, Borchers CH. Use of proteinase K nonspecific digestion for selective and comprehensive identification of interpeptide cross-links: application to prion proteins. Mol Cell Proteomics 2012; 11:013524; PMID:22438564; http://dx.doi.org/10.1074/mcp.M111.013524
    • (2012) Mol Cell Proteomics , vol.11 , pp. 013524
    • Petrotchenko, E.V.1    Serpa, J.J.2    Hardie, D.B.3    Berjanskii, M.4    Suriyamongkol, B.P.5    Wishart, D.S.6    Borchers, C.H.7
  • 22
    • 84891956974 scopus 로고    scopus 로고
    • A New Paradigm for Enzymatic Control of alpha- Cleavage and beta-Cleavage of the Prion Protein
    • (Forthcoming); PMID:24247244
    • McDonald AJ, Dibble JP, Evans EG, Millhauser GL. A New Paradigm for Enzymatic Control of alpha- Cleavage and beta-Cleavage of the Prion Protein. J Biol Chem 2014; (Forthcoming); PMID:24247244; http://dx.doi.org/10.1074/jbc. M113.502351.
    • (2014) J Biol Chem
    • McDonald, A.J.1    Dibble, J.P.2    Evans, E.G.3    Millhauser, G.L.4
  • 23
    • 28444470228 scopus 로고    scopus 로고
    • PrP(Sc) typing by N-terminal sequencing and mass spectrometry
    • PMID:11214924
    • Chen SG, Zou W, Parchi P, Gambetti P. PrP(Sc) typing by N-terminal sequencing and mass spectrometry. Arch Virol Suppl 2000; 209-16; PMID:11214924
    • (2000) Arch Virol , Issue.SUPPL. , pp. 209-216
    • Chen, S.G.1    Zou, W.2    Parchi, P.3    Gambetti, P.4
  • 24
    • 62149128180 scopus 로고    scopus 로고
    • High-resolution differentiation of transmissible spongiform encephalopathy strains by quantitative N-terminal amino acid profiling (N-TAAP) of PK-digested abnormal prion protein
    • PMID:19053160
    • Gielbert A, Davis LA, Sayers AR, Hope J, Gill AC, Sauer MJ. High-resolution differentiation of transmissible spongiform encephalopathy strains by quantitative N-terminal amino acid profiling (N-TAAP) of PK-digested abnormal prion protein. J Mass Spectrom 2009; 44:384-96; PMID:19053160; http://dx.doi.org/10.1002/jms.1516
    • (2009) J Mass Spectrom , vol.44 , pp. 384-396
    • Gielbert, A.1    Davis, L.A.2    Sayers, A.R.3    Hope, J.4    Gill, A.C.5    Sauer, M.J.6
  • 25
    • 84874398957 scopus 로고    scopus 로고
    • Quantitative profiling of PrP(Sc) peptides by high-performance liquid chromatography mass spectrometry to investigate the diversity of prions
    • PMID:23357236
    • Gielbert A, Davis LA, Sayers AR, Tang Y, Hope J, Sauer MJ. Quantitative profiling of PrP(Sc) peptides by high-performance liquid chromatography mass spectrometry to investigate the diversity of prions. Anal Biochem 2013; 436:36-44; PMID:23357236; http://dx.doi.org/10.1016/j.ab.2013.01.015
    • (2013) Anal Biochem , vol.436 , pp. 36-44
    • Gielbert, A.1    Davis, L.A.2    Sayers, A.R.3    Tang, Y.4    Hope, J.5    Sauer, M.J.6
  • 26
    • 45749138009 scopus 로고    scopus 로고
    • Sc from scrapie-infected and bovine spongiform encephalopathy-infected mice
    • DOI 10.1080/13547500801903719, PII 793156474
    • Howells LC, Anderson S, Coldham NG, Sauer MJ. Transmissible spongiform encephalopathy strainassociated diversity of N-terminal proteinase K cleavage sites of PrP(Sc) from scrapie-infected and bovine spongiform encephalopathy-infected mice. Biomarkers 2008; 13:393-412; PMID:18484354; http://dx.doi.org/10.1080/13547500801903719 (Pubitemid 351865815)
    • (2008) Biomarkers , vol.13 , Issue.4 , pp. 393-412
    • Howells, L.C.1    Anderson, S.2    Coldham, N.C.3    Sauer, M.4
  • 27
    • 49349117873 scopus 로고    scopus 로고
    • Scrapie prion protein structural constraints obtained by limited proteolysis and mass spectrometry
    • PMID:18621059
    • Sajnani G, Pastrana MA, Dynin I, Onisko B, Requena JR. Scrapie prion protein structural constraints obtained by limited proteolysis and mass spectrometry. J Mol Biol 2008; 382:88-98; PMID:18621059; http://dx.doi.org/10. 1016/j. jmb.2008.06.070
    • (2008) J Mol Biol , vol.382 , pp. 88-98
    • Sajnani, G.1    Pastrana, M.A.2    Dynin, I.3    Onisko, B.4    Requena, J.R.5
  • 31
    • 77950379326 scopus 로고    scopus 로고
    • Fatal transmissible amyloid encephalopathy: A new type of prion disease associated with lack of prion protein membrane anchoring
    • PMID:20221436
    • Chesebro B, Race B, Meade-White K, Lacasse R, Race R, Klingeborn M, Striebel J, Dorward D, McGovern G, Jeffrey M. Fatal transmissible amyloid encephalopathy: a new type of prion disease associated with lack of prion protein membrane anchoring. PLoS Pathog 2010; 6:e1000800; PMID:20221436; http://dx.doi.org/10.1371/journal.ppat.1000800
    • (2010) PLoS Pathog , vol.6
    • Chesebro, B.1    Race, B.2    Meade-White, K.3    Lacasse, R.4    Race, R.5    Klingeborn, M.6    Striebel, J.7    Dorward, D.8    McGovern, G.9    Jeffrey, M.10
  • 32
    • 79953785159 scopus 로고    scopus 로고
    • Structural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange
    • PMID:21441913
    • Smirnovas V, Baron GS, Offerdahl DK, Raymond GJ, Caughey B, Surewicz WK. Structural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange. Nat Struct Mol Biol 2011; 18:504-6; PMID:21441913; http://dx.doi. org/10.1038/nsmb.2035
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 504-506
    • Smirnovas, V.1    Baron, G.S.2    Offerdahl, D.K.3    Raymond, G.J.4    Caughey, B.5    Surewicz, W.K.6
  • 36
    • 80052976271 scopus 로고    scopus 로고
    • Identification and removal of proteins that co-purify with infectious prion protein improves the analysis of its secondary structure
    • PMID:21805638
    • Moore RA, Timmes AG, Wilmarth PA, Safronetz D, Priola SA. Identification and removal of proteins that co-purify with infectious prion protein improves the analysis of its secondary structure. Proteomics 2011; 11:3853-65; PMID:21805638; http://dx.doi. org/10.1002/pmic.201100253
    • (2011) Proteomics , vol.11 , pp. 3853-3865
    • Moore, R.A.1    Timmes, A.G.2    Wilmarth, P.A.3    Safronetz, D.4    Priola, S.A.5
  • 37
    • 66049152925 scopus 로고    scopus 로고
    • Design of anti- and proaggregation variants to assess the effects of methionine oxidation in human prion protein
    • PMID:19416900
    • Wolschner C, Giese A, Kretzschmar HA, Huber R, Moroder L, Budisa N. Design of anti- and proaggregation variants to assess the effects of methionine oxidation in human prion protein. Proc Natl Acad Sci U S A 2009; 106:7756-61; PMID:19416900; http:// dx.doi.org/10.1073/pnas.0902688106
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 7756-7761
    • Wolschner, C.1    Giese, A.2    Kretzschmar, H.A.3    Huber, R.4    Moroder, L.5    Budisa, N.6
  • 38
    • 59349116776 scopus 로고    scopus 로고
    • Methionine sulfoxides on prion protein Helix-3 switch on the alpha-fold destabilization required for conversion
    • PMID:19172188
    • Colombo G, Meli M, Morra G, Gabizon R, Gasset M. Methionine sulfoxides on prion protein Helix-3 switch on the alpha-fold destabilization required for conversion. PLoS One 2009; 4:e4296; PMID:19172188; http://dx.doi.org/10.1371/ journal. pone.0004296
    • (2009) PLoS One , vol.4
    • Colombo, G.1    Meli, M.2    Morra, G.3    Gabizon, R.4    Gasset, M.5
  • 39
    • 84865234351 scopus 로고    scopus 로고
    • Methionine oxidation perturbs the structural core of the prion protein and suggests a generic misfolding pathway
    • PMID:22654104
    • Younan ND, Nadal RC, Davies P, Brown DR, Viles JH. Methionine oxidation perturbs the structural core of the prion protein and suggests a generic misfolding pathway. J Biol Chem 2012; 287:28263-75; PMID:22654104; http://dx.doi.org/10.1074/jbc. M112.354779
    • (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
  • 41
    • 77958126446 scopus 로고    scopus 로고
    • Oxidation of Helix-3 methionines precedes the formation of PK resistant PrP
    • PMID:20625387
    • Canello T, Frid K, Gabizon R, Lisa S, Friedler A, Moskovitz J, Gasset M, Gabizon R. Oxidation of Helix-3 methionines precedes the formation of PK resistant PrP. PLoS Pathog 2010; 6:e1000977; PMID:20625387; http://dx.doi.org/ 10.1371/journal. ppat.1000977
    • (2010) PLoS Pathog , vol.6
    • Canello, T.1    Frid, K.2    Gabizon, R.3    Lisa, S.4    Friedler, A.5    Moskovitz, J.6    Gasset, M.7    Gabizon, R.8
  • 42
    • 64549133370 scopus 로고    scopus 로고
    • Detection of oxidized methionine in selected proteins, cellular extracts and blood serums by novel anti-methionine sulfoxide antibodies
    • PMID:19388147
    • Oien DB, Canello T, Gabizon R, Gasset M, Lundquist BL, Burns JM, Moskovitz J. Detection of oxidized methionine in selected proteins, cellular extracts and blood serums by novel anti-methionine sulfoxide antibodies. Arch Biochem Biophys 2009; 485:35-40; PMID:19388147; http://dx.doi.org/10.1016/j. abb.2009.01.020
    • (2009) Arch Biochem Biophys , vol.485 , pp. 35-40
    • Oien, D.B.1    Canello, T.2    Gabizon, R.3    Gasset, M.4    Lundquist, B.L.5    Burns, J.M.6    Moskovitz, J.7
  • 43
    • 12844267504 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases: Ubiquitous enzymes involved in antioxidant defense, protein regulation, and prevention of aging-associated diseases
    • DOI 10.1016/j.bbapap.2004.09.003, PII S1570963904002419, Mewthionine Oxidation and Methionine Sulfoxide Reductases
    • Moskovitz J. Methionine sulfoxide reductases: ubiquitous enzymes involved in antioxidant defense, protein regulation, and prevention of aging-associated diseases. Biochim Biophys Acta 2005; 1703:213-9; PMID:15680229; http://dx.doi.org/10.1016/j. bbapap.2004.09.003 (Pubitemid 40170444)
    • (2005) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1703 , Issue.2 , pp. 213-219
    • Moskovitz, J.1
  • 45
    • 44549088533 scopus 로고    scopus 로고
    • The methionine sulfoxide reductases: Catalysis and substrate specificities
    • PMID:18302927
    • Boschi-Muller S, Gand A, Branlant G. The methionine sulfoxide reductases: Catalysis and substrate specificities. Arch Biochem Biophys 2008; 474:266-73; PMID:18302927; http://dx.doi. org/10.1016/j.abb.2008.02.007
    • (2008) Arch Biochem Biophys , vol.474 , pp. 266-273
    • Boschi-Muller, S.1    Gand, A.2    Branlant, G.3
  • 46
    • 12844264123 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases: History and cellular role in protecting against oxidative damage
    • DOI 10.1016/j.bbapap.2004.10.004, PII S1570963904002870, Mewthionine Oxidation and Methionine Sulfoxide Reductases
    • Weissbach H, Resnick L, Brot N. Methionine sulfoxide reductases: history and cellular role in protecting against oxidative damage. Biochim Biophys Acta 2005; 1703:203-12. (Pubitemid 40170443)
    • (2005) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1703 , Issue.2 , pp. 203-212
    • Weissbach, H.1    Resnick, L.2    Brot, N.3
  • 50
    • 28244486826 scopus 로고    scopus 로고
    • Methionine oxidation interferes with conversion of the prion protein into the fibrillar proteinase K-resistant conformation
    • DOI 10.1021/bi051369+
    • Breydo L, Bocharova OV, Makarava N, Salnikov VV, Anderson M, Baskakov IV. Methionine oxidation interferes with conversion of the prion protein into the fibrillar proteinase K-resistant conformation. Biochemistry 2005; 44:15534-43; PMID:16300402; http://dx.doi.org/10.1021/bi051369+ (Pubitemid 41706137)
    • (2005) Biochemistry , vol.44 , Issue.47 , pp. 15534-15543
    • Breydo, L.1    Bocharova, O.V.2    Makarava, N.3    Salnikov, V.V.4    Anderson, M.5    Baskakov, I.V.6
  • 51
    • 74949142621 scopus 로고    scopus 로고
    • Oligomers of the prion protein fragment 106-126 are likely assembled from beta-hairpins in solution, and methionine oxidation inhibits assembly without altering the peptide's monomeric conformation
    • PMID:20020713
    • Grabenauer M, Wu C, Soto P, Shea JE, Bowers MT. Oligomers of the prion protein fragment 106-126 are likely assembled from beta-hairpins in solution, and methionine oxidation inhibits assembly without altering the peptide's monomeric conformation. J Am Chem Soc 2010; 132:532-9; PMID:20020713; http://dx.doi.org/10.1021/ja905595k
    • (2010) J Am Chem Soc , vol.132 , pp. 532-539
    • Grabenauer, M.1    Wu, C.2    Soto, P.3    Shea, J.E.4    Bowers, M.T.5
  • 53
    • 2342613564 scopus 로고    scopus 로고
    • Prevention of artifactual protein oxidation generated during sodium dodecyl sulfate-gel electrophoresis
    • Sun G, Anderson VE. Prevention of artifactual protein oxidation generated during sodium dodecyl sulfate-gel electrophoresis. Electrophoresis 2004; 25:959-65; PMID:15095433; http://dx.doi. org/10.1002/elps.200305800 (Pubitemid 38578931)
    • (2004) Electrophoresis , vol.25 , Issue.7-8 , pp. 959-965
    • Sun, G.1    Anderson, V.E.2
  • 54
    • 0031812471 scopus 로고    scopus 로고
    • The identification of peptide modifications derived from gel-separated proteins using electrospray triple quadrupole and ion trap analyses
    • DOI 10.1002/elps.1150190614
    • Swiderek KM, Davis MT, Lee TD. The identification of peptide modifications derived from gel-separated proteins using electrospray triple quadrupole and ion trap analyses. Electrophoresis 1998; 19:989-97; PMID:9638945; http://dx.doi.org/10.1002/ elps.1150190614 (Pubitemid 28239968)
    • (1998) Electrophoresis , vol.19 , Issue.6 , pp. 989-997
    • Swiderek, K.M.1    Davis, M.T.2    Lee, T.D.3
  • 55
    • 0034480310 scopus 로고    scopus 로고
    • Electrospray mass and tandem mass spectrometry identification of ozone oxidation products of amino acids and small peptides
    • DOI 10.1016/S1044-0305(00)00116-1, PII S1044030500001161
    • Kotiaho T, Eberlin MN, 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 Spectrom2000; 11:526-35; PMID:10833026; http://dx.doi. org/10.1016/S1044-0305(00)00116-1 (Pubitemid 34527129)
    • (2000) Journal of the American Society for Mass Spectrometry , vol.11 , Issue.6 , pp. 526-535
    • Kotiaho, T.1    Eberlin, M.N.2    Vainiotalo, P.3    Kostiainen, R.4
  • 56
    • 0029040377 scopus 로고
    • Mass spectrometric identification of amino acid transformations during oxidation of peptides and proteins: Modifications of methionine and tyrosine
    • PMID:7856883
    • Chowdhury SK, Eshraghi J, Wolfe H, Forde D, Hlavac AG, Johnston D. Mass spectrometric identification of amino acid transformations during oxidation of peptides and proteins: modifications of methionine and tyrosine. Anal Chem 1995; 67:390-8; PMID:7856883; http://dx.doi.org/10.1021/ ac00098a026
    • (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
  • 57
    • 0038825874 scopus 로고    scopus 로고
    • Detection and characterization of methionine oxidation in peptides by collision-induced dissociation and electron capture dissociation
    • DOI 10.1016/S1044-0305(03)00201-0
    • Guan Z, Yates NA, Bakhtiar R. Detection and characterization of methionine oxidation in peptides by collision-induced dissociation and electron capture dissociation. J Am Soc Mass Spectrom 2003; 14:605-13; PMID:12781462; http://dx.doi.org/10.1016/ S1044-0305(03)00201-0 (Pubitemid 36870969)
    • (2003) Journal of the American Society for Mass Spectrometry , vol.14 , Issue.6 , pp. 605-613
    • Guan, Z.1    Yates, N.A.2    Bakhtiar, R.3
  • 58
    • 33847648434 scopus 로고    scopus 로고
    • Oxidation artifacts in the electrospray mass spectrometry of Aβ peptide
    • DOI 10.1021/ac061743r
    • Chen M, Cook KD. Oxidation artifacts in the electrospray mass spectrometry of Abeta Peptide. Anal Chem 2007; 79:2031-6; PMID:17249640; http://dx.doi.org/10.1021/ac061743r (Pubitemid 46355235)
    • (2007) Analytical Chemistry , vol.79 , Issue.5 , pp. 2031-2036
    • Chen, M.1    Cook, K.D.2
  • 59
    • 0027647713 scopus 로고
    • Oxidation of peptides during electrospray ionization
    • PMID:8374164
    • Morand K, Talbo G, Mann M. Oxidation of peptides during electrospray ionization. Rapid Commun Mass Spectrom 1993; 7:738-43; PMID:8374164; http:// dx.doi.org/10.1002/rcm.1290070811
    • (1993) Rapid Commun Mass Spectrom , vol.7 , pp. 738-743
    • Morand, K.1    Talbo, G.2    Mann, M.3
  • 60
    • 84875649985 scopus 로고    scopus 로고
    • Oxidation of methionine 216 in sheep and elk prion protein is highly dependent upon the amino acid at position 218 but is not important for prion propagation
    • PMID:23458153
    • Silva CJ, Dynin I, Erickson ML, Requena JR, Balachandran A, Hui C, Onisko BC, Carter JM. Oxidation of methionine 216 in sheep and elk prion protein is highly dependent upon the amino acid at position 218 but is not important for prion propagation. Biochemistry 2013; 52:2139-47; PMID:23458153; http://dx.doi.org/10.1021/ bi3016795
    • (2013) Biochemistry , vol.52 , pp. 2139-2147
    • Silva, C.J.1    Dynin, I.2    Erickson, M.L.3    Requena, J.R.4    Balachandran, A.5    Hui, C.6    Onisko, B.C.7    Carter, J.M.8
  • 61
    • 77749286409 scopus 로고    scopus 로고
    • Assessing the role of oxidized methionine at position 213 in the formation of prions in hamsters
    • PMID:20121218
    • Silva CJ, Onisko BC, Dynin I, Erickson ML, Vensel WH, Requena JR, Antaki EM, Carter JM. Assessing the role of oxidized methionine at position 213 in the formation of prions in hamsters. Biochemistry 2010; 49:1854-61; PMID:20121218; http://dx.doi. org/10.1021/bi901850n
    • (2010) Biochemistry , vol.49 , pp. 1854-1861
    • Silva, C.J.1    Onisko, B.C.2    Dynin, I.3    Erickson, M.L.4    Vensel, W.H.5    Requena, J.R.6    Antaki, E.M.7    Carter, J.M.8
  • 63
    • 37649006667 scopus 로고    scopus 로고
    • Sensitive, preclinical detection of prions in brain by nanospray liquid chromatography/tandem mass spectrometry
    • PMID:18000838
    • Onisko BC, Silva CJ, Dynin I, Erickson M, Vensel WH, Hnasko R, Requena JR, Carter JM. Sensitive, preclinical detection of prions in brain by nanospray liquid chromatography/tandem mass spectrometry. Rapid Commun Mass Spectrom 2007; 21:4023-6; PMID:18000838; http://dx.doi.org/10.1002/ rcm.3310
    • (2007) Rapid Commun Mass Spectrom , vol.21 , pp. 4023-4026
    • Onisko, B.C.1    Silva, C.J.2    Dynin, I.3    Erickson, M.4    Vensel, W.H.5    Hnasko, R.6    Requena, J.R.7    Carter, J.M.8
  • 64
    • 33645813378 scopus 로고    scopus 로고
    • Mass spectrometry and protein analysis
    • PMID:16614208
    • Domon B, Aebersold R. Mass spectrometry and protein analysis. Science 2006; 312:212-7; PMID:16614208; http://dx.doi.org/10.1126/ science.1124619
    • (2006) Science , vol.312 , pp. 212-217
    • Domon, B.1    Aebersold, R.2
  • 66
    • 84861990380 scopus 로고    scopus 로고
    • Selected reaction monitoringbased proteomics: Workflows, potential, pitfalls and future directions
    • PMID:22669653
    • Picotti P, Aebersold R. Selected reaction monitoringbased proteomics: workflows, potential, pitfalls and future directions. Nat Methods 2012; 9:555-66; PMID:22669653; http://dx.doi.org/10.1038/ nmeth.2015
    • (2012) Nat Methods , vol.9 , pp. 555-566
    • Picotti, P.1    Aebersold, R.2
  • 67
    • 0026321753 scopus 로고
    • Copurification of Sp33-37 and scrapie agent from hamster brain prior to detectable histopathology and clinical disease
    • PMID:1684986
    • Bolton DC, Rudelli RD, Currie JR, Bendheim PE. Copurification of Sp33-37 and scrapie agent from hamster brain prior to detectable histopathology and clinical disease. J Gen Virol 1991; 72:2905-13; PMID:1684986; http://dx.doi. org/10.1099/0022-1317-72-12-2905
    • (1991) J Gen Virol , vol.72 , pp. 2905-2913
    • Bolton, D.C.1    Rudelli, R.D.2    Currie, J.R.3    Bendheim, P.E.4
  • 69
    • 84896913023 scopus 로고    scopus 로고
    • Oxidation of methionine in PrP is dependent upon the oxidant and the amino acid two positions removed
    • Silva CJ, Dynin I, Erickson ML, Hui C, Carter JM. Oxidation of methionine in PrP is dependent upon the oxidant and the amino acid two positions removed. Prion 2013; 7(Supplement):81
    • (2013) Prion , vol.7 , Issue.SUPPL. , pp. 81
    • Silva, C.J.1    Dynin, I.2    Erickson, M.L.3    Hui, C.4    Carter, J.M.5
  • 71
    • 79952171020 scopus 로고    scopus 로고
    • Utility of mass spectrometry in the diagnosis of prion diseases
    • PMID:21288014
    • Silva CJ, Onisko BC, Dynin I, Erickson ML, Requena JR, Carter JM. Utility of mass spectrometry in the diagnosis of prion diseases. Anal Chem 2011; 83:1609-15; PMID:21288014; http://dx.doi. org/10.1021/ac102527w
    • (2011) Anal Chem , vol.83 , pp. 1609-1615
    • Silva, C.J.1    Onisko, B.C.2    Dynin, I.3    Erickson, M.L.4    Requena, J.R.5    Carter, J.M.6
  • 72
    • 0025091084 scopus 로고
    • Identification of glycoinositol phospholipid linked and truncated forms of the scrapie prion protein
    • Stahl N, Baldwin MA, Burlingame AL, Prusiner SB. Identification of glycoinositol phospholipid linked and truncated forms of the scrapie prion protein. Biochemistry 1990; 29:8879-84; PMID:1980209; http://dx.doi.org/10.1021/ bi00490a001 (Pubitemid 20311960)
    • (1990) Biochemistry , vol.29 , Issue.38 , pp. 8879-8884
    • Stahl, N.1    Baldwin, M.A.2    Burlingame, A.L.3    Prusiner, S.B.4
  • 73
    • 48749106043 scopus 로고    scopus 로고
    • Mass spectrometric detection of proteins in non-aqueous media - The case of prion proteins in biodiesel
    • Douma MD, Kerr GM, Brown RS, Keller BO, Oleschuk RD. Mass spectrometric detection of proteins in non-aqueous media - The case of prion proteins in biodiesel. Can J Chem 2008; 86:774-81; http://dx.doi.org/10.1139/v08-083
    • (2008) Can J Chem , vol.86 , pp. 774-781
    • Douma, M.D.1    Kerr, G.M.2    Brown, R.S.3    Keller, B.O.4    Oleschuk, R.D.5
  • 74
    • 84865725559 scopus 로고    scopus 로고
    • Absolute quantification of prion protein (90-231) using stable isotope-labeled chymotryptic peptide standards in a LC-MRM AQUA workflow
    • PMID:22714949
    • Sturm R, Sheynkman G, Booth C, Smith LM, Pedersen JA, Li L. Absolute quantification of prion protein (90-231) using stable isotope-labeled chymotryptic peptide standards in a LC-MRM AQUA workflow. J Am Soc Mass Spectrom 2012; 23:1522-33; PMID:22714949; http://dx.doi. org/10.1007/s13361-012-0411-1
    • (2012) J Am Soc Mass Spectrom , vol.23 , pp. 1522-1533
    • Sturm, R.1    Sheynkman, G.2    Booth, C.3    Smith, L.M.4    Pedersen, J.A.5    Li, L.6
  • 75
    • 84877956744 scopus 로고    scopus 로고
    • Urine proteins identified by two-dimensional differential gel electrophoresis facilitate the differential diagnoses of scrapie
    • PMID:23704971
    • Lamoureux L, Simon SL, Plews M, Ruddat V, Brunet S, Graham C, Czub S, Knox JD. Urine proteins identified by two-dimensional differential gel electrophoresis facilitate the differential diagnoses of scrapie. PLoS One 2013; 8:e64044; PMID:23704971; http://dx.doi.org/10.1371/ journal.pone.0064044
    • (2013) PLoS One , vol.8
    • Lamoureux, L.1    Simon, S.L.2    Plews, M.3    Ruddat, V.4    Brunet, S.5    Graham, C.6    Czub, S.7    Knox, J.D.8
  • 78
    • 79958200862 scopus 로고    scopus 로고
    • A quantitative proteomic approach to prion disease biomarker research: Delving into the glycoproteome
    • PMID:21469646
    • Wei X, Herbst A, Ma D, Aiken J, Li L. A quantitative proteomic approach to prion disease biomarker research: delving into the glycoproteome. J Proteome Res 2011; 10:2687-702; PMID:21469646; http:// dx.doi.org/10.1021/pr2000495
    • (2011) J Proteome Res , vol.10 , pp. 2687-2702
    • Wei, X.1    Herbst, A.2    Ma, D.3    Aiken, J.4    Li, L.5
  • 80
    • 84897004699 scopus 로고    scopus 로고
    • Analysis of the hippocampal proteome in ME7 prion disease reveals a predominant astrocytic signature and highlights the brain-restricted production of clusterin in chronic neurodegeneration
    • (Forthcoming); PMID:24366862
    • Asuni AA, Gray B, Bailey J, Skipp P, Perry VH, O'Connor V. Analysis of the hippocampal proteome in ME7 prion disease reveals a predominant astrocytic signature and highlights the brain-restricted production of clusterin in chronic neurodegeneration. J Biol Chem 2013; (Forthcoming); PMID:24366862
    • (2013) J Biol Chem
    • Asuni, A.A.1    Gray, B.2    Bailey, J.3    Skipp, P.4    Perry, V.H.5    O'Connor, V.6
  • 83
    • 84863182338 scopus 로고    scopus 로고
    • Comparative peptidome analyses of the profiles of the peptides ranging from 1-10 KD in CSF samples pooled from probable sporadic CJD and non-CJD patients
    • PMID:22453178
    • Chen C, Xiao D, Zhou W, Zhang YC, Shi Q, Tian C, Zhang J, Zhou CX, Zhang JZ, Dong XP. Comparative peptidome analyses of the profiles of the peptides ranging from 1-10 KD in CSF samples pooled from probable sporadic CJD and non-CJD patients. Prion 2012; 6:46-51; PMID:22453178; http://dx.doi.org/10.4161/ pri.6.1.18082
    • (2012) Prion , vol.6 , pp. 46-51
    • Chen, C.1    Xiao, D.2    Zhou, W.3    Zhang, Y.C.4    Shi, Q.5    Tian, C.6    Zhang, J.7    Zhou, C.X.8    Zhang, J.Z.9    Dong, X.P.10
  • 85
    • 70350502841 scopus 로고    scopus 로고
    • Proteomic analyses of recombinant human follicle-stimulating hormone and urinaryderived gonadotropin preparations
    • PMID:19769189
    • Kuwabara Y, Mine K, Katayama A, Inagawa T, Akira S, Takeshita T. Proteomic analyses of recombinant human follicle-stimulating hormone and urinaryderived gonadotropin preparations. J Reprod Med 2009; 54:459-66; PMID:19769189
    • (2009) J Reprod Med , vol.54 , pp. 459-466
    • Kuwabara, Y.1    Mine, K.2    Katayama, A.3    Inagawa, T.4    Akira, S.5    Takeshita, T.6
  • 87
    • 63649115218 scopus 로고    scopus 로고
    • Identification of proteins co-purifying with scrapie infectivity
    • PMID:19367687
    • Petrakis S, Malinowska A, Dadlez M, Sklaviadis T. Identification of proteins co-purifying with scrapie infectivity. J Proteomics 2009; 72:690-4; PMID:19367687; http://dx.doi.org/10.1016/j. jprot.2009.01.025
    • (2009) J Proteomics , vol.72 , pp. 690-694
    • Petrakis, S.1    Malinowska, A.2    Dadlez, M.3    Sklaviadis, T.4
  • 88
    • 2542583141 scopus 로고    scopus 로고
    • Time-controlled transcardiac perfusion cross-linking for the study of protein interactions in complex tissues
    • DOI 10.1038/nbt969
    • Schmitt-Ulms G, Hansen K, Liu J, Cowdrey C, Yang J, DeArmond SJ, Cohen FE, Prusiner SB, Baldwin MA. Time-controlled transcardiac perfusion crosslinking for the study of protein interactions in complex tissues. Nat Biotechnol 2004; 22:724-31; PMID:15146195; http://dx.doi.org/10.1038/nbt969 (Pubitemid 38702829)
    • (2004) Nature Biotechnology , vol.22 , Issue.6 , pp. 724-731
    • Schmitt-Ulms, G.1    Hansen, K.2    Liu, J.3    Cowdrey, C.4    Yang, J.5    DeArmond, S.J.6    Cohen, F.E.7    Prusiner, S.B.8    Baldwin, M.A.9
  • 89
    • 84902553731 scopus 로고    scopus 로고
    • Anchorless 23-230 PrP(C) Interactomics for Elucidation of PrP(C) Protective Role
    • (Forthcoming); PMID:24390569
    • Zafar S, Asif AR, Ramljak S, Tahir W, Schmitz M, Zerr I. Anchorless 23-230 PrP(C) Interactomics for Elucidation of PrP(C) Protective Role. Mol Neurobiol 2014; (Forthcoming); PMID:24390569; http://dx.doi.org/10.1007/s12035- 013-8616-2
    • (2014) Mol Neurobiol
    • Zafar, S.1    Asif, A.R.2    Ramljak, S.3    Tahir, W.4    Schmitz, M.5    Zerr, I.6
  • 90
    • 84875220211 scopus 로고    scopus 로고
    • Characterization of peptides obtained from digests of bovine brain which accelerate structural conversions of the recombinant bovine prion protein
    • PMID:23376025
    • Nokihara K, Yajima S, Hitara A, Sogon T, Yasuhara T. Characterization of peptides obtained from digests of bovine brain which accelerate structural conversions of the recombinant bovine prion protein. FEBS Lett 2013; 587:673-6; PMID:23376025; http://dx.doi. org/10.1016/j.febslet.2013.01.033
    • (2013) FEBS Lett , vol.587 , pp. 673-676
    • Nokihara, K.1    Yajima, S.2    Hitara, A.3    Sogon, T.4    Yasuhara, T.5
  • 91
    • 33749422892 scopus 로고    scopus 로고
    • A nanoparticle-based immobilization assay for prion-kinetics study
    • PMID:16916458
    • Kouassi GK, Irudayaraj J. A nanoparticle-based immobilization assay for prion-kinetics study. J Nanobiotechnology 2006; 4:8; PMID:16916458; http://dx.doi.org/10.1186/1477-3155-4-8
    • (2006) J Nanobiotechnology , vol.4 , pp. 8
    • Kouassi, G.K.1    Irudayaraj, J.2
  • 92
    • 0021023167 scopus 로고
    • A protease-resistant protein is a structural component of the scrapie prion
    • McKinley MP, Bolton DC, Prusiner SB. A proteaseresistant protein is a structural component of the scrapie prion. Cell 1983; 35:57-62; PMID:6414721; http://dx.doi.org/10.1016/0092-8674(83)90207-6 (Pubitemid 14240218)
    • (1983) Cell , vol.35 , Issue.1 , pp. 57-62
    • McKinley, M.P.1    Bolton, D.C.2    Prusiner, S.B.3
  • 93
    • 70350225414 scopus 로고    scopus 로고
    • Polystyrene beads as an alternative support material for epitope identification of a prion-antibody interaction using proteolytic excision-mass spectrometry
    • PMID:19787344
    • Pimenova T, Meier L, Roschitzki B, Paraschiv G, Przybylski M, Zenobi R. Polystyrene beads as an alternative support material for epitope identification of a prion-antibody interaction using proteolytic excision-mass spectrometry. Anal Bioanal Chem 2009; 395:1395-401; PMID:19787344; http:// dx.doi.org/10.1007/s00216-009-3119-8
    • (2009) Anal Bioanal Chem , vol.395 , pp. 1395-1401
    • Pimenova, T.1    Meier, L.2    Roschitzki, B.3    Paraschiv, G.4    Przybylski, M.5    Zenobi, R.6
  • 94
    • 0037127206 scopus 로고    scopus 로고
    • Mapping Cu(II) binding sites in prion proteins by diethyl pyrocarbonate modification and matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometric footprinting
    • DOI 10.1074/jbc.M108744200
    • Qin K, Yang Y, Mastrangelo P, Westaway D. Mapping Cu(II) binding sites in prion proteins by diethyl pyrocarbonate modification and matrix-assisted laser desorption ionization-time of flight (MALDITOF) mass spectrometric footprinting. J Biol Chem 2002; 277:1981-90; PMID:11698407; http://dx.doi. org/10.1074/jbc.M108744200 (Pubitemid 34968778)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.3 , pp. 1981-1990
    • Qin, K.1    Yang, Y.2    Mastrangelo, P.3    Westaway, D.4
  • 95
    • 39749136172 scopus 로고    scopus 로고
    • Epitope mapping on bovine prion protein using chemical cross-linking and mass spectrometry
    • DOI 10.1002/jms.1280
    • Pimenova T, Nazabal A, Roschitzki B, Seebacher J, Rinner O, Zenobi R. Epitope mapping on bovine prion protein using chemical cross-linking and mass spectrometry. J Mass Spectrom 2008; 43:185-95; PMID:17924399; http://dx.doi.org/10.1002/ jms.1280 (Pubitemid 351303439)
    • (2008) Journal of Mass Spectrometry , vol.43 , Issue.2 , pp. 185-195
    • Pimenova, T.1    Nazabal, A.2    Roschitzki, B.3    Seebacher, J.4    Rinner, O.5    Zenobi, R.6
  • 96
    • 79958024318 scopus 로고    scopus 로고
    • Probing structural differences between PrP(C) and PrP(Sc) by surface nitration and acetylation: Evidence of conformational change in the C-terminus
    • PMID:21526750
    • Gong B, Ramos A, Vázquez-Fernández E, Silva CJ, Alonso J, Liu Z, Requena JR. Probing structural differences between PrP(C) and PrP(Sc) by surface nitration and acetylation: evidence of conformational change in the C-terminus. Biochemistry 2011; 50:4963-72; PMID:21526750; http://dx.doi. org/10.1021/bi102073j
    • (2011) Biochemistry , vol.50 , pp. 4963-4972
    • Gong, B.1    Ramos, A.2    Vázquez-Fernández, E.3    Silva, C.J.4    Alonso, J.5    Liu, Z.6    Requena, J.R.7
  • 98
    • 84861745028 scopus 로고    scopus 로고
    • Using small molecule reagents to selectively modify epitopes based on their conformation
    • PMID:22436143
    • Silva CJ. Using small molecule reagents to selectively modify epitopes based on their conformation. Prion 2012; 6:163-73; PMID:22436143; http://dx.doi. org/10.4161/pri.18795
    • (2012) Prion , vol.6 , pp. 163-173
    • Silva, C.J.1
  • 99
    • 0031720905 scopus 로고    scopus 로고
    • Eight prion strains have PrP(Sc) molecules with different conformations
    • DOI 10.1038/2654
    • Safar J, Wille H, Itri V, Groth D, Serban H, Torchia M, Cohen FE, Prusiner SB. Eight prion strains have PrP(Sc) molecules with different conformations. Nat Med 1998; 4:1157-65; PMID:9771749; http:// dx.doi.org/10.1038/2654 (Pubitemid 28468829)
    • (1998) Nature Medicine , vol.4 , Issue.10 , pp. 1157-1165
    • Safar, J.1    Wille, H.2    Itri, V.3    Groth, D.4    Serban, H.5    Torchia, M.6    Cohen, F.E.7    Prusiner, S.B.8
  • 100
    • 84896927312 scopus 로고    scopus 로고
    • Using synthetic small molecule reagents and antibodies to distiguish among PrP conformers-New uses for old antibodies
    • Silva C, Erickson M, Dynin I, Carter M. Using synthetic small molecule reagents and antibodies to distiguish among PrP conformers-New uses for old antibodies. Prion 2012; 6(Supplement):90
    • (2012) Prion , vol.6 , Issue.SUPPL. , pp. 90
    • Silva, C.1    Erickson, M.2    Dynin, I.3    Carter, M.4
  • 101
    • 84896988686 scopus 로고    scopus 로고
    • Distinguishing between PrPC and PrPSc using small molecule reagents
    • Silva CJ, Erickson ML, Dynin I, Carter JM. Distinguishing between PrPC and PrPSc using small molecule reagents. Prion 2013; 7(Supplement):90
    • (2013) Prion , vol.7 , Issue.SUPPL. , pp. 90
    • Silva, C.J.1    Erickson, M.L.2    Dynin, I.3    Carter, J.M.4
  • 102
    • 84883688262 scopus 로고    scopus 로고
    • Self-propagation of pathogenic protein aggregates in neurodegenerative diseases
    • PMID:24005412
    • Jucker M, Walker LC. Self-propagation of pathogenic protein aggregates in neurodegenerative diseases. Nature 2013; 501:45-51; PMID:24005412; http:// dx.doi.org/10.1038/nature12481
    • (2013) Nature , vol.501 , pp. 45-51
    • Jucker, M.1    Walker, L.C.2
  • 103
    • 84896970296 scopus 로고    scopus 로고
    • Prion-like activity of Cu/Zn superoxide dismutase: Implications for amyotrophic lateral sclerosis
    • (Forthcoming); PMID:24394345
    • Grad L, Cashman NR. Prion-like activity of Cu/Zn superoxide dismutase: Implications for amyotrophic lateral sclerosis. Prion 2014; (Forthcoming); PMID:24394345
    • (2014) Prion
    • Grad, L.1    Cashman, N.R.2
  • 104
    • 84895775448 scopus 로고    scopus 로고
    • Characterizing the Dynamics of ?-Synuclein Oligomers Using Hydrogen/Deuterium Exchange Monitored by Mass Spectrometry
    • PMID:24191706
    • Mysling S, Betzer C, Jensen PH, Jorgensen TJ. Characterizing the Dynamics of ?-Synuclein Oligomers Using Hydrogen/Deuterium Exchange Monitored by Mass Spectrometry. Biochemistry 2013; 52:9097-103; PMID:24191706; http://dx.doi. org/10.1021/bi4009193
    • (2013) Biochemistry , vol.52 , pp. 9097-9103
    • Mysling, S.1    Betzer, C.2    Jensen, P.H.3    Jorgensen, T.J.4
  • 105
    • 33745813117 scopus 로고    scopus 로고
    • Local unfolding in a destabilized, pathogenic variant of superoxide dismutase 1 observed with H/D exchange and mass spectrometry
    • DOI 10.1074/jbc.M600623200
    • Shaw BF, Durazo A, Nersissian AM, Whitelegge JP, Faull KF, Valentine JS. Local unfolding in a destabilized, pathogenic variant of superoxide dismutase 1 observed with H/D exchange and mass spectrometry. J Biol Chem 2006; 281:18167-76; PMID:16644738; http://dx.doi.org/10.1074/jbc. M600623200 (Pubitemid 44035616)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.26 , pp. 18167-18176
    • Shaw, B.F.1    Durazo, A.2    Nersissian, A.M.3    Whitelegge, J.P.4    Faull, K.F.5    Valentine, J.S.6
  • 106
    • 84872326598 scopus 로고    scopus 로고
    • Characterization of superoxide dismutase 1 (SOD-1) by electrospray ionizationion mobility mass spectrometry
    • PMID:23303748
    • Borges-Alvarez M, Benavente F, Vilaseca M, Barbosa J, Sanz-Nebot V. Characterization of superoxide dismutase 1 (SOD-1) by electrospray ionizationion mobility mass spectrometry. J Mass Spectrom 2013; 48:60-7; PMID:23303748; http://dx.doi. org/10.1002/jms.3128
    • (2013) J Mass Spectrom , vol.48 , pp. 60-67
    • Borges-Alvarez, M.1    Benavente, F.2    Vilaseca, M.3    Barbosa, J.4    Sanz-Nebot, V.5
  • 107
    • 84863854172 scopus 로고    scopus 로고
    • An online nano- LC-ESI-FTICR-MS method for comprehensive characterization of endogenous fragments from amyloid ? and amyloid precursor protein in human and cat cerebrospinal fluid
    • PMID:22576872
    • Brinkmalm G, Portelius E, Öhrfelt A, Mattsson N, Persson R, Gustavsson MK, Vite CH, Gobom J, Månsson JE, Nilsson J, et al. An online nano- LC-ESI-FTICR-MS method for comprehensive characterization of endogenous fragments from amyloid ? and amyloid precursor protein in human and cat cerebrospinal fluid. J Mass Spectrom 2012; 47:591-603; PMID:22576872; http://dx.doi. org/10.1002/jms.2987
    • (2012) J Mass Spectrom , vol.47 , pp. 591-603
    • Brinkmalm, G.1    Portelius, E.2    Öhrfelt, A.3    Mattsson, N.4    Persson, R.5    Gustavsson, M.K.6    Vite, C.H.7    Gobom, J.8    Månsson, J.E.9    Nilsson, J.10
  • 110
    • 70349144524 scopus 로고    scopus 로고
    • Preferentially increased nitration of alpha-synuclein at tyrosine-39 in a cellular oxidative model of Parkinson's disease
    • PMID:19697948
    • Danielson SR, Held JM, Schilling B, Oo M, Gibson BW, Andersen JK. Preferentially increased nitration of alpha-synuclein at tyrosine-39 in a cellular oxidative model of Parkinson's disease. Anal Chem 2009; 81:7823-8; PMID:19697948; http://dx.doi. org/10.1021/ac901176t
    • (2009) Anal Chem , vol.81 , pp. 7823-7828
    • Danielson, S.R.1    Held, J.M.2    Schilling, B.3    Oo, M.4    Gibson, B.W.5    Andersen, J.K.6
  • 111
    • 51649095905 scopus 로고    scopus 로고
    • Phosphoproteomic analysis of human brain by calcium phosphate precipitation and mass spectrometry
    • PMID:18510355
    • Xia Q, Cheng D, Duong DM, Gearing M, Lah JJ, Levey AI, Peng J. Phosphoproteomic analysis of human brain by calcium phosphate precipitation and mass spectrometry. J Proteome Res 2008; 7:2845-51; PMID:18510355; http://dx.doi.org/10.1021/ pr8000496
    • (2008) J Proteome Res , vol.7 , pp. 2845-2851
    • Xia, Q.1    Cheng, D.2    Duong, D.M.3    Gearing, M.4    Lah, J.J.5    Levey, A.I.6    Peng, J.7
  • 112
    • 42649111286 scopus 로고    scopus 로고
    • Proteomic identification of novel proteins associated with Lewy bodies
    • DOI 10.2741/2973
    • Xia Q, Liao L, Cheng D, Duong DM, Gearing M, Lah JJ, Levey AI, Peng J. Proteomic identification of novel proteins associated with Lewy bodies. Front Biosci 2008; 13:3850-6; PMID:18508479; http:// dx.doi.org/10.2741/2973 (Pubitemid 351594664)
    • (2008) Frontiers in Bioscience , vol.13 , Issue.10 , pp. 3850-3856
    • Xia, Q.1    Liao, L.2    Cheng, D.3    Duong, D.M.4    Gearing, M.5    Lah, J.J.6    Levey, A.I.7    Peng, J.8
  • 113
    • 84864965648 scopus 로고    scopus 로고
    • Biophysical properties and cellular toxicity of covalent crosslinked oligomers of ?-synuclein formed by photoinduced side-chain tyrosyl radicals
    • PMID:22771470
    • Borsarelli CD, Falomir-Lockhart LJ, Ostatná V, Fauerbach JA, Hsiao HH, Urlaub H, Palecek E, Jares-Erijman EA, Jovin TM. Biophysical properties and cellular toxicity of covalent crosslinked oligomers of ?-synuclein formed by photoinduced side-chain tyrosyl radicals. Free Radic Biol Med 2012; 53:1004-15; PMID:22771470; http://dx.doi.org/10.1016/j. freeradbiomed.2012.06.035
    • (2012) Free Radic Biol Med , vol.53 , pp. 1004-1015
    • Borsarelli, C.D.1    Falomir-Lockhart, L.J.2    Ostatná, V.3    Fauerbach, J.A.4    Hsiao, H.H.5    Urlaub, H.6    Palecek, E.7    Jares-Erijman, E.A.8    Jovin, T.M.9
  • 114
    • 0034602442 scopus 로고    scopus 로고
    • Oxidative damage linked to neurodegeneration by selective alpha-synuclein nitration in synucleinopathy lesions
    • PMID:11062131
    • Giasson BI, Duda JE, Murray IV, Chen Q, Souza JM, Hurtig HI, Ischiropoulos H, Trojanowski JQ, Lee VM. Oxidative damage linked to neurodegeneration by selective alpha-synuclein nitration in synucleinopathy lesions. Science 2000; 290:985-9; PMID:11062131; http://dx.doi.org/10.1126/ science.290.5493.985
    • (2000) Science , vol.290 , pp. 985-989
    • Giasson, B.I.1    Duda, J.E.2    Murray, I.V.3    Chen, Q.4    Souza, J.M.5    Hurtig, H.I.6    Ischiropoulos, H.7    Trojanowski, J.Q.8    Lee, V.M.9
  • 116
    • 0029661424 scopus 로고    scopus 로고
    • Analysis of heterogeneous βA4 peptides in human cerebrospinal fluid and blood by a newly developed sensitive western blot assay
    • DOI 10.1074/jbc.271.37.22908
    • Ida N, Hartmann T, Pantel J, Schröder J, Zerfass R, Förstl H, Sandbrink R, Masters CL, Beyreuther K. Analysis of heterogeneous A4 peptides in human cerebrospinal fluid and blood by a newly developed sensitive Western blot assay. J Biol Chem 1996; 271:22908-14; PMID:8798471; http://dx.doi. org/10.1074/jbc.271.37.22908 (Pubitemid 26304742)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.37 , pp. 22908-22914
    • Ida, N.1    Hartmann, T.2    Pantel, J.3    Schroder, J.4    Zerfass, R.5    Forstl, H.6    Sandbrink, R.7    Masters, C.L.8    Beyreuther, K.9
  • 117
    • 0024109687 scopus 로고
    • Epitopes that span the tau molecule are shared with paired helical filaments
    • PMID:2483104
    • Kosik KS, Orecchio LD, Binder L, Trojanowski JQ, Lee VM, Lee G. Epitopes that span the tau molecule are shared with paired helical filaments. Neuron 1988; 1:817-25; PMID:2483104; http://dx.doi. org/10.1016/0896-6273(88)90129-8
    • (1988) Neuron , vol.1 , pp. 817-825
    • Kosik, K.S.1    Orecchio, L.D.2    Binder, L.3    Trojanowski, J.Q.4    Lee, V.M.5    Lee, G.6
  • 118
    • 12644260802 scopus 로고    scopus 로고
    • The structural basis of monoclonal antibody Alz50's selectivity for Alzheimer's disease pathology
    • DOI 10.1074/jbc.271.51.32789
    • Carmel G, Mager EM, Binder LI, Kuret J. The structural basis of monoclonal antibody Alz50's selectivity for Alzheimer's disease pathology. J Biol Chem 1996; 271:32789-95; PMID:8955115; http:// dx.doi.org/10.1074/jbc.271. 51.32789 (Pubitemid 27008707)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.51 , pp. 32789-32795
    • Carmel, G.1    Mager, E.M.2    Binder, L.I.3    Kuret, J.4
  • 119
    • 33644756734 scopus 로고    scopus 로고
    • Fine epitope mapping of monoclonal antibodies specific to human α-synuclein
    • DOI 10.1016/j.neulet.2005.11.058, PII S030439400501373X
    • Choi JY, Park HJ, Seong YM, Choi EY, Min BR, Rhim H. Fine epitope mapping of monoclonal antibodies specific to human alpha-synuclein. Neurosci Lett 2006; 397:53-8; PMID:16380207; http://dx.doi.org/10.1016/j.neulet.2005.11.058 (Pubitemid 43340458)
    • (2006) Neuroscience Letters , vol.397 , Issue.1-2 , pp. 53-58
    • Choi, J.-Y.1    Park, H.-J.2    Seong, Y.-M.3    Choi, E.Y.4    Min, B.-R.5    Rhim, H.6


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