메뉴 건너뛰기




Volumn 27, Issue 15, 2007, Pages 5445-5455

Prion protein repeat expansion results in increased aggregation and reveals phenotypic variability

Author keywords

[No Author keywords available]

Indexed keywords

CHIMERIC PROTEIN; OLIGOPEPTIDE; PRION PROTEIN;

EID: 34547204037     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.02127-06     Document Type: Article
Times cited : (39)

References (54)
  • 1
    • 10944273371 scopus 로고    scopus 로고
    • Specificity of prion assembly in vivo
    • Bagriantsev, S., and S. W. Liebman. 2004. Specificity of prion assembly in vivo. J. Biol. Chem. 279:51042-51048.
    • (2004) J. Biol. Chem , vol.279 , pp. 51042-51048
    • Bagriantsev, S.1    Liebman, S.W.2
  • 2
    • 0028997297 scopus 로고
    • Non-genetic propagation of strain-specific properties of scrapie prion protein
    • Bessen, R. A., D. A. Kocisko, G. J. Raymond, S. Nandan, P. T. Lansbury, and B. Caughey. 1995. Non-genetic propagation of strain-specific properties of scrapie prion protein. Nature 375:698-700.
    • (1995) Nature , vol.375 , pp. 698-700
    • Bessen, R.A.1    Kocisko, D.A.2    Raymond, G.J.3    Nandan, S.4    Lansbury, P.T.5    Caughey, B.6
  • 3
    • 0026558780 scopus 로고
    • Identification of two biologically distinct strains of transmissible mink encephalopathy in hamsters
    • Bessen, R. A., and R. F. Marsh. 1992. Identification of two biologically distinct strains of transmissible mink encephalopathy in hamsters. J. Gen. Virol. 73(Pt. 2):329-334.
    • (1992) J. Gen. Virol , vol.73 , Issue.PART. 2 , pp. 329-334
    • Bessen, R.A.1    Marsh, R.F.2
  • 5
    • 0035803490 scopus 로고    scopus 로고
    • Borchsenius, A. S., R. D. Wegrzyn, G. P. Newnam, S. G. Inge-Vechtomov, and Y. O. Chernoff. 2001. Yeast prion protein derivative defective in aggregate shearing and production of new 'seeds'. EMBO J. 20:6683-6691.
    • Borchsenius, A. S., R. D. Wegrzyn, G. P. Newnam, S. G. Inge-Vechtomov, and Y. O. Chernoff. 2001. Yeast prion protein derivative defective in aggregate shearing and production of new 'seeds'. EMBO J. 20:6683-6691.
  • 6
    • 0036215385 scopus 로고    scopus 로고
    • Similar and divergent features in mammalian and yeast prions
    • Bousset, L., and R. Melki. 2002. Similar and divergent features in mammalian and yeast prions. Microbes Infect. 4:461-469.
    • (2002) Microbes Infect , vol.4 , pp. 461-469
    • Bousset, L.1    Melki, R.2
  • 8
    • 27544439092 scopus 로고    scopus 로고
    • Transgenic mice expressing bovine PrP with a four extra repeat octapeptide insert mutation show a spontaneous, non-transmissible, neurodegenerative disease and an expedited course of BSE infection
    • Castilla, J., A. Gutierrez-Adan, A. Bran, B. Pintado, F. J. Salguero, B. Parra, F. D. Segundo, M. A. Ramirez, A. Rabano, M. J. Cano, and J. M. Torres. 2005. Transgenic mice expressing bovine PrP with a four extra repeat octapeptide insert mutation show a spontaneous, non-transmissible, neurodegenerative disease and an expedited course of BSE infection. FEBS Lett. 579:6237-6246.
    • (2005) FEBS Lett , vol.579 , pp. 6237-6246
    • Castilla, J.1    Gutierrez-Adan, A.2    Bran, A.3    Pintado, B.4    Salguero, F.J.5    Parra, B.6    Segundo, F.D.7    Ramirez, M.A.8    Rabano, A.9    Cano, M.J.10    Torres, J.M.11
  • 12
    • 0034625069 scopus 로고    scopus 로고
    • Accumulation of protease-resistant prion protein (PrP) and apoptosis of cerebellar granule cells in transgenic mice expressing a PrP insertional mutation
    • Chiesa, R., B. Drisaldi, E. Quaglio, A. Migheli, P. Piccardo, B. Ghetti, and D. A. Harris. 2000. Accumulation of protease-resistant prion protein (PrP) and apoptosis of cerebellar granule cells in transgenic mice expressing a PrP insertional mutation. Proc. Natl. Acad. Sci. USA 97:5574-5579.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5574-5579
    • Chiesa, R.1    Drisaldi, B.2    Quaglio, E.3    Migheli, A.4    Piccardo, P.5    Ghetti, B.6    Harris, D.A.7
  • 13
    • 0032427904 scopus 로고    scopus 로고
    • Neurological illness in transgenic mice expressing a prion protein with an insertional mutation
    • Chiesa, R., P. Piccardo, B. Ghetti, and D. A. Harris. 1998. Neurological illness in transgenic mice expressing a prion protein with an insertional mutation. Neuron 21:1339-1351.
    • (1998) Neuron , vol.21 , pp. 1339-1351
    • Chiesa, R.1    Piccardo, P.2    Ghetti, B.3    Harris, D.A.4
  • 15
    • 0034916581 scopus 로고    scopus 로고
    • Prion diseases of humans and animals: Their causes and molecular basis
    • Collinge, J. 2001. Prion diseases of humans and animals: their causes and molecular basis. Annu. Rev. Neurosci. 24:519-550.
    • (2001) Annu. Rev. Neurosci , vol.24 , pp. 519-550
    • Collinge, J.1
  • 17
    • 0032568793 scopus 로고    scopus 로고
    • A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion
    • DePace, A. H., A. Santoso, P. Hillner, and J. S. Weissman. 1998. A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion. Cell 93:1241-1252.
    • (1998) Cell , vol.93 , pp. 1241-1252
    • DePace, A.H.1    Santoso, A.2    Hillner, P.3    Weissman, J.S.4
  • 24
    • 0037385558 scopus 로고    scopus 로고
    • Phenotypic variability in the brains of a family with a prion disease characterized by a 144-base pair insertion in the prion protein gene
    • King, A., L. Doey, M. Rossor, S. Mead, J. Collinge, and P. Lantos. 2003. Phenotypic variability in the brains of a family with a prion disease characterized by a 144-base pair insertion in the prion protein gene. Neuropathol. Appl. Neurobiol. 29:98-105.
    • (2003) Neuropathol. Appl. Neurobiol , vol.29 , pp. 98-105
    • King, A.1    Doey, L.2    Rossor, M.3    Mead, S.4    Collinge, J.5    Lantos, P.6
  • 25
    • 1642617641 scopus 로고    scopus 로고
    • Protein-only transmission of three yeast prion strains
    • King, C. Y., and R. Diaz-Avalos. 2004. Protein-only transmission of three yeast prion strains. Nature 428:319-323.
    • (2004) Nature , vol.428 , pp. 319-323
    • King, C.Y.1    Diaz-Avalos, R.2
  • 28
    • 20444474976 scopus 로고    scopus 로고
    • Structural insights into a yeast prion illuminate nucleation and strain diversity
    • Krishnan, R., and S. L. Lindquist. 2005. Structural insights into a yeast prion illuminate nucleation and strain diversity. Nature 435:765-772.
    • (2005) Nature , vol.435 , pp. 765-772
    • Krishnan, R.1    Lindquist, S.L.2
  • 30
    • 0034723391 scopus 로고    scopus 로고
    • Creating a protein-based element of inheritance
    • Li, L., and S. Lindquist. 2000. Creating a protein-based element of inheritance. Science 287:661-664.
    • (2000) Science , vol.287 , pp. 661-664
    • Li, L.1    Lindquist, S.2
  • 31
    • 0033527045 scopus 로고    scopus 로고
    • Oligopeptide-repeat expansions modulate 'protein-only' inheritance in yeast
    • Liu, J. J., and S. Lindquist. 1999. Oligopeptide-repeat expansions modulate 'protein-only' inheritance in yeast. Nature 400:573-576.
    • (1999) Nature , vol.400 , pp. 573-576
    • Liu, J.J.1    Lindquist, S.2
  • 33
    • 34249941302 scopus 로고    scopus 로고
    • Copper and the prion protein: Methods, structures, function, and disease
    • Millhauser, G. L. 2007. Copper and the prion protein: methods, structures, function, and disease. Annu. Rev. Phys. Chem. 58:299-320.
    • (2007) Annu. Rev. Phys. Chem , vol.58 , pp. 299-320
    • Millhauser, G.L.1
  • 34
    • 33644540192 scopus 로고    scopus 로고
    • Octapeptide repeat insertions increase the rate of protease-resistant prion protein formation
    • Moore, R. A., C. Herzog, J. Errett, D. A. Kocisko, K. M. Arnold, S. F. Hayes, and S. A. Priola. 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    Hayes, S.F.6    Priola, S.A.7
  • 35
    • 0028953840 scopus 로고
    • Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds
    • Mumberg, D., R. Muller, and M. Funk. 1995. Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds. Gene 156:119-122.
    • (1995) Gene , vol.156 , pp. 119-122
    • Mumberg, D.1    Muller, R.2    Funk, M.3
  • 36
    • 0036310663 scopus 로고    scopus 로고
    • Guanidine hydrochloride inhibits the generation of prion "seeds" but not prion protein aggregation in yeast
    • Ness, F., P. Ferreira, B. S. Cox, and M. F. Tuite. 2002. Guanidine hydrochloride inhibits the generation of prion "seeds" but not prion protein aggregation in yeast. Mol. Cell. Biol. 22:5593-5605.
    • (2002) Mol. Cell. Biol , vol.22 , pp. 5593-5605
    • Ness, F.1    Ferreira, P.2    Cox, B.S.3    Tuite, M.F.4
  • 38
    • 0035341212 scopus 로고    scopus 로고
    • Oligopeptide repeats in the yeast protein Sup35p stabilize intermolecular prion interactions
    • Parham, S. N., C. G. Resende, and M. F. Tuite. 2001. Oligopeptide repeats in the yeast protein Sup35p stabilize intermolecular prion interactions. EMBO J. 20:2111-2119.
    • (2001) EMBO J , vol.20 , pp. 2111-2119
    • Parham, S.N.1    Resende, C.G.2    Tuite, M.F.3
  • 39
    • 0029780647 scopus 로고    scopus 로고
    • Support for the prion hypothesis for inheritance of a phenotypic trait in yeast
    • Patino, M. M., J. J. Liu, J. R. Glover, and S. Lindquist. 1996. Support for the prion hypothesis for inheritance of a phenotypic trait in yeast. Science 273: 622-626.
    • (1996) Science , vol.273 , pp. 622-626
    • Patino, M.M.1    Liu, J.J.2    Glover, J.R.3    Lindquist, S.4
  • 41
    • 0027520888 scopus 로고
    • Conversion of truncated and elongated prion proteins into the scrapie isoform in cultured cells
    • Rogers, M., F. Yehiely, M. Scott, and S. B. Prusiner. 1993. Conversion of truncated and elongated prion proteins into the scrapie isoform in cultured cells. Proc. Natl. Acad. Sci. USA 90:3182-3186.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3182-3186
    • Rogers, M.1    Yehiely, F.2    Scott, M.3    Prusiner, S.B.4
  • 42
    • 0034758487 scopus 로고    scopus 로고
    • The role of conformational flexibility in prion propagation and maintenance for Sup35p
    • Scheibel, T., and S. L. Lindquist. 2001. The role of conformational flexibility in prion propagation and maintenance for Sup35p. Nat. Struct. Biol. 8:958-962.
    • (2001) Nat. Struct. Biol , vol.8 , pp. 958-962
    • Scheibel, T.1    Lindquist, S.L.2
  • 43
    • 1642633056 scopus 로고    scopus 로고
    • Conformational variations in an infectious protein determine prion strain differences
    • Tanaka, M., P. Chien, N. Naber, R. Cooke, and J. S. Weissman. 2004. Conformational variations in an infectious protein determine prion strain differences. Nature 428:323-328.
    • (2004) Nature , vol.428 , pp. 323-328
    • Tanaka, M.1    Chien, P.2    Naber, N.3    Cooke, R.4    Weissman, J.S.5
  • 44
    • 17044435107 scopus 로고    scopus 로고
    • Mechanism of cross-species prion transmission: An infectious conformation compatible with two highly divergent yeast prion proteins
    • Tanaka, M., P. Chien, K. Yonekura, and J. S. Weissman. 2005. Mechanism of cross-species prion transmission: an infectious conformation compatible with two highly divergent yeast prion proteins. Cell 121:49-62.
    • (2005) Cell , vol.121 , pp. 49-62
    • Tanaka, M.1    Chien, P.2    Yonekura, K.3    Weissman, J.S.4
  • 45
    • 0030011971 scopus 로고    scopus 로고
    • Experimental transmission of Creutzfeldt-Jakob disease and related diseases to rodents
    • Tateishi, J., T. Kitamoto, M. Z. Hoque, and H. Furukawa. 1996. Experimental transmission of Creutzfeldt-Jakob disease and related diseases to rodents. Neurology 46:532-537.
    • (1996) Neurology , vol.46 , pp. 532-537
    • Tateishi, J.1    Kitamoto, T.2    Hoque, M.Z.3    Furukawa, H.4
  • 47
    • 31444452768 scopus 로고    scopus 로고
    • The battle of the fold: Chaperones take on prions
    • True, H. L. 2006. The battle of the fold: chaperones take on prions. Trends Genet. 22:110-117.
    • (2006) Trends Genet , vol.22 , pp. 110-117
    • True, H.L.1
  • 49
    • 0036403732 scopus 로고    scopus 로고
    • Prions as protein-based genetic elements
    • Uptain, S. M., and S. Lindquist. 2002. Prions as protein-based genetic elements. Annu. Rev. Microbiol. 56:703-741.
    • (2002) Annu. Rev. Microbiol , vol.56 , pp. 703-741
    • Uptain, S.M.1    Lindquist, S.2
  • 50
    • 0035890264 scopus 로고    scopus 로고
    • +] are distinguished by their efficiencies of prion-mediated conformational conversion
    • +] are distinguished by their efficiencies of prion-mediated conformational conversion. EMBO J. 20:6236-6245.
    • (2001) EMBO J , vol.20 , pp. 6236-6245
    • Uptain, S.M.1    Sawicki, G.J.2    Caughey, B.3    Lindquist, S.4
  • 52
    • 0141849458 scopus 로고    scopus 로고
    • Molecular and clinical classification of human prion disease
    • Wadsworth, J. D., A. F. Hill, J. A. Beck, and J. Collinge. 2003. Molecular and clinical classification of human prion disease. Br. Med. Bull. 66:241-254.
    • (2003) Br. Med. Bull , vol.66 , pp. 241-254
    • Wadsworth, J.D.1    Hill, A.F.2    Beck, J.A.3    Collinge, J.4
  • 53
    • 33744959528 scopus 로고    scopus 로고
    • Prion proteins with insertion mutations have altered N-terminal conformation and increased ligand binding activity and are more susceptible to oxidative attack
    • Yin, S., S. Yu, C. Li, P. Wong, B. Chang, F. Xiao, S. C. Kang, H. Yan, G. Xiao, J. Grassi, P. Tien, and M. S. Sy. 2006. Prion proteins with insertion mutations have altered N-terminal conformation and increased ligand binding activity and are more susceptible to oxidative attack. J. Biol. Chem. 281: 10698-10705.
    • (2006) J. Biol. Chem , vol.281 , pp. 10698-10705
    • Yin, S.1    Yu, S.2    Li, C.3    Wong, P.4    Chang, B.5    Xiao, F.6    Kang, S.C.7    Yan, H.8    Xiao, G.9    Grassi, J.10    Tien, P.11    Sy, M.S.12


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.