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Volumn 289, Issue 15, 2014, Pages 10660-10667

A proposed mechanism for the promotion of prion conversion involving a strictly conserved tyrosine residue in the α2- β2 loop of PrPC

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC COMPOUNDS; MAMMALS; PLANTS (BOTANY);

EID: 84898651807     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.549030     Document Type: Article
Times cited : (36)

References (53)
  • 1
    • 0028779748 scopus 로고
    • Epidemiological observations on spongiform encephalopathies in captive wild animals in the British Isles
    • Kirkwood, J. K., and Cunningham, A. A. (1994) Epidemiological observations on spongiform encephalopathies in captive wild animals in the British Isles. Vet. Rec. 135, 296-303
    • (1994) Vet. Rec. , vol.135 , pp. 296-303
    • Kirkwood, J.K.1    Cunningham, A.A.2
  • 2
    • 0027762340 scopus 로고
    • Bovine spongiform encephalopathy and its association with the feeding of ruminant-derived protein
    • Taylor, D. M. (1993) Bovine spongiform encephalopathy and its association with the feeding of ruminant-derived protein. Dev. Biol. Stand. 80, 215-224
    • (1993) Dev. Biol. Stand. , vol.80 , pp. 215-224
    • Taylor, D.M.1
  • 3
    • 0038243152 scopus 로고    scopus 로고
    • Ministry of Agriculture, Fisheries and Food, Ministry of Agriculture, Fisheries and Food, London
    • Ministry of Agriculture, Fisheries and Food (2000) Bovine Spongiform Encephalopathy in Great Britain: A Progress Report, p. 71, Ministry of Agriculture, Fisheries and Food, London
    • (2000) Bovine Spongiform Encephalopathy in Great Britain: A Progress Report , pp. 71
  • 6
    • 84872470789 scopus 로고    scopus 로고
    • Mucosal transmission and pathogenesis of chronic wasting disease in ferrets
    • Perrott, M. R., Sigurdson, C. J., Mason, G. L., and Hoover, E. A. (2013) Mucosal transmission and pathogenesis of chronic wasting disease in ferrets. J. Gen. Virol. 94, 432-442
    • (2013) J. Gen. Virol. , vol.94 , pp. 432-442
    • Perrott, M.R.1    Sigurdson, C.J.2    Mason, G.L.3    Hoover, E.A.4
  • 8
    • 34250359350 scopus 로고    scopus 로고
    • A natural case of chronic wasting disease in a free-ranging moose (Alces alces shirasi)
    • Baeten, L. A., Powers, B. E., Jewell, J. E., Spraker, T. R., and Miller, M. W. (2007) A natural case of chronic wasting disease in a free-ranging moose (Alces alces shirasi). J. Wildl. Dis. 43, 309-314
    • (2007) J. Wildl. Dis. , vol.43 , pp. 309-314
    • Baeten, L.A.1    Powers, B.E.2    Jewell, J.E.3    Spraker, T.R.4    Miller, M.W.5
  • 11
    • 0030836511 scopus 로고    scopus 로고
    • NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231)
    • Riek, R., Hornemann, S., Wider, G., Glockshuber, R., and Wüthrich, K. (1997) NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). FEBS Lett. 413, 282-288
    • (1997) FEBS Lett. , vol.413 , pp. 282-288
    • Riek, R.1    Hornemann, S.2    Wider, G.3    Glockshuber, R.4    Wüthrich, K.5
  • 13
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner, S. B. (1982) Novel proteinaceous infectious particles cause scrapie. Science 216, 136-144
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 15
    • 0027200415 scopus 로고
    • Swaledale sheep affected by natural scrapie differ significantly in PrP genotype frequencies from healthy sheep and those selected for reduced incidence of scrapie
    • Hunter, N., Goldmann, W., Benson, G., Foster, J. D., and Hope, J. (1993) Swaledale sheep affected by natural scrapie differ significantly in PrP genotype frequencies from healthy sheep and those selected for reduced incidence of scrapie. J. Gen. Virol. 74, 1025-1031
    • (1993) J. Gen. Virol. , vol.74 , pp. 1025-1031
    • Hunter, N.1    Goldmann, W.2    Benson, G.3    Foster, J.D.4    Hope, J.5
  • 16
    • 0031561158 scopus 로고    scopus 로고
    • Natural scrapie and PrP genotype: Case-control studies in British sheep
    • Hunter, N., Goldmann, W., Foster, J. D., Cairns, D., and Smith, G. (1997) Natural scrapie and PrP genotype: case-control studies in British sheep. Vet. Rec. 141, 137-140
    • (1997) Vet. Rec. , vol.141 , pp. 137-140
    • Hunter, N.1    Goldmann, W.2    Foster, J.D.3    Cairns, D.4    Smith, G.5
  • 18
    • 0028822204 scopus 로고
    • A single hamster PrP amino acid blocks conversion to protease-resistant PrP in scrapie-infected mouse neuroblastoma cells
    • Priola, S. A., and Chesebro, B. (1995) A single hamster PrP amino acid blocks conversion to protease-resistant PrP in scrapie-infected mouse neuroblastoma cells. J. Virol. 69, 7754-7758
    • (1995) J. Virol. , vol.69 , pp. 7754-7758
    • Priola, S.A.1    Chesebro, B.2
  • 19
    • 0035041973 scopus 로고    scopus 로고
    • Efficient conversion of normal prion protein (PrP) by abnormal hamster PrP is determined by homology at amino acid residue 155
    • Priola, S. A., Chabry, J., and Chan, K. (2001) Efficient conversion of normal prion protein (PrP) by abnormal hamster PrP is determined by homology at amino acid residue 155. J. Virol. 75, 4673-4680
    • (2001) J. Virol. , vol.75 , pp. 4673-4680
    • Priola, S.A.1    Chabry, J.2    Chan, K.3
  • 22
    • 70049109405 scopus 로고    scopus 로고
    • Trans-dominant inhibition of prion propagation in vitro is not mediated by an accessory cofactor
    • Geoghegan, J. C., Miller, M. B., Kwak, A. H., Harris, B. T., and Supattapone, S. (2009) Trans-dominant inhibition of prion propagation in vitro is not mediated by an accessory cofactor. PLoS Pathog. 5, e1000535
    • (2009) PLoS Pathog. , vol.5
    • Geoghegan, J.C.1    Miller, M.B.2    Kwak, A.H.3    Harris, B.T.4    Supattapone, S.5
  • 23
    • 0037301367 scopus 로고    scopus 로고
    • Multiple amino acid residues within the rabbit prion protein inhibit formation of its abnormal isoform
    • Vorberg, I., Groschup, M. H., Pfaff, E., and Priola, S. A. (2003) Multiple amino acid residues within the rabbit prion protein inhibit formation of its abnormal isoform. J. Virol. 77, 2003-2009
    • (2003) J. Virol. , vol.77 , pp. 2003-2009
    • Vorberg, I.1    Groschup, M.H.2    Pfaff, E.3    Priola, S.A.4
  • 25
    • 84858374665 scopus 로고    scopus 로고
    • The amyloid state of proteins in human diseases
    • Eisenberg, D., and Jucker, M. (2012) The amyloid state of proteins in human diseases. Cell 148, 1188-1203
    • (2012) Cell , vol.148 , pp. 1188-1203
    • Eisenberg, D.1    Jucker, M.2
  • 26
    • 77956941468 scopus 로고    scopus 로고
    • Crystallographic studies of prion protein (PrP) segments suggest how structural changes encoded by polymorphism at residue 129 modulate susceptibility to human prion disease
    • Apostol, M. I., Sawaya, M. R., Cascio, D., and Eisenberg, D. (2010) Crystallographic studies of prion protein (PrP) segments suggest how structural changes encoded by polymorphism at residue 129 modulate susceptibility to human prion disease. J. Biol. Chem. 285, 29671-29675
    • (2010) J. Biol. Chem. , vol.285 , pp. 29671-29675
    • Apostol, M.I.1    Sawaya, M.R.2    Cascio, D.3    Eisenberg, D.4
  • 27
    • 79953183597 scopus 로고    scopus 로고
    • Atomic structures suggest determinants of transmission barriers in mammalian prion disease
    • Apostol, M. I., Wiltzius, J. J., Sawaya, M. R., Cascio, D., and Eisenberg, D. (2011) Atomic structures suggest determinants of transmission barriers in mammalian prion disease. Biochemistry 50, 2456-2463
    • (2011) Biochemistry , vol.50 , pp. 2456-2463
    • Apostol, M.I.1    Wiltzius, J.J.2    Sawaya, M.R.3    Cascio, D.4    Eisenberg, D.5
  • 28
    • 1842766124 scopus 로고    scopus 로고
    • Molecular basis of barriers for interspecies transmissibility of mammalian prions
    • Vanik, D. L., Surewicz, K. A., and Surewicz, W. K. (2004) Molecular basis of barriers for interspecies transmissibility of mammalian prions. Mol. Cell 14, 139-145
    • (2004) Mol. Cell , vol.14 , pp. 139-145
    • Vanik, D.L.1    Surewicz, K.A.2    Surewicz, W.K.3
  • 31
    • 77953808355 scopus 로고    scopus 로고
    • Horse prion protein NMR structure and comparisons with related variants of the mouse prion protein
    • Pérez, D. R., Damberger, F. F., and Wüthrich, K. (2010) Horse prion protein NMR structure and comparisons with related variants of the mouse prion protein. J. Mol. Biol. 400, 121-128
    • (2010) J. Mol. Biol. , vol.400 , pp. 121-128
    • Pérez, D.R.1    Damberger, F.F.2    Wüthrich, K.3
  • 33
    • 62449340410 scopus 로고    scopus 로고
    • A structural overview of the vertebrate prion proteins
    • Pastore, A., and Zagari, A. (2007) A structural overview of the vertebrate prion proteins. Prion 1, 185-197
    • (2007) Prion , vol.1 , pp. 185-197
    • Pastore, A.1    Zagari, A.2
  • 39
    • 0345306764 scopus 로고    scopus 로고
    • Design of a novel globular protein fold with atomic-level accuracy
    • Kuhlman, B., Dantas, G., Ireton, G. C., Varani, G., Stoddard, B. L., and Baker, D. (2003) Design of a novel globular protein fold with atomic-level accuracy. Science 302, 1364-1368
    • (2003) Science , vol.302 , pp. 1364-1368
    • Kuhlman, B.1    Dantas, G.2    Ireton, G.C.3    Varani, G.4    Stoddard, B.L.5    Baker, D.6
  • 40
    • 36749048724 scopus 로고    scopus 로고
    • Prediction of the structure of symmetrical protein assemblies
    • André, I., Bradley, P., Wang, C., and Baker, D. (2007) Prediction of the structure of symmetrical protein assemblies. Proc. Natl. Acad. Sci. U.S.A. 104, 17656-17661
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 17656-17661
    • André, I.1    Bradley, P.2    Wang, C.3    Baker, D.4
  • 42
    • 79958731755 scopus 로고    scopus 로고
    • Heparin enhances the cell-protein misfolding cyclic amplification efficiency of variant Creutzfeldt-Jakob disease
    • Yokoyama, T., Takeuchi, A., Yamamoto, M., Kitamoto, T., Ironside, J. W., and Morita, M. (2011) Heparin enhances the cell-protein misfolding cyclic amplification efficiency of variant Creutzfeldt-Jakob disease. Neurosci. Lett. 498, 119-123
    • (2011) Neurosci. Lett. , vol.498 , pp. 119-123
    • Yokoyama, T.1    Takeuchi, A.2    Yamamoto, M.3    Kitamoto, T.4    Ironside, J.W.5    Morita, M.6
  • 45
    • 0035859102 scopus 로고    scopus 로고
    • Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding
    • Saborio, G. P., Permanne, B., and 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
  • 48
    • 33746849285 scopus 로고    scopus 로고
    • Prion strain-dependent differences in conversion of mutant prion proteins in cell culture
    • Atarashi, R., Sim, V. L., Nishida, N., Caughey, B., and Katamine, S. (2006) Prion strain-dependent differences in conversion of mutant prion proteins in cell culture. J. Virol. 80, 7854-7862
    • (2006) J. Virol. , vol.80 , pp. 7854-7862
    • Atarashi, R.1    Sim, V.L.2    Nishida, N.3    Caughey, B.4    Katamine, S.5
  • 49
    • 0028928171 scopus 로고
    • Identification of five allelic variants of the sheep PrP gene and their association with natural scrapie
    • Belt, P. B., Muileman, I. H., Schreuder, B. E., Bos-de-Ruijter, J., Gielkens, A. L., and Smits, M. A. (1995) Identification of five allelic variants of the sheep PrP gene and their association with natural scrapie. J. Gen. Virol. 76, 509-517
    • (1995) J. Gen. Virol. , vol.76 , pp. 509-517
    • Belt, P.B.1    Muileman, I.H.2    Schreuder, B.E.3    Bos-De-Ruijter, J.4    Gielkens, A.L.5    Smits, M.A.6
  • 51
    • 84867245306 scopus 로고    scopus 로고
    • Prion protein mPrP[F175A](121-231): Structure and stability in solution
    • Christen, B., Hornemann, S., Damberger, F. F., and Wüthrich, K. (2012) Prion protein mPrP[F175A](121-231): structure and stability in solution. J. Mol. Biol. 423, 496-502
    • (2012) J. Mol. Biol. , vol.423 , pp. 496-502
    • Christen, B.1    Hornemann, S.2    Damberger, F.F.3    Wüthrich, K.4
  • 52
    • 67349152665 scopus 로고    scopus 로고
    • Prion protein NMR structure from tammar wallaby (Macropus eugenii) shows that the α2-α2 loop is modulated by long-range sequence effects
    • Christen, B., Hornemann, S., Damberger, F. F., and Wüthrich, K. (2009) Prion protein NMR structure from tammar wallaby (Macropus eugenii) shows that the α2-α2 loop is modulated by long-range sequence effects. J. Mol. Biol. 389, 833-845
    • (2009) J. Mol. Biol. , vol.389 , pp. 833-845
    • Christen, B.1    Hornemann, S.2    Damberger, F.F.3    Wüthrich, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.