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Volumn 4, Issue 3, 2009, Pages 295-307

Structure of mammalian prions

Author keywords

Cross linking; Electron microscopy; FTIR; HET s; Limited proteolysis; Prion; Prion strains; Proteinase K; PrPSc structure

Indexed keywords

PRION PROTEIN; PROTEINASE K;

EID: 70350119663     PISSN: 17460794     EISSN: None     Source Type: Journal    
DOI: 10.2217/fvl.09.8     Document Type: Review
Times cited : (4)

References (52)
  • 2
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • Stefani M, Dobson CM: Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J. Mol. Med. 81, 678-699 (2003).
    • (2003) J. Mol. Med , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 3
    • 33644817188 scopus 로고    scopus 로고
    • Prion domains: Sequences structures and interactions
    • Ross ED, Minton A, Wickner RB: Prion domains: sequences structures and interactions. Nat. Cell Biol. 7, 1039-1044 (2005).
    • (2005) Nat. Cell Biol , vol.7 , pp. 1039-1044
    • Ross, E.D.1    Minton, A.2    Wickner, R.B.3
  • 4
    • 0842281643 scopus 로고    scopus 로고
    • Mammalian prion biology: One century of evolving concepts
    • Aguzzi A, Polymenidou M: Mammalian prion biology: one century of evolving concepts. Cell 116, 1-20 (2004).
    • (2004) Cell , vol.116 , pp. 1-20
    • Aguzzi, A.1    Polymenidou, M.2
  • 5
    • 0031729399 scopus 로고    scopus 로고
    • Prion diseases in man
    • Ironside JW: Prion diseases in man. J. Pathol. 186, 227-234 (1998).
    • (1998) J. Pathol , vol.186 , pp. 227-234
    • Ironside, J.W.1
  • 6
    • 53249095492 scopus 로고    scopus 로고
    • Increased oxidation, glycoxidation, and lipoxidation of brain proteins in prion disease
    • Pamplona R, Naudí A, Gavín R et al.: Increased oxidation, glycoxidation, and lipoxidation of brain proteins in prion disease. Free Radic. Biol. Med. 45, 1159-1166 (2008).
    • (2008) Free Radic. Biol. Med , vol.45 , pp. 1159-1166
    • Pamplona, R.1    Naudí, A.2    Gavín, R.3
  • 7
    • 50049084898 scopus 로고    scopus 로고
    • A prion disease of cervids: Chronic wasting disease
    • Sigurdson CJ: A prion disease of cervids: chronic wasting disease. Vet. Res. 39, 41-48 (2008).
    • (2008) Vet. Res , vol.39 , pp. 41-48
    • Sigurdson, C.J.1
  • 8
    • 0038497542 scopus 로고
    • Molecular structure of nucleic acids; a structure for deoxyribose nucleic acid
    • Watson JD, Crick FHC: Molecular structure of nucleic acids; a structure for deoxyribose nucleic acid. Nature 171, 737-738 (1953).
    • (1953) Nature , vol.171 , pp. 737-738
    • Watson, J.D.1    Crick, F.H.C.2
  • 9
    • 40849120669 scopus 로고    scopus 로고
    • Amyloid fibrils of the HET-s (218-289) prion form a β-solenoid with a triangular hydrophobic core
    • Wasmer C, Lange A, Van Melckebeke H, Siemer AB, Riek R, Meier BH: Amyloid fibrils of the HET-s (218-289) prion form a β-solenoid with a triangular hydrophobic core. Science 319, 1523-1526 (2008).
    • (2008) Science , vol.319 , pp. 1523-1526
    • Wasmer, C.1    Lange, A.2    Van Melckebeke, H.3    Siemer, A.B.4    Riek, R.5    Meier, B.H.6
  • 10
    • 0027195933 scopus 로고
    • Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett JT, Lansbury PT Jr: Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73, 1055-1058 (1993).
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr, P.T.2
  • 11
    • 0031711595 scopus 로고    scopus 로고
    • Pathologic conformations of prion proteins
    • Cohen E, Prusiner SB: Pathologic conformations of prion proteins. Annu. Rev. Biochem. 67, 793-819 (1998).
    • (1998) Annu. Rev. Biochem , vol.67 , pp. 793-819
    • Cohen, E.1    Prusiner, S.B.2
  • 14
    • 33846811599 scopus 로고    scopus 로고
    • β-sheet core of human prion protein amyloid fibrils as determined by hydrogen/deuterium exchange
    • Lu X, Wintrode PL, Surewicz WK: β-sheet core of human prion protein amyloid fibrils as determined by hydrogen/deuterium exchange. Proc. Natl Acad. Sci. USA 104, 1510-1515 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 1510-1515
    • Lu, X.1    Wintrode, P.L.2    Surewicz, W.K.3
  • 15
    • 34249951500 scopus 로고    scopus 로고
    • Prion and non-prion amyloids of the HET-s prion forming domain
    • Sabaté R, Baxa U, Benkemoun L et al.: Prion and non-prion amyloids of the HET-s prion forming domain. J. Mol. Biol. 370, 768-783 (2007).
    • (2007) J. Mol. Biol , vol.370 , pp. 768-783
    • Sabaté, R.1    Baxa, U.2    Benkemoun, L.3
  • 16
    • 53549129515 scopus 로고    scopus 로고
    • Infectious and noninfectious amyloids of the HET-s (218-289) prion have different NMR spectra
    • Wasmer C, Soragni A, Sabaté R et al.: Infectious and noninfectious amyloids of the HET-s (218-289) prion have different NMR spectra. Angew. Chem. Int. Ed. Engl. 47, 5839-5841 (2008).
    • (2008) Angew. Chem. Int. Ed. Engl , vol.47 , pp. 5839-5841
    • Wasmer, C.1    Soragni, A.2    Sabaté, R.3
  • 17
    • 0021023167 scopus 로고
    • A protease resistant protein is a structural component of the scrapie prion
    • McKinley MP, Bolton DC, Prusiner SB: A protease resistant protein is a structural component of the scrapie prion. Cell 35, 57-62 (1983).
    • (1983) Cell , vol.35 , pp. 57-62
    • McKinley, M.P.1    Bolton, D.C.2    Prusiner, S.B.3
  • 18
    • 0034079165 scopus 로고    scopus 로고
    • Adaptation and selection of prion protein strain conformations following interspecies transmission of transmissible mink encephalopathies
    • Bartz JC, Bessen RA, McKenzie D, Marsh RF, Aiken JM: Adaptation and selection of prion protein strain conformations following interspecies transmission of transmissible mink encephalopathies. J. Virol. 74, 5542-5547 (2000).
    • (2000) J. Virol , vol.74 , pp. 5542-5547
    • Bartz, J.C.1    Bessen, R.A.2    McKenzie, D.3    Marsh, R.F.4    Aiken, J.M.5
  • 19
    • 0141577720 scopus 로고    scopus 로고
    • Identification of novel proteinase K-resistant C-terminal fragments of PrP in Creutzfeldt-Jakob disease
    • Zou WQ, Capellari S, Parchi P, Sy MS, Gambetti P, Chen SG: Identification of novel proteinase K-resistant C-terminal fragments of PrP in Creutzfeldt-Jakob disease. J. Biol. Chem. 278, 40429-40436 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 40429-40436
    • Zou, W.Q.1    Capellari, S.2    Parchi, P.3    Sy, M.S.4    Gambetti, P.5    Chen, S.G.6
  • 20
    • 4644259154 scopus 로고    scopus 로고
    • Identification of distinct N-terminal truncated forms of prion protein in different Creutzfeldt-Jakob disease subtypes
    • Zanusso G, Farinazzo A, Prelli F et al.: Identification of distinct N-terminal truncated forms of prion protein in different Creutzfeldt-Jakob disease subtypes. J. Biol. Chem. 279, 38936-38942 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 38936-38942
    • Zanusso, G.1    Farinazzo, A.2    Prelli, F.3
  • 21
    • 0028043661 scopus 로고
    • Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy
    • Bessen RA, Marsh RF: Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy. J. Virol. 68, 7859-7868 (1994).
    • (1994) J. Virol , vol.68 , pp. 7859-7868
    • Bessen, R.A.1    Marsh, R.F.2
  • 22
    • 12944253111 scopus 로고    scopus 로고
    • Genetic influence on the structural variations of the abnormal prion protein
    • Parchi P, Zou W, Wang W et al.: Genetic influence on the structural variations of the abnormal prion protein. Proc. Natl Acad. Sci. USA 97, 10168-10172 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 10168-10172
    • Parchi, P.1    Zou, W.2    Wang, W.3
  • 23
    • 0020490156 scopus 로고
    • Identification of a protein that purifies with the scrapie prion
    • Bolton DC, McKinley MP, Prusiner SB: Identification of a protein that purifies with the scrapie prion. Science 218, 1309-1311 (1982).
    • (1982) Science , vol.218 , pp. 1309-1311
    • Bolton, D.C.1    McKinley, M.P.2    Prusiner, S.B.3
  • 24
    • 0027332116 scopus 로고
    • Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins
    • Pan KM, Baldwin M, Nguyen J et al.: Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins. Proc. Natl Acad. Sci. USA 90, 10962-10966 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 10962-10966
    • Pan, K.M.1    Baldwin, M.2    Nguyen, J.3
  • 25
    • 0025944507 scopus 로고
    • Secondary structure analysis of the scrapie-associated protein PrP27-30 in water by infrared spectroscopy
    • Caughey B, Dong A, Bhat KS, Ernst D, Hayes SF, Caughey WS: Secondary structure analysis of the scrapie-associated protein PrP27-30 in water by infrared spectroscopy. Biochemistry 30, 7672-7680 (1991).
    • (1991) Biochemistry , vol.30 , pp. 7672-7680
    • Caughey, B.1    Dong, A.2    Bhat, K.S.3    Ernst, D.4    Hayes, S.F.5    Caughey, W.S.6
  • 26
    • 0033610870 scopus 로고    scopus 로고
    • Strain-dependent differences in β-sheet conformations of abnormal prion protein
    • Caughey B, Raymond GJ, Bessen RA: Strain-dependent differences in β-sheet conformations of abnormal prion protein. J. Biol. Chem. 273, 32230-32235 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 32230-32235
    • Caughey, B.1    Raymond, G.J.2    Bessen, R.A.3
  • 27
    • 33745058355 scopus 로고    scopus 로고
    • Structural differences between TSEs strains investigated by FT-IR spectroscopy
    • Spassov S, Beekes M, Naumann D: Structural differences between TSEs strains investigated by FT-IR spectroscopy. Biochim. Biophys. Acta 1760, 1138-1149 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 1138-1149
    • Spassov, S.1    Beekes, M.2    Naumann, D.3
  • 28
    • 0037155213 scopus 로고    scopus 로고
    • The HET-s prion protein of the filamentous fungus Podospora anserina aggregates in vitro into amyloid fibrils
    • Dos Reis S, Coulary-Salin B, Forges V, Lascu I, Bégueret J, Saupe SJ: The HET-s prion protein of the filamentous fungus Podospora anserina aggregates in vitro into amyloid fibrils. J. Biol. Chem. 277, 5703-5706 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 5703-5706
    • Dos Reis, S.1    Coulary-Salin, B.2    Forges, V.3    Lascu, I.4    Bégueret, J.5    Saupe, S.J.6
  • 29
    • 0034076545 scopus 로고    scopus 로고
    • Do parallel β-helix proteins have a unique Fourier transform infrared spectrum?
    • Khurana R, Fink AL: Do parallel β-helix proteins have a unique Fourier transform infrared spectrum? Biophys. J. 78, 994-1000 (2000).
    • (2000) Biophys. J , vol.78 , pp. 994-1000
    • Khurana, R.1    Fink, A.L.2
  • 30
    • 33745620145 scopus 로고    scopus 로고
    • Two-rung model of a left-handed β-helix for prions explains species barrier and strain variation in Transmissible Spongiform Encephalopathies
    • Langedijk JPM, Fuentes G, Boshuizen R, Bonvin AMJJ: Two-rung model of a left-handed β-helix for prions explains species barrier and strain variation in Transmissible Spongiform Encephalopathies. J. Mol. Biol. 360, 907-920 (2006).
    • (2006) J. Mol. Biol , vol.360 , pp. 907-920
    • Langedijk, J.P.M.1    Fuentes, G.2    Boshuizen, R.3    Bonvin, A.M.J.J.4
  • 32
    • 0026062496 scopus 로고
    • Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis
    • McKinley MP, Meyer RK, Kenaga L et al.: Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis. J. Virol. 65, 1340-1351 (1991).
    • (1991) J. Virol , vol.65 , pp. 1340-1351
    • McKinley, M.P.1    Meyer, R.K.2    Kenaga, L.3
  • 33
    • 70350127011 scopus 로고    scopus 로고
    • Doctoral thesis, University of Santiago de Compostela, Spain
    • ISBN 978-984-691-4733-4737
    • Pastrana MA: Doctoral thesis, University of Santiago de Compostela, Spain, ISBN 978-984-691-4733-4737 (2008).
    • (2008)
    • Pastrana, M.A.1
  • 34
    • 67650767364 scopus 로고    scopus 로고
    • Ultrastructures and strain comparison of under-glycosylated scrapie prion fibrils
    • In Press
    • Sim VL, Caughey B: Ultrastructures and strain comparison of under-glycosylated scrapie prion fibrils. Neurobiol. Aging (2008) (In Press).
    • (2008) Neurobiol. Aging
    • Sim, V.L.1    Caughey, B.2
  • 35
    • 58149375262 scopus 로고    scopus 로고
    • Cryo-immunogold electron microscopy for prions: Toward identification of a conversion site
    • Godsave SF, Wille H, Kujala P et al.: Cryo-immunogold electron microscopy for prions: toward identification of a conversion site. J. Neurosci. 28, 12489-12499 (2008).
    • (2008) J. Neurosci , vol.28 , pp. 12489-12499
    • Godsave, S.F.1    Wille, H.2    Kujala, P.3
  • 37
    • 0033375223 scopus 로고    scopus 로고
    • Methods for studying prion protein (PrP) metabolism and formation of protease-resistant PrP in cell culture and cell-free systems
    • Caughey B, Raymond GJ, Priola SA et al.: Methods for studying prion protein (PrP) metabolism and formation of protease-resistant PrP in cell culture and cell-free systems. Mol. Biotechnol. 13, 45-55 (1999).
    • (1999) Mol. Biotechnol , vol.13 , pp. 45-55
    • Caughey, B.1    Raymond, G.J.2    Priola, S.A.3
  • 38
    • 20344394154 scopus 로고    scopus 로고
    • Anchorless prion protein results in infectious amyloid disease without clinical scrapie
    • Cheesebro B, Trifilo M, Race R et al.: Anchorless prion protein results in infectious amyloid disease without clinical scrapie. Science 308, 1435-1439 (2005).
    • (2005) Science , vol.308 , pp. 1435-1439
    • Cheesebro, B.1    Trifilo, M.2    Race, R.3
  • 39
    • 0029149975 scopus 로고
    • X-ray diffraction of scrapie prion rods and PrP peptides
    • Nguyen JT, Inouye H, Baldwin MA et al.: X-ray diffraction of scrapie prion rods and PrP peptides. J. Mol. Biol. 252, 412-422 (1995).
    • (1995) J. Mol. Biol , vol.252 , pp. 412-422
    • Nguyen, J.T.1    Inouye, H.2    Baldwin, M.A.3
  • 40
    • 1442330474 scopus 로고    scopus 로고
    • From conversion to aggregation: Protofibril formation of the prion protein
    • DeMarco M, Daggett V: From conversion to aggregation: Protofibril formation of the prion protein. Proc. Natl Acad. Sci. USA 101, 2293-2298 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 2293-2298
    • DeMarco, M.1    Daggett, V.2
  • 41
    • 0031592937 scopus 로고    scopus 로고
    • A conformational transition at the N terminus of the prion protein features in formation of the scrapie isoform
    • Peretz D, Williamson RA, Matsunaga Y et al.: A conformational transition at the N terminus of the prion protein features in formation of the scrapie isoform. J. Mol. Biol. 273, 614-622 (1997).
    • (1997) J. Mol. Biol , vol.273 , pp. 614-622
    • Peretz, D.1    Williamson, R.A.2    Matsunaga, Y.3
  • 42
    • 0031710237 scopus 로고    scopus 로고
    • Mapping the prion protein using recombinant antibodies
    • Williamson RA, Peretz D, Pinilla C et al.: Mapping the prion protein using recombinant antibodies. J. Virol. 72, 9413-9418 (1998).
    • (1998) J. Virol , vol.72 , pp. 9413-9418
    • Williamson, R.A.1    Peretz, D.2    Pinilla, C.3
  • 43
    • 0037133587 scopus 로고    scopus 로고
    • Structural studies of the scrapie prion protein by electron crystallography
    • Wille H, Michelitsch M, Guénebaut V et al.: Structural studies of the scrapie prion protein by electron crystallography. Proc. Natl Acad. Sci. USA 99, 3563-3568 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 3563-3568
    • Wille, H.1    Michelitsch, M.2    Guénebaut, V.3
  • 44
    • 35748972976 scopus 로고    scopus 로고
    • Electron crystallography of the scrapie prion protein complexed with heavy metals
    • Wille H, Govaerts C, Borovinskiy A et al.: Electron crystallography of the scrapie prion protein complexed with heavy metals. Arch. Biochem. Biophys. 467, 239-248 (2007).
    • (2007) Arch. Biochem. Biophys , vol.467 , pp. 239-248
    • Wille, H.1    Govaerts, C.2    Borovinskiy, A.3
  • 45
    • 2942616602 scopus 로고    scopus 로고
    • Evidence for assembly of prions with left-handed β-helices into trimers
    • Govaerts C, Wille H, Prusiner SB, Cohen FE. Evidence for assembly of prions with left-handed β-helices into trimers. Proc. Natl Acad. Sci. USA. 101, 8342-8347 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 8342-8347
    • Govaerts, C.1    Wille, H.2    Prusiner, S.B.3    Cohen, F.E.4
  • 46
    • 23944494699 scopus 로고    scopus 로고
    • Structure of infectious prions: Stabilization by domain swapping
    • Yang S, Levine H, Onuchic JN, Cox DL: Structure of infectious prions: stabilization by domain swapping. FASEB J. 19, 1778-1782 (2005).
    • (2005) FASEB J , vol.19 , pp. 1778-1782
    • Yang, S.1    Levine, H.2    Onuchic, J.N.3    Cox, D.L.4
  • 47
    • 33845932931 scopus 로고    scopus 로고
    • Structural properties of prion protein protofibrils and fibrils: An experimental assessment of atomic models
    • DeMarco ML, Silveira J, Caughey B, Daggett V: Structural properties of prion protein protofibrils and fibrils: an experimental assessment of atomic models. Biochemistry 45, 15573-15582 (2006).
    • (2006) Biochemistry , vol.45 , pp. 15573-15582
    • DeMarco, M.L.1    Silveira, J.2    Caughey, B.3    Daggett, V.4
  • 48
    • 0347286732 scopus 로고    scopus 로고
    • Chemical cross-linking and mass spectrometry for mapping three-dimensional structures of proteins and protein complexes
    • Sinz A: Chemical cross-linking and mass spectrometry for mapping three-dimensional structures of proteins and protein complexes. J. Mass Specrom. 38, 1225-1237 (2003).
    • (2003) J. Mass Specrom , vol.38 , pp. 1225-1237
    • Sinz, A.1
  • 49
    • 23044458520 scopus 로고    scopus 로고
    • Sc structure using chemical cross-linking and mass spectrometry: Evidence of the proximity of Gly90 amino termini in the PrP27-30 aggregate
    • Sc structure using chemical cross-linking and mass spectrometry: evidence of the proximity of Gly90 amino termini in the PrP27-30 aggregate. Biochemistry 44, 10100-10109 (2005).
    • (2005) Biochemistry , vol.44 , pp. 10100-10109
    • Onisko, B.1    Fernandez, E.G.2    Freire, M.L.3
  • 50
    • 49349117873 scopus 로고    scopus 로고
    • Scrapie prion protein structural constraints obtained by limited proteolysis and mass spectrometry
    • 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. 382, 88-98 (2008).
    • (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
  • 51
    • 0032539578 scopus 로고    scopus 로고
    • The structural aspects of limited proteolysis of native proteins
    • Hubbard SJ: The structural aspects of limited proteolysis of native proteins. Biochim. Biophys. Acta 1382, 191-206 (1998).
    • (1998) Biochim. Biophys. Acta , vol.1382 , pp. 191-206
    • Hubbard, S.J.1
  • 52
    • 34547638271 scopus 로고    scopus 로고
    • Ultrasensitive detection of scrapie prion protein using seeded conversion of recombinant prion protein
    • Atarashi R, Moore RA, Sim VL et al.: Ultrasensitive detection of scrapie prion protein using seeded conversion of recombinant prion protein. Nat. Methods 4, 645-650 (2007).
    • (2007) Nat. Methods , vol.4 , pp. 645-650
    • Atarashi, R.1    Moore, R.A.2    Sim, V.L.3


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