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Volumn 281, Issue 1, 2002, Pages 1-8

The physiological functions of prion protein

Author keywords

Cellular prion protein; Interacting proteins; Pathological isoform; Physiological functions; Signal transduction cascades

Indexed keywords

ADENOSINE TRIPHOSPHATASE; AMYLOID BETA PROTEIN; COPPER; COPPER ZINC SUPEROXIDE DISMUTASE; ISOPROTEIN; PRION PROTEIN; PROTEIN PRECURSOR;

EID: 0036440530     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.2002.5655     Document Type: Article
Times cited : (25)

References (104)
  • 1
    • 0027421540 scopus 로고
    • Genetic and infectious prion diseases
    • Prusiner, S. B. (1993). Genetic and infectious prion diseases. Arch. Neurol. 50, 1129-1153.
    • (1993) Arch. Neurol. , vol.50 , pp. 1129-1153
    • Prusiner, S.B.1
  • 3
    • 0036213357 scopus 로고    scopus 로고
    • Prion diseases: Epidemiology in man
    • Pedersen, N. S., and Smith, E. (2002). Prion diseases: Epidemiology in man. APMIS 110, 14-22.
    • (2002) APMIS , vol.110 , pp. 14-22
    • Pedersen, N.S.1    Smith, E.2
  • 5
    • 0034856144 scopus 로고    scopus 로고
    • Gerstmann-Straussler-Scheinker syndrome, fatal familial insomnia, and kuru: A review of these less common human transmissible spongiform encephalopathies
    • Collins, S., McLean, C. A., and Masters, C. L. (2001). Gerstmann-Straussler-Scheinker syndrome, fatal familial insomnia, and kuru: A review of these less common human transmissible spongiform encephalopathies. J. Clin. Neurosci. 8, 387-397.
    • (2001) J. Clin. Neurosci. , vol.8 , pp. 387-397
    • Collins, S.1    McLean, C.A.2    Masters, C.L.3
  • 7
    • 0020490156 scopus 로고
    • Identification of a protein that purifies with the scrapie prion
    • Bolton, D. C., McKinley, M. P., and Prusiner, S. B. (1982). Identification of a protein that purifies with the scrapie prion. Science 218, 1309-1311.
    • (1982) Science , vol.218 , pp. 1309-1311
    • Bolton, D.C.1    McKinley, M.P.2    Prusiner, S.B.3
  • 8
    • 0021752457 scopus 로고
    • Purification and structural studies of a major scrapie prion protein
    • Prusiner, S. B., Groth, D. F., Bolton, D. C., Kent, S. B., and Hood, L. E. (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    Groth, D.F.2    Bolton, D.C.3    Kent, S.B.4    Hood, L.E.5
  • 9
  • 10
    • 0033983771 scopus 로고    scopus 로고
    • Prion diseases, blood and the immune system: Concerns and reality
    • Aguzzi, A. (2000). Prion diseases, blood and the immune system: Concerns and reality. Haematologica 85, 3-10.
    • (2000) Haematologica , vol.85 , pp. 3-10
    • Aguzzi, A.1
  • 12
    • 0026696176 scopus 로고
    • Presence of prion protein in peripheral tissues of Libyan Jews with Creutzfeldt-Jakob disease
    • Meiner, Z., Halimi, M., Polakiewicz, R. D., Prusiner, S. B., and Gabizon, R. (1992). Presence of prion protein in peripheral tissues of Libyan Jews with Creutzfeldt-Jakob disease. Neurology 42, 1355-1360.
    • (1992) Neurology , vol.42 , pp. 1355-1360
    • Meiner, Z.1    Halimi, M.2    Polakiewicz, R.D.3    Prusiner, S.B.4    Gabizon, R.5
  • 13
    • 0028047285 scopus 로고
    • Insights into the role of the immune system in prion diseases
    • Berg, L. J. (1994). Insights into the role of the immune system in prion diseases. Proc. Natl. Acad. Sci. USA 91, 429-432.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 429-432
    • Berg, L.J.1
  • 14
    • 0036267207 scopus 로고    scopus 로고
    • Atypical inflammation in the central nervous system in prion disease
    • Perry, V. H., Cunningham, C., and Boche, D. (2002). Atypical inflammation in the central nervous system in prion disease. Curr. Opin. Neurol. 15, 349-354.
    • (2002) Curr. Opin. Neurol. , vol.15 , pp. 349-354
    • Perry, V.H.1    Cunningham, C.2    Boche, D.3
  • 15
    • 0028143841 scopus 로고
    • Mouse cortical cells lacking cellular PrP survive in culture with a neurotoxic PrP fragment
    • Brown, D. R., Herms, J., and Kretzschmar, H. A. (1994). Mouse cortical cells lacking cellular PrP survive in culture with a neurotoxic PrP fragment. Neuroreport 5, 2057-2060.
    • (1994) Neuroreport , vol.5 , pp. 2057-2060
    • Brown, D.R.1    Herms, J.2    Kretzschmar, H.A.3
  • 20
    • 0023663071 scopus 로고
    • Scrapie prion protein contains a phosphatidylinositol glycolipid
    • Stahl, N., Borchelt, D. R., Hsiao, K., and Prusiner, S. B. (1987). Scrapie prion protein contains a phosphatidylinositol glycolipid. Cell 51, 229-240.
    • (1987) Cell , vol.51 , pp. 229-240
    • Stahl, N.1    Borchelt, D.R.2    Hsiao, K.3    Prusiner, S.B.4
  • 22
    • 0026780714 scopus 로고
    • Glycosylinositol phospholipid anchors of the scrapie and cellular prion proteins contain sialic acid
    • Stahl, N., Baldwin, M. A., Hecker, R., Pan, K. M., Burlingame, A. L., and Prusiner, S. B. (1992). Glycosylinositol phospholipid anchors of the scrapie and cellular prion proteins contain sialic acid. Biochemistry 31, 5043-5053.
    • (1992) Biochemistry , vol.31 , pp. 5043-5053
    • Stahl, N.1    Baldwin, M.A.2    Hecker, R.3    Pan, K.M.4    Burlingame, A.L.5    Prusiner, S.B.6
  • 24
    • 0024545093 scopus 로고
    • Prion protein biosynthesis in scrapie-infected and uninfected neuroblastoma cells
    • Caughey, B., Race, R. E., Ernst, D., Buchmeier, M. J., and Chesebro, B. (1989). Prion protein biosynthesis in scrapie-infected and uninfected neuroblastoma cells. J. Virol. 63, 175-181.
    • (1989) J. Virol. , vol.63 , pp. 175-181
    • Caughey, B.1    Race, R.E.2    Ernst, D.3    Buchmeier, M.J.4    Chesebro, B.5
  • 26
    • 0035865271 scopus 로고    scopus 로고
    • Membrane topology influences N-glycosylation of the prion protein
    • Walmsley, A. R., Zeng, F., and Hooper, N. M. (2001). Membrane topology influences N-glycosylation of the prion protein. EMBO J. 20, 703-712.
    • (2001) EMBO J. , vol.20 , pp. 703-712
    • Walmsley, A.R.1    Zeng, F.2    Hooper, N.M.3
  • 27
    • 0027520888 scopus 로고
    • Conversion of truncated and elongated prion proteins into the scrapie isoform in cultured cells
    • Rogers, M., Yehiely, F., Scott, M., and Prusiner, S. B. (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
  • 29
    • 0025746722 scopus 로고
    • Prions and prion proteins
    • Stahl, N., and Prusiner, S. B. (1991). Prions and prion proteins. FASEB J. 5, 2799-2807.
    • (1991) FASEB J. , vol.5 , pp. 2799-2807
    • Stahl, N.1    Prusiner, S.B.2
  • 31
    • 0035836694 scopus 로고    scopus 로고
    • A role for intermolecular disulfide bonds in prion diseases?
    • Welker, E., Wedemeyer, W. J., and Scheraga, H. A. (2001). A role for intermolecular disulfide bonds in prion diseases? Proc. Natl. Acad. Sci. USA 98, 4334-4336.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4334-4336
    • Welker, E.1    Wedemeyer, W.J.2    Scheraga, H.A.3
  • 32
    • 0011735173 scopus 로고    scopus 로고
    • Intramolecular versus intermolecular disulfide bonds in prion proteins
    • Welker, E., Raymond, L. D., Scheraga, H. A., and Caughey, B. (2002). Intramolecular versus intermolecular disulfide bonds in prion proteins. J. Biol. Chem. 24, 24.
    • (2002) J. Biol. Chem. , vol.24 , pp. 24
    • Welker, E.1    Raymond, L.D.2    Scheraga, H.A.3    Caughey, B.4
  • 38
    • 0030579560 scopus 로고    scopus 로고
    • Prionics or the kinetic basis of prion diseases
    • Eigen, M. (1996). Prionics or the kinetic basis of prion diseases. Biophys. Chem. 63, A1-18.
    • (1996) Biophys. Chem. , vol.63
    • Eigen, M.1
  • 39
    • 0025087141 scopus 로고
    • Acquisition of protease resistance by prion proteins in scrapie- infected cells does not require asparagine-linked glycosylation
    • Taraboulos, A., Rogers, M., Borchelt, D. R., McKinley, M. P., Scott, M., Serban, D., and Prusiner, S. B. (1990). Acquisition of protease resistance by prion proteins in scrapie- infected cells does not require asparagine-linked glycosylation. Proc. Natl. Acad. Sci. USA 87, 8262-8266.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8262-8266
    • Taraboulos, A.1    Rogers, M.2    Borchelt, D.R.3    McKinley, M.P.4    Scott, M.5    Serban, D.6    Prusiner, S.B.7
  • 40
    • 0030799062 scopus 로고    scopus 로고
    • Blockade of glycosylation promotes acquisition of scrapie-like properties by the prion protein in cultured cells
    • Lehmann, S., and Harris, D. A. (1997). Blockade of glycosylation promotes acquisition of scrapie-like properties by the prion protein in cultured cells. J. Biol. Chem. 272, 21479-21487.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21479-21487
    • Lehmann, S.1    Harris, D.A.2
  • 41
    • 0028240984 scopus 로고
    • Properties of the scrapie prion protein: Quantitative analysis of protease resistance
    • Oesch, B., Jensen, M., Nilsson, P., and Fogh, J. (1994). Properties of the scrapie prion protein: Quantitative analysis of protease resistance. Biochemistry 33, 5926-5931.
    • (1994) Biochemistry , vol.33 , pp. 5926-5931
    • Oesch, B.1    Jensen, M.2    Nilsson, P.3    Fogh, J.4
  • 43
    • 0032802332 scopus 로고    scopus 로고
    • Cellular biology of prion diseases
    • Harris, D. A. (1999). Cellular biology of prion diseases. Clin. Microbiol. Rev. 12, 429-444.
    • (1999) Clin. Microbiol. Rev. , vol.12 , pp. 429-444
    • Harris, D.A.1
  • 44
    • 0011735402 scopus 로고    scopus 로고
    • Filipin prevents pathological prion protein accumulation by reducing endocytosis and inducing cellular PrP release
    • Marella, M., Lehmann, S., Grassi, J., and Chabry, J. (2002). Filipin prevents pathological prion protein accumulation by reducing endocytosis and inducing cellular PrP release. J. Biol. Chem. 6, 6.
    • (2002) J. Biol. Chem. , vol.6 , pp. 6
    • Marella, M.1    Lehmann, S.2    Grassi, J.3    Chabry, J.4
  • 45
    • 0028966735 scopus 로고
    • Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibit formation of the scrapie isoform
    • Taraboulos, A., Scott, M., Semenov, A., Avrahami, D., Laszlo, L., Prusiner, S. B., and Avraham, D. (1995). Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibit 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    Laszlo, L.5    Prusiner, S.B.6    Avraham, D.7
  • 48
    • 0031047646 scopus 로고    scopus 로고
    • Sleep and sleep regulation in normal and prion protein-deficient mice
    • Tobler, I., Deboer, T., and Fischer, M. (1997). Sleep and sleep regulation in normal and prion protein-deficient mice. J. Neurosci. 17, 1869-1879.
    • (1997) J. Neurosci. , vol.17 , pp. 1869-1879
    • Tobler, I.1    Deboer, T.2    Fischer, M.3
  • 50
    • 0029971378 scopus 로고    scopus 로고
    • Hippocampal slices from prion protein null mice: Disrupted Ca(2+)- activated K+ currents
    • Colling, S. B., Collinge, J., and Jefferys, J. G. (1996). Hippocampal slices from prion protein null mice: Disrupted Ca(2+)- activated K+ currents. Neurosci. Lett. 209, 49-52.
    • (1996) Neurosci. Lett. , vol.209 , pp. 49-52
    • Colling, S.B.1    Collinge, J.2    Jefferys, J.G.3
  • 52
    • 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., Sailer, A., Hegyi, I., Klein, M. A., Rulicke, T., Fischer, M., Brandner, S., Aguzzi, A., and Weissmann, C. (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    Rulicke, T.5    Fischer, M.6    Brandner, S.7    Aguzzi, A.8    Weissmann, C.9
  • 53
    • 0036213980 scopus 로고    scopus 로고
    • Species-barrier-independent prion replication in apparently resistant species
    • Hill, A. E., and Collinge, J. (2002). Species-barrier-independent prion replication in apparently resistant species. APMIS 110, 44-53.
    • (2002) APMIS , vol.110 , pp. 44-53
    • Hill, A.E.1    Collinge, J.2
  • 54
    • 0036216807 scopus 로고    scopus 로고
    • Transmission of prion disease
    • Blattler, T. (2002). Transmission of prion disease. APMIS 110, 71-78.
    • (2002) APMIS , vol.110 , pp. 71-78
    • Blattler, T.1
  • 55
    • 0037172849 scopus 로고    scopus 로고
    • Drug therapy in human and experimental transmissible spongiform encephalopathy
    • Brown, P. (2002). Drug therapy in human and experimental transmissible spongiform encephalopathy. Neurology 58, 1720-1725.
    • (2002) Neurology , vol.58 , pp. 1720-1725
    • Brown, P.1
  • 58
    • 0035099673 scopus 로고    scopus 로고
    • A novel erythroid-specific marker of transmissible spongiform encephalopathies
    • Miele, G., Manson, J., and Clinton, M. (2001). A novel erythroid-specific marker of transmissible spongiform encephalopathies. Nat. Med. 7, 361-364.
    • (2001) Nat. Med. , vol.7 , pp. 361-364
    • Miele, G.1    Manson, J.2    Clinton, M.3
  • 59
    • 0035943651 scopus 로고    scopus 로고
    • A protease-resistant prion protein isoform is present in urine of animals and humans affected with prion diseases
    • Shaked, G. M., Shaked, Y., Kariv-Inbal, Z., Halimi, M., Avraham, I., and Gabizon, R. (2001). A protease-resistant prion protein isoform is present in urine of animals and humans affected with prion diseases. J. Biol. Chem. 276, 31479-31482.
    • (2001) J. Biol. Chem. , vol.276 , pp. 31479-31482
    • Shaked, G.M.1    Shaked, Y.2    Kariv-Inbal, Z.3    Halimi, M.4    Avraham, I.5    Gabizon, R.6
  • 60
    • 0036070010 scopus 로고    scopus 로고
    • Bye-bye urinary gonadotrophins?: Is there a risk of prion disease after the administration of urinary-derived gonadotrophins?
    • Balen, A. (2002). Bye-bye urinary gonadotrophins?: Is there a risk of prion disease after the administration of urinary-derived gonadotrophins? Hum. Reprod. 17, 1676-1680.
    • (2002) Hum. Reprod. , vol.17 , pp. 1676-1680
    • Balen, A.1
  • 61
    • 0028883341 scopus 로고
    • Copper binding to the N-terminal tandem repeat regions of mammalian and avian prion protein
    • Hornshaw, M. P., McDermott, J. R., and Candy, J. M. (1995). Copper binding to the N-terminal tandem repeat regions of mammalian and avian prion protein. Biochem. Biophys. Res. Commun. 207, 621-629.
    • (1995) Biochem. Biophys. Res. Commun. , vol.207 , pp. 621-629
    • Hornshaw, M.P.1    McDermott, J.R.2    Candy, J.M.3
  • 62
    • 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., and Dyson, H. J. (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
  • 63
    • 0031030025 scopus 로고    scopus 로고
    • Prion protein fragment 106-126 differentially induces heme oxygenase-1 mRNA in cultured neurons and astroglial cells
    • Rizzardini, M., Chiesa, R., Angeretti, N., Lucca, E., Salmona, M., Forloni, G., and Cantoni, L. (1997). Prion protein fragment 106-126 differentially induces heme oxygenase-1 mRNA in cultured neurons and astroglial cells. J. Neurochem. 68, 715-720.
    • (1997) J. Neurochem. , vol.68 , pp. 715-720
    • Rizzardini, M.1    Chiesa, R.2    Angeretti, N.3    Lucca, E.4    Salmona, M.5    Forloni, G.6    Cantoni, L.7
  • 64
    • 0036124813 scopus 로고    scopus 로고
    • Oxidative stress and the prion protein in transmissible spongiform encephalopathies
    • Milhavet, O., and Lehmann, S. (2002). Oxidative stress and the prion protein in transmissible spongiform encephalopathies. Brain Res. Brain Res. Rev. 38, 328-339.
    • (2002) Brain Res. Brain Res. Rev. , vol.38 , pp. 328-339
    • Milhavet, O.1    Lehmann, S.2
  • 65
    • 0032169565 scopus 로고    scopus 로고
    • Prion protein expression and superoxide dismutase activity
    • Brown, D. R., and Besinger, A. (1998). Prion protein expression and superoxide dismutase activity. Biochem. J. 334, 423-429.
    • (1998) Biochem. J. , vol.334 , pp. 423-429
    • Brown, D.R.1    Besinger, A.2
  • 66
    • 0032887626 scopus 로고    scopus 로고
    • The role of copper in neurodegenerative disease
    • Waggoner, D. J., Bartnikas, T. B., and Gitlin, J. D. (1999). The role of copper in neurodegenerative disease. Neurobiol. Dis. 6, 221-230.
    • (1999) Neurobiol. Dis. , vol.6 , pp. 221-230
    • Waggoner, D.J.1    Bartnikas, T.B.2    Gitlin, J.D.3
  • 67
    • 0036263267 scopus 로고    scopus 로고
    • The molecular basis of copper homeostasis copper-related disorders
    • Llanos, R. M., and Mercer, J. F. (2002). The molecular basis of copper homeostasis copper-related disorders. DNA Cell Biol. 21, 259-270.
    • (2002) DNA Cell Biol. , vol.21 , pp. 259-270
    • Llanos, R.M.1    Mercer, J.F.2
  • 69
    • 0037085360 scopus 로고    scopus 로고
    • Regulation of the cellular prion protein gene expression depends on chromatin conformation
    • Cabral, A. L., Lee, K. S., and Martins, V. R. (2002). Regulation of the cellular prion protein gene expression depends on chromatin conformation. J. Biol. Chem. 277, 5675-5682.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5675-5682
    • Cabral, A.L.1    Lee, K.S.2    Martins, V.R.3
  • 70
    • 0033038181 scopus 로고    scopus 로고
    • Host and transmissible spongiform encephalopathy agent strain control glycosylation of PrP
    • Somerville, R. A. (1999). Host and transmissible spongiform encephalopathy agent strain control glycosylation of PrP. J. Gen. Virol. 80, 1865-1872.
    • (1999) J. Gen. Virol. , vol.80 , pp. 1865-1872
    • Somerville, R.A.1
  • 72
  • 73
    • 0027204276 scopus 로고
    • A prion protein cycles between the cell surface and an endocytic compartment in cultured neuroblastoma cells
    • Shyng, S. L., Huber, M. T., and Harris, D. A. (1993). A prion protein cycles between the cell surface and an endocytic compartment in cultured neuroblastoma cells. J. Biol. Chem. 268, 15922-15928.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15922-15928
    • Shyng, S.L.1    Huber, M.T.2    Harris, D.A.3
  • 74
    • 0032509499 scopus 로고    scopus 로고
    • Copper stimulates endocytosis of the prion protein
    • Pauly, P. C., and Harris, D. A. (1998). Copper stimulates endocytosis of the prion protein. J. Biol. Chem. 273, 33107-33110.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33107-33110
    • Pauly, P.C.1    Harris, D.A.2
  • 75
    • 0034790685 scopus 로고    scopus 로고
    • Internalization of mammalian fluorescent cellular prion protein and N- terminal deletion mutants in living cells
    • Lee, K. S., Magalhaes, A. C., Zanata, S. M., Brentani, R. R., Martins, V. R., and Prado, M. A. (2001). Internalization of mammalian fluorescent cellular prion protein and N- terminal deletion mutants in living cells. J. Neurochem. 79, 79-87.
    • (2001) J. Neurochem. , vol.79 , pp. 79-87
    • Lee, K.S.1    Magalhaes, A.C.2    Zanata, S.M.3    Brentani, R.R.4    Martins, V.R.5    Prado, M.A.6
  • 76
    • 0029564913 scopus 로고
    • Sulfated glycans stimulate endocytosis of the cellular isoform of the prion protein, PrPC, in cultured cells
    • Shyng, S. L., Lehmann, S., Moulder, K. L., and Harris, D. A. (1995). Sulfated glycans stimulate endocytosis of the cellular isoform of the prion protein, PrPC, in cultured cells. J. Biol. Chem. 270, 30221-30229.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30221-30229
    • Shyng, S.L.1    Lehmann, S.2    Moulder, K.L.3    Harris, D.A.4
  • 79
    • 0031014448 scopus 로고    scopus 로고
    • Ionic effects of the Alzheimer's disease beta-amyloid precursor protein and its metabolic fragments
    • Fraser, S. P., Suh, Y. H., and Djamgoz, M. B. (1997). Ionic effects of the Alzheimer's disease beta-amyloid precursor protein and its metabolic fragments. Trends Neurosci. 20, 67-72.
    • (1997) Trends Neurosci. , vol.20 , pp. 67-72
    • Fraser, S.P.1    Suh, Y.H.2    Djamgoz, M.B.3
  • 80
    • 0026570528 scopus 로고
    • Beta-amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity
    • Mattson, M. P., Cheng, B., Davis, D., Bryant, K., Lieberburg, I., and Rydel, R. E. (1992). Beta-amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity. J. Neurosci. 12, 376-389.
    • (1992) J. Neurosci. , vol.12 , pp. 376-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3    Bryant, K.4    Lieberburg, I.5    Rydel, R.E.6
  • 81
    • 0034640372 scopus 로고    scopus 로고
    • Alzheimer's beta-amyloid, human islet amylin, and prion protein fragment evoke intracellular free calcium elevations by a common mechanism in a hypothalamic GnRH neuronal cell line
    • Kawahara, M., Kuroda, Y., Arispe, N., and Rojas, E. (2000). Alzheimer's beta-amyloid, human islet amylin, and prion protein fragment evoke intracellular free calcium elevations by a common mechanism in a hypothalamic GnRH neuronal cell line. J. Biol. Chem. 275, 14077-14083.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14077-14083
    • Kawahara, M.1    Kuroda, Y.2    Arispe, N.3    Rojas, E.4
  • 82
    • 0030044018 scopus 로고    scopus 로고
    • Pore formation by the cytotoxic islet amyloid peptide amylin
    • Mirzabekov, T. A., Lin, M. C., and Kagan, B. L. (1996). Pore formation by the cytotoxic islet amyloid peptide amylin. J. Biol. Chem. 271, 1988-1992.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1988-1992
    • Mirzabekov, T.A.1    Lin, M.C.2    Kagan, B.L.3
  • 83
    • 0029670048 scopus 로고    scopus 로고
    • Zn2+ interaction with Alzheimer amyloid beta protein calcium channels
    • Arispe, N., Pollard, H. B., and Rojas, E. (1996). Zn2+ interaction with Alzheimer amyloid beta protein calcium channels. Proc. Natl. Acad. Sci. USA 93, 1710-1715.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1710-1715
    • Arispe, N.1    Pollard, H.B.2    Rojas, E.3
  • 84
    • 0031024927 scopus 로고    scopus 로고
    • Channel formation by a neurotoxic prion protein fragment
    • Lin, M. C., Mirzabekov, T., and Kagan, B. L. (1997). Channel formation by a neurotoxic prion protein fragment. J. Biol. Chem. 272, 44-47.
    • (1997) J. Biol. Chem. , vol.272 , pp. 44-47
    • Lin, M.C.1    Mirzabekov, T.2    Kagan, B.L.3
  • 86
    • 0035033675 scopus 로고    scopus 로고
    • Prion protein affects Ca2+-activated K+ currents in cerebellar purkinje cells
    • Herms, J. W., Tings, T., Dunker, S., and Kretzschmar, H. A. (2001). Prion protein affects Ca2+-activated K+ currents in cerebellar purkinje cells. Neurobiol. Dis. 8, 324-330.
    • (2001) Neurobiol. Dis. , vol.8 , pp. 324-330
    • Herms, J.W.1    Tings, T.2    Dunker, S.3    Kretzschmar, H.A.4
  • 87
    • 0034319190 scopus 로고    scopus 로고
    • Molecular mechanism of neurodegeneration induced by Alzheimer's beta- amyloid protein: Channel formation and disruption of calcium homeostasis
    • Kawahara, M., and Kuroda, Y. (2000). Molecular mechanism of neurodegeneration induced by Alzheimer's beta- amyloid protein: Channel formation and disruption of calcium homeostasis. Brain Res. Bull. 53, 389-397.
    • (2000) Brain Res. Bull. , vol.53 , pp. 389-397
    • Kawahara, M.1    Kuroda, Y.2
  • 88
    • 0033528286 scopus 로고    scopus 로고
    • Activation of microglial cells by PrP and beta-amyloid fragments raises intracellular calcium through L-type voltage sensitive calcium channels
    • Silei, V., Fabrizi, C., Venturini, G., Salmona, M., Bugiani, O., Tagliavini, F., and Lauro, G. M. (1999). Activation of microglial cells by PrP and beta-amyloid fragments raises intracellular calcium through L-type voltage sensitive calcium channels. Brain Res. 818, 168-170.
    • (1999) Brain Res. , vol.818 , pp. 168-170
    • Silei, V.1    Fabrizi, C.2    Venturini, G.3    Salmona, M.4    Bugiani, O.5    Tagliavini, F.6    Lauro, G.M.7
  • 89
    • 0027458091 scopus 로고
    • Heparin-like molecules bind differentially to prion-proteins and change their intracellular metabolic fate
    • Gabizon, R., Meiner, Z., Halimi, M., and Ben-Sasson, S. A. (1993). Heparin-like molecules bind differentially to prion-proteins and change their intracellular metabolic fate. J. Cell Physiol. 157, 319-325.
    • (1993) J. Cell Physiol. , vol.157 , pp. 319-325
    • Gabizon, R.1    Meiner, Z.2    Halimi, M.3    Ben-Sasson, S.A.4
  • 90
    • 0035977053 scopus 로고    scopus 로고
    • PrPC directly interacts with proteins involved in signaling pathways
    • Spielhaupter, C., and Schatzl, H. M. (2001). PrPC directly interacts with proteins involved in signaling pathways. J. Biol. Chem. 276, 44604-44612.
    • (2001) J. Biol. Chem. , vol.276 , pp. 44604-44612
    • Spielhaupter, C.1    Schatzl, H.M.2
  • 91
    • 0034707048 scopus 로고    scopus 로고
    • Binding of disease-associated prion protein to plasminogen
    • Fischer, M. B., Roeckl, C., Parizek, P., Schwarz, H. P., and Aguzzi, A. (2000). Binding of disease-associated prion protein to plasminogen. Nature 408, 479-483.
    • (2000) Nature , vol.408 , pp. 479-483
    • Fischer, M.B.1    Roeckl, C.2    Parizek, P.3    Schwarz, H.P.4    Aguzzi, A.5
  • 92
    • 0035938902 scopus 로고    scopus 로고
    • Plasminogen binds to disease-associated prion protein of multiple species
    • Maissen, M., Roeckl, C., Glatzel, M., Goldmann, W., and Aguzzi, A. (2001). Plasminogen binds to disease-associated prion protein of multiple species. Lancet 357, 2026-2028.
    • (2001) Lancet , vol.357 , pp. 2026-2028
    • Maissen, M.1    Roeckl, C.2    Glatzel, M.3    Goldmann, W.4    Aguzzi, A.5
  • 93
    • 0036301061 scopus 로고    scopus 로고
    • Prion protein interaction with glycosaminoglycan occurs with the formation of oligomeric complexes stabilized by Cu(II) bridges
    • Gonzalez-Iglesias, R., Pajares, M. A., Ocal, C., Carlos Espinosa, J., Oesch, B., and Gasset, M. (2002). Prion protein interaction with glycosaminoglycan occurs with the formation of oligomeric complexes stabilized by Cu(II) bridges. J. Mol. Biol. 319, 527-540.
    • (2002) J. Mol. Biol. , vol.319 , pp. 527-540
    • Gonzalez-Iglesias, R.1    Pajares, M.A.2    Ocal, C.3    Carlos Espinosa, J.4    Oesch, B.5    Gasset, M.6
  • 95
    • 0034613113 scopus 로고    scopus 로고
    • Laminin-induced PC-12 cell differentiation is inhibited following laser inactivation of cellular prion protein
    • Graner, E., Mercadante, A. F., Zanata, S. M., Martins, V. R., Jay, D. G., and Brentani, R. R. (2000). Laminin-induced PC-12 cell differentiation is inhibited following laser inactivation of cellular prion protein. FEBS Lett. 482, 257-260.
    • (2000) FEBS Lett. , vol.482 , pp. 257-260
    • Graner, E.1    Mercadante, A.F.2    Zanata, S.M.3    Martins, V.R.4    Jay, D.G.5    Brentani, R.R.6
  • 96
    • 0031436335 scopus 로고    scopus 로고
    • The human 37-kDa laminin receptor precursor interacts with the prion protein in eukaryotic cells
    • Rieger, R., Edenhofer, F., Lasmezas, C. I., and Weiss, S. (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    Lasmezas, C.I.3    Weiss, S.4
  • 97
    • 0031053932 scopus 로고    scopus 로고
    • Laminin and the mechanism of neuronal outgrowth
    • Luckenbill-Edds, L. (1997). Laminin and the mechanism of neuronal outgrowth. Brain Res. Brain Res. Rev. 23, 1-27.
    • (1997) Brain Res. Brain Res. Rev. , vol.23 , pp. 1-27
    • Luckenbill-Edds, L.1
  • 98
    • 0031260229 scopus 로고    scopus 로고
    • Increase of intracellular free Ca2+ in microglia activated by prion protein fragment
    • Herms, J. W., Madlung, A., Brown, D. R., and Kretzschmar, H. A. (1997). Increase of intracellular free Ca2+ in microglia activated by prion protein fragment. Glia 21, 253-257.
    • (1997) Glia , vol.21 , pp. 253-257
    • Herms, J.W.1    Madlung, A.2    Brown, D.R.3    Kretzschmar, H.A.4
  • 99
    • 0033080919 scopus 로고    scopus 로고
    • Identification of microglial signal transduction pathways mediating a neurotoxic response to amyloidogenic fragments of beta-amyloid and prion proteins
    • Combs, C. K., Johnson, D. E., Cannady, S. B., Lehman, T. M., and Landreth, G. E. (1999). Identification of microglial signal transduction pathways mediating a neurotoxic response to amyloidogenic fragments of beta-amyloid and prion proteins. J. Neurosci. 19, 928-939.
    • (1999) J. Neurosci. , vol.19 , pp. 928-939
    • Combs, C.K.1    Johnson, D.E.2    Cannady, S.B.3    Lehman, T.M.4    Landreth, G.E.5
  • 100
    • 0033900833 scopus 로고    scopus 로고
    • Gene expression profile in prion protein-deficient fibroblasts in culture
    • Satoh, J., Kuroda, Y., and Katamine, S. (2000). Gene expression profile in prion protein-deficient fibroblasts in culture. Am. J. Pathol. 157, 59-68.
    • (2000) Am. J. Pathol. , vol.157 , pp. 59-68
    • Satoh, J.1    Kuroda, Y.2    Katamine, S.3
  • 101
    • 0035164003 scopus 로고    scopus 로고
    • Segregation of heterotrimeric G proteins in cell surface microdomains. G(q) binds caveolin to concentrate in caveolae, whereas G(i) and G(s) target lipid rafts by default
    • Oh, P., and Schnitzer, J. E. (2001). Segregation of heterotrimeric G proteins in cell surface microdomains. G(q) binds caveolin to concentrate in caveolae, whereas G(i) and G(s) target lipid rafts by default. Mol. Biol. Cell 12, 685-698.
    • (2001) Mol. Biol. Cell. , vol.12 , pp. 685-698
    • Oh, P.1    Schnitzer, J.E.2


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