메뉴 건너뛰기




Volumn 74, Issue 9, 2000, Pages 4351-4360

Dominant-negative inhibition of prion formation diminished by deletion mutagenesis of the prion protein

Author keywords

[No Author keywords available]

Indexed keywords

PRION PROTEIN;

EID: 0033999341     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.74.9.4351-4360.2000     Document Type: Article
Times cited : (88)

References (65)
  • 2
    • 0028043661 scopus 로고
    • Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy
    • Bessen, R. A., and R. F. Marsh. 1994. Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy. J. Virol. 68:7859-7868.
    • (1994) J. Virol. , vol.68 , pp. 7859-7868
    • Bessen, R.A.1    Marsh, R.F.2
  • 3
    • 0025304678 scopus 로고
    • Scrapie and cellular prion proteins differ in their kinetics of synthesis and topology in cultured cells
    • Borchelt, D. R., M. Scott, A. Taraboulos, N. Stahl, and S. B. Prusiner. 1990. Scrapie and cellular prion proteins differ in their kinetics of synthesis and topology in cultured cells. J. Cell Biol. 110:743-752.
    • (1990) J. Cell Biol. , vol.110 , pp. 743-752
    • Borchelt, D.R.1    Scott, M.2    Taraboulos, A.3    Stahl, N.4    Prusiner, S.B.5
  • 5
    • 0024366602 scopus 로고
    • Precise targeting of the pathology of the sialoglycoprotein, PrP, and vacuolar degeneration in mouse scrapie
    • Bruce, M. E., P. A. McBride, and C. F. Farquhar. 1989. Precise targeting of the pathology of the sialoglycoprotein, PrP, and vacuolar degeneration in mouse scrapie. Neurosci. Lett. 102:1-6.
    • (1989) Neurosci. Lett. , vol.102 , pp. 1-6
    • Bruce, M.E.1    McBride, P.A.2    Farquhar, C.F.3
  • 8
    • 0025991466 scopus 로고
    • The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive
    • Caughey, B., and G. J. Raymond, 1991. The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive. J. Biol. Chem. 266:18217-18223.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18217-18223
    • Caughey, B.1    Raymond, G.J.2
  • 9
    • 0031711595 scopus 로고    scopus 로고
    • Pathologic conformations of prion proteins
    • Cohen, F. E., and S. B. Prusiner. 1998. Pathologic conformations of prion proteins. Annu. Rev. Biochem. 67:793-819.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 793-819
    • Cohen, F.E.1    Prusiner, S.B.2
  • 15
    • 0028926204 scopus 로고
    • Glycolipid-anchored proteins in neuroblastoma cells form detergent-resistant complexes without caveolin
    • Gorodinsky, A., and D. A. Harris. 1995. Glycolipid-anchored proteins in neuroblastoma cells form detergent-resistant complexes without caveolin. J. Cell Biol. 129:619-627.
    • (1995) J. Cell Biol. , vol.129 , pp. 619-627
    • Gorodinsky, A.1    Harris, D.A.2
  • 17
    • 0025272049 scopus 로고
    • Lipofection of cDNAs in the embryonic vertebrate central nervous system
    • Holt, C. E., N. Garlick, and E. Cornel. 1990. Lipofection of cDNAs in the embryonic vertebrate central nervous system. Neuron 4:203-214.
    • (1990) Neuron , vol.4 , pp. 203-214
    • Holt, C.E.1    Garlick, N.2    Cornel, E.3
  • 18
    • 0030572627 scopus 로고    scopus 로고
    • Autonomous and reversible folding of a soluble amino-terminally truncated segment of the mouse prion protein
    • Hornemann, S., and R Glockshuber. 1996. Autonomous and reversible folding of a soluble amino-terminally truncated segment of the mouse prion protein. J. Mol. Biol. 262:614-619.
    • (1996) J. Mol. Biol. , vol.262 , pp. 614-619
    • Hornemann, S.1    Glockshuber, R.2
  • 19
    • 0028844207 scopus 로고
    • Copper binding to the N-terminal tandem repeat region of mammalian and avian prion protein: Structural studies using synthetic peptides
    • Hornshaw, M. P., J. R. McDermott, J. M. Candy, and J. H. Lakey. 1995. Copper binding to the N-terminal tandem repeat region of mammalian and avian prion protein: structural studies using synthetic peptides. Biochem. Biophys. Res. Commun. 214:993-999.
    • (1995) Biochem. Biophys. Res. Commun. , vol.214 , pp. 993-999
    • Hornshaw, M.P.1    McDermott, J.R.2    Candy, J.M.3    Lakey, J.H.4
  • 21
    • 0031576748 scopus 로고    scopus 로고
    • Association between natural scrapie and PrP genotype in a flock of Suffolk sheep in Scotland
    • Hunter, N., L. Moore, B. D. Hosie, W. S. Dingwall, and A. Greig. 1997. Association between natural scrapie and PrP genotype in a flock of Suffolk sheep in Scotland. Vet. Rec. 140:59-63.
    • (1997) Vet. Rec. , vol.140 , pp. 59-63
    • Hunter, N.1    Moore, L.2    Hosie, B.D.3    Dingwall, W.S.4    Greig, A.5
  • 23
    • 0030964917 scopus 로고    scopus 로고
    • COOH-terminal sequence of the cellular prion protein directs subcellular trafficking and controls conversion into the scrapie isoform
    • Kaneko, K., M. Vey, M. Scott, S. Pilkuhn, F. E. Cohen, and S. B. Prusiner. 1997. COOH-terminal sequence of the cellular prion protein directs subcellular trafficking and controls conversion into the scrapie isoform. Proc. Natl. Acad. Sci. USA 94:2333-2338.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2333-2338
    • Kaneko, K.1    Vey, M.2    Scott, M.3    Pilkuhn, S.4    Cohen, F.E.5    Prusiner, S.B.6
  • 25
    • 0025874253 scopus 로고
    • Expression of a constitutively activated mutant of the β-isozyme of protein kinase C in cardiac myocytes stimulates the promoter of the β-myosin heavy chain isogene
    • Kariya, K., L. R. Karns, and P. C. Simpson. 1991. Expression of a constitutively activated mutant of the β-isozyme of protein kinase C in cardiac myocytes stimulates the promoter of the β-myosin heavy chain isogene. J. Biol. Chem. 266:10023-10026.
    • (1991) J. Biol. Chem. , vol.266 , pp. 10023-10026
    • Kariya, K.1    Karns, L.R.2    Simpson, P.C.3
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 0030480271 scopus 로고    scopus 로고
    • Recombinant scrapie-like prion protein of 106 amino acids is soluble
    • Muramoto, T., M. Scott, F. E. Cohen, and S. B. Prusiner. 1996. Recombinant scrapie-like prion protein of 106 amino acids is soluble. Proc. Natl. Acad. Sci. USA 93:15457-15462.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 15457-15462
    • Muramoto, T.1    Scott, M.2    Cohen, F.E.3    Prusiner, S.B.4
  • 30
    • 0030894380 scopus 로고    scopus 로고
    • Characterization of detergent-insoluble complexes containing the cellular prion protein and its scrapie isoform
    • Naslavsky, N., R. Stein, A. Yanai, G. Friedlander, and A. Taraboulos. 1997. Characterization of detergent-insoluble complexes containing the cellular prion protein and its scrapie isoform. J. Biol. Chem. 272:6324-6331.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6324-6331
    • Naslavsky, N.1    Stein, R.2    Yanai, A.3    Friedlander, G.4    Taraboulos, A.5
  • 31
    • 0025297921 scopus 로고
    • Identification of cellular proteins binding to the scrapie prion protein
    • Oesch, B., D. B. Teplow, N. Stahl, D. Serban, L. E. Hood, and S. B. Prusiner. 1990. Identification of cellular proteins binding to the scrapie prion protein. Biochemistry 29:5848-5855.
    • (1990) Biochemistry , vol.29 , pp. 5848-5855
    • Oesch, B.1    Teplow, D.B.2    Stahl, N.3    Serban, D.4    Hood, L.E.5    Prusiner, S.B.6
  • 33
    • 0027074458 scopus 로고
    • Purification and properties of the cellular prion protein from Syrian hamster brain
    • Pan, K.-M., N. Stahl, and S. B. Prusiner. 1992. Purification and properties of the cellular prion protein from Syrian hamster brain. Protein Sci. 1:1343-1352.
    • (1992) Protein Sci. , vol.1 , pp. 1343-1352
    • Pan, K.-M.1    Stahl, N.2    Prusiner, S.B.3
  • 35
    • 0032496218 scopus 로고    scopus 로고
    • Abnormal properties of prion protein with insertional mutations in different cell types
    • Priola, S. A., and B. Chesebro. 1998. Abnormal properties of prion protein with insertional mutations in different cell types. J. Biol. Chem. 273:11980-11985.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11980-11985
    • Priola, S.A.1    Chesebro, B.2
  • 36
    • 0024634456 scopus 로고
    • Creutzfeldt-Jakob disease and scrapie prions
    • Prusiner, S. B. 1989. Creutzfeldt-Jakob disease and scrapie prions. Alzheimer Dis. Assoc. Disord. 3:52-78.
    • (1989) Alzheimer Dis. Assoc. Disord. , vol.3 , pp. 52-78
    • Prusiner, S.B.1
  • 37
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • Prusiner, S. B. 1991. Molecular biology of prion diseases. Science 252:1515-1522.
    • (1991) Science , vol.252 , pp. 1515-1522
    • Prusiner, S.B.1
  • 38
    • 0021752457 scopus 로고
    • Purification and structural studies of a major scrapie prion protein
    • Prusiner, S. B., D. F. D. C. Bolton, S. B. Kent, and L. E. Hood. 1984. Purification and structural studies of a major scrapie prion protein. Cell 38:127-134.
    • (1984) Cell , vol.38 , pp. 127-134
    • Prusiner, S.B.1    Bolton, D.F.D.C.2    Kent, S.B.3    Hood, L.E.4
  • 41
    • 0033616564 scopus 로고    scopus 로고
    • Ectopic expression of prion protein (PrP) in T lymphocytes or hepatocytes of PrP knockout mice is insufficient to sustain prion replication
    • Raeber, A. J., A. Sailer, I. Hegyi, M. A. Klein, T. Rulike, M. Fischer, S. Brandner, A. Aguzzi, and C. Weissmann. 1999. Ectopic expression of prion protein (PrP) in T lymphocytes or hepatocytes of PrP knockout mice is insufficient to sustain prion replication. Proc. Natl. Acad. Sci. USA 96:3987-3992.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3987-3992
    • Raeber, A.J.1    Sailer, A.2    Hegyi, I.3    Klein, M.A.4    Rulike, T.5    Fischer, M.6    Brandner, S.7    Aguzzi, A.8    Weissmann, C.9
  • 42
    • 0022595656 scopus 로고
    • Transmissible and non-transmissible neurodegenerative disease: Similarities in age of onset and genetics in relation to aetiology
    • Ridley, R. M., H. F. Baker, and T. J. Crow. 1986. Transmissible and non-transmissible neurodegenerative disease: similarities in age of onset and genetics in relation to aetiology. Psychol. Med. 16:199-207.
    • (1986) Psychol. Med. , vol.16 , pp. 199-207
    • Ridley, R.M.1    Baker, H.F.2    Crow, T.J.3
  • 43
    • 0031436335 scopus 로고    scopus 로고
    • The human 37-kDa laminin receptor precursor interacts with the prion protein in eukaryotic cells
    • Rieger, R., F. Edenhofer, C. I. Lasmézas, and S. Weiss. 1997. The human 37-kDa laminin receptor precursor interacts with the prion protein in eukaryotic cells. Nat. Med. 3:1383-1388.
    • (1997) Nat. Med. , vol.3 , pp. 1383-1388
    • Rieger, R.1    Edenhofer, F.2    Lasmézas, C.I.3    Weiss, S.4
  • 45
    • 0025837194 scopus 로고
    • Epitope mapping of the Syrian hamster prion protein utilizing chimeric and mutant genes in a vaccinia virus expression system
    • Rogers, M., D. Serban, T. Gyuris, M. Scott, T. Torchia, and S. B. Prusiner. 1991. Epitope mapping of the Syrian hamster prion protein utilizing chimeric and mutant genes in a vaccinia virus expression system. J. Immunol. 147: 3568-3574.
    • (1991) J. Immunol. , vol.147 , pp. 3568-3574
    • Rogers, M.1    Serban, D.2    Gyuris, T.3    Scott, M.4    Torchia, T.5    Prusiner, S.B.6
  • 46
    • 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
  • 49
    • 0027086835 scopus 로고
    • Chimeric prion protein expression in cultured cells and transgenic mice
    • Scott, M. R., R. Köhler, D. Foster, and S. B. Prusiner. 1992. Chimeric prion protein expression in cultured cells and transgenic mice. Protein Sci. 1:986-997.
    • (1992) Protein Sci. , vol.1 , pp. 986-997
    • Scott, M.R.1    Köhler, R.2    Foster, D.3    Prusiner, S.B.4
  • 50
    • 0025103308 scopus 로고
    • Rapid detection of Creutzfeldt-Jakob disease and scrapie prion proteins
    • Serban, D., A. Taraboulos, S. J. DeArmond, and S. B. Prusiner. 1990. Rapid detection of Creutzfeldt-Jakob disease and scrapie prion proteins. Neurology 40:110-117.
    • (1990) Neurology , vol.40 , pp. 110-117
    • Serban, D.1    Taraboulos, A.2    DeArmond, S.J.3    Prusiner, S.B.4
  • 51
    • 0031842845 scopus 로고    scopus 로고
    • Codon 219 Lys allele of PRNP is not found in sporadic Creutzfeldt-Jakob disease
    • Shibuya, S., J. Higuchi, R.-W. Shin, J. Tateishi, and T. Kitamoto. 1998. Codon 219 Lys allele of PRNP is not found in sporadic Creutzfeldt-Jakob disease. Ann. Neurol. 43:826-828.
    • (1998) Ann. Neurol. , vol.43 , pp. 826-828
    • Shibuya, S.1    Higuchi, J.2    Shin, R.-W.3    Tateishi, J.4    Kitamoto, T.5
  • 52
    • 0345698661 scopus 로고    scopus 로고
    • Protective prion protein polymorphisms against sporadic Creutzfeldt-Jakob disease
    • Shibuya, S., J. Higuchi, R.-W. Shin, J. Tateishi, and T. Kitamoto. 1998. Protective prion protein polymorphisms against sporadic Creutzfeldt-Jakob disease. Lancet 351:419.
    • (1998) Lancet , vol.351 , pp. 419
    • Shibuya, S.1    Higuchi, J.2    Shin, R.-W.3    Tateishi, J.4    Kitamoto, T.5
  • 55
    • 0024671191 scopus 로고
    • The saga of IMAC and MIT
    • Sulkowski, E. 1989. The saga of IMAC and MIT. Bioessays 10:170-175.
    • (1989) Bioessays , vol.10 , pp. 170-175
    • Sulkowski, E.1
  • 57
    • 0028966735 scopus 로고
    • Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibits formation of the scrapie isoform
    • Taraboulos, A., M. Scott, A. Semenov, D. Avrahami, L. Laszio, and S. B. Prusiner. 1995. Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibits formation of the scrapie isoform. J. Cell Biol. 129:121-132.
    • (1995) J. Cell Biol. , vol.129 , pp. 121-132
    • Taraboulos, A.1    Scott, M.2    Semenov, A.3    Avrahami, D.4    Laszio, L.5    Prusiner, S.B.6
  • 59
    • 0028882424 scopus 로고
    • Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein
    • Telling, G. C., M. Scott, J. Mastrianni, R. Gabizon, M. Torchia, F. E. Cohen, S. J. DeArmond, and S. B. Prusiner. 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    Cohen, F.E.6    DeArmond, S.J.7    Prusiner, S.B.8
  • 61
    • 0033515029 scopus 로고    scopus 로고
    • Copper binding to the prion protein: Structural implications of four identical cooperative binding sites
    • Viles, J. H., F. E. Cohen, S. B. Prusiner, D. B. Goodin, P. E. Wright, and H. J. Dyson. 1999, Copper binding to the prion protein: structural implications of four identical cooperative binding sites. Proc. Natl. Acad. Sci. USA 96:2042-2047.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 2042-2047
    • Viles, J.H.1    Cohen, F.E.2    Prusiner, S.B.3    Goodin, D.B.4    Wright, P.E.5    Dyson, H.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.