메뉴 건너뛰기




Volumn 106, Issue 40, 2009, Pages 16990-16995

Natural and synthetic prion structure from X-ray fiber diffraction

Author keywords

helix; Amyloid; Neurodegeneration; Protein; PrP

Indexed keywords

AMYLOID; PRION PROTEIN;

EID: 70350134002     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0909006106     Document Type: Article
Times cited : (179)

References (52)
  • 1
    • 35748946237 scopus 로고    scopus 로고
    • eds Knipe DM, Howley PM (Lippincott Williams & Wilkins, Philadelphia)
    • Prusiner SB (2007) in Fields Virology, eds Knipe DM, Howley PM (Lippincott Williams & Wilkins, Philadelphia), pp 3059-3091.
    • (2007) Fields Virology , pp. 3059-3091
    • Prusiner, S.B.1
  • 2
    • 0026062496 scopus 로고
    • Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis
    • McKinley MP, et al. (1991) Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis. J Virol 65:1340-1351.
    • (1991) J Virol , vol.65 , pp. 1340-1351
    • McKinley, M.P.1
  • 3
    • 18544376071 scopus 로고    scopus 로고
    • Prion protein recruits its neuronal receptor NCAM to lipid rafts to activate p59fyn and to enhance neurite outgrowth
    • Santuccione A, Sytnyk V, Leshchyns'ka I, Schachner M (2005) Prion protein recruits its neuronal receptor NCAM to lipid rafts to activate p59fyn and to enhance neurite outgrowth. J Cell Biol 169:341-354.
    • (2005) J Cell Biol , vol.169 , pp. 341-354
    • Santuccione, A.1    Sytnyk, V.2    Leshchyns'Ka, I.3    Schachner, M.4
  • 4
    • 40449128239 scopus 로고    scopus 로고
    • The chemistry of copper binding to PrP: Is there sufficient evidence to elucidate a role for copper in protein function?
    • DOI 10.1042/BJ20071477
    • Davies P, Brown DR (2008) The chemistry of copper binding to PrP: Is there sufficient evidence to elucidate a role for copper in protein function? Biochem J 410:237-244. (Pubitemid 351346181)
    • (2008) Biochemical Journal , vol.410 , Issue.2 , pp. 237-244
    • Davies, P.1    Brown, D.R.2
  • 5
    • 0021019026 scopus 로고
    • Scrapie prions aggregate to form amyloid-like birefringent rods
    • Prusiner SB, et al. (1983) Scrapie prions aggregate to form amyloid-like birefringent rods. Cell 35:349-358.
    • (1983) Cell , vol.35 , pp. 349-358
    • Prusiner, S.B.1
  • 6
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • Chiti F, Dobson CM (2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75:333-366. (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 7
    • 0001419932 scopus 로고
    • The X-ray interpretation of denaturation and the structure of the seed globulins
    • Astbury WT, Dickinson S, Bailey K (1935) The X-ray interpretation of denaturation and the structure of the seed globulins. Biochem J 29:2351-2360.
    • (1935) Biochem J , vol.29 , pp. 2351-2360
    • Astbury, W.T.1    Dickinson, S.2    Bailey, K.3
  • 9
    • 0014097803 scopus 로고
    • Ribonucleic acid components of BAI strain a (myeloblastosis) avian tumor virus
    • Bonar RA, et al. (1967) Ribonucleic acid components of BAI strain A (myeloblastosis) avian tumor virus. Cancer Res 27:1138-1157.
    • (1967) Cancer Res , vol.27 , pp. 1138-1157
    • Bonar, R.A.1
  • 10
    • 0014351967 scopus 로고
    • X-ray diffraction studies on amyloid filaments
    • Eanes ED, Glenner GG (1968) X-ray diffraction studies on amyloid filaments. J Histochem Cytochem 16:673-678.
    • (1968) J Histochem Cytochem , vol.16 , pp. 673-678
    • Eanes, E.D.1    Glenner, G.G.2
  • 11
    • 0025944507 scopus 로고
    • Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy
    • Caughey BW, et al. (1991) Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy. Biochemistry 30:7672-7680.
    • (1991) Biochemistry , vol.30 , pp. 7672-7680
    • Caughey, B.W.1
  • 13
    • 0029149975 scopus 로고
    • X-ray diffraction of scrapie prion rods and PrP peptides
    • Nguyen JT, et al. (1995) X-ray diffraction of scrapie prion rods and PrP peptides. J Mol Biol 252:412-422.
    • (1995) J Mol Biol , vol.252 , pp. 412-422
    • Nguyen, J.T.1
  • 17
    • 40849120669 scopus 로고    scopus 로고
    • Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core
    • Wasmer C, et al. (2008) Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core. Science 319:1523-1526.
    • (2008) Science , vol.319 , pp. 1523-1526
    • Wasmer, C.1
  • 18
    • 33644941607 scopus 로고    scopus 로고
    • Elongated oligomers assemble into mammalian PrP amyloid fibrils
    • Tattum MH, et al. (2006) Elongated oligomers assemble into mammalian PrP amyloid fibrils. J Mol Biol 357:975-985.
    • (2006) J Mol Biol , vol.357 , pp. 975-985
    • Tattum, M.H.1
  • 19
    • 0034725542 scopus 로고    scopus 로고
    • Structural changes in a hydrophobic domain of the prion protein induced by hydration and by Ala → Val and Pro → Leu substitutions
    • DOI 10.1006/jmbi.2000.3926
    • Inouye H, et al. (2000) Structural changes in a hydrophobic domain of the prion protein induced by hydration and by Ala→Val and Pro→Leu substitutions. J Mol Biol 300:1283-1296. (Pubitemid 30695608)
    • (2000) Journal of Molecular Biology , vol.300 , Issue.5 , pp. 1283-1296
    • Inouye, H.1    Bond, J.2    Baldwin, M.A.3    Ball, H.L.4    Prusiner, S.B.5    Kirschner, D.A.6
  • 21
    • 34249290108 scopus 로고    scopus 로고
    • Atomic structures of amyloid cross-beta spines reveal varied steric zippers
    • Sawaya MR, et al. (2007) Atomic structures of amyloid cross-beta spines reveal varied steric zippers. Nature 447:453-457.
    • (2007) Nature , vol.447 , pp. 453-457
    • Sawaya, M.R.1
  • 22
    • 3442889359 scopus 로고    scopus 로고
    • Synthetic mammalians prions
    • Legname G, et al. (2004) Synthetic mammalians prions. Science 305:673-676.
    • (2004) Science , vol.305 , pp. 673-676
    • Legname, G.1
  • 23
    • 0014975302 scopus 로고
    • Murine amyloid fibril protein: Isolation, purification and characterization
    • Glenner GG, et al. (1971) Murine amyloid fibril protein: Isolation, purification and characterization. J Histochem Cytochem 19:16-28.
    • (1971) J Histochem Cytochem , vol.19 , pp. 16-28
    • Glenner, G.G.1
  • 25
    • 33747298984 scopus 로고
    • Liquid crystalline substances from virus-infected plants
    • Bawden FC, Pirie NW, Bernal JD, Fankuchen I (1936) Liquid crystalline substances from virus-infected plants. Nature 138:1051-1052.
    • (1936) Nature , vol.138 , pp. 1051-1052
    • Bawden, F.C.1    Pirie, N.W.2    Bernal, J.D.3    Fankuchen, I.4
  • 26
    • 0006757280 scopus 로고
    • Tobacco mosaic virus: Application of the method of isomorphous replacement to the determination of helical parameters and radial density distribution
    • Franklin RE, Holmes KC (1958) Tobacco mosaic virus: Application of the method of isomorphous replacement to the determination of helical parameters and radial density distribution. Acta Crystallogr 11:213-220.
    • (1958) Acta Crystallogr , vol.11 , pp. 213-220
    • Franklin, R.E.1    Holmes, K.C.2
  • 27
    • 0027411230 scopus 로고
    • Structure of β-crystallite assemblies formed by Alzheimer β-amyloid protein analogues: Analysis by x-ray diffraction
    • Inouye H, Fraser PE, Kirschner DA (1993) Structure of β-crystallite assemblies formed by Alzheimer β-amyloid protein analogues: Analysis by X-ray diffraction. Biophys J 64:502-519. (Pubitemid 23093863)
    • (1993) Biophysical Journal , vol.64 , Issue.2 I , pp. 502-519
    • Inouye, H.1    Fraser, P.E.2    Kirschner, D.A.3
  • 28
    • 0019617748 scopus 로고
    • X-ray studies on phospholipid bilayers I. Polymorphic forms of dimyristoyl lecithin
    • Suwalsky M, Tapia J (1981) X-ray studies on phospholipid bilayers I. Polymorphic forms of dimyristoyl lecithin. Z Naturforsch C 36:875-879.
    • (1981) Z Naturforsch C , vol.36 , pp. 875-879
    • Suwalsky, M.1    Tapia, J.2
  • 29
    • 0020212370 scopus 로고
    • X-ray studies on phospholipid bilayers II. Polymorphic forms of dipalmitoyl phosphatidylethanolamine
    • Suwalsky M, Knight E (1982) X-ray studies on phospholipid bilayers II. Polymorphic forms of dipalmitoyl phosphatidylethanolamine. Z Naturforsch C 37:1157-1160.
    • (1982) Z Naturforsch C , vol.37 , pp. 1157-1160
    • Suwalsky, M.1    Knight, E.2
  • 30
    • 0033569687 scopus 로고    scopus 로고
    • Molecular modelling indicates that the pathological conformations of prion proteins might be beta-helical
    • Downing DT, Lazo ND (1999) Molecular modelling indicates that the pathological conformations of prion proteins might be beta-helical. Biochem J 343:453-460.
    • (1999) Biochem J , vol.343 , pp. 453-460
    • Downing, D.T.1    Lazo, N.D.2
  • 31
    • 37649000487 scopus 로고    scopus 로고
    • Molecular architecture of human prion protein amyloid: A parallel, in-register beta-structure
    • Cobb NJ, Sönnichsen H, McHaourab H, Surewicz WK (2007) Molecular architecture of human prion protein amyloid: A parallel, in-register beta-structure. Proc Natl Acad Sci USA 104:18946-18951.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 18946-18951
    • Cobb, N.J.1    Sönnichsen, H.2    McHaourab, H.3    Surewicz, W.K.4
  • 33
    • 33845932931 scopus 로고    scopus 로고
    • Structural properties of prion protein protofibrils and fibrils: An experimental assessment of atomic models
    • DOI 10.1021/bi0612723
    • DeMarco ML, Silveira J, Caughey B, Daggett V (2006) Structural properties of prion protein protofibrils and fibrils: An experimental assessment of atomic models. Biochemistry 45:15573-15582. (Pubitemid 46032478)
    • (2006) Biochemistry , vol.45 , Issue.51 , pp. 15573-15582
    • Demarco, M.L.1    Silveira, J.2    Caughey, B.3    Daggett, V.4
  • 38
    • 0028028685 scopus 로고
    • Negative staining: A brief assessment of current technical benefits, limitations and future possibilities
    • Harris JR, Horne RW (1994) Negative staining: A brief assessment of current technical benefits, limitations and future possibilities. Micron 25:5-13.
    • (1994) Micron , vol.25 , pp. 5-13
    • Harris, J.R.1    Horne, R.W.2
  • 39
  • 40
    • 0033551196 scopus 로고    scopus 로고
    • Site-specific characterization of the N-linked glycans of murine prion protein by high-performance liquid chromatography/electrospray mass spectrometry and exoglycosidase digestions
    • Stimson E, Hope J, Chong A, Burlingame AL (1999) Site-specific characterization of the N-linked glycans of murine prion protein by high-performance liquid chromatography/electrospray mass spectrometry and exoglycosidase digestions. Biochemistry 38:4885-4895. (Pubitemid 129514830)
    • (1999) Biochemistry , vol.38 , Issue.15 , pp. 4885-4895
    • Stimson, E.1    Hope, J.2    Chong, A.3    Burlingame, A.L.4
  • 41
    • 0026189252 scopus 로고
    • X-ray and computer modeling studies on gellan-related polymers: Molecular structures of welan, S-657, and rhamsan
    • Lee EJ, Chandrasekaran R (1991) X-ray and computer modeling studies on gellan-related polymers: Molecular structures of welan, S-657, and rhamsan. Carbohydr Res 214:11-24.
    • (1991) Carbohydr Res , vol.214 , pp. 11-24
    • Lee, E.J.1    Chandrasekaran, R.2
  • 43
    • 23244431836 scopus 로고    scopus 로고
    • Search for a prion-specific nucleic acid
    • Safar JG, et al. (2005) Search for a prion-specific nucleic acid. J Virol 79:10796-10806.
    • (2005) J Virol , vol.79 , pp. 10796-10806
    • Safar, J.G.1
  • 44
    • 0342638904 scopus 로고
    • The effect of disorientation on the intensity distribution of non-crystalline fibres
    • Stubbs G (1974) The effect of disorientation on the intensity distribution of non-crystalline fibres. Acta Crystallogr A 30:639-645.
    • (1974) Acta Crystallogr a , vol.30 , pp. 639-645
    • Stubbs, G.1
  • 45
    • 0029888121 scopus 로고    scopus 로고
    • Propagation of the yeast prion-like [psi+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor
    • Paushkin SV, Kushnirov VV, Smirnov VN, Ter-AvanesyanMD(1996) Propagation of the yeast prion-like [psi+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor. EMBO J 15:3127-3134.
    • (1996) EMBO J , vol.15 , pp. 3127-3134
    • Paushkin, S.V.1    Kushnirov, V.V.2    Smirnov, V.N.3    Ter-Avanesyan, M.D.4
  • 46
    • 0020285570 scopus 로고
    • Further purification and characterization of scrapie prions
    • Prusiner SB, et al. (1982) Further purification and characterization of scrapie prions. Biochemistry 21:6942-6950.
    • (1982) Biochemistry , vol.21 , pp. 6942-6950
    • Prusiner, S.B.1
  • 49
    • 38349164999 scopus 로고    scopus 로고
    • Enclosed chambers for humidity control and sample containment in fiber diffraction
    • McDonald M, Kendall A, Tanaka M, Weissman JS, Stubbs G (2008) Enclosed chambers for humidity control and sample containment in fiber diffraction. J Appl Crystallogr 41:206-209.
    • (2008) J Appl Crystallogr , vol.41 , pp. 206-209
    • McDonald, M.1    Kendall, A.2    Tanaka, M.3    Weissman, J.S.4    Stubbs, G.5
  • 50
    • 34248369857 scopus 로고    scopus 로고
    • Biological small-angle X-ray scattering facility at the Stanford Synchrotron Radiation Laboratory
    • DOI 10.1107/S0021889807009624, PII S0021889807009624
    • Smolsky IL, et al. (2007) Biological small-angle X-ray scattering facility at the Stanford Synchrotron Radiation Laboratory. J Appl Crystallogr 40:s453-s458. (Pubitemid 46732739)
    • (2007) Journal of Applied Crystallography , vol.40 , Issue.SUPPL. 1
    • Smolsky, I.L.1    Liu, P.2    Niebuhr, M.3    Ito, K.4    Weiss, T.M.5    Tsuruta, H.6
  • 51
    • 33748762238 scopus 로고    scopus 로고
    • WCEN: A computer program for initial processing of fiber diffraction patterns
    • DOI 10.1107/S0021889806025386
    • Bian W, Wang H, McCullough I, Stubbs G (2006) WCEN: A computer program for initial processing of fiber diffraction. J Appl Crystallogr 39:752-756. (Pubitemid 44414087)
    • (2006) Journal of Applied Crystallography , vol.39 , Issue.5 , pp. 752-756
    • Bian, W.1    Wang, H.2    McCullough, I.3    Stubbs, G.4
  • 52
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • DOI 10.1002/elps.1150181505
    • Guex N, Peitsch MC (1997) SWISSMODEL and SWISSPDB VIEWER: An environment for protein modeling. Electrophoresis 18:2714-2723. (Pubitemid 28059943)
    • (1997) Electrophoresis , vol.18 , Issue.15 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.