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Volumn 5, Issue 2, 2011, Pages 49-51

Photodegradation illuminates the role of polyanions in prion infectivity

Author keywords

Incorporation; Photodegradation; Polyanion; Prion; PrP

Indexed keywords

POLYANION; PRION PROTEIN;

EID: 79959388976     PISSN: 19336896     EISSN: 1933690X     Source Type: Journal    
DOI: 10.4161/pri.5.2.16155     Document Type: Note
Times cited : (7)

References (21)
  • 3
    • 77951979579 scopus 로고    scopus 로고
    • Mammalian prions generated from bacterially expressed prion protein in the absence of any mammalian cofactors
    • Kim JI, Cali I, Surewicz K, Kong Q, Raymond GJ, Atarashi R, et al. Mammalian prions generated from bacterially expressed prion protein in the absence of any mammalian cofactors. J Biol Chem 2010; 285:14083-7.
    • (2010) J Biol Chem , vol.285 , pp. 14083-14087
    • Kim, J.I.1    Cali, I.2    Surewicz, K.3    Kong, Q.4    Raymond, G.J.5    Atarashi, R.6
  • 5
    • 0142184333 scopus 로고    scopus 로고
    • RNA molecules stimulate prion protein conversion
    • DOI 10.1038/nature01979
    • Deleault NR, Lucassen RW, Supattapone S. RNA molecules stimulate prion protein conversion. Nature 2003; 425:717-20. (Pubitemid 37314314)
    • (2003) Nature , vol.425 , Issue.6959 , pp. 717-720
    • Deleault, N.R.1    Lucassen, R.W.2    Supattapone, S.3
  • 6
    • 22844438894 scopus 로고    scopus 로고
    • Protease-resistant prion protein amplification reconstituted with partially purified substrates and synthetic polyanions
    • DOI 10.1074/jbc.M503973200
    • Deleault NR, Geoghegan JC, Nishina K, Kascsak R, Williamson RA, Supattapone S. Protease-resistant Prion Protein Amplification Reconstituted with Partially Purified Substrates and Synthetic Polyanions. J Biol Chem 2005; 280:26873-9. (Pubitemid 41040721)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.29 , pp. 26873-26879
    • Deleault, N.R.1    Geoghegan, J.C.2    Nishina, K.3    Kascsak, R.4    Williamson, R.A.5    Supattapone, S.6
  • 9
    • 77649213673 scopus 로고    scopus 로고
    • Generating a Prion with Bacterially Expressed Recombinant Prion Protein
    • Wang F, Wang X, Yuan CG, Ma J. Generating a Prion with Bacterially Expressed Recombinant Prion Protein. Science 2010; 327:1132-5.
    • (2010) Science , vol.327 , pp. 1132-1135
    • Wang, F.1    Wang, X.2    Yuan, C.G.3    Ma, J.4
  • 10
    • 0035253848 scopus 로고    scopus 로고
    • sc-dependent cell-free formation of protease-resistant prion protein
    • DOI 10.1093/emboj/20.3.377
    • Wong C, Xiong LW, Horiuchi M, Raymond L, Wehrly K, Chesebro B, et al. Sulfated glycans and elevated temperature stimulate PrP(Sc)-dependent cell-free formation of protease-resistant prion protein. EMBO J 2001; 20:377-86. (Pubitemid 32126974)
    • (2001) EMBO Journal , vol.20 , Issue.3 , pp. 377-386
    • Wong, C.1    Xiong, L.-W.2    Horiuchi, M.3    Raymond, L.4    Wehrly, K.5    Chesebro, B.6    Caughey, B.7
  • 11
    • 0035957944 scopus 로고    scopus 로고
    • Reconstitution of prion infectivity from solubilized protease-resistant PrP and nonprotein components of prion rods
    • Shaked GM, Meiner Z, Avraham I, Taraboulos A, Gabizon R. Reconstitution of prion infectivity from solubilized protease-resistant PrP and nonprotein components of prion rods. J Biol Chem 2001; 276:14324-8.
    • (2001) J Biol Chem , vol.276 , pp. 14324-14328
    • Shaked, G.M.1    Meiner, Z.2    Avraham, I.3    Taraboulos, A.4    Gabizon, R.5
  • 13
    • 0037166240 scopus 로고    scopus 로고
    • Identification of the heparan sulfate binding sites in the cellular prion protein
    • DOI 10.1074/jbc.M110406200
    • Warner RG, Hundt C, Weiss S, Turnbull JE. Identification of the heparan sulfate binding sites in the cellular prion protein. J Biol Chem 2002; 277:18421-30. (Pubitemid 34952388)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.21 , pp. 18421-18430
    • Warner, R.G.1    Hundt, C.2    Weiss, S.3    Turnbull, J.E.4
  • 14
    • 0028256222 scopus 로고
    • Binding of the protease-sensitive form of prion protein PrP to sulfated glycosaminoglycan and Congo red
    • Caughey B, Brown K, Raymond GJ, Katzenstein GE, Thresher W Binding of the protease-sensitive form of PrP (prion protein) to sulfated glycosaminoglycan and congo red [corrected]. J Virol 1994; 68:2135-41. (Pubitemid 24091890)
    • (1994) Journal of Virology , vol.68 , Issue.4 , pp. 2135-2141
    • Caughey, B.1    Brown, K.2    Raymond, G.J.3    Katzenstein, G.E.4    Thresher, W.5
  • 16
    • 0037446508 scopus 로고    scopus 로고
    • In Vitro Amplification of Protease-Resistant Prion Protein Requires Free Sulfhydryl Groups
    • Lucassen R, Nishina K, Supattapone S. In Vitro Amplification of Protease-Resistant Prion Protein Requires Free Sulfhydryl Groups. Biochemistry 2003; 42:4127-35.
    • (2003) Biochemistry , vol.42 , pp. 4127-4135
    • Lucassen, R.1    Nishina, K.2    Supattapone, S.3
  • 17
    • 17444413067 scopus 로고    scopus 로고
    • In vitro generation of infectious scrapie prions
    • Castilla J, Saa P, Hetz C, Soto C. In vitro generation of infectious scrapie prions. Cell 2005; 121:195-206.
    • (2005) Cell , vol.121 , pp. 195-206
    • Castilla, J.1    Saa, P.2    Hetz, C.3    Soto, C.4
  • 18
    • 0035859102 scopus 로고    scopus 로고
    • Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding
    • DOI 10.1038/35081095
    • Saborio GP, Permanne B, Soto C. Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 2001; 411:810-3. (Pubitemid 32588105)
    • (2001) Nature , vol.411 , Issue.6839 , pp. 810-813
    • Saborio, G.P.1    Permanne, B.2    Soto, C.3
  • 19
    • 69449099838 scopus 로고    scopus 로고
    • Reduction of prion infectivity and levels of scrapie prion protein by lithium aluminum hydride: Implications for RNA in prion diseases
    • Jeong BH, Kim NH, Jin JK, Choi JK, Lee YJ, Kim JI, et al. Reduction of prion infectivity and levels of scrapie prion protein by lithium aluminum hydride: implications for RNA in prion diseases. J Neuropathol Exp Neurol 2009; 68:870-9.
    • (2009) J Neuropathol Exp Neurol , vol.68 , pp. 870-879
    • Jeong, B.H.1    Kim, N.H.2    Jin, J.K.3    Choi, J.K.4    Lee, Y.J.5    Kim, J.I.6
  • 20
    • 79952213489 scopus 로고    scopus 로고
    • In situ photodegradation of incorporated polyanion does not alter prion infectivity
    • Piro JR, Harris BT, Supattapone S. In situ photodegradation of incorporated polyanion does not alter prion infectivity. PLoS Pathog 2011; 7:1002001.
    • (2011) PLoS Pathog , vol.7 , pp. 1002001
    • Piro, J.R.1    Harris, B.T.2    Supattapone, S.3
  • 21
    • 77951923337 scopus 로고    scopus 로고
    • Species-dependent differences in cofactor utilization for formation of the protease-resistant prion protein in vitro
    • Deleault NR, Kascsak R, Geoghegan JC, Supattapone S. Species-dependent differences in cofactor utilization for formation of the protease-resistant prion protein in vitro. Biochemistry 2010; 49:3928-34.
    • (2010) Biochemistry , vol.49 , pp. 3928-3934
    • Deleault, N.R.1    Kascsak, R.2    Geoghegan, J.C.3    Supattapone, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.