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Volumn 40, Issue , 2006, Pages 25-45

Discovering DNA encodes heredity and prions are infectious proteins

Author keywords

Bioassays; Biological information; Genes; Nucleic acids; Prions; Proteins; Purification

Indexed keywords

DNA; PRION PROTEIN; RNA;

EID: 33845681207     PISSN: 00664197     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.genet.40.121505.133522     Document Type: Review
Times cited : (15)

References (123)
  • 1
    • 0028298531 scopus 로고
    • Endogenous viral complexes with long RNA cosediment with the agent of Creutzfeldt-Jakob disease
    • Akowitz A, Sklaviadis T, Manuelidis L. 1994. Endogenous viral complexes with long RNA cosediment with the agent of Creutzfeldt-Jakob disease. Nucleic Acids Res. 22:1101-7
    • (1994) Nucleic Acids Res. , vol.22 , pp. 1101-1107
    • Akowitz, A.1    Sklaviadis, T.2    Manuelidis, L.3
  • 2
    • 84968115343 scopus 로고
    • The transformation in vitro of R pneumococci into S forms of different specific types by the use of filtered pneumococcus extracts
    • Alloway JL. 1932. The transformation in vitro of R pneumococci into S forms of different specific types by the use of filtered pneumococcus extracts. J. Exp. Med. 55:91-99
    • (1932) J. Exp. Med. , vol.55 , pp. 91-99
    • Alloway, J.L.1
  • 3
    • 26844522623 scopus 로고
    • Further observations on the use of pneumococcus extracts in effecting transformation of type in vitro
    • Alloway JL. 1933. Further observations on the use of pneumococcus extracts in effecting transformation of type in vitro. J. Exp. Med. 57:265-78
    • (1933) J. Exp. Med. , vol.57 , pp. 265-278
    • Alloway, J.L.1
  • 4
    • 0014211846 scopus 로고
    • Does the agent of scrapie replicate without nucleic acid?
    • Alper T, Cramp WA, Haig DA, Clarke MC. 1967. Does the agent of scrapie replicate without nucleic acid? Nature 214:764-66
    • (1967) Nature , vol.214 , pp. 764-766
    • Alper, T.1    Cramp, W.A.2    Haig, D.A.3    Clarke, M.C.4
  • 5
    • 84983711696 scopus 로고
    • Studies on the chemical nature of the substance inducing transformation of pneumococcal types. Induction of transformation by a deoxyribonucleic acid fraction isolated from pneumococcus type III
    • Avery OT, MacLeod CM, McCarty M. 1944. Studies on the chemical nature of the substance inducing transformation of pneumococcal types. Induction of transformation by a deoxyribonucleic acid fraction isolated from pneumococcus type III. J. Exp. Med. 79:137-57
    • (1944) J. Exp. Med. , vol.79 , pp. 137-157
    • Avery, O.T.1    MacLeod, C.M.2    McCarty, M.3
  • 7
    • 0022476747 scopus 로고
    • Scrapie and cellular PrP isoforms are encoded by the same chromosomal gene
    • Basler K, Oesch B, Scott M, Westaway D, Wälchli M, et al. 1986. Scrapie and cellular PrP isoforms are encoded by the same chromosomal gene. Cell 46:417-28
    • (1986) Cell , vol.46 , pp. 417-428
    • Basler, K.1    Oesch, B.2    Scott, M.3    Westaway, D.4    Wälchli, M.5
  • 8
    • 0035022139 scopus 로고    scopus 로고
    • Spiroplasma sp. 16S rDNA in Creutzfeldt-Jakob disease and scrapie as shown by PCR and DNA sequence analysis
    • Bastian FO, Foster JW. 2001. Spiroplasma sp. 16S rDNA in Creutzfeldt-Jakob disease and scrapie as shown by PCR and DNA sequence analysis. J. Neuropathol. Exp. Neurol. 60:613-20
    • (2001) J. Neuropathol. Exp. Neurol. , vol.60 , pp. 613-620
    • Bastian, F.O.1    Foster, J.W.2
  • 9
    • 0001194208 scopus 로고
    • Genetic control of biochemical reactions in Neurospora
    • Beadle G, Tatum E. 1941. Genetic control of biochemical reactions in Neurospora. Proc. Natl. Acad. Sci. USA 27:499-506
    • (1941) Proc. Natl. Acad. Sci. USA , vol.27 , pp. 499-506
    • Beadle, G.1    Tatum, E.2
  • 12
    • 0028043661 scopus 로고
    • Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy
    • Bessen RA, Marsh RF. 1994. Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy. J. Virol. 68:7859-68
    • (1994) J. Virol. , vol.68 , pp. 7859-7868
    • Bessen, R.A.1    Marsh, R.F.2
  • 13
    • 0020490156 scopus 로고
    • Identification of a protein that purifies with the scrapie prion
    • Bolton DC, McKinley MP, Prusiner SB. 1982. Identification of a protein that purifies with the scrapie prion. Science 218:1309-11
    • (1982) Science , vol.218 , pp. 1309-1311
    • Bolton, D.C.1    McKinley, M.P.2    Prusiner, S.B.3
  • 14
    • 36949088975 scopus 로고
    • An unstable intermediate carrying information from genes to ribosomes for protein synthesis
    • Brenner S, Jacob F, Meselson M. 1961. An unstable intermediate carrying information from genes to ribosomes for protein synthesis. Nature 190:576-81
    • (1961) Nature , vol.190 , pp. 576-581
    • Brenner, S.1    Jacob, F.2    Meselson, M.3
  • 15
    • 8644260825 scopus 로고    scopus 로고
    • Transmission of prions from mule deer and elk with chronic wasting disease to transgenic mice expressing cervid PrP
    • Browning SR, Mason GL, Seward T, Green M, Eliason GA, et al. 2004. Transmission of prions from mule deer and elk with chronic wasting disease to transgenic mice expressing cervid PrP. J. Virol. 78:13345-50
    • (2004) J. Virol. , vol.78 , pp. 13345-13350
    • Browning, S.R.1    Mason, G.L.2    Seward, T.3    Green, M.4    Eliason, G.A.5
  • 16
    • 0141515178 scopus 로고    scopus 로고
    • TSE strain variation: An investigation into prion disease diversity
    • Bruce ME. 2003. TSE strain variation: an investigation into prion disease diversity. Br. Med. Bull. 66:99-108
    • (2003) Br. Med. Bull. , vol.66 , pp. 99-108
    • Bruce, M.E.1
  • 17
    • 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
  • 19
    • 0028276015 scopus 로고
    • Prion isolate specified allotypic interactions between the cellular and scrapie prion proteins in congenic and transgenic mice
    • Carlson GA, Ebeling C, Yang SL, Telling G, Torchia M, et al. 1994. Prion isolate specified allotypic interactions between the cellular and scrapie prion proteins in congenic and transgenic mice. Proc. Natl. Acad. Sci. USA 91:5690-94
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5690-5694
    • Carlson, G.A.1    Ebeling, C.2    Yang, S.L.3    Telling, G.4    Torchia, M.5
  • 22
    • 49749206702 scopus 로고
    • Encephalopathy in mice produced by inoculation with scrapie brain material
    • Chandler RL. 1961. Encephalopathy in mice produced by inoculation with scrapie brain material. Lancet 1:1378-79
    • (1961) Lancet , vol.1 , pp. 1378-1379
    • Chandler, R.L.1
  • 23
    • 0141849876 scopus 로고    scopus 로고
    • Introduction to the transmissible spongiform encephalopathies or prion diseases
    • Chesebro B. 2003. Introduction to the transmissible spongiform encephalopathies or prion diseases. Br. Med. Bull. 66:1-20
    • (2003) Br. Med. Bull. , vol.66 , pp. 1-20
    • Chesebro, B.1
  • 24
    • 4644323663 scopus 로고    scopus 로고
    • Biomedicine. A fresh look at BSE
    • Chesebro B. 2004. Biomedicine. A fresh look at BSE. Science 305:1918-21
    • (2004) Science , vol.305 , pp. 1918-1921
    • Chesebro, B.1
  • 25
    • 0021884354 scopus 로고
    • Identification of scrapie prion protein-specific mRNA in scrapie-infected and uninfected brain
    • Chesebro B, Race R, Wehrly K, Nishio J, Bloom M, et al. 1985. Identification of scrapie prion protein-specific mRNA in scrapie-infected and uninfected brain. Nature 315:331-33
    • (1985) Nature , vol.315 , pp. 331-333
    • Chesebro, B.1    Race, R.2    Wehrly, K.3    Nishio, J.4    Bloom, M.5
  • 26
    • 0034761946 scopus 로고    scopus 로고
    • Florid plaques in ovine PrP transgenic mice infected with an experimental ovine BSE
    • Crozet C, Bencsik A, Flamant F, Lezmi S, Samarut J, Baron T. 2001. Florid plaques in ovine PrP transgenic mice infected with an experimental ovine BSE. EMBO Rep. 2:952-56
    • (2001) EMBO Rep. , vol.2 , pp. 952-956
    • Crozet, C.1    Bencsik, A.2    Flamant, F.3    Lezmi, S.4    Samarut, J.5    Baron, T.6
  • 27
    • 0035025625 scopus 로고    scopus 로고
    • Efficient transmission of two different sheet scrapie isolates in transgenic mice expressing the ovine PrP gene
    • Crozet C, Flamant F, Bencsik A, Aubert D, Samarut J, Baron T. 2001. Efficient transmission of two different sheet scrapie isolates in transgenic mice expressing the ovine PrP gene. J. Virol. 75:5328-34
    • (2001) J. Virol. , vol.75 , pp. 5328-5334
    • Crozet, C.1    Flamant, F.2    Bencsik, A.3    Aubert, D.4    Samarut, J.5    Baron, T.6
  • 28
    • 0000049491 scopus 로고
    • Experimental transmission of trembling to the goat
    • Cuillé J, Chelle PL. 1939. Experimental transmission of trembling to the goat. C.R. Seances Acad. Sci. 208:1058-60
    • (1939) C.R. Seances Acad. Sci. , vol.208 , pp. 1058-1060
    • Cuillé, J.1    Chelle, P.L.2
  • 29
    • 85025408120 scopus 로고
    • The transformation of pneumococcal types. II. The inconvertibility of type-specific S pneumococci
    • Dawson MH. 1930. The transformation of pneumococcal types. II. The inconvertibility of type-specific S pneumococci. J. Exp. Med. 51:123-47
    • (1930) J. Exp. Med. , vol.51 , pp. 123-147
    • Dawson, M.H.1
  • 30
    • 0001272060 scopus 로고
    • In vitro transformation of pneumococcal types. I. A technique for inducing transformation of pneumococcal types in vitro
    • Dawson MH, Sia RHP. 1931. in vitro transformation of pneumococcal types. I. A technique for inducing transformation of pneumococcal types in vitro. J. Exp. Med. 54:681-99
    • (1931) J. Exp. Med. , vol.54 , pp. 681-699
    • Dawson, M.H.1    Sia, R.H.P.2
  • 34
    • 0021203930 scopus 로고
    • Antibodies to protein of scrapie-associated fibrils
    • Diringer H, Rahn HC, Bade L. 1984. Antibodies to protein of scrapie-associated fibrils. Lancet 2:345
    • (1984) Lancet , vol.2 , pp. 345
    • Diringer, H.1    Rahn, H.C.2    Bade, L.3
  • 35
    • 0031456947 scopus 로고    scopus 로고
    • Structure of the recombinant full-length hamster prion protein PrP(29-231): The N terminus is highly flexible
    • Donne DG, Viles JH, Groth D, Mehlhorn I, James TL, et al. 1997. Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible. Proc. Natl. Acad. Sci. USA 94:13452-57
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13452-13457
    • Donne, D.G.1    Viles, J.H.2    Groth, D.3    Mehlhorn, I.4    James, T.L.5
  • 36
    • 85012708269 scopus 로고
    • Decomposition of the capsular polysaccharide of pneumococcus type III by a bacterial enzyme
    • Dubos R, Avery OT. 1931. Decomposition of the capsular polysaccharide of pneumococcus type III by a bacterial enzyme. J. Exp. Med. 54:51-71
    • (1931) J. Exp. Med. , vol.54 , pp. 51-71
    • Dubos, R.1    Avery, O.T.2
  • 39
    • 0343364948 scopus 로고
    • Purified prion proteins and scrapie infectivity copartition into liposomes
    • Gabizon R, McKinley MP, Prusiner SB. 1987. Purified prion proteins and scrapie infectivity copartition into liposomes. Proc. Natl. Acad. Sci. USA 84:4017-21
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 4017-4021
    • Gabizon, R.1    McKinley, M.P.2    Prusiner, S.B.3
  • 40
    • 33845632465 scopus 로고
    • Encephalomyelitis of mice. II. A method for the measurement of virus activity
    • Gard S. 1940. Encephalomyelitis of mice. II. A method for the measurement of virus activity. J. Exp. Med. 72:69-77
    • (1940) J. Exp. Med. , vol.72 , pp. 69-77
    • Gard, S.1
  • 41
    • 84872473797 scopus 로고
    • Advances in veterinary research
    • Gordon WS. 1946. Advances in veterinary research. Vet. Res. 58:516-20
    • (1946) Vet. Res. , vol.58 , pp. 516-520
    • Gordon, W.S.1
  • 43
    • 84920056771 scopus 로고
    • Significance of pneumococcal types
    • Griffith F. 1928. Significance of pneumococcal types. J. Hygiene 27:113-59
    • (1928) J. Hygiene , vol.27 , pp. 113-159
    • Griffith, F.1
  • 44
    • 0014190760 scopus 로고
    • Self-replication and scrapie
    • Griffith JS. 1967. Self-replication and scrapie. Nature 215:1043-44
    • (1967) Nature , vol.215 , pp. 1043-1044
    • Griffith, J.S.1
  • 46
    • 0002610948 scopus 로고
    • Independent functions of viral protein and nucleic acid in growth of bacteriophage
    • Hershey AD, Chase M. 1952. Independent functions of viral protein and nucleic acid in growth of bacteriophage. J. Gen. Physiol. 36:39-56
    • (1952) J. Gen. Physiol. , vol.36 , pp. 39-56
    • Hershey, A.D.1    Chase, M.2
  • 47
    • 0032892306 scopus 로고    scopus 로고
    • Protease-resistant prion protein produced in vitro lacks detectable infectivity
    • Hill AF, Antoniou M, Collinge J. 1999. Protease-resistant prion protein produced in vitro lacks detectable infectivity. J. Gen. Virol. 80:11-14
    • (1999) J. Gen. Virol. , vol.80 , pp. 11-14
    • Hill, A.F.1    Antoniou, M.2    Collinge, J.3
  • 48
    • 0024519771 scopus 로고
    • Linkage of a prion protein missense variant to Gerstmann-Sträussler syndrome
    • Hsiao K, Baker HF, Crow TJ, Poulter M, Owen F, et al. 1989. Linkage of a prion protein missense variant to Gerstmann-Sträussler syndrome. Nature 338:342-45
    • (1989) Nature , vol.338 , pp. 342-345
    • Hsiao, K.1    Baker, H.F.2    Crow, T.J.3    Poulter, M.4    Owen, F.5
  • 49
    • 0028608963 scopus 로고
    • Serial transmission in rodents of neurodegeneration from transgenic mice expressing mutant prion protein
    • Hsiao KK, Groth D, Scott M, Yang SL, Serban H, et al. 1994. Serial transmission in rodents of neurodegeneration from transgenic mice expressing mutant prion protein. Proc. Natl. Acad. Sci. USA 91:9126-30
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9126-9130
    • Hsiao, K.K.1    Groth, D.2    Scott, M.3    Yang, S.L.4    Serban, H.5
  • 50
    • 0015318003 scopus 로고
    • Scrapie: A prototype slow infection
    • Hunter GD. 1972. Scrapie: a prototype slow infection. J. Infect. Dis. 125:427-40
    • (1972) J. Infect. Dis. , vol.125 , pp. 427-440
    • Hunter, G.D.1
  • 51
    • 0034723133 scopus 로고    scopus 로고
    • A synthetic peptide initiates Gerstmann-Sträussler-Scheinker (GSS) disease in transgenic mice
    • Kaneko K, Ball HL, Wille H, Zhang H, Groth D, et al. 2000. A synthetic peptide initiates Gerstmann-Sträussler-Scheinker (GSS) disease in transgenic mice. J. Mol. Biol. 295:997-1007
    • (2000) J. Mol. Biol. , vol.295 , pp. 997-1007
    • Kaneko, K.1    Ball, H.L.2    Wille, H.3    Zhang, H.4    Groth, D.5
  • 52
    • 0026604959 scopus 로고
    • Further analysis of nucleic acids in purified scrapie prion preparations by improved return refocussing gel electrophoresis (RRGE)
    • Kellings K, Meyer N, Mirenda C, Prusiner SB, Riesner D. 1992. Further analysis of nucleic acids in purified scrapie prion preparations by improved return refocussing gel electrophoresis (RRGE). J. Gen. Virol. 73:1025-29
    • (1992) J. Gen. Virol. , vol.73 , pp. 1025-1029
    • Kellings, K.1    Meyer, N.2    Mirenda, C.3    Prusiner, S.B.4    Riesner, D.5
  • 53
    • 0020481648 scopus 로고
    • Scrapie agent: Prions or virinos?
    • Kimberlin RH. 1982. Scrapie agent: prions or virinos? Nature 297:107-8
    • (1982) Nature , vol.297 , pp. 107-108
    • Kimberlin, R.H.1
  • 54
    • 1642617641 scopus 로고    scopus 로고
    • Protein-only transmission of three yeast prion strains
    • King CY, Diaz-Avalos R. 2004. Protein-only transmission of three yeast prion strains. Nature 428:319-23
    • (2004) Nature , vol.428 , pp. 319-323
    • King, C.Y.1    Diaz-Avalos, R.2
  • 56
    • 0037447071 scopus 로고    scopus 로고
    • Abbreviated incubation times for human prions in mice expressing a chimeric mouse-human prion protein transgene
    • Korth C, Kaneko K, Groth D, Heye N, Telling G, et al. 2003. Abbreviated incubation times for human prions in mice expressing a chimeric mouse-human prion protein transgene. Proc. Natl. Acad. Sci. USA 100:4784-89
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4784-4789
    • Korth, C.1    Kaneko, K.2    Groth, D.3    Heye, N.4    Telling, G.5
  • 58
    • 33845638363 scopus 로고
    • Intestinal nucleotidase and polynucleotidase
    • Levene PA, Dillon RT. 1932. Intestinal nucleotidase and polynucleotidase. J. Biol. Chem. 96:461-77
    • (1932) J. Biol. Chem. , vol.96 , pp. 461-477
    • Levene, P.A.1    Dillon, R.T.2
  • 61
    • 0016469066 scopus 로고
    • Comparison of scrapie and transmissible mink encephalopathy in hamsters. II. Clinical signs, pathology and pathogeriesis
    • Marsh RF, Kimberlin RH. 1975. Comparison of scrapie and transmissible mink encephalopathy in hamsters. II. Clinical signs, pathology and pathogeriesis. J. Infect. Dis. 131:104-10
    • (1975) J. Infect. Dis. , vol.131 , pp. 104-110
    • Marsh, R.F.1    Kimberlin, R.H.2
  • 62
    • 0001271852 scopus 로고
    • Purification and properties of desoxyribonuclease isolated from beef pancreas
    • McCarty M. 1946. Purification and properties of desoxyribonuclease isolated from beef pancreas. J. Gen. Physiol. 29:123-39
    • (1946) J. Gen. Physiol. , vol.29 , pp. 123-139
    • McCarty, M.1
  • 64
    • 0028118813 scopus 로고
    • A retrospective look: How we identified the pneumococcal transforming substance as DNA
    • McCarty M. 1994. A retrospective look: how we identified the pneumococcal transforming substance as DNA. J. Exp. Med. 179:385-94
    • (1994) J. Exp. Med. , vol.179 , pp. 385-394
    • McCarty, M.1
  • 65
    • 84956944553 scopus 로고
    • Studies on the chemical nature of the substance inducing transformation of pneumococcal types. II. Effect of desoxyribonuclease on the biological activity of the transforming substance
    • McCarty M, Avery OT. 1946. Studies on the chemical nature of the substance inducing transformation of pneumococcal types. II. Effect of desoxyribonuclease on the biological activity of the transforming substance. J. Exp. Med. 83:89-96
    • (1946) J. Exp. Med. , vol.83 , pp. 89-96
    • McCarty, M.1    Avery, O.T.2
  • 66
    • 33845604521 scopus 로고
    • Studies on the chemical nature of the substance inducing transformation of pneumococcal types. III. An improved method for the isolation of the transforming substance and its application to pneumococcus Types II, III, and VI
    • McCarty M, Avery OT. 1946. Studies on the chemical nature of the substance inducing transformation of pneumococcal types. III. An improved method for the isolation of the transforming substance and its application to pneumococcus Types II, III, and VI. J. Exp. Med. 83:97-104
    • (1946) J. Exp. Med. , vol.83 , pp. 97-104
    • McCarty, M.1    Avery, O.T.2
  • 67
    • 0021023167 scopus 로고
    • A protease-resistant protein is a structural component of the scrapie prion
    • McKinley MP, Bolton DC, Prusiner SB. 1983. A protease-resistant protein is a structural component of the scrapie prion. Cell 35:57-62
    • (1983) Cell , vol.35 , pp. 57-62
    • McKinley, M.P.1    Bolton, D.C.2    Prusiner, S.B.3
  • 68
    • 0026062496 scopus 로고
    • Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis
    • McKinley MP, Meyer RK, Kenaga L, Rahbar F, Cotter R, et al. 1991. Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis. J. Virol. 65:1340-51
    • (1991) J. Virol. , vol.65 , pp. 1340-1351
    • McKinley, M.P.1    Meyer, R.K.2    Kenaga, L.3    Rahbar, F.4    Cotter, R.5
  • 69
    • 15844419908 scopus 로고    scopus 로고
    • High-level expression and characterization of a purified 142-residue polypeptide of the prion protein
    • Mehlhornl, Groth D, Stockel J, Moffat B, Reilly D, et al. 1996. High-level expression and characterization of a purified 142-residue polypeptide of the prion protein. Biochemistry 35:5528-37
    • (1996) Biochemistry , vol.35 , pp. 5528-5537
    • Mehlhorn, L.1    Groth, D.2    Stockel, J.3    Moffat, B.4    Reilly, D.5
  • 71
  • 72
    • 85014219951 scopus 로고
    • Chromosin, a desoxyribose nucleoprotein complex of the cell nucleus
    • Mirsky AE, Pollister AW. 1946. Chromosin, a desoxyribose nucleoprotein complex of the cell nucleus. J. Gen. Physiol. 30:117-48
    • (1946) J. Gen. Physiol. , vol.30 , pp. 117-148
    • Mirsky, A.E.1    Pollister, A.W.2
  • 73
    • 0001684042 scopus 로고
    • Variable and constant components of chromosomes
    • Mirsky AE, Ris H. 1949. Variable and constant components of chromosomes. Nature 163:666-67
    • (1949) Nature , vol.163 , pp. 666-667
    • Mirsky, A.E.1    Ris, H.2
  • 74
    • 0030854797 scopus 로고    scopus 로고
    • Molecular and genetic characterization of the capsule biosynthesis locus of Streptococcuspneumoniae type 19B
    • Morona JK, Morona R, Paton JC. 1997. Molecular and genetic characterization of the capsule biosynthesis locus of Streptococcuspneumoniae type 19B. J. Bacteriol. 179:4953-58
    • (1997) J. Bacteriol. , vol.179 , pp. 4953-4958
    • Morona, J.K.1    Morona, R.2    Paton, J.C.3
  • 75
    • 0036375067 scopus 로고    scopus 로고
    • A critical review of the nature of the spongiform encephalopathy agent: Protein theory versus virus theory
    • Narang H. 2002. A critical review of the nature of the spongiform encephalopathy agent: protein theory versus virus theory. Exp. Biol. Med. 227:4-19
    • (2002) Exp. Biol. Med. , vol.227 , pp. 4-19
    • Narang, H.1
  • 76
    • 22944447360 scopus 로고
    • Beiträge zur Variabilität der Pneumokokken
    • Neufeld F, Levinthal W. 1928. Beiträge zur Variabilität der Pneumokokken. Z. Immunitätsforsch. 55:324-40
    • (1928) Z. Immunitätsforsch. , vol.55 , pp. 324-340
    • Neufeld, F.1    Levinthal, W.2
  • 77
    • 0001358802 scopus 로고
    • RNA codewords and protein synthesis. The effect of trinucleotides upon the binding of sRNA to ribosomes
    • Nirenberg M, Leder P. 1964. RNA codewords and protein synthesis. The effect of trinucleotides upon the binding of sRNA to ribosomes. Science 145:1399-407
    • (1964) Science , vol.145 , pp. 1399-1407
    • Nirenberg, M.1    Leder, P.2
  • 79
    • 0027332116 scopus 로고
    • Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins
    • Pan KM, Baldwin M, Nguyen J, Gasset M, Serban A, et al. 1993. Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins. Proc. Natl. Acad. Sci. USA 90:10962-66
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10962-10966
    • Pan, K.M.1    Baldwin, M.2    Nguyen, J.3    Gasset, M.4    Serban, A.5
  • 80
    • 0024296125 scopus 로고
    • Fifty years with scrapie: A personal reminiscence
    • Pattison IH. 1988. Fifty years with scrapie: a personal reminiscence. Vet. Rec. 123:661-66
    • (1988) Vet. Rec. , vol.123 , pp. 661-666
    • Pattison, I.H.1
  • 81
    • 0037071874 scopus 로고    scopus 로고
    • A change in the conformation of prions accompanies the emergence of a new prion strain
    • Peretz D, Williamson RA, Legname G, Matsunaga Y, Vergara J, et al. 2002. A change in the conformation of prions accompanies the emergence of a new prion strain. Neuron 34:921-32
    • (2002) Neuron , vol.34 , pp. 921-932
    • Peretz, D.1    Williamson, R.A.2    Legname, G.3    Matsunaga, Y.4    Vergara, J.5
  • 82
    • 10744228370 scopus 로고    scopus 로고
    • Identification of competence pheromone responsive genes in Streptococcus pneumoniae by use of DNA microarrays
    • Peterson SN, Sung CK, Cline R, Desai BV, Snesrud EC, et al. 2004. Identification of competence pheromone responsive genes in Streptococcus pneumoniae by use of DNA microarrays. Mol. Microbiol. 51:1051-70
    • (2004) Mol. Microbiol. , vol.51 , pp. 1051-1070
    • Peterson, S.N.1    Sung, C.K.2    Cline, R.3    Desai, B.V.4    Snesrud, E.C.5
  • 83
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner SB. 1982. Novel proteinaceous infectious particles cause scrapie. Science 216:136-44
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 86
    • 0003661592 scopus 로고    scopus 로고
    • Prusiner SB, ed. Cold Spring Harbor: Cold Spring Harbor Lab. Press
    • 85a. Prusiner SB, ed. 2004. Prion Biology and Diseases. Cold Spring Harbor: Cold Spring Harbor Lab. Press
    • (2004) Prion Biology and Diseases
  • 89
    • 0027491308 scopus 로고
    • Ablation of the prion protein (PrP) gene in mice prevents scrapie and facilitates production of anti-PrP antibodies
    • Prusiner SB, Groth D, Serban A, Koehler R, Foster D, et al. 1993. Ablation of the prion protein (PrP) gene in mice prevents scrapie and facilitates production of anti-PrP antibodies. Proc. Natl. Acad. Sci. USA 90:10608-12
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10608-10612
    • Prusiner, S.B.1    Groth, D.2    Serban, A.3    Koehler, R.4    Foster, D.5
  • 91
    • 0021752457 scopus 로고
    • Purification and structural studies of a major scrapie prion protein
    • Prusiner SB, Groth DF, Bolton DC, Kent SB, Hood LE. 1984. Purification and structural studies of a major scrapie prion protein. Cell 38:127-34
    • (1984) Cell , vol.38 , pp. 127-134
    • Prusiner, S.B.1    Groth, D.F.2    Bolton, D.C.3    Kent, S.B.4    Hood, L.E.5
  • 92
    • 0019324430 scopus 로고
    • Molecular properties, partial purification, and assay by incubation period measurements of the hamster scrapie agent
    • Prusiner SB, Groth DF, Cochran SP, Masiarz FR, McKinley MP, Martinez HM. 1980. Molecular properties, partial purification, and assay by incubation period measurements of the hamster scrapie agent. Biochemistry 21:4883-91
    • (1980) Biochemistry , vol.21 , pp. 4883-4891
    • Prusiner, S.B.1    Groth, D.F.2    Cochran, S.P.3    Masiarz, F.R.4    McKinley, M.P.5    Martinez, H.M.6
  • 93
    • 0018188825 scopus 로고
    • Partial purification and evidence for multiple molecular forms of the scrapie agent
    • Prusiner SB, Hadlow WJ, Garfin DE, Cochran SP, Baringer JR, et al. 1978. Partial purification and evidence for multiple molecular forms of the scrapie agent. Biochemistry 17:4993-97
    • (1978) Biochemistry , vol.17 , pp. 4993-4997
    • Prusiner, S.B.1    Hadlow, W.J.2    Garfin, D.E.3    Cochran, S.P.4    Baringer, J.R.5
  • 97
    • 0025244011 scopus 로고
    • Transgenetic studies implicate interactions between homologous PrP isoforms in scrapie prion replication
    • Prusiner SB, Scott M, Foster D, Pan KM, Groth D, et al. 1990. Transgenetic studies implicate interactions between homologous PrP isoforms in scrapie prion replication. Cell 63:673-86
    • (1990) Cell , vol.63 , pp. 673-686
    • Prusiner, S.B.1    Scott, M.2    Foster, D.3    Pan, K.M.4    Groth, D.5
  • 98
    • 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, Wuthrich K. 1997. NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). FEBS Lett. 413:282-88
    • (1997) FEBS Lett. , vol.413 , pp. 282-288
    • Riek, R.1    Hornemann, S.2    Wider, G.3    Glockshuber, R.4    Wuthrich, K.5
  • 99
    • 0025836630 scopus 로고
    • The scrapie agent: "A virus by any other name"
    • Rohwer RG. 1991. The scrapie agent: "a virus by any other name". Curr. Top. Microbiol. Immunol. 172:195-232
    • (1991) Curr. Top. Microbiol. Immunol. , vol.172 , pp. 195-232
    • Rohwer, R.G.1
  • 101
    • 13144275223 scopus 로고    scopus 로고
    • Identification of a prion protein epitope modulating transmission of bovine spongiform encephalopathy prions to transgenic mice
    • Scott MR, Safar J, Telling G, Nguyen O, Groth D, et al. 1997. Identification of a prion protein epitope modulating transmission of bovine spongiform encephalopathy prions to transgenic mice. Proc. Natl. Acad. Sci. USA 94:14279-84
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14279-14284
    • Scott, M.R.1    Safar, J.2    Telling, G.3    Nguyen, O.4    Groth, D.5
  • 102
    • 0008831659 scopus 로고
    • Eine neue physikalische enteiweissungsmethode zur darstellung biologisch Wirksamen substanzen
    • Sevag MG. 1934. Eine neue physikalische Enteiweissungsmethode zur Darstellung biologisch Wirksamen Substanzen. Biochem. Z. 273:419 102.
    • (1934) Biochem. Z. , vol.273 , pp. 419102
    • Sevag, M.G.1
  • 103
    • 33845607670 scopus 로고
    • In vitro transformation of pneumococcal types. II. The nature of the factor responsible for the transformation of pneumococcal types
    • Sia RHP, Dawson MH. 1931. In vitro transformation of pneumococcal types. II. The nature of the factor responsible for the transformation of pneumococcal types. J. Exp. Med. 54:701-10
    • (1931) J. Exp. Med. , vol.54 , pp. 701-710
    • Sia, R.H.P.1    Dawson, M.H.2
  • 105
    • 0027534612 scopus 로고
    • Structural analysis of the scrapie prion protein using mass spectrometry and amino acid sequencing
    • Stahl N, Baldwin MA, Teplow DB, Hood L, Gibson BW, et al. 1993. Structural analysis of the scrapie prion protein using mass spectrometry and amino acid sequencing. Biochemistry 32:1991-2002
    • (1993) Biochemistry , vol.32 , pp. 1991-2002
    • Stahl, N.1    Baldwin, M.A.2    Teplow, D.B.3    Hood, L.4    Gibson, B.W.5
  • 106
    • 0000256952 scopus 로고
    • Isolation of a crystalline protein possessing the properties of tobacco mosaic virus
    • Stanley WM. 1935. Isolation of a crystalline protein possessing the properties of tobacco mosaic virus. Science 81:644-45
    • (1935) Science , vol.81 , pp. 644-645
    • Stanley, W.M.1
  • 107
    • 0014841864 scopus 로고
    • The "undiscovered" discovery
    • Stanley WM. 1970. The "undiscovered" discovery. Arch. Environ. Health 21:256-62
    • (1970) Arch. Environ. Health , vol.21 , pp. 256-262
    • Stanley, W.M.1
  • 108
    • 0035152345 scopus 로고    scopus 로고
    • Identification of two prion protein regions that modify scrapie incubation time
    • Supattapone S, Muramoto T, Legname G, Mehlhorn I, Cohen FE, et al. 2001. Identification of two prion protein regions that modify scrapie incubation time. J. Virol. 75:1408-13
    • (2001) J. Virol. , vol.75 , pp. 1408-1413
    • Supattapone, S.1    Muramoto, T.2    Legname, G.3    Mehlhorn, I.4    Cohen, F.E.5
  • 109
    • 0026033998 scopus 로고
    • Amyloid protein of Gerstmann-Sträussler-Scheinker disease (Indiana kindred) is an 11 kd fragment of prion protein with an N-terminal glycine at codon 58
    • Tagliavini F, Prelli F, Ghiso J, Bugiani O, Serban D, et al. 1991. Amyloid protein of Gerstmann-Sträussler-Scheinker disease (Indiana kindred) is an 11 kd fragment of prion protein with an N-terminal glycine at codon 58. EMBO J. 10:513-19
    • (1991) EMBO J. , vol.10 , pp. 513-519
    • Tagliavini, F.1    Prelli, F.2    Ghiso, J.3    Bugiani, O.4    Serban, D.5
  • 110
    • 1642633056 scopus 로고    scopus 로고
    • Conformational variations in an infectious protein determine prion strain differences
    • Tanaka M, Chien P, Naber N, Cooke R, Weissman JS. 2004. Conformational variations in an infectious protein determine prion strain differences. Nature 428:323-28
    • (2004) Nature , vol.428 , pp. 323-328
    • Tanaka, M.1    Chien, P.2    Naber, N.3    Cooke, R.4    Weissman, J.S.5
  • 111
    • 0029740354 scopus 로고    scopus 로고
    • Interactions between wild-type and mutant prion proteins modulate neurodegeneration in transgenic mice
    • Telling GC, Haga T, Torchia M, Tremblay P, DeArmond SJ, Prusiner SB. 1996. Interactions between wild-type and mutant prion proteins modulate neurodegeneration in transgenic mice. Genes Dev. 10:1736-50
    • (1996) Genes Dev. , vol.10 , pp. 1736-1750
    • Telling, G.C.1    Haga, T.2    Torchia, M.3    Tremblay, P.4    DeArmond, S.J.5    Prusiner, S.B.6
  • 112
    • 12644272790 scopus 로고    scopus 로고
    • Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity
    • Telling GC, Parchi P, DeArmond SJ, Cortelli P, Montagna P, et al. 1996. Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity. Science 274:2079-82
    • (1996) Science , vol.274 , pp. 2079-2082
    • Telling, G.C.1    Parchi, P.2    DeArmond, S.J.3    Cortelli, P.4    Montagna, P.5
  • 113
    • 0028882424 scopus 로고
    • Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein
    • Telling GC, Scott M, Mastrianni J, Gabizon R, Torchia M, et al. 1995. Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 83:79-90
    • (1995) Cell , vol.83 , pp. 79-90
    • Telling, G.C.1    Scott, M.2    Mastrianni, J.3    Gabizon, R.4    Torchia, M.5
  • 114
    • 0035919670 scopus 로고    scopus 로고
    • Complete genome sequence of a virulent isolate of Streptococcuspneumoniae
    • Tettelin H, Nelson KE, Paulsen IT, Eisen JA, Read TD, et al. 2001. Complete genome sequence of a virulent isolate of Streptococcuspneumoniae. Science 293:498-506
    • (2001) Science , vol.293 , pp. 498-506
    • Tettelin, H.1    Nelson, K.E.2    Paulsen, I.T.3    Eisen, J.A.4    Read, T.D.5
  • 116
    • 0034973230 scopus 로고    scopus 로고
    • Markedly increased susceptibility to natural sheep scrapie of transgenic mice expressing ovine PrP
    • Vilotte JL, Soulier S, Essalmani R, Stinnakre MG, Vaiman D, et al. 2001. Markedly increased susceptibility to natural sheep scrapie of transgenic mice expressing ovine PrP. J. Virol. 75:5977-84
    • (2001) J. Virol. , vol.75 , pp. 5977-5984
    • Vilotte, J.L.1    Soulier, S.2    Essalmani, R.3    Stinnakre, M.G.4    Vaiman, D.5
  • 117
    • 33749048664 scopus 로고
    • Genetical implication of the structure of deoxyribose nucleic acid
    • Watson JD, Crick FHC. 1953. Genetical implication of the structure of deoxyribose nucleic acid. Nature 171:964-67
    • (1953) Nature , vol.171 , pp. 964-967
    • Watson, J.D.1    Crick, F.H.C.2
  • 118
    • 0038497542 scopus 로고
    • A structure for deoxyribose nucleic acids
    • Watson JD, Crick FHC. 1953. A structure for deoxyribose nucleic acids. Nature 171:737-38
    • (1953) Nature , vol.171 , pp. 737-738
    • Watson, J.D.1    Crick, F.H.C.2
  • 119
    • 0025800143 scopus 로고
    • A "unified theory" of prion propagation
    • Weissmann C. 1991. A "unified theory" of prion propagation. Nature 352:679-83
    • (1991) Nature , vol.352 , pp. 679-683
    • Weissmann, C.1
  • 120
    • 0028308104 scopus 로고
    • [URE3] as an altered URE2 protein: Evidence for a prion analog in Saccharomyces cerevisiae
    • Wickner RB. 1994. [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science 264:566-69
    • (1994) Science , vol.264 , pp. 566-569
    • Wickner, R.B.1


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