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Volumn 32, Issue 21, 2012, Pages 7345-7355

A new mechanism for transmissible prion diseases

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; PRION PROTEIN; PROTEINASE K; RECOMBINANT PROTEIN;

EID: 84861309020     PISSN: 02706474     EISSN: 15292401     Source Type: Journal    
DOI: 10.1523/JNEUROSCI.6351-11.2012     Document Type: Article
Times cited : (63)

References (44)
  • 1
    • 72149125838 scopus 로고    scopus 로고
    • The transcellular spread of cytosolic amyloids, prions, and prionoids
    • Aguzzi A, Rajendran L (2009) The transcellular spread of cytosolic amyloids, prions, and prionoids. Neuron 64:783-790.
    • (2009) Neuron , vol.64 , pp. 783-790
    • Aguzzi, A.1    Rajendran, L.2
  • 2
    • 79953286302 scopus 로고    scopus 로고
    • The strain-encoded relationship between PrP replication, stability and processing in neurons is predictive of the incubation period of disease
    • Ayers JI, Schutt CR, Shikiya RA, Aguzzi A, Kincaid AE, Bartz JC (2011) The strain-encoded relationship between PrP replication, stability and processing in neurons is predictive of the incubation period of disease. PLoS Pathog 7:e1001317.
    • (2011) PLoS Pathog , vol.7
    • Ayers, J.I.1    Schutt, C.R.2    Shikiya, R.A.3    Aguzzi, A.4    Kincaid, A.E.5    Bartz, J.C.6
  • 3
    • 50849113452 scopus 로고    scopus 로고
    • A C-terminal protease-resistant prion fragment distinguishes ovine "CH1641-like" scrapie from bovine classical and L-type BSE in ovine transgenic mice
    • Baron T, Bencsik A, Vulin J, Biacabe AG, Morignat E, Verchere J, Betemps D (2008) A C-terminal protease-resistant prion fragment distinguishes ovine "CH1641-like" scrapie from bovine classical and L-type BSE in ovine transgenic mice. PLoS Pathog 4:e1000137.
    • (2008) PLoS Pathog , vol.4
    • Baron, T.1    Bencsik, A.2    Vulin, J.3    Biacabe, A.G.4    Morignat, E.5    Verchere, J.6    Betemps, D.7
  • 4
    • 34249947345 scopus 로고    scopus 로고
    • Converting the prion protein: What makes the protein infectious
    • Baskakov IV, Breydo L (2007) Converting the prion protein: What makes the protein infectious. Biochim Biophys Acta 1772:692-703.
    • (2007) Biochim Biophys Acta , vol.1772 , pp. 692-703
    • Baskakov, I.V.1    Breydo, L.2
  • 5
    • 34948908239 scopus 로고    scopus 로고
    • H-type bovine spongiform encephalopathy: Complex molecular features and similarities with human prion diseases
    • Biacabe AG, Jacobs JG, Bencsik A, Langeveld JP, Baron TG (2007) H-type bovine spongiform encephalopathy: complex molecular features and similarities with human prion diseases. Prion 1:61-68.
    • (2007) Prion , vol.1 , pp. 61-68
    • Biacabe, A.G.1    Jacobs, J.G.2    Bencsik, A.3    Langeveld, J.P.4    Baron, T.G.5
  • 6
    • 12544257523 scopus 로고    scopus 로고
    • In vitro conversion of full length mammalian prion protein produces amyloid form with physical property of PrPSc
    • Bocharova OV, Breydo L, Parfenov AS, Salnikov VV, Baskakov IV (2005a) In vitro conversion of full length mammalian prion protein produces amyloid form with physical property of PrPSc. J Mol Biol 346:645-659.
    • (2005) J Mol Biol , vol.346 , pp. 645-659
    • Bocharova, O.V.1    Breydo, L.2    Parfenov, A.S.3    Salnikov, V.V.4    Baskakov, I.V.5
  • 8
    • 0023205075 scopus 로고
    • Biological evidence that the scrapie agent has an independent genome
    • Bruce ME, Dickinson AG (1987) Biological evidence that the scrapie agent has an independent genome. J Gen Virol 68:79-89.
    • (1987) J Gen Virol , vol.68 , pp. 79-89
    • Bruce, M.E.1    Dickinson, A.G.2
  • 9
    • 0031711595 scopus 로고    scopus 로고
    • Pathologic conformations of prion proteins
    • Cohen FE, Prusiner SB (1998) Pathologic conformations of prion proteins. Annu Rev Biochem 67:793-819.
    • (1998) Annu Rev Biochem , vol.67 , pp. 793-819
    • Cohen, F.E.1    Prusiner, S.B.2
  • 13
  • 14
    • 54449083425 scopus 로고    scopus 로고
    • The effects of prion protein proteolysis and disaggregation on the strain properties of hamster scrapie
    • Deleault AM, Deleault NR, Harris BT, Rees JR, Supattapone S (2008) The effects of prion protein proteolysis and disaggregation on the strain properties of hamster scrapie. J Gen Virol 89:2642-2650.
    • (2008) J Gen Virol , vol.89 , pp. 2642-2650
    • Deleault, A.M.1    Deleault, N.R.2    Harris, B.T.3    Rees, J.R.4    Supattapone, S.5
  • 15
    • 0142184333 scopus 로고    scopus 로고
    • RNAmolecules stimulate prion protein conversion
    • Deleault NR, Lucassen RW, Supattapone S (2003) RNAmolecules stimulate prion protein conversion. Nature 425:717-720.
    • (2003) Nature , vol.425 , pp. 717-720
    • Deleault, N.R.1    Lucassen, R.W.2    Supattapone, S.3
  • 16
    • 22844438894 scopus 로고    scopus 로고
    • Protease-resistant prion protein amplification reconstituted with partially purified substrates and synthetic polyanions
    • Deleault NR, Geoghegan JC, Nishina K, Kascsak R, Williamson RA, Supattapone S (2005) Protease-resistant prion protein amplification reconstituted with partially purified substrates and synthetic polyanions. J Biol Chem 280:26873-26879.
    • (2005) J Biol Chem , vol.280 , pp. 26873-26879
    • Deleault, N.R.1    Geoghegan, J.C.2    Nishina, K.3    Kascsak, R.4    Williamson, R.A.5    Supattapone, S.6
  • 18
    • 77951923337 scopus 로고    scopus 로고
    • Speciesdependent differences in cofactor utilization for formation of the protease-resistant prion protein in vitro
    • Deleault NR, Kascsak R, Geoghegan JC, Supattapone S (2010) Speciesdependent differences in cofactor utilization for formation of the protease-resistant prion protein in vitro. Biochemistry 49:3928-3934.
    • (2010) Biochemistry , vol.49 , pp. 3928-3934
    • Deleault, N.R.1    Kascsak, R.2    Geoghegan, J.C.3    Supattapone, S.4
  • 19
    • 77249133010 scopus 로고    scopus 로고
    • Prion-like mechanisms on neurodegenerative diseases
    • Frost B, Diamond MI (2010) Prion-like mechanisms on neurodegenerative diseases. Nat Rev Neurosci 11:155-159.
    • (2010) Nat Rev Neurosci , vol.11 , pp. 155-159
    • Frost, B.1    Diamond, M.I.2
  • 21
    • 80052702962 scopus 로고    scopus 로고
    • Relationship between conformational stability and amplification efficiency of prions
    • Gonzalez-Montalban N, Makarava N, Savtchenko R, Baskakov IV (2011b) Relationship between conformational stability and amplification efficiency of prions. Biochemistry 50:7933-7940.
    • (2011) Biochemistry , vol.50 , pp. 7933-7940
    • Gonzalez-Montalban, N.1    Makarava, N.2    Savtchenko, R.3    Baskakov, I.V.4
  • 25
    • 47049117171 scopus 로고    scopus 로고
    • The same primary structure of the prion protein yields two distinct self-propagating states
    • Makarava N, Baskakov IV (2008) The same primary structure of the prion protein yields two distinct self-propagating states. J Biol Chem 283:15988-15996.
    • (2008) J Biol Chem , vol.283 , pp. 15988-15996
    • Makarava, N.1    Baskakov, I.V.2
  • 30
    • 71549169557 scopus 로고    scopus 로고
    • Could they all be prion diseases?
    • Miller G (2009) Could they all be prion diseases? Science 326:1337-1339.
    • (2009) Science , vol.326 , pp. 1337-1339
    • Miller, G.1
  • 31
    • 0042381231 scopus 로고    scopus 로고
    • Heterogeneity and regulation of cellular prion protein glycoforms in neuronal cell lines
    • Monnet C, Marthiens V, Enslen H, Frobert Y, Sobel A, Mège RM (2003) Heterogeneity and regulation of cellular prion protein glycoforms in neuronal cell lines. Eur J Neurosci 18:542-548.
    • (2003) Eur J Neurosci , vol.18 , pp. 542-548
    • Monnet, C.1    Marthiens, V.2    Enslen, H.3    Frobert, Y.4    Sobel, A.5    Mège, R.M.6
  • 33
    • 4043157677 scopus 로고    scopus 로고
    • Preclinical vCJD after blood transfusion in a PRNP codon 129 heterozygous patient
    • Peden AH, Head MW, Ritchie DL, Bell JE, Ironside JW (2004) Preclinical vCJD after blood transfusion in a PRNP codon 129 heterozygous patient. Lancet 364:527-529.
    • (2004) Lancet , vol.364 , pp. 527-529
    • Peden, A.H.1    Head, M.W.2    Ritchie, D.L.3    Bell, J.E.4    Ironside, J.W.5
  • 34
    • 80051714126 scopus 로고    scopus 로고
    • Seeding specificity and ultrastructural characteristics of infectious recombinant pPrions
    • Piro JR, Wang F, Walsh DJ, Rees JR, Ma J, Supattapone S (2011) Seeding specificity and ultrastructural characteristics of infectious recombinant pPrions. Biochemistry 50:7111-7116.
    • (2011) Biochemistry , vol.50 , pp. 7111-7116
    • Piro, J.R.1    Wang, F.2    Walsh, D.J.3    Rees, J.R.4    Ma, J.5    Supattapone, S.6
  • 35
    • 0030822582 scopus 로고    scopus 로고
    • Prion diseases and the BSE crisis
    • Prusiner SB (1997) Prion diseases and the BSE crisis. Science 278:245-251.
    • (1997) Science , vol.278 , pp. 245-251
    • Prusiner, S.B.1
  • 37
    • 0037184107 scopus 로고    scopus 로고
    • Changes in the glycosylation pattern of prion protein in murine scrapie
    • Russelakis-Carneiro M, Saborio GP, Anderes L, Soto C (2002) Changes in the glycosylation pattern of prion protein in murine scrapie. J Biol Chem 277:36872-36877.
    • (2002) J Biol Chem , vol.277 , pp. 36872-36877
    • Russelakis-Carneiro, M.1    Saborio, G.P.2    Anderes, L.3    Soto, C.4
  • 38
    • 33845944898 scopus 로고    scopus 로고
    • Ultra-efficient replication of infectious prions by automated protein misfolding cyclic amplification
    • Saá P, Castilla J, Soto C (2006) Ultra-efficient replication of infectious prions by automated protein misfolding cyclic amplification. J Biol Chem 281:35245-35252.
    • (2006) J Biol Chem , vol.281 , pp. 35245-35252
    • Saá, P.1    Castilla, J.2    Soto, C.3
  • 40
    • 33745058355 scopus 로고    scopus 로고
    • Structural differences between TSEs strains investigated by FT-IR spectroscopy
    • Spassov S, Beekes M, Naumann D (2006) Structural differences between TSEs strains investigated by FT-IR spectroscopy. Biochim Biophys Acta 1760:1138-1149.
    • (2006) Biochim Biophys Acta , vol.1760 , pp. 1138-1149
    • Spassov, S.1    Beekes, M.2    Naumann, D.3
  • 41
    • 39049119728 scopus 로고    scopus 로고
    • Conformational stability of PrP amyloid firbils controls their smallest possible fragment size
    • Sun Y, Makarava N, Lee CI, Laksanalamai P, Robb FT, Baskakov IV (2008) Conformational stability of PrP amyloid firbils controls their smallest possible fragment size. J Mol Biol 376:1155-1167.
    • (2008) J Mol Biol , vol.376 , pp. 1155-1167
    • Sun, Y.1    Makarava, N.2    Lee, C.I.3    Laksanalamai, P.4    Robb, F.T.5    Baskakov, I.V.6
  • 42
    • 77649213673 scopus 로고    scopus 로고
    • Generating a Prion Bacterially Expressed Recombinant Prion Protein
    • Wang F, Wang X, Yuan CG, Ma J (2010) Generating a Prion Bacterially Expressed Recombinant Prion Protein. Science 327:1132-1135.
    • (2010) Science , vol.327 , pp. 1132-1135
    • Wang, F.1    Wang, X.2    Yuan, C.G.3    Ma, J.4
  • 44
    • 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 (2003) Identification of novel proteinase K-resistant C-terminal fragments of PrP in Creutzfeldt-Jakob disease. J Biol Chem 278:40429-40436.
    • (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.