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Volumn 5, Issue 8, 2010, Pages

Glycosaminoglycan sulphation affects the seeded misfolding of a mutant prion protein

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOSAMINOGLYCAN; HEPARAN SULFATE; MUTANT PROTEIN; NUCLEIC ACID; POLYANION; PRION PROTEIN; SULFATE;

EID: 77957896276     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0012351     Document Type: Article
Times cited : (22)

References (69)
  • 1
    • 0347915581 scopus 로고    scopus 로고
    • Transmissible spongiform encephalopathies
    • Collins SJ, Lawson VA, Masters CL (2004) Transmissible spongiform encephalopathies. Lancet 363: 51-61.
    • (2004) Lancet , vol.363 , pp. 51-61
    • Collins, S.J.1    Lawson, V.A.2    Masters, C.L.3
  • 3
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner SB (1982) Novel proteinaceous infectious particles cause scrapie. Science 216: 136-144.
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 5
    • 0037446508 scopus 로고    scopus 로고
    • In vitro amplification of proteaseresistant prion protein requires free sulfhydryl groups
    • Lucassen R, Nishina K, Supattapone S (2003) In vitro amplification of proteaseresistant prion protein requires free sulfhydryl groups. Biochemistry 42: 4127-4135.
    • (2003) Biochemistry , vol.42 , pp. 4127-4135
    • Lucassen, R.1    Nishina, K.2    Supattapone, S.3
  • 6
    • 0035859102 scopus 로고    scopus 로고
    • Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding
    • Saborio GP, Permanne B, Soto C (2001) Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 411: 810-813.
    • (2001) Nature , vol.411 , pp. 810-813
    • Saborio, G.P.1    Permanne, B.2    Soto, C.3
  • 7
    • 17444413067 scopus 로고    scopus 로고
    • In vitro generation of infectious scrapie prions
    • Castilla J, Saa P, Hetz C, Soto C (2005) In vitro generation of infectious scrapie prions. Cell 121: 195-206.
    • (2005) Cell , vol.121 , pp. 195-206
    • Castilla, J.1    Saa, P.2    Hetz, C.3    Soto, C.4
  • 8
    • 33750310849 scopus 로고    scopus 로고
    • Prions and their partners in crime
    • Caughey B, Baron GS (2006) Prions and their partners in crime. Nature 443: 803-810.
    • (2006) Nature , vol.443 , pp. 803-810
    • Caughey, B.1    Baron, G.S.2
  • 9
    • 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, et al. Mammalian prions generated from bacterially expressed prion protein in the absence of any mammalian cofactors. J Biol Chem 285: 14083-14087.
    • 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
  • 12
    • 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 327: 1132-1135.
    • Science , vol.327 , pp. 1132-1135
    • Wang, F.1    Wang, X.2    Yuan, C.G.3    Ma, J.4
  • 13
    • 0041735109 scopus 로고    scopus 로고
    • Small, highly structured RNAs participate in the conversion of human recombinant PrP(Sen) to PrP(Res) in vitro
    • Adler V, Zeiler B, Kryukov V, Kascsak R, Rubenstein R, et al. (2003) Small, highly structured RNAs participate in the conversion of human recombinant PrP(Sen) to PrP(Res) in vitro. J Mol Biol 332: 47-57.
    • (2003) J Mol Biol , vol.332 , pp. 47-57
    • Adler, V.1    Zeiler, B.2    Kryukov, V.3    Kascsak, R.4    Rubenstein, R.5
  • 14
    • 0142184333 scopus 로고    scopus 로고
    • RNA molecules stimulate prion protein conversion
    • Deleault NR, Lucassen RW, Supattapone S (2003) RNA molecules 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
  • 15
    • 0036371353 scopus 로고    scopus 로고
    • PrPC has nucleic acid chaperoning properties similar to the nucleocapsid protein of HIV-1
    • Derrington E, Gabus C, Leblanc P, Chnaidermann J, Grave L, et al. (2002) PrPC has nucleic acid chaperoning properties similar to the nucleocapsid protein of HIV-1. C R Acad Sci III 325: 17-23.
    • (2002) C R Acad Sci , vol.3 , Issue.325 , pp. 17-23
    • Derrington, E.1    Gabus, C.2    Leblanc, P.3    Chnaidermann, J.4    Grave, L.5
  • 16
    • 0035815107 scopus 로고    scopus 로고
    • The prion protein has DNA strand transfer properties similar to retroviral nucleocapsid protein
    • Gabus C, Auxilien S, Pechoux C, Dormont D, Swietnicki W, et al. (2001) The prion protein has DNA strand transfer properties similar to retroviral nucleocapsid protein. J Mol Biol 307: 1011-1021.
    • (2001) J Mol Biol , vol.307 , pp. 1011-1021
    • Gabus, C.1    Auxilien, S.2    Pechoux, C.3    Dormont, D.4    Swietnicki, W.5
  • 17
    • 0035380709 scopus 로고    scopus 로고
    • The prion protein has RNA binding and chaperoning properties characteristic of nucleocapsid protein NCP7 of HIV-1
    • Gabus C, Derrington E, Leblanc P, Chnaiderman J, Dormont D, et al. (2001) The prion protein has RNA binding and chaperoning properties characteristic of nucleocapsid protein NCP7 of HIV-1. J Biol Chem 276: 19301-19309.
    • (2001) J Biol Chem , vol.276 , pp. 19301-19309
    • Gabus, C.1    Derrington, E.2    Leblanc, P.3    Chnaiderman, J.4    Dormont, D.5
  • 18
    • 0036970469 scopus 로고    scopus 로고
    • DNA-induced partial unfolding of prion protein leads to its polymerisation to amyloid
    • Nandi PK, Leclerc E, Nicole JC, Takahashi M (2002) DNA-induced partial unfolding of prion protein leads to its polymerisation to amyloid. J Mol Biol 322: 153-161.
    • (2002) J Mol Biol , vol.322 , pp. 153-161
    • Nandi, P.K.1    Leclerc, E.2    Nicole, J.C.3    Takahashi, M.4
  • 19
    • 7944223439 scopus 로고    scopus 로고
    • Nucleic acid and prion protein interaction produces spherical amyloids which can function in vivo as coats of spongiform encephalopathy agent
    • Nandi PK, Nicole JC (2004) Nucleic acid and prion protein interaction produces spherical amyloids which can function in vivo as coats of spongiform encephalopathy agent. J Mol Biol 344: 827-837.
    • (2004) J Mol Biol , vol.344 , pp. 827-837
    • Nandi, P.K.1    Nicole, J.C.2
  • 22
    • 0037465821 scopus 로고    scopus 로고
    • Structural changes of the prion protein in lipid membranes leading to aggregation and fibrillization
    • Kazlauskaite J, Sanghera N, Sylvester I, Venien-Bryan C, Pinheiro TJ (2003) Structural changes of the prion protein in lipid membranes leading to aggregation and fibrillization. Biochemistry 42: 3295-3304.
    • (2003) Biochemistry , vol.42 , pp. 3295-3304
    • Kazlauskaite, J.1    Sanghera, N.2    Sylvester, I.3    Venien-Bryan, C.4    Pinheiro, T.J.5
  • 23
    • 15544379325 scopus 로고    scopus 로고
    • Aggregation and fibrillization of prions in lipid membranes
    • Kazlauskaite J, Pinheiro TJ (2005) Aggregation and fibrillization of prions in lipid membranes. Biochem Soc Symp. pp 211-222.
    • (2005) Biochem Soc Symp , pp. 211-222
    • Kazlauskaite, J.1    Pinheiro, T.J.2
  • 24
    • 0036306046 scopus 로고    scopus 로고
    • Binding of prion protein to lipid membranes and implications for prion conversion
    • Sanghera N, Pinheiro TJ (2002) Binding of prion protein to lipid membranes and implications for prion conversion. J Mol Biol 315: 1241-1256.
    • (2002) J Mol Biol , vol.315 , pp. 1241-1256
    • Sanghera, N.1    Pinheiro, T.J.2
  • 26
    • 19444376065 scopus 로고    scopus 로고
    • PrPSc incorporation to cells requires endogenous glycosaminoglycan expression
    • Hijazi N, Kariv-Inbal Z, Gasset M, Gabizon R (2005) PrPSc incorporation to cells requires endogenous glycosaminoglycan expression. J Biol Chem 280: 17057-17061.
    • (2005) J Biol Chem , vol.280 , pp. 17057-17061
    • Hijazi, N.1    Kariv-Inbal, Z.2    Gasset, M.3    Gabizon, R.4
  • 27
    • 19444376451 scopus 로고    scopus 로고
    • Heparan sulfate is a cellular receptor for purified infectious prions
    • Horonchik L, Tzaban S, Ben-Zaken O, Yedidia Y, Rouvinski A, et al. (2005) Heparan sulfate is a cellular receptor for purified infectious prions. J Biol Chem 280: 17062-17067.
    • (2005) J Biol Chem , vol.280 , pp. 17062-17067
    • Horonchik, L.1    Tzaban, S.2    Ben-Zaken, O.3    Yedidia, Y.4    Rouvinski, A.5
  • 28
    • 0027458091 scopus 로고
    • Heparin-like molecules bind differentially to prion-proteins and change their intracellular metabolic fate
    • Gabizon R, Meiner Z, Halimi M, Ben-Sasson SA (1993) Heparin-like molecules bind differentially to prion-proteins and change their intracellular metabolic fate. J Cell Physiol 157: 319-325.
    • (1993) J Cell Physiol , vol.157 , pp. 319-325
    • Gabizon, R.1    Meiner, Z.2    Halimi, M.3    Ben-Sasson, S.A.4
  • 29
    • 0029564913 scopus 로고
    • Sulfated glycans stimulate endocytosis of the cellular isoform of the prion protein, PrPC, in cultured cells
    • Shyng SL, Lehmann S, Moulder KL, Harris DA (1995) Sulfated glycans stimulate endocytosis of the cellular isoform of the prion protein, PrPC, in cultured cells. J Biol Chem 270: 30221-30229.
    • (1995) J Biol Chem , vol.270 , pp. 30221-30229
    • Shyng, S.L.1    Lehmann, S.2    Moulder, K.L.3    Harris, D.A.4
  • 30
    • 0141994735 scopus 로고    scopus 로고
    • Cellular heparan sulfate participates in the metabolism of prions
    • Ben-Zaken O, Tzaban S, Tal Y, Horonchik L, Esko JD, et al. (2003) Cellular heparan sulfate participates in the metabolism of prions. J Biol Chem 278: 40041-40049.
    • (2003) J Biol Chem , vol.278 , pp. 40041-40049
    • Ben-Zaken, O.1    Tzaban, S.2    Tal, Y.3    Horonchik, L.4    Esko, J.D.5
  • 32
    • 0025243737 scopus 로고
    • Immunolocalization of heparan sulfate proteoglycans to the prion protein amyloid plaques of Gerstmann-Straussler syndrome, Creutzfeldt-Jakob disease and scrapie
    • Snow AD, Wight TN, Nochlin D, Koike Y, Kimata K, et al. (1990) Immunolocalization of heparan sulfate proteoglycans to the prion protein amyloid plaques of Gerstmann-Straussler syndrome, Creutzfeldt-Jakob disease and scrapie. Lab Invest 63: 601-611.
    • (1990) Lab Invest , vol.63 , pp. 601-611
    • Snow, A.D.1    Wight, T.N.2    Nochlin, D.3    Koike, Y.4    Kimata, K.5
  • 33
    • 0042854755 scopus 로고    scopus 로고
    • A novel generation of heparan sulfate mimetics for the treatment of prion diseases
    • Adjou KT, Simoneau S, Sales N, Lamoury F, Dormont D, et al. (2003) A novel generation of heparan sulfate mimetics for the treatment of prion diseases. J Gen Virol 84: 2595-2603.
    • (2003) J Gen Virol , vol.84 , pp. 2595-2603
    • Adjou, K.T.1    Simoneau, S.2    Sales, N.3    Lamoury, F.4    Dormont, D.5
  • 34
    • 2342623474 scopus 로고    scopus 로고
    • Treatment of transmissible spongiform encephalopathy by intraventricular drug infusion in animal models
    • Doh-ura K, Ishikawa K, Murakami-Kubo I, Sasaki K, Mohri S, et al. (2004) Treatment of transmissible spongiform encephalopathy by intraventricular drug infusion in animal models. J Virol 78: 4999-5006.
    • (2004) J Virol , vol.78 , pp. 4999-5006
    • Doh-Ura, K.1    Ishikawa, K.2    Murakami-Kubo, I.3    Sasaki, K.4    Mohri, S.5
  • 35
    • 41849091490 scopus 로고    scopus 로고
    • Intraventricular pentosan polysulphate in human prion diseases: An observational study in the UK
    • Bone I, Belton L, Walker AS, Darbyshire J (2008) Intraventricular pentosan polysulphate in human prion diseases: an observational study in the UK. Eur J Neurol 15: 458-464.
    • (2008) Eur J Neurol , vol.15 , pp. 458-464
    • Bone, I.1    Belton, L.2    Walker, A.S.3    Darbyshire, J.4
  • 36
    • 34248145176 scopus 로고    scopus 로고
    • Long term survival in a patient with variant Creutzfeldt-Jakob disease treated with intraventricular pentosan polysulphate
    • Parry A, Baker I, Stacey R, Wimalaratna S (2007) Long term survival in a patient with variant Creutzfeldt-Jakob disease treated with intraventricular pentosan polysulphate. J Neurol Neurosurg Psychiatry 78: 733-734.
    • (2007) J Neurol Neurosurg Psychiatry , vol.78 , pp. 733-734
    • Parry, A.1    Baker, I.2    Stacey, R.3    Wimalaratna, S.4
  • 37
    • 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.
    • Science
    • Wang, F.1    Wang, X.2    Yuan, C.G.3    Ma, J.4
  • 38
    • 0035253848 scopus 로고    scopus 로고
    • Sulfated glycans and elevated temperature stimulate PrP(Sc)-dependent cell-free formation of protease-resistant prion protein
    • Wong C, Xiong LW, Horiuchi M, Raymond L, Wehrly K, et al. (2001) Sulfated glycans and elevated temperature stimulate PrP(Sc)-dependent cell-free formation of protease-resistant prion protein. Embo J 20: 377-386.
    • (2001) Embo J , vol.20 , pp. 377-386
    • Wong, C.1    Xiong, L.W.2    Horiuchi, M.3    Raymond, L.4    Wehrly, K.5
  • 39
    • 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, et al. (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
  • 40
    • 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 49: 3928-3934.
    • Biochemistry , vol.49 , pp. 3928-3934
    • Deleault, N.R.1    Kascsak, R.2    Geoghegan, J.C.3    Supattapone, S.4
  • 41
    • 29244449320 scopus 로고    scopus 로고
    • Correlative studies support lipid peroxidation is linked to PrP(res) propagation as an early primary pathogenic event in prion disease
    • Brazier MW, Lewis V, Ciccotosto GD, Klug GM, Lawson VA, et al. (2006) Correlative studies support lipid peroxidation is linked to PrP(res) propagation as an early primary pathogenic event in prion disease. Brain Res Bull 68: 346-354.
    • (2006) Brain Res Bull , vol.68 , pp. 346-354
    • Brazier, M.W.1    Lewis, V.2    Ciccotosto, G.D.3    Klug, G.M.4    Lawson, V.A.5
  • 42
    • 0029863648 scopus 로고    scopus 로고
    • Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie
    • Fischer M, Rulicke T, Raeber A, Sailer A, Moser M, et al. (1996) Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie. Embo J 15: 1255-1264.
    • (1996) Embo J , vol.15 , pp. 1255-1264
    • Fischer, M.1    Rulicke, T.2    Raeber, A.3    Sailer, A.4    Moser, M.5
  • 43
    • 37549039459 scopus 로고    scopus 로고
    • Unifying electrostatic mechanism for phosphates and sulfates in cell signaling
    • Kovacic P, Draskovich CD, Pozos RS (2007) Unifying electrostatic mechanism for phosphates and sulfates in cell signaling. J Recept Signal Transduct Res 27: 433-443.
    • (2007) J Recept Signal Transduct Res , vol.27 , pp. 433-443
    • Kovacic, P.1    Draskovich, C.D.2    Pozos, R.S.3
  • 45
    • 45849084257 scopus 로고    scopus 로고
    • Unifying electrostatic mechanism for metal cations in receptors and cell signaling
    • Kovacic P (2008) Unifying electrostatic mechanism for metal cations in receptors and cell signaling. J Recept Signal Transduct Res 28: 153-161.
    • (2008) J Recept Signal Transduct Res , vol.28 , pp. 153-161
    • Kovacic, P.1
  • 46
    • 0035849540 scopus 로고    scopus 로고
    • On the mechanism of alpha-helix to beta-sheet transition in the recombinant prion protein
    • Morillas M, Vanik DL, Surewicz WK (2001) On the mechanism of alpha-helix to beta-sheet transition in the recombinant prion protein. Biochemistry 40: 6982-6987.
    • (2001) Biochemistry , vol.40 , pp. 6982-6987
    • Morillas, M.1    Vanik, D.L.2    Surewicz, W.K.3
  • 47
    • 4644331407 scopus 로고    scopus 로고
    • Ionic strength and transition metals control PrPSc protease resistance and conversion-inducing activity
    • Nishina K, Jenks S, Supattapone S (2004) Ionic strength and transition metals control PrPSc protease resistance and conversion-inducing activity. J Biol Chem 279: 40788-40794.
    • (2004) J Biol Chem , vol.279 , pp. 40788-40794
    • Nishina, K.1    Jenks, S.2    Supattapone, S.3
  • 48
    • 0036301061 scopus 로고    scopus 로고
    • Prion protein interaction with glycosaminoglycan occurs with the formation of oligomeric complexes stabilized by Cu(II) bridges
    • Gonzalez-Iglesias R, Pajares MA, Ocal C, Espinosa JC, Oesch B, et al. (2002) Prion protein interaction with glycosaminoglycan occurs with the formation of oligomeric complexes stabilized by Cu(II) bridges. J Mol Biol 319: 527-540.
    • (2002) J Mol Biol , vol.319 , pp. 527-540
    • Gonzalez-Iglesias, R.1    Pajares, M.A.2    Ocal, C.3    Espinosa, J.C.4    Oesch, B.5
  • 49
    • 0037166240 scopus 로고    scopus 로고
    • Identification of the heparan sulfate binding sites in the cellular prion protein
    • Warner RG, Hundt C, Weiss S, Turnbull JE (2002) Identification of the heparan sulfate binding sites in the cellular prion protein. J Biol Chem 277: 18421-18430.
    • (2002) J Biol Chem , vol.277 , pp. 18421-18430
    • Warner, R.G.1    Hundt, C.2    Weiss, S.3    Turnbull, J.E.4
  • 50
    • 77957917801 scopus 로고    scopus 로고
    • Structure of the flexible amino terminal domain of prion protein bound to a sulfated glycan
    • Taubner LM, Bienkiewicz EA, Copie V, Caughey B (2009) Structure of the flexible amino terminal domain of prion protein bound to a sulfated glycan. J Mol Biol.
    • (2009) J Mol Biol
    • Taubner, L.M.1    Bienkiewicz, E.A.2    Copie, V.3    Caughey, B.4
  • 52
    • 0033574264 scopus 로고    scopus 로고
    • Familial prion disease mutation alters the secondary structure of recombinant mouse prion protein: Implications for the mechanism of prion formation
    • Cappai R, Stewart L, Jobling MF, Thyer JM, White AR, et al. (1999) Familial prion disease mutation alters the secondary structure of recombinant mouse prion protein: implications for the mechanism of prion formation. Biochemistry 38: 3280-3284.
    • (1999) Biochemistry , vol.38 , pp. 3280-3284
    • Cappai, R.1    Stewart, L.2    Jobling, M.F.3    Thyer, J.M.4    White, A.R.5
  • 53
    • 34250644988 scopus 로고    scopus 로고
    • Human prion proteins with pathogenic mutations share common conformational changes resulting in enhanced binding to glycosaminoglycans
    • Yin S, Pham N, Yu S, Li C, Wong P, et al. (2007) Human prion proteins with pathogenic mutations share common conformational changes resulting in enhanced binding to glycosaminoglycans. Proc Natl Acad Sci U S A 104: 7546-7551.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 7546-7551
    • Yin, S.1    Pham, N.2    Yu, S.3    Li, C.4    Wong, P.5
  • 54
    • 28444449883 scopus 로고    scopus 로고
    • A single amino acid alteration in murine PrP dramatically alters TSE incubation time
    • Manson JC, Barron R, Jamieson E, Baybutt H, Tuzi N, et al. (2000) A single amino acid alteration in murine PrP dramatically alters TSE incubation time. Arch Virol Suppl. pp 95-102.
    • (2000) Arch Virol Suppl , pp. 95-102
    • Manson, J.C.1    Barron, R.2    Jamieson, E.3    Baybutt, H.4    Tuzi, N.5
  • 55
  • 56
    • 51249111719 scopus 로고    scopus 로고
    • Mouseadapted sporadic human Creutzfeldt-Jakob disease prions propagate in cell culture
    • Lawson VA, Vella LJ, Stewart JD, Sharples RA, Klemm H, et al. (2008) Mouseadapted sporadic human Creutzfeldt-Jakob disease prions propagate in cell culture. Int J Biochem Cell Biol 40: 2793-2801.
    • (2008) Int J Biochem Cell Biol , vol.40 , pp. 2793-2801
    • Lawson, V.A.1    Vella, L.J.2    Stewart, J.D.3    Sharples, R.A.4    Klemm, H.5
  • 57
    • 33947709328 scopus 로고    scopus 로고
    • Packaging of prions into exosomes is associated with a novel pathway of PrP processing
    • Vella LJ, Sharples RA, Lawson VA, Masters CL, Cappai R, et al. (2007) Packaging of prions into exosomes is associated with a novel pathway of PrP processing. J Pathol 211: 582-590.
    • (2007) J Pathol , vol.211 , pp. 582-590
    • Vella, L.J.1    Sharples, R.A.2    Lawson, V.A.3    Masters, C.L.4    Cappai, R.5
  • 58
    • 0022897789 scopus 로고
    • Chlorate-a potent inhibitor of protein sulfation in intact cells
    • Baeuerle PA, Huttner WB (1986) Chlorate-a potent inhibitor of protein sulfation in intact cells. Biochem Biophys Res Commun 141: 870-877.
    • (1986) Biochem Biophys Res Commun , vol.141 , pp. 870-877
    • Baeuerle, P.A.1    Huttner, W.B.2
  • 59
    • 0030050733 scopus 로고    scopus 로고
    • Mutant and infectious prion proteins display common biochemical properties in cultured cells
    • Lehmann S, Harris DA (1996) Mutant and infectious prion proteins display common biochemical properties in cultured cells. J Biol Chem 271: 1633-1637.
    • (1996) J Biol Chem , vol.271 , pp. 1633-1637
    • Lehmann, S.1    Harris, D.A.2
  • 60
    • 0032553530 scopus 로고    scopus 로고
    • Familial mutations and the thermodynamic stability of the recombinant human prion protein
    • Swietnicki W, Petersen RB, Gambetti P, Surewicz WK (1998) Familial mutations and the thermodynamic stability of the recombinant human prion protein. J Biol Chem 273: 31048-31052.
    • (1998) J Biol Chem , vol.273 , pp. 31048-31052
    • Swietnicki, W.1    Petersen, R.B.2    Gambetti, P.3    Surewicz, W.K.4
  • 61
    • 0018384549 scopus 로고
    • Transmission of chronic spongiform encephalopathy with kuru plaques from humans to small rodents
    • Tateishi J, Ohta M, Koga M, Sato Y, Kuroiwa Y (1979) Transmission of chronic spongiform encephalopathy with kuru plaques from humans to small rodents. Ann Neurol 5: 581-584.
    • (1979) Ann Neurol , vol.5 , pp. 581-584
    • Tateishi, J.1    Ohta, M.2    Koga, M.3    Sato, Y.4    Kuroiwa, Y.5
  • 62
    • 0030007616 scopus 로고    scopus 로고
    • Transmission of human prion diseases to rodents
    • Tateishi J (1996) Transmission of human prion diseases to rodents. Seminars in Virology 7: 175-180.
    • (1996) Seminars In Virology , vol.7 , pp. 175-180
    • Tateishi, J.1
  • 63
    • 33644540192 scopus 로고    scopus 로고
    • Octapeptide repeat insertions increase the rate of protease-resistant prion protein formation
    • Moore RA, Herzog C, Errett J, Kocisko DA, Arnold KM, et al. (2006) Octapeptide repeat insertions increase the rate of protease-resistant prion protein formation. Protein Sci 15: 609-619.
    • (2006) Protein Sci , vol.15 , pp. 609-619
    • Moore, R.A.1    Herzog, C.2    Errett, J.3    Kocisko, D.A.4    Arnold, K.M.5
  • 64
    • 0033579485 scopus 로고    scopus 로고
    • Selective effects of sodium chlorate treatment on the sulfation of heparan sulfate
    • Safaiyan F, Kolset SO, Prydz K, Gottfridsson E, Lindahl U, et al. (1999) Selective effects of sodium chlorate treatment on the sulfation of heparan sulfate. J Biol Chem 274: 36267-36273.
    • (1999) J Biol Chem , vol.274 , pp. 36267-36273
    • Safaiyan, F.1    Kolset, S.O.2    Prydz, K.3    Gottfridsson, E.4    Lindahl, U.5
  • 65
    • 0033569860 scopus 로고    scopus 로고
    • Glycosaminoglycan analysis in brain stems from animals infected with the bovine spongiform encephalopathy agent
    • Papakonstantinou E, Karakiulakis G, Roth M, Verghese-Nikolakaki S, Dawson M, et al. (1999) Glycosaminoglycan analysis in brain stems from animals infected with the bovine spongiform encephalopathy agent. Arch Biochem Biophys 370: 250-257.
    • (1999) Arch Biochem Biophys , vol.370 , pp. 250-257
    • Papakonstantinou, E.1    Karakiulakis, G.2    Roth, M.3    Verghese-Nikolakaki, S.4    Dawson, M.5
  • 66
    • 0014275162 scopus 로고
    • Some biological characters of cell lines derived from normal rabbit kidney
    • Christofinis GJ, Beale AJ (1968) Some biological characters of cell lines derived from normal rabbit kidney. J Pathol Bacteriol 95: 377-381.
    • (1968) J Pathol Bacteriol , vol.95 , pp. 377-381
    • Christofinis, G.J.1    Beale, A.J.2
  • 67
    • 0035957345 scopus 로고    scopus 로고
    • Ex vivo propagation of infectious sheep scrapie agent in heterologous epithelial cells expressing ovine prion protein
    • Vilette D, Andreoletti O, Archer F, Madelaine MF, Vilotte JL, et al. (2001) Ex vivo propagation of infectious sheep scrapie agent in heterologous epithelial cells expressing ovine prion protein. Proc Natl Acad Sci U S A 98: 4055-4059.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 4055-4059
    • Vilette, D.1    Andreoletti, O.2    Archer, F.3    Madelaine, M.F.4    Vilotte, J.L.5
  • 68
    • 35048854978 scopus 로고    scopus 로고
    • Enzymatic detergent treatment protocol that reduces protease-resistant prion protein load and infectivity from surgical-steel monofilaments contaminated with a human-derived prion strain
    • Lawson VA, Stewart JD, Masters CL (2007) Enzymatic detergent treatment protocol that reduces protease-resistant prion protein load and infectivity from surgical-steel monofilaments contaminated with a human-derived prion strain. J Gen Virol 88: 2905-2914.
    • (2007) J Gen Virol , vol.88 , pp. 2905-2914
    • Lawson, V.A.1    Stewart, J.D.2    Masters, C.L.3
  • 69
    • 34648822337 scopus 로고    scopus 로고
    • PrPc does not mediate internalization of PrPSc but is required at an early stage for de novo prion infection of Rov cells
    • Paquet S, Daude N, Courageot MP, Chapuis J, Laude H, et al. (2007) PrPc does not mediate internalization of PrPSc but is required at an early stage for de novo prion infection of Rov cells. J Virol 81: 10786-10791.
    • (2007) J Virol , vol.81 , pp. 10786-10791
    • Paquet, S.1    Daude, N.2    Courageot, M.P.3    Chapuis, J.4    Laude, H.5


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