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Volumn 7, Issue 3, 2013, Pages 193-197

Conserved amyloid core structure of stop mutants of the human prion protein

Author keywords

Amyloid; Prion; Stop mutant; Structure; Trimer

Indexed keywords

AMYLOID; HYDROXYL RADICAL; MUTANT PROTEIN; PRION PROTEIN;

EID: 84879807166     PISSN: 19336896     EISSN: 1933690X     Source Type: Journal    
DOI: 10.4161/pri.23956     Document Type: Article
Times cited : (10)

References (27)
  • 1
    • 41749088672 scopus 로고    scopus 로고
    • Molecular mechanisms of prion pathogenesis
    • PMID:18233951
    • Aguzzi A, Sigurdson C, Heikenwaelder M. Molecular mechanisms of prion pathogenesis. Annu Rev Pathol 2008; 3:11-40; PMID:18233951; http://dx.doi.org/ 10.1146/annurev.pathmechdis.3.121806.154326.
    • (2008) Annu Rev Pathol , vol.3 , pp. 11-40
    • Aguzzi, A.1    Sigurdson, C.2    Heikenwaelder, M.3
  • 2
    • 0029085108 scopus 로고
    • Human prion diseases
    • PMID:7582044
    • Parchi P, Gambetti P. Human prion diseases. Curr Opin Neurol 1995; 8:286-93; PMID:7582044; http://dx.doi.org/10.1097/00019052-199508000-00007.
    • (1995) Curr Opin Neurol , vol.8 , pp. 286-293
    • Parchi, P.1    Gambetti, P.2
  • 3
    • 0033909535 scopus 로고    scopus 로고
    • High prevalence of pathogenic mutations in patients with early-onset dementia detected by sequence analyses of four different genes
    • PMID:10631141
    • Finckh U, Müller-Thomsen T, Mann U, Eggers C, Marksteiner J, Meins W, et al. High prevalence of pathogenic mutations in patients with early-onset dementia detected by sequence analyses of four different genes. Am J Hum Genet 2000; 66:110-7; PMID:10631141; http://dx.doi.org/10.1086/302702.
    • (2000) Am J Hum Genet , vol.66 , pp. 110-117
    • Finckh, U.1    Müller-Thomsen, T.2    Mann, U.3    Eggers, C.4    Marksteiner, J.5    Meins, W.6
  • 4
    • 79955397626 scopus 로고    scopus 로고
    • Familial prion disease with Alzheimer disease-like tau pathology and clinical phenotype
    • PMID:21416485
    • Jayadev S, Nochlin D, Poorkaj P, Steinbart EJ, Mastrianni JA, Montine TJ, et al. Familial prion disease with Alzheimer disease-like tau pathology and clinical phenotype. Ann Neurol 2011; 69:712-20; PMID:21416485; http://dx.doi.org/10.1002/ana.22264.
    • (2011) Ann Neurol , vol.69 , pp. 712-720
    • Jayadev, S.1    Nochlin, D.2    Poorkaj, P.3    Steinbart, E.J.4    Mastrianni, J.A.5    Montine, T.J.6
  • 5
    • 0142091396 scopus 로고    scopus 로고
    • Nucleation-dependent conformational conversion of the Y145Stop variant of human prion protein: Structural clues for prion propagation
    • PMID:14519851
    • Kundu B, Maiti NR, Jones EM, Surewicz KA, Vanik DL, Surewicz WK. Nucleation-dependent conformational conversion of the Y145Stop variant of human prion protein: structural clues for prion propagation. Proc Natl Acad Sci U S A 2003; 100:12069-74; PMID:14519851; http://dx.doi.org/10.1073/pnas.2033281100.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 12069-12074
    • Kundu, B.1    Maiti, N.R.2    Jones, E.M.3    Surewicz, K.A.4    Vanik, D.L.5    Surewicz, W.K.6
  • 6
    • 33749574062 scopus 로고    scopus 로고
    • Prion protein helix1 promotes aggregation but is not converted into beta-sheet
    • PMID:17012240
    • Watzlawik J, Skora L, Frense D, Griesinger C, Zweckstetter M, Schulz-Schaeffer WJ, et al. Prion protein helix1 promotes aggregation but is not converted into beta-sheet. J Biol Chem 2006; 281:30242-50; PMID:17012240; http://dx.doi.org/10.1074/jbc.M605141200.
    • (2006) J Biol Chem , vol.281 , pp. 30242-30250
    • Watzlawik, J.1    Skora, L.2    Frense, D.3    Griesinger, C.4    Zweckstetter, M.5    Schulz-Schaeffer, W.J.6
  • 7
    • 84873313592 scopus 로고    scopus 로고
    • Burial of the polymorphic residue 129 in amyloid fibrils of prion stop mutants
    • PMID:23209282
    • Skora L, Fonseca-Ornelas L, Hofele RV, Riedel D, Giller K, Watzlawik J, et al. Burial of the polymorphic residue 129 in amyloid fibrils of prion stop mutants. J Biol Chem 2013; 288:2994-3002; PMID:23209282; http://dx.doi.org/10. 1074/jbc.M112.423715.
    • (2013) J Biol Chem , vol.288 , pp. 2994-3002
    • Skora, L.1    Fonseca-Ornelas, L.2    Hofele, R.V.3    Riedel, D.4    Giller, K.5    Watzlawik, J.6
  • 8
    • 84870355272 scopus 로고    scopus 로고
    • Determination of amyloid core structure using chemical shifts
    • PMID:23033250
    • Skora L, Zweckstetter M. Determination of amyloid core structure using chemical shifts. Protein Sci 2012; 21:1948-53; PMID:23033250; http://dx.doi.org/10.1002/pro.2170.
    • (2012) Protein Sci , vol.21 , pp. 1948-1953
    • Skora, L.1    Zweckstetter, M.2
  • 9
    • 44049102092 scopus 로고    scopus 로고
    • Molecular conformation and dynamics of the Y145Stop variant of human prion protein in amyloid fibrils
    • PMID:18436646
    • Helmus JJ, Surewicz K, Nadaud PS, Surewicz WK, Jaroniec CP. Molecular conformation and dynamics of the Y145Stop variant of human prion protein in amyloid fibrils. Proc Natl Acad Sci U S A 2008; 105:6284-9; PMID:18436646; http://dx.doi.org/10.1073/pnas.0711716105.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 6284-6289
    • Helmus, J.J.1    Surewicz, K.2    Nadaud, P.S.3    Surewicz, W.K.4    Jaroniec, C.P.5
  • 10
    • 0034931126 scopus 로고    scopus 로고
    • Three-dimensional structures of prion proteins
    • PMID:11447697
    • Wüthrich K, Riek R. Three-dimensional structures of prion proteins. Adv Protein Chem 2001; 57:55-82; PMID:11447697; http://dx.doi.org/10.1016/S0065- 3233(01)57018-7.
    • (2001) Adv Protein Chem , vol.57 , pp. 55-82
    • Wüthrich, K.1    Riek, R.2
  • 11
    • 13344295093 scopus 로고    scopus 로고
    • Vascular variant of prion protein cerebral amyloidosis with tau-positive neurofibrillary tangles: The phenotype of the stop codon 145 mutation in PRNP
    • PMID:8570627
    • Ghetti B, Piccardo P, Spillantini MG, Ichimiya Y, Porro M, Perini F, et al. Vascular variant of prion protein cerebral amyloidosis with tau-positive neurofibrillary tangles: the phenotype of the stop codon 145 mutation in PRNP. Proc Natl Acad Sci U S A 1996; 93:744-8; PMID:8570627; http://dx.doi.org/10. 1073/pnas.93.2.744.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 744-748
    • Ghetti, B.1    Piccardo, P.2    Spillantini, M.G.3    Ichimiya, Y.4    Porro, M.5    Perini, F.6
  • 12
    • 77449089995 scopus 로고    scopus 로고
    • Prion protein amyloidosis with divergent phenotype associated with two novel nonsense mutations in PRNP
    • PMID:19911184
    • Jansen C, Parchi P, Capellari S, Vermeij AJ, Corrado P, Baas F, et al. Prion protein amyloidosis with divergent phenotype associated with two novel nonsense mutations in PRNP. Acta Neuropathol 2010; 119:189-97; PMID:19911184; http://dx.doi.org/10.1007/s00401-009-0609-x.
    • (2010) Acta Neuropathol , vol.119 , pp. 189-197
    • Jansen, C.1    Parchi, P.2    Capellari, S.3    Vermeij, A.J.4    Corrado, P.5    Baas, F.6
  • 13
    • 0026033998 scopus 로고
    • Amyloid protein of Gerstmann-Sträussler-Scheinker disease (Indiana kindred) is an 11 kd fragment of prion protein with an N-terminal glycine at codon 58
    • PMID:1672107
    • Tagliavini F, Prelli F, Ghiso J, Bugiani O, Serban D, Prusiner SB, et al. Amyloid protein of Gerstmann-Sträussler-Scheinker disease (Indiana kindred) is an 11 kd fragment of prion protein with an N-terminal glycine at codon 58. EMBO J 1991; 10:513-9; PMID:1672107.
    • (1991) EMBO J , vol.10 , pp. 513-519
    • Tagliavini, F.1    Prelli, F.2    Ghiso, J.3    Bugiani, O.4    Serban, D.5    Prusiner, S.B.6
  • 14
    • 2942616602 scopus 로고    scopus 로고
    • Evidence for assembly of prions with left-handed beta-helices into trimers
    • PMID:15155909
    • Govaerts C, Wille H, Prusiner SB, Cohen FE. Evidence for assembly of prions with left-handed beta-helices into trimers. Proc Natl Acad Sci U S A 2004; 101:8342-7; PMID:15155909; http://dx.doi.org/10.1073/pnas.0402254101.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 8342-8347
    • Govaerts, C.1    Wille, H.2    Prusiner, S.B.3    Cohen, F.E.4
  • 15
    • 35748972976 scopus 로고    scopus 로고
    • Electron crystallography of the scrapie prion protein complexed with heavy metals
    • PMID:17935686
    • Wille H, Govaerts C, Borovinskiy A, Latawiec D, Downing KH, Cohen FE, et al. Electron crystallography of the scrapie prion protein complexed with heavy metals. Arch Biochem Biophys 2007; 467:239-48; PMID:17935686; http://dx.doi.org/10.1016/j.abb.2007.08.010.
    • (2007) Arch Biochem Biophys , vol.467 , pp. 239-248
    • Wille, H.1    Govaerts, C.2    Borovinskiy, A.3    Latawiec, D.4    Downing, K.H.5    Cohen, F.E.6
  • 16
    • 10744220713 scopus 로고    scopus 로고
    • Structural properties of Gerstmann-Straussler-Scheinker disease amyloid protein
    • PMID:12970341
    • Salmona M, Morbin M, Massignan T, Colombo L, Mazzoleni G, Capobianco R, et al. Structural properties of Gerstmann-Straussler-Scheinker disease amyloid protein. J Biol Chem 2003; 278:48146-53; PMID:12970341; http://dx.doi.org/10. 1074/jbc.M307295200.
    • (2003) J Biol Chem , vol.278 , pp. 48146-48153
    • Salmona, M.1    Morbin, M.2    Massignan, T.3    Colombo, L.4    Mazzoleni, G.5    Capobianco, R.6
  • 17
    • 78649905337 scopus 로고    scopus 로고
    • Amyloid structure and assembly: Insights from scanning transmission electron microscopy
    • PMID:20868754
    • Goldsbury C, Baxa U, Simon MN, Steven AC, Engel A, Wall JS, et al. Amyloid structure and assembly: insights from scanning transmission electron microscopy. J Struct Biol 2011; 173:1-13; PMID:20868754; http://dx.doi.org/10. 1016/j.jsb.2010.09.018.
    • (2011) J Struct Biol , vol.173 , pp. 1-13
    • Goldsbury, C.1    Baxa, U.2    Simon, M.N.3    Steven, A.C.4    Engel, A.5    Wall, J.S.6
  • 18
    • 3242877815 scopus 로고    scopus 로고
    • ClusPro: A fully automated algorithm for proteinprotein docking
    • (Web Server issue); PMID:15215358
    • Comeau SR, Gatchell DW, Vajda S, Camacho CJ. ClusPro: a fully automated algorithm for proteinprotein docking. Nucleic Acids Res 2004; 32(Web Server issue):W96-9; PMID:15215358; http://dx.doi.org/10.1093/nar/gkh354.
    • (2004) Nucleic Acids Res , vol.32
    • Comeau, S.R.1    Gatchell, D.W.2    Vajda, S.3    Camacho, C.J.4
  • 19
    • 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
  • 20
    • 57449091884 scopus 로고    scopus 로고
    • Molecular structural basis for polymorphism in Alzheimer's beta-amyloid fibrils
    • PMID:19015532
    • Paravastu AK, Leapman RD, Yau WM, Tycko R. Molecular structural basis for polymorphism in Alzheimer's beta-amyloid fibrils. Proc Natl Acad Sci U S A 2008; 105:18349-54; PMID:19015532; http://dx.doi.org/10.1073/pnas.0806270105.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 18349-18354
    • Paravastu, A.K.1    Leapman, R.D.2    Yau, W.M.3    Tycko, R.4
  • 21
    • 33846811599 scopus 로고    scopus 로고
    • Beta-sheet core of human prion protein amyloid fibrils as determined by hydrogen/deuterium exchange
    • PMID:17242357
    • Lu X, Wintrode PL, Surewicz WK. Beta-sheet core of human prion protein amyloid fibrils as determined by hydrogen/deuterium exchange. Proc Natl Acad Sci U S A 2007; 104:1510-5; PMID:17242357; http://dx.doi.org/10.1073/pnas. 0608447104.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 1510-1515
    • Lu, X.1    Wintrode, P.L.2    Surewicz, W.K.3
  • 22
    • 17744379376 scopus 로고    scopus 로고
    • Synthetic prions generated in vitro are similar to a newly identified subpopulation of PrPSc from sporadic Creutzfeldt-Jakob Disease
    • PMID:15802644
    • Bocharova OV, Breydo L, Salnikov VV, Gill AC, Baskakov IV. Synthetic prions generated in vitro are similar to a newly identified subpopulation of PrPSc from sporadic Creutzfeldt-Jakob Disease. Protein Sci 2005; 14:1222-32; PMID:15802644; http://dx.doi.org/10.1110/ps.041186605.
    • (2005) Protein Sci , vol.14 , pp. 1222-1232
    • Bocharova, O.V.1    Breydo, L.2    Salnikov, V.V.3    Gill, A.C.4    Baskakov, I.V.5
  • 23
    • 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
  • 24
    • 0344326239 scopus 로고    scopus 로고
    • Analysis of 27 mammalian and 9 avian PrPs reveals high conservation of flexible regions of the prion protein
    • PMID:10373359
    • Wopfner F, Weidenhöfer G, Schneider R, von Brunn A, Gilch S, Schwarz TF, et al. Analysis of 27 mammalian and 9 avian PrPs reveals high conservation of flexible regions of the prion protein. J Mol Biol 1999; 289:1163-78; PMID:10373359; http://dx.doi.org/10.1006/jmbi.1999.2831.
    • (1999) J Mol Biol , vol.289 , pp. 1163-1178
    • Wopfner, F.1    Weidenhöfer, G.2    Schneider, R.3    Von Brunn, A.4    Gilch, S.5    Schwarz, T.F.6
  • 25
    • 0031594587 scopus 로고    scopus 로고
    • Overexpression of nonconvertible PrPc delta114-121 in scrapie-infected mouse neuroblastoma cells leads to trans-dominant inhibition of wild-type PrP(Sc) accumulation
    • PMID:9445012
    • Hölscher C, Delius H, Bürkle A. Overexpression of nonconvertible PrPc delta114-121 in scrapie-infected mouse neuroblastoma cells leads to trans-dominant inhibition of wild-type PrP(Sc) accumulation. J Virol 1998; 72:1153-9; PMID:9445012.
    • (1998) J Virol , vol.72 , pp. 1153-1159
    • Hölscher, C.1    Delius, H.2    Bürkle, A.3
  • 26
    • 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
  • 27
    • 0032612579 scopus 로고    scopus 로고
    • Ab initio protein structure prediction of CASP III targets using ROSETTA
    • PMID:10526365; 3+<171::AIDPROT21>3.0.CO;2-Z
    • Simons KT, Bonneau R, Ruczinski I, Baker D. Ab initio protein structure prediction of CASP III targets using ROSETTA. Proteins 1999; (Suppl 3): 171-6; PMID:10526365; http://dx.doi.org/10.1002/(SICI)1097-0134(1999)37:3+<171:: AIDPROT21>3.0.CO;2-Z.
    • (1999) Proteins , Issue.SUPPL. 3 , pp. 171-176
    • Simons, K.T.1    Bonneau, R.2    Ruczinski, I.3    Baker, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.