메뉴 건너뛰기




Volumn 292, Issue 4, 1999, Pages 797-817

Ataxia in prion protein (PrP)-deficient mice is associated with upregulation of the novel PrP-like protein doppel

Author keywords

Ataxia; Neurodegeneration; Prion; PrP; Purkinje neuron

Indexed keywords

DOPPEL; MESSENGER RNA; PRION PROTEIN; PROTEIN; UNCLASSIFIED DRUG;

EID: 0033215478     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3108     Document Type: Article
Times cited : (477)

References (75)
  • 2
    • 0031864543 scopus 로고    scopus 로고
    • The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 1998
    • Bairoch A., Apweiler R. The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 1998. Nucl. Acids Res. 26:1998;38-42.
    • (1998) Nucl. Acids Res. , vol.26 , pp. 38-42
    • Bairoch, A.1    Apweiler, R.2
  • 3
    • 0028071564 scopus 로고
    • The SWISS-PROT protein sequence data bank: Current status
    • Bairoch A., Boeckmann B. The SWISS-PROT protein sequence data bank: current status. Nucl. Acids Res. 22:1991;3578-3580.
    • (1991) Nucl. Acids Res. , vol.22 , pp. 3578-3580
    • Bairoch, A.1    Boeckmann, B.2
  • 8
    • 0020793569 scopus 로고
    • A technique for radiolabeling DNA restriction endonuclease fragments to high specificity activity
    • Feinberg A. P., Vogelstein B. A technique for radiolabeling DNA restriction endonuclease fragments to high specificity activity. Anal. Biochem. 132:1983;6-13.
    • (1983) Anal. Biochem. , vol.132 , pp. 6-13
    • Feinberg, A.P.1    Vogelstein, B.2
  • 11
    • 0030920440 scopus 로고    scopus 로고
    • Mutational analysis of the C-terminal signal peptide of bovine liver 5′-nucleotidase for GPI anchoring: A study on the significance of the hydrophilic spacer region
    • Furukawa Y., Tsukamoto K., Ikezawa H. Mutational analysis of the C-terminal signal peptide of bovine liver 5′-nucleotidase for GPI anchoring: a study on the significance of the hydrophilic spacer region. Biochim. Biophys. Acta. 1328:1997;185-196.
    • (1997) Biochim. Biophys. Acta , vol.1328 , pp. 185-196
    • Furukawa, Y.1    Tsukamoto, K.2    Ikezawa, H.3
  • 12
    • 0344130595 scopus 로고
    • Molecular cloning and structural analysis of a candidate chicken prion protein
    • S. B. Prusiner, J. Collinge, J. Powell, & B. Anderton. London: Ellis Horwood
    • Gabriel J.-M., Oesch B., Kretzschmar H., Scott M., Prusiner S. B. Molecular cloning and structural analysis of a candidate chicken prion protein. Prusiner S. B., Collinge J., Powell J., Anderton B. Prion Diseases of Humans and Animals. 1992;407-431 Ellis Horwood, London.
    • (1992) Prion Diseases of Humans and Animals , pp. 407-431
    • Gabriel, J.-M.1    Oesch, B.2    Kretzschmar, H.3    Scott, M.4    Prusiner, S.B.5
  • 13
    • 0028926204 scopus 로고
    • Glycolipid-anchored proteins in neuroblastoma cells from detergent-resistant complexes without caveolin
    • Goordinsky A., Harris D. A. Glycolipid-anchored proteins in neuroblastoma cells from detergent-resistant complexes without caveolin. J. Cell Biol. 129:1995;619-627.
    • (1995) J. Cell Biol. , vol.129 , pp. 619-627
    • Goordinsky, A.1    Harris, D.A.2
  • 14
    • 0025823394 scopus 로고
    • A prion-like protein from chicken brain copurifies with an acetylcholine receptor-inducing activity
    • Harris D. A., Falls D. L., Johnson F. A., Fischbach G. D. A prion-like protein from chicken brain copurifies with an acetylcholine receptor-inducing activity. Proc. Natl Acad. Sci. USA. 88:1991;7664-7668.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 7664-7668
    • Harris, D.A.1    Falls, D.L.2    Johnson, F.A.3    Fischbach, G.D.4
  • 17
    • 0028793453 scopus 로고
    • Patch-clamp analysis of synaptic transmission to cerebellar purkinje cells of prion protein knockout mice
    • Herms J. W., Kretzschmar H. A., Titz S., Keller B. U. Patch-clamp analysis of synaptic transmission to cerebellar purkinje cells of prion protein knockout mice. Eur. J. Neurosci. 7:1995;2508-2512.
    • (1995) Eur. J. Neurosci , vol.7 , pp. 2508-2512
    • Herms, J.W.1    Kretzschmar, H.A.2    Titz, S.3    Keller, B.U.4
  • 18
    • 0000207681 scopus 로고
    • TMbase - A database of membrane spanning protein segments
    • Hofman K., Stoffel W. TMbase - a database of membrane spanning protein segments. Biol. Chem. Hoppe-Seyler. 374:1993;166.
    • (1993) Biol. Chem. Hoppe-Seyler , vol.374 , pp. 166
    • Hofman, K.1    Stoffel, W.2
  • 19
    • 0028883341 scopus 로고
    • Copper binding to the N-terminal tandem repeat regions of mammalian and avian prion protein
    • Hornshaw M. P., McDermott J. R., Candy J. M. Copper binding to the N-terminal tandem repeat regions of mammalian and avian prion protein. Biochem. Biophys. Res. Commun. 207:1995;621-629.
    • (1995) Biochem. Biophys. Res. Commun. , vol.207 , pp. 621-629
    • Hornshaw, M.P.1    McDermott, J.R.2    Candy, J.M.3
  • 21
    • 0025681138 scopus 로고
    • Spontaneous neurodegeneration in transgenic mice with mutant prion protein
    • Hsiao K. K., Scott M., Foster D., Groth D. F., DeArmond S. J., Prusiner S. B. Spontaneous neurodegeneration in transgenic mice with mutant prion protein. Science. 250:1990;1587-1590.
    • (1990) Science , vol.250 , pp. 1587-1590
    • Hsiao, K.K.1    Scott, M.2    Foster, D.3    Groth, D.F.4    Dearmond, S.J.5    Prusiner, S.B.6
  • 24
    • 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., Vey M., Scott M., Pilkuhn S., Cohen F. E., Prusiner S. B. COOH-terminal sequence of the cellular prion protein directs subcellular trafficking and controls conversion into the scrapie isoform. Proc. Natl Acad. Sci. USA. 94:1997a;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
  • 26
    • 0023665902 scopus 로고
    • An analysis of 5′-noncoding sequences for 699 vertebrate messenger RNAs
    • Kozak M. An analysis of 5′-noncoding sequences for 699 vertebrate messenger RNAs. Nucl. Acids Res. 15:1987;8125-8148.
    • (1987) Nucl. Acids Res. , vol.15 , pp. 8125-8148
    • Kozak, M.1
  • 27
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski R. A., MacArthur M. W., Moss D. S., Thornton J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26:1993;283-291.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 29
    • 0029913807 scopus 로고    scopus 로고
    • Evolutionary trace method defines binding surfaces common to protein families
    • Lichtarge O., Bourne H. R., Cohen F. E. Evolutionary trace method defines binding surfaces common to protein families. J. Mol. Biol. 257:1996;342-358.
    • (1996) J. Mol. Biol. , vol.257 , pp. 342-358
    • Lichtarge, O.1    Bourne, H.R.2    Cohen, F.E.3
  • 31
    • 0029916617 scopus 로고    scopus 로고
    • Mice deficient for prion protein exhibit normal neuronal excitability and synaptic transmission in the hippocampus
    • Lledo P.-M., Tremblay P., DeArmond S. J., Prusiner S. B., Nicoll R. A. Mice deficient for prion protein exhibit normal neuronal excitability and synaptic transmission in the hippocampus. Proc. Natl Acad. Sci. USA. 93:1996;2403-2407.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 2403-2407
    • Lledo, P.-M.1    Tremblay, P.2    Dearmond, S.J.3    Prusiner, S.B.4    Nicoll, R.A.5
  • 32
    • 0031030396 scopus 로고    scopus 로고
    • Characterization of a prion protein (PrP) gene from rabbit; A species with apparent resistance to infection by prions
    • Loftus B., Rogers M. Characterization of a prion protein (PrP) gene from rabbit; a species with apparent resistance to infection by prions. Gene. 184:1997;215-219.
    • (1997) Gene , vol.184 , pp. 215-219
    • Loftus, B.1    Rogers, M.2
  • 33
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Luthy R., Bowie J. U., Eisenberg D. Assessment of protein models with three-dimensional profiles. Nature. 356:1992;83-85.
    • (1992) Nature , vol.356 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 34
    • 17144434438 scopus 로고    scopus 로고
    • Cotranscription and intergenic splicing of human galactose-1-phosphate uridylyltransferase and interleukin-11 receptor alpha-chain genes generate a fusion mRNA in normal cells. Implication for the production of multidomain proteins during evolution
    • Magrangeas F., Pitiot G., Dubois S., Bragado-Nilsson E., Cherel M., Jobert S., Lebeau B., Boisteau O., Lethe B., Mallet J., Jacques Y., Minivielles S. Cotranscription and intergenic splicing of human galactose-1-phosphate uridylyltransferase and interleukin-11 receptor alpha-chain genes generate a fusion mRNA in normal cells. Implication for the production of multidomain proteins during evolution. J. Biol. Chem. 273:1998;16005-16010.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16005-16010
    • Magrangeas, F.1    Pitiot, G.2    Dubois, S.3    Bragado-Nilsson, E.4    Cherel, M.5    Jobert, S.6    Lebeau, B.7    Boisteau, O.8    Lethe, B.9    Mallet, J.10    Jacques, Y.11    Minivielles, S.12
  • 35
    • 0028420937 scopus 로고
    • 129/Ola mice carrying a null mutation in PrP that abolishes mRNA production are developmentally normal
    • Manson J. C., Clarke A. R., Hooper M. L., Aitchison L., McConnell I., Hope J. 129/Ola mice carrying a null mutation in PrP that abolishes mRNA production are developmentally normal. Mol. Neurobiol. 8:1994;121-127.
    • (1994) Mol. Neurobiol. , vol.8 , pp. 121-127
    • Manson, J.C.1    Clarke, A.R.2    Hooper, M.L.3    Aitchison, L.4    McConnell, I.5    Hope, J.6
  • 37
    • 0029092955 scopus 로고
    • Double replacement gene targeting for the production of a series of mouse strains with different prion protein gene alterations
    • Moore R. C., Redhead N. J., Selfridge J., Hope J., Manson J. C., Melton D. W. Double replacement gene targeting for the production of a series of mouse strains with different prion protein gene alterations. Biotechnology. 13:1995;999-1004.
    • (1995) Biotechnology , vol.13 , pp. 999-1004
    • Moore, R.C.1    Redhead, N.J.2    Selfridge, J.3    Hope, J.4    Manson, J.C.5    Melton, D.W.6
  • 39
    • 0026319199 scopus 로고
    • Protein folding and association - insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K. A., Honig B. Protein folding and association - insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11:1991;281-296.
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 40
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H., Engelbrecht J., Brunak S., von Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10:1997;1-6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 42
    • 0029993449 scopus 로고    scopus 로고
    • Know your neighbours: Three phenotypes in null mutants of the myogenic bHLH gene MRF4
    • Olson E. N., Arnold H. H., Rigby P. W., Wold B. J. Know your neighbours: three phenotypes in null mutants of the myogenic bHLH gene MRF4. Cell. 85:1996;1-4.
    • (1996) Cell , vol.85 , pp. 1-4
    • Olson, E.N.1    Arnold, H.H.2    Rigby, P.W.3    Wold, B.J.4
  • 43
    • 0027074458 scopus 로고
    • Purification and properties of the cellular prion protein from Syrian hamster brain
    • Pan K.-M., Stahl N., Prusiner S. B. Purification and properties of the cellular prion protein from Syrian hamster brain. Protein Sci. 1:1992;1343-1352.
    • (1992) Protein Sci. , vol.1 , pp. 1343-1352
    • Pan, K.-M.1    Stahl, N.2    Prusiner, S.B.3
  • 44
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson W. R., Lipman D. J. Improved tools for biological sequence comparison. Proc. Natl Acad. Sci. USA. 85:1988;2444-2448.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 48
    • 0025643347 scopus 로고
    • Intracellular accumulation of the cellular prion protein after mutagenesis of its Asn-linked glycosylation sites
    • Rogers M., Taraboulos A., Scott M., Groth D., Prusiner S. B. Intracellular accumulation of the cellular prion protein after mutagenesis of its Asn-linked glycosylation sites. Glycobiology. 1:1990;101-109.
    • (1990) Glycobiology , vol.1 , pp. 101-109
    • Rogers, M.1    Taraboulos, A.2    Scott, M.3    Groth, D.4    Prusiner, S.B.5
  • 49
    • 0017226461 scopus 로고
    • Familial neurological disease associated with spongiform encephalopathy
    • Rosenthal N. P., Keesey J., Carandall B., Brown W. J. Familial neurological disease associated with spongiform encephalopathy. Arch. Neurol. 33:1976;252-259.
    • (1976) Arch. Neurol. , vol.33 , pp. 252-259
    • Rosenthal, N.P.1    Keesey, J.2    Carandall, B.3    Brown, W.J.4
  • 50
    • 0028820122 scopus 로고
    • Accumulation of proteinase K-resistant prion protein (PrP) is restricted by the expression level of normal PrP in mice inoculated with a mouse-adapted strain of the Creutzfeldt-Jakob disease agent
    • Sakaguchi S., Katamine S., Shigematus K., Nakatani A., Moriuchi R., Nishida N., Kurokawa K., Nakaoke R., Sato H., Jishage K., Kuno J., Noda T., Miyamoto T. Accumulation of proteinase K-resistant prion protein (PrP) is restricted by the expression level of normal PrP in mice inoculated with a mouse-adapted strain of the Creutzfeldt-Jakob disease agent. J. Virol. 69:1995;7586-7592.
    • (1995) J. Virol. , vol.69 , pp. 7586-7592
    • Sakaguchi, S.1    Katamine, S.2    Shigematus, K.3    Nakatani, A.4    Moriuchi, R.5    Nishida, N.6    Kurokawa, K.7    Nakaoke, R.8    Sato, H.9    Jishage, K.10    Kuno, J.11    Noda, T.12    Miyamoto, T.13
  • 52
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A., Blundell T. L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234:1993;779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 55
    • 0027086835 scopus 로고
    • Chimeric prion protein expression in cultured cells and transgenic mice
    • Scott M. R., Köhler R., Foster D., Prusiner S. B. Chimeric prion protein expression in cultured cells and transgenic mice. Protein Sci. 1:1992;986-997.
    • (1992) Protein Sci. , vol.1 , pp. 986-997
    • Scott, M.R.1    Köhler, R.2    Foster, D.3    Prusiner, S.B.4
  • 57
    • 0023663071 scopus 로고
    • Scrapie prion protein contains a phosphatidylinositol glycolipid
    • Stahl N., Borchelt D. R., Hsiao K., Prusiner S. B. Scrapie prion protein contains a phosphatidylinositol glycolipid. Cell. 51:1987;229-240.
    • (1987) Cell , vol.51 , pp. 229-240
    • Stahl, N.1    Borchelt, D.R.2    Hsiao, K.3    Prusiner, S.B.4
  • 60
    • 0024671191 scopus 로고
    • The saga of IMAC and MIT
    • Sulkowski E. The saga of IMAC and MIT. Bioessays. 10:1989;170-175.
    • (1989) Bioessays , vol.10 , pp. 170-175
    • Sulkowski, E.1
  • 61
    • 0028966735 scopus 로고
    • Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibits formation of the scrapie isoform
    • Taraboulos A., Scott M., Semenov A., Avrahami D., Laszlo L., Prusiner S. B. Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibits formation of the scrapie isoform. J. Cell Biol. 129:1995;121-132.
    • (1995) J. Cell Biol. , vol.129 , pp. 121-132
    • Taraboulos, A.1    Scott, M.2    Semenov, A.3    Avrahami, D.4    Laszlo, L.5    Prusiner, S.B.6
  • 62
    • 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., Scott M., Mastrianni J., Gabizon R., Torchia M., Cohen F. E., DeArmond S. J., Prusiner S. B. Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell. 83:1995;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
  • 63
    • 0029740354 scopus 로고    scopus 로고
    • Interactions between wild-type and mutant prion proteins modulate neurodegeneration in transgenic mice
    • Telling G. C., Haga T., Torchia M., Tremblay P., DeArmond S. J., Prusiner S. B. Interactions between wild-type and mutant prion proteins modulate neurodegeneration in transgenic mice. Genes Dev. 10:1996;1736-1750.
    • (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
  • 66
    • 0026351408 scopus 로고
    • Locating protein-coding regions in human DNA sequences by a multiple sensor-neural network approach
    • Uberbacher E. C., Mural R. J. Locating protein-coding regions in human DNA sequences by a multiple sensor-neural network approach. Proc. Natl Acad. Sci. USA. 88:1991;11261-11265.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 11261-11265
    • Uberbacher, E.C.1    Mural, R.J.2
  • 68
    • 0033515029 scopus 로고    scopus 로고
    • Copper binding to the prion protein: Structural implications of four identical cooperative binding sites
    • Viles J. H., Cohen F. E., Prusiner S. B., Goodin D. B., Wright P. E., Dyson H. J. Copper binding to the prion protein: structural implications of four identical cooperative binding sites. Proc. Natl Acad. Sci. USA. 96:1999;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
  • 69
    • 0026716643 scopus 로고
    • Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule
    • von Heijne G. Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule. J. Mol. Biol. 225:1992;487-494.
    • (1992) J. Mol. Biol. , vol.225 , pp. 487-494
    • Von Heijne, G.1
  • 70
    • 0022642301 scopus 로고
    • Conservation of the cellular gene encoding the scrapie prion protein
    • Westaway D., Prusiner S. B. Conservation of the cellular gene encoding the scrapie prion protein. Nucl. Acids Res. 14:1986;2035-2044.
    • (1986) Nucl. Acids Res. , vol.14 , pp. 2035-2044
    • Westaway, D.1    Prusiner, S.B.2
  • 74
    • 0028052363 scopus 로고
    • Degeneration of skeletal muscle, peripheral nerves, and the central nervous system in transgenic mice overexpressing wild-type prion proteins
    • Westaway D., DeArmond S. J., Catetano-Canlas J., Groth D., Foster D., Yang S.-L., Torchia M., Carlson G. A., Prusiner S. B. Degeneration of skeletal muscle, peripheral nerves, and the central nervous system in transgenic mice overexpressing wild-type prion proteins. Cell. 76:1994b;117-129.
    • (1994) Cell , vol.76 , pp. 117-129
    • Westaway, D.1    Dearmond, S.J.2    Catetano-Canlas, J.3    Groth, D.4    Foster, D.5    Yang, S.-L.6    Torchia, M.7    Carlson, G.A.8    Prusiner, S.B.9
  • 75
    • 0028867956 scopus 로고
    • Preferred sites of glycosylphosphatidylinositol modification in folate receptors and constraints in the primary structure of the hydrophobic portion of the signal
    • Yan W., Ratnam M. Preferred sites of glycosylphosphatidylinositol modification in folate receptors and constraints in the primary structure of the hydrophobic portion of the signal. Biochemistry. 34:1995;14594-14600.
    • (1995) Biochemistry , vol.34 , pp. 14594-14600
    • Yan, W.1    Ratnam, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.