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Volumn 18, Issue 2, 2013, Pages 209-230

Prion protein and its role in signal transduction

Author keywords

AKT; Calcium; MAP kinases; PKA; PKC; Prion; Signaling; Src

Indexed keywords

2',3' CYCLIC NUCLEOTIDE 3' PHOPHODIESTERASE; AMYLOID BETA PROTEIN; BINDING PROTEIN; CASPASE 3; CYCLIC AMP DEPENDENT PROTEIN KINASE; GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORED PROTEIN; LAMININ; LAMININ RECEPTOR; LAMININ RECEPTOR PRECURSOR; M6 A; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MYELIN ASSOCIATED GLYCOPROTEIN; NERVE CELL ADHESION MOLECULE; NEUROFASCIN; P0 GLYCOPROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE; PRION PROTEIN; PROTEIN KINASE B; PROTEIN KINASE C; PROTEIN KINASE FYN; STRESS INDUCIBLE PROTEIN 1; UNCLASSIFIED DRUG;

EID: 84877630656     PISSN: 14258153     EISSN: 16891392     Source Type: Journal    
DOI: 10.2478/s11658-013-0085-0     Document Type: Review
Times cited : (23)

References (114)
  • 1
    • 0017643758 scopus 로고
    • Unconventional viruses and the origin and disappearance of kuru
    • Gajdusek, D. C. Unconventional viruses and the origin and disappearance of kuru. Science197 (1977) 943-960.
    • (1977) Science , vol.197 , pp. 943-960
    • Gajdusek, D.C.1
  • 2
    • 0024262335 scopus 로고
    • Molecular structure, biology, and genetics of prions
    • Prusiner, S. B. Molecular structure, biology, and genetics of prions. Adv. Virus. Res. 35 (1988) 83-136.
    • (1988) Adv. Virus. Res. , vol.35 , pp. 83-136
    • Prusiner, S.B.1
  • 4
    • 74249084312 scopus 로고    scopus 로고
    • De novo mammalian prion synthesis
    • Benetti, F. and Legname, G. De novo mammalian prion synthesis. Prion3 (2009) 213-219.
    • (2009) Prion , vol.3 , pp. 213-219
    • Benetti, F.1    Legname, G.2
  • 6
    • 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. Purification and structural studies of a major scrapie prion protein. Cell38 (1984) 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
  • 12
    • 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. Copper binding to the prion protein: structural implications of four identical cooperative binding sites. Proc. Natl. Acad. Sci. USA96 (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
  • 14
    • 0025091084 scopus 로고
    • Identification of glycoinositol phospholipid linked and truncated forms of the scrapie prion protein
    • Stahl, N., Baldwin, M. A., Burlingame, A. L. and Prusiner, S. B. Identification of glycoinositol phospholipid linked and truncated forms of the scrapie prion protein. Biochemistry29 (1990) 8879-8884.
    • (1990) Biochemistry , vol.29 , pp. 8879-8884
    • Stahl, N.1    Baldwin, M.A.2    Burlingame, A.L.3    Prusiner, S.B.4
  • 16
    • 0030894380 scopus 로고    scopus 로고
    • Characterization of detergent-insoluble complexes containing the cellular prion protein and its scrapie isoform
    • Naslavsky, N., Stein, R., Yanai, A., Friedlander, G. and Taraboulos, A. Characterization of detergent-insoluble complexes containing the cellular prion protein and its scrapie isoform. J. Biol. Chem. 272 (1997) 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
  • 17
    • 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. A prion protein cycles between the cell surface and an endocytic compartment in cultured neuroblastoma cells. J. Biol. Chem. 268 (1993) 15922-15928.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15922-15928
    • Shyng, S.L.1    Huber, M.T.2    Harris, D.A.3
  • 18
    • 0031692336 scopus 로고    scopus 로고
    • The caveolae membrane system
    • Anderson, R. G. The caveolae membrane system. Annu. Rev. Biochem. 67 (1998) 199-225.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 199-225
    • Anderson, R.G.1
  • 19
    • 33645290776 scopus 로고    scopus 로고
    • The prion protein and lipid rafts
    • Taylor, D. R. and Hooper, N. M. The prion protein and lipid rafts. Mol. Membr. Biol. 23 (2006) 89-99.
    • (2006) Mol. Membr. Biol. , vol.23 , pp. 89-99
    • Taylor, D.R.1    Hooper, N.M.2
  • 20
    • 0026775909 scopus 로고
    • Evidence for synthesis of scrapie prion proteins in the endocytic pathway
    • Borchelt, D. R., Taraboulos, A. and Prusiner, S. B. Evidence for synthesis of scrapie prion proteins in the endocytic pathway. J. Biol. Chem. 267 (1992) 16188-16199.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16188-16199
    • Borchelt, D.R.1    Taraboulos, A.2    Prusiner, S.B.3
  • 21
    • 79952795300 scopus 로고    scopus 로고
    • Infrared microspectroscopy: a multiple-screening platform for investigating singlecell biochemical perturbations upon prion infection
    • Didonna, A., Vaccari, L., Bek, A. and Legname, G. Infrared microspectroscopy: a multiple-screening platform for investigating singlecell biochemical perturbations upon prion infection. ACS Chem. Neurosci. 2 (2011) 160-174.
    • (2011) ACS Chem. Neurosci. , vol.2 , pp. 160-174
    • Didonna, A.1    Vaccari, L.2    Bek, A.3    Legname, G.4
  • 23
    • 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. and 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
  • 29
    • 84863714721 scopus 로고    scopus 로고
    • The role of Bax and caspase-3 in doppel-induced apoptosis of cerebellar granule cells
    • Didonna, A., Sussman, J., Benetti, F. and Legname, G. The role of Bax and caspase-3 in doppel-induced apoptosis of cerebellar granule cells. Prion6 (2012) 309-316.
    • (2012) Prion , vol.6 , pp. 309-316
    • Didonna, A.1    Sussman, J.2    Benetti, F.3    Legname, G.4
  • 30
    • 0036470471 scopus 로고    scopus 로고
    • Post-natal knockout of prion protein alters hippocampal CA1 properties, but does not result in neurodegeneration
    • Mallucci, G. R., Ratte, S., Asante, E. A., Linehan, J., Gowland, I., Jefferys, J. G. and Collinge, J. Post-natal knockout of prion protein alters hippocampal CA1 properties, but does not result in neurodegeneration. EMBO J. 21 (2002) 202-210.
    • (2002) EMBO J. , vol.21 , pp. 202-210
    • Mallucci, G.R.1    Ratte, S.2    Asante, E.A.3    Linehan, J.4    Gowland, I.5    Jefferys, J.G.6    Collinge, J.7
  • 36
    • 0035158321 scopus 로고    scopus 로고
    • Antioxidant activity related to copper binding of native prion protein
    • Brown, D. R., Clive, C. and Haswell, S. J. Antioxidant activity related to copper binding of native prion protein. J. Neurochem. 76 (2001) 69-76.
    • (2001) J. Neurochem. , vol.76 , pp. 69-76
    • Brown, D.R.1    Clive, C.2    Haswell, S.J.3
  • 37
    • 0031047646 scopus 로고    scopus 로고
    • Sleep and sleep regulation in normal and prion protein-deficient mice
    • Tobler, I., Deboer, T. and Fischer, M. Sleep and sleep regulation in normal and prion protein-deficient mice. J. Neurosci. 17 (1997) 1869-1879.
    • (1997) J. Neurosci. , vol.17 , pp. 1869-1879
    • Tobler, I.1    Deboer, T.2    Fischer, M.3
  • 40
    • 33144456321 scopus 로고    scopus 로고
    • Prion protein is expressed on long-term repopulating hematopoietic stem cells and is important for their self-renewal
    • Zhang, C. C., Steele, A. D., Lindquist, S. and Lodish, H. F. Prion protein is expressed on long-term repopulating hematopoietic stem cells and is important for their self-renewal. Proc. Natl. Acad. Sci. USA103 (2006) 2184-2189.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 2184-2189
    • Zhang, C.C.1    Steele, A.D.2    Lindquist, S.3    Lodish, H.F.4
  • 41
    • 33748713915 scopus 로고    scopus 로고
    • The role of the cellular prion protein in the immune system
    • Isaacs, J. D., Jackson, G. S. and Altmann, D. M. The role of the cellular prion protein in the immune system. Clin. Exp. Immunol. 146 (2006) 1-8.
    • (2006) Clin. Exp. Immunol. , vol.146 , pp. 1-8
    • Isaacs, J.D.1    Jackson, G.S.2    Altmann, D.M.3
  • 44
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson, T. Protein modules and signalling networks. Nature373 (1995) 573-580.
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 52
    • 61349201380 scopus 로고    scopus 로고
    • Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers
    • Lauren, J., Gimbel, D. A., Nygaard, H. B., Gilbert, J. W. and Strittmatter, S. M. Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers. Nature457 (2009) 1128-1132.
    • (2009) Nature , vol.457 , pp. 1128-1132
    • Lauren, J.1    Gimbel, D.A.2    Nygaard, H.B.3    Gilbert, J.W.4    Strittmatter, S.M.5
  • 53
    • 77955617917 scopus 로고    scopus 로고
    • The prion protein as a receptor for amyloid-beta
    • Kessels, H. W., Nguyen, L. N., Nabavi, S. and Malinow, R. The prion protein as a receptor for amyloid-beta. Nature466 (2010) E3-4; discussion E4-5.
    • (2010) Nature , vol.466
    • Kessels, H.W.1    Nguyen, L.N.2    Nabavi, S.3    Malinow, R.4
  • 57
    • 2942618768 scopus 로고    scopus 로고
    • A renaissance for SRC
    • Yeatman, T. J. A renaissance for SRC. Nat. Rev. Cancer4 (2004) 470-480.
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 470-480
    • Yeatman, T.J.1
  • 58
    • 0027971705 scopus 로고
    • NCAM-dependent neurite outgrowth is inhibited in neurons from Fyn-minus mice
    • Beggs, H. E., Soriano, P. and Maness, P. F. NCAM-dependent neurite outgrowth is inhibited in neurons from Fyn-minus mice. J. Cell Biol. 127 (1994) 825-833.
    • (1994) J. Cell Biol. , vol.127 , pp. 825-833
    • Beggs, H.E.1    Soriano, P.2    Maness, P.F.3
  • 59
    • 18544376071 scopus 로고    scopus 로고
    • Prion protein recruits its neuronal receptor NCAM to lipid rafts to activate p59fyn and to enhance neurite outgrowth
    • Santuccione, A., Sytnyk, V., Leshchyns'ka, I. and Schachner, M. Prion protein recruits its neuronal receptor NCAM to lipid rafts to activate p59fyn and to enhance neurite outgrowth. J. Cell Biol. 169 (2005) 341-354.
    • (2005) J. Cell Biol. , vol.169 , pp. 341-354
    • Santuccione, A.1    Sytnyk, V.2    Leshchyns'ka, I.3    Schachner, M.4
  • 60
    • 28844477599 scopus 로고    scopus 로고
    • Recombinant prion protein induces rapid polarization and development of synapses in embryonic rat hippocampal neurons in vitro
    • Kanaani, J., Prusiner, S. B., Diacovo, J., Baekkeskov, S. and Legname, G. Recombinant prion protein induces rapid polarization and development of synapses in embryonic rat hippocampal neurons in vitro. J. Neurochem. 95 (2005) 1373-1386.
    • (2005) J. Neurochem. , vol.95 , pp. 1373-1386
    • Kanaani, J.1    Prusiner, S.B.2    Diacovo, J.3    Baekkeskov, S.4    Legname, G.5
  • 61
    • 21844452161 scopus 로고    scopus 로고
    • Unchanged scrapie pathology in brain tissue of tyrosine kinase Fyn-deficient mice
    • Schwarz, A., Burwinkel, M., Riemer, C., Schultz, J. and Baier, M. Unchanged scrapie pathology in brain tissue of tyrosine kinase Fyn-deficient mice. Neurodegener. Dis. 1 (2004) 266-268.
    • (2004) Neurodegener. Dis. , vol.1 , pp. 266-268
    • Schwarz, A.1    Burwinkel, M.2    Riemer, C.3    Schultz, J.4    Baier, M.5
  • 62
    • 13244255633 scopus 로고    scopus 로고
    • Prion-associated increases in Src-family kinases
    • Nixon, R. R. Prion-associated increases in Src-family kinases. J. Biol. Chem. 280 (2005) 2455-2462.
    • (2005) J. Biol. Chem. , vol.280 , pp. 2455-2462
    • Nixon, R.R.1
  • 63
    • 33646174831 scopus 로고    scopus 로고
    • Increased Src kinase level results in increased protein tyrosine phosphorylation in scrapieinfected neuronal cell lines
    • Gyllberg, H., Lofgren, K., Lindegren, H. and Bedecs, K. Increased Src kinase level results in increased protein tyrosine phosphorylation in scrapieinfected neuronal cell lines. FEBS Lett. 580 (2006) 2603-2608.
    • (2006) FEBS Lett. , vol.580 , pp. 2603-2608
    • Gyllberg, H.1    Lofgren, K.2    Lindegren, H.3    Bedecs, K.4
  • 64
    • 77955296897 scopus 로고    scopus 로고
    • Aberrant ERK 1/2 complex activation and localization in scrapie-infected GT1-1 cells
    • Didonna, A. and Legname, G. Aberrant ERK 1/2 complex activation and localization in scrapie-infected GT1-1 cells. Mol. Neurodegener. 5 (2010) 29.
    • (2010) Mol. Neurodegener. , vol.5 , pp. 29
    • Didonna, A.1    Legname, G.2
  • 66
    • 0345687168 scopus 로고    scopus 로고
    • NADPH oxidase and extracellular regulated kinases 1/2 are targets of prion protein signaling in neuronal and nonneuronal cells
    • Schneider, B., Mutel, V., Pietri, M., Ermonval, M., Mouillet-Richard, S. and Kellermann, O. NADPH oxidase and extracellular regulated kinases 1/2 are targets of prion protein signaling in neuronal and nonneuronal cells. Proc. Natl. Acad. Sci. USA100 (2003) 13326-13331.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13326-13331
    • Schneider, B.1    Mutel, V.2    Pietri, M.3    Ermonval, M.4    Mouillet-Richard, S.5    Kellermann, O.6
  • 67
    • 85010209286 scopus 로고    scopus 로고
    • MAP kinases and histone modification
    • Suganuma, T. and Workman, J. L. MAP kinases and histone modification. J. Mol. Cell. Biol. 34 (2010) 1543-1551.
    • (2010) J. Mol. Cell. Biol. , vol.34 , pp. 1543-1551
    • Suganuma, T.1    Workman, J.L.2
  • 68
    • 30544444183 scopus 로고    scopus 로고
    • Interaction of cellular prion and stress-inducible protein 1 promotes neuritogenesis and neuroprotection by distinct signaling pathways
    • Lopes, M. H., Hajj, G. N., Muras, A. G., Mancini, G. L., Castro, R. M., Ribeiro, K. C., Brentani, R. R., Linden, R. and Martins, V. R. Interaction of cellular prion and stress-inducible protein 1 promotes neuritogenesis and neuroprotection by distinct signaling pathways. J. Neurosci. 25 (2005) 11330-11339.
    • (2005) J. Neurosci. , vol.25 , pp. 11330-11339
    • Lopes, M.H.1    Hajj, G.N.2    Muras, A.G.3    Mancini, G.L.4    Castro, R.M.5    Ribeiro, K.C.6    Brentani, R.R.7    Linden, R.8    Martins, V.R.9
  • 69
  • 70
    • 12544257289 scopus 로고    scopus 로고
    • Pathological prion protein exposure switches on neuronal mitogen-activated protein kinase pathway resulting in microglia recruitment
    • Marella, M., Gaggioli, C., Batoz, M., Deckert, M., Tartare-Deckert, S. and Chabry, J. Pathological prion protein exposure switches on neuronal mitogen-activated protein kinase pathway resulting in microglia recruitment. J. Biol. Chem. 280 (2005) 1529-1534.
    • (2005) J. Biol. Chem. , vol.280 , pp. 1529-1534
    • Marella, M.1    Gaggioli, C.2    Batoz, M.3    Deckert, M.4    Tartare-Deckert, S.5    Chabry, J.6
  • 71
    • 26844548845 scopus 로고    scopus 로고
    • Activation of mitogen-activated protein kinases in hamster brains infected with 263K scrapie agent
    • Lee, H. P., Jun, Y. C., Choi, J. K., Kim, J. I., Carp, R. I. and Kim, Y. S. Activation of mitogen-activated protein kinases in hamster brains infected with 263K scrapie agent. J. Neurochem. 95 (2005) 584-593.
    • (2005) J. Neurochem. , vol.95 , pp. 584-593
    • Lee, H.P.1    Jun, Y.C.2    Choi, J.K.3    Kim, J.I.4    Carp, R.I.5    Kim, Y.S.6
  • 73
    • 34648836753 scopus 로고    scopus 로고
    • ERK1/2 and p38 MAP kinases control prion protein fragment 90-231-induced astrocyte proliferation and microglia activation
    • Thellung, S., Villa, V., Corsaro, A., Pellistri, F., Venezia, V., Russo, C., Aceto, A., Robello, M. and Florio, T. ERK1/2 and p38 MAP kinases control prion protein fragment 90-231-induced astrocyte proliferation and microglia activation. Glia55 (2007) 1469-1485.
    • (2007) Glia , vol.55 , pp. 1469-1485
    • Thellung, S.1    Villa, V.2    Corsaro, A.3    Pellistri, F.4    Venezia, V.5    Russo, C.6    Aceto, A.7    Robello, M.8    Florio, T.9
  • 74
    • 0031194455 scopus 로고    scopus 로고
    • Prion protein-deficient cells show altered response to oxidative stress due to decreased SOD-1 activity
    • Brown, D. R., Schulz-Schaeffer, W. J., Schmidt, B. and Kretzschmar, H. A. Prion protein-deficient cells show altered response to oxidative stress due to decreased SOD-1 activity. Exp. Neurol. 146 (1997) 104-112.
    • (1997) Exp. Neurol. , vol.146 , pp. 104-112
    • Brown, D.R.1    Schulz-Schaeffer, W.J.2    Schmidt, B.3    Kretzschmar, H.A.4
  • 75
    • 24944524825 scopus 로고    scopus 로고
    • Inhibitors of the mitogen-activated protein kinase kinase 1/2 signaling pathway clear prion-infected cells from PrPSc
    • Nordstrom, E. K., Luhr, K. M., Ibanez, C. and Kristensson, K. Inhibitors of the mitogen-activated protein kinase kinase 1/2 signaling pathway clear prion-infected cells from PrPSc. J. Neurosci. 25 (2005) 8451-8456.
    • (2005) J. Neurosci. , vol.25 , pp. 8451-8456
    • Nordstrom, E.K.1    Luhr, K.M.2    Ibanez, C.3    Kristensson, K.4
  • 76
    • 42449102282 scopus 로고    scopus 로고
    • Resistance of cell lines to prion toxicity aided by phospho-ERK expression
    • Uppington, K. M. and Brown, D. R. Resistance of cell lines to prion toxicity aided by phospho-ERK expression. J. Neurochem. 105 (2008) 842-852.
    • (2008) J. Neurochem. , vol.105 , pp. 842-852
    • Uppington, K.M.1    Brown, D.R.2
  • 77
    • 77952170820 scopus 로고    scopus 로고
    • Specificity and spatial dynamics of protein kinase A signaling organized by A-kinase-anchoring proteins
    • Pidoux, G. and Tasken, K. Specificity and spatial dynamics of protein kinase A signaling organized by A-kinase-anchoring proteins. J. Mol. Endocrinol. 44 (2010) 271-284.
    • (2010) J. Mol. Endocrinol. , vol.44 , pp. 271-284
    • Pidoux, G.1    Tasken, K.2
  • 78
    • 80053305618 scopus 로고    scopus 로고
    • Cross-talk between calcium and protein kinase A in the regulation of cell migration
    • Howe, A. K. Cross-talk between calcium and protein kinase A in the regulation of cell migration. Curr. Opin. Cell Biol. 23 (2011) 554-561.
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 554-561
    • Howe, A.K.1
  • 81
    • 84867705071 scopus 로고    scopus 로고
    • Protein kinase C (PKC) isozyme-specific substrates and their design
    • Kang, J. H., Toita, R., Kim, C. W. and Katayama, Y. Protein kinase C (PKC) isozyme-specific substrates and their design. Biotechnol. Adv. 30 (2012) 1662-1672.
    • (2012) Biotechnol. Adv. , vol.30 , pp. 1662-1672
    • Kang, J.H.1    Toita, R.2    Kim, C.W.3    Katayama, Y.4
  • 82
    • 77956932796 scopus 로고    scopus 로고
    • 12-O-tetradecanoylphorbol-1, 3-acetate induces the negative regulation of protein kinase B by protein kinase Calpha during gastric cancer cell apoptosis
    • Zhang, B. and Xia, C. 12-O-tetradecanoylphorbol-1, 3-acetate induces the negative regulation of protein kinase B by protein kinase Calpha during gastric cancer cell apoptosis. Cell. Mol. Biol. Lett. 15 (2010) 377-394.
    • (2010) Cell. Mol. Biol. Lett. , vol.15 , pp. 377-394
    • Zhang, B.1    Xia, C.2
  • 84
    • 1342273153 scopus 로고    scopus 로고
    • Immunoseparation of prion protein-enriched domains from other detergent-resistant membrane fractions, isolated from neuronal cells
    • Botto, L., Masserini, M., Cassetti, A. and Palestini, P. Immunoseparation of prion protein-enriched domains from other detergent-resistant membrane fractions, isolated from neuronal cells. FEBS Lett. 557 (2004) 143-147.
    • (2004) FEBS Lett. , vol.557 , pp. 143-147
    • Botto, L.1    Masserini, M.2    Cassetti, A.3    Palestini, P.4
  • 87
    • 84855718266 scopus 로고    scopus 로고
    • 17beta-Estradiol promotes cell proliferation in rat osteoarthritis model chondrocytes via PI3K/Akt pathway
    • Huang, J. G., Xia, C., Zheng, X. P., Yi, T. T., Wang, X. Y., Song, G. and Zhang, B. 17beta-Estradiol promotes cell proliferation in rat osteoarthritis model chondrocytes via PI3K/Akt pathway. Cell. Mol. Biol. Lett. 16 (2011) 564-575.
    • (2011) Cell. Mol. Biol. Lett. , vol.16 , pp. 564-575
    • Huang, J.G.1    Xia, C.2    Zheng, X.P.3    Yi, T.T.4    Wang, X.Y.5    Song, G.6    Zhang, B.7
  • 88
    • 0345505687 scopus 로고    scopus 로고
    • Prion protein as trans-interacting partner for neurons is involved in neurite outgrowth and neuronal survival
    • Chen, S., Mange, A., Dong, L., Lehmann, S. and Schachner, M. Prion protein as trans-interacting partner for neurons is involved in neurite outgrowth and neuronal survival. Mol. Cell. Neurosci. 22 (2003) 227-233.
    • (2003) Mol. Cell. Neurosci. , vol.22 , pp. 227-233
    • Chen, S.1    Mange, A.2    Dong, L.3    Lehmann, S.4    Schachner, M.5
  • 89
    • 33646695909 scopus 로고    scopus 로고
    • Deletion of cellular prion protein results in reduced Akt activation, enhanced postischemic caspase-3 activation, and exacerbation of ischemic brain injury
    • Weise, J., Sandau, R., Schwarting, S., Crome, O., Wrede, A., Schulz-Schaeffer, W., Zerr, I. and Bahr, M. Deletion of cellular prion protein results in reduced Akt activation, enhanced postischemic caspase-3 activation, and exacerbation of ischemic brain injury. Stroke37 (2006) 1296-1300.
    • (2006) Stroke , vol.37 , pp. 1296-1300
    • Weise, J.1    Sandau, R.2    Schwarting, S.3    Crome, O.4    Wrede, A.5    Schulz-Schaeffer, W.6    Zerr, I.7    Bahr, M.8
  • 90
    • 43049116184 scopus 로고    scopus 로고
    • Overexpression of cellular prion protein alters postischemic Erk1/2 phosphorylation but not Akt phosphorylation and protects against focal cerebral ischemia
    • Weise, J., Doeppner, T. R., Muller, T., Wrede, A., Schulz-Schaeffer, W., Zerr, I., Witte, O. W. and Bahr, M. Overexpression of cellular prion protein alters postischemic Erk1/2 phosphorylation but not Akt phosphorylation and protects against focal cerebral ischemia. Restor. Neurol. Neurosci. 26 (2008) 57-64.
    • (2008) Restor. Neurol. Neurosci. , vol.26 , pp. 57-64
    • Weise, J.1    Doeppner, T.R.2    Muller, T.3    Wrede, A.4    Schulz-Schaeffer, W.5    Zerr, I.6    Witte, O.W.7    Bahr, M.8
  • 93
    • 73949085497 scopus 로고    scopus 로고
    • Hypoxia protects neuronal cells from human prion protein fragment-induced apoptosis
    • Seo, J. S., Seol, J. W., Moon, M. H., Jeong, J. K., Lee, Y. J. and Park, S. Y. Hypoxia protects neuronal cells from human prion protein fragment-induced apoptosis. J. Neurochem. 112 (2010) 715-722.
    • (2010) J. Neurochem. , vol.112 , pp. 715-722
    • Seo, J.S.1    Seol, J.W.2    Moon, M.H.3    Jeong, J.K.4    Lee, Y.J.5    Park, S.Y.6
  • 95
    • 84872551479 scopus 로고    scopus 로고
    • Multilevel complexity of calcium signaling: Modeling angiogenesis
    • Munaron, L. and Scianna, M. Multilevel complexity of calcium signaling: Modeling angiogenesis. World J. Biol. Chem. 3 (2012) 121-126.
    • (2012) World J. Biol. Chem. , vol.3 , pp. 121-126
    • Munaron, L.1    Scianna, M.2
  • 96
    • 79959519400 scopus 로고    scopus 로고
    • Possible role for Ca2+ in the pathophysiology of the prion protein?
    • Peggion, C., Bertoli, A. and Sorgato, M. C. Possible role for Ca2+ in the pathophysiology of the prion protein? Biofactors37 (2011) 241-249.
    • (2011) Biofactors , vol.37 , pp. 241-249
    • Peggion, C.1    Bertoli, A.2    Sorgato, M.C.3
  • 97
    • 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. Hippocampal slices from prion protein null mice: disrupted Ca(2+)-activated K+ currents. Neurosci. Lett. 209 (1996) 49-52.
    • (1996) Neurosci. Lett. , vol.209 , pp. 49-52
    • Colling, S.B.1    Collinge, J.2    Jefferys, J.G.3
  • 98
    • 0033817026 scopus 로고    scopus 로고
    • Altered intracellular calcium homeostasis in cerebellar granule cells of prion protein-deficient mice
    • Herms, J. W., Korte, S., Gall, S., Schneider, I., Dunker, S. and Kretzschmar, H. A. Altered intracellular calcium homeostasis in cerebellar granule cells of prion protein-deficient mice. J. Neurochem. 75 (2000) 1487-1492.
    • (2000) J. Neurochem. , vol.75 , pp. 1487-1492
    • Herms, J.W.1    Korte, S.2    Gall, S.3    Schneider, I.4    Dunker, S.5    Kretzschmar, H.A.6
  • 99
    • 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. Prion protein affects Ca2+-activated K+ currents in cerebellar purkinje cells. Neurobiol. Dis. 8 (2001) 324-330.
    • (2001) Neurobiol. Dis. , vol.8 , pp. 324-330
    • Herms, J.W.1    Tings, T.2    Dunker, S.3    Kretzschmar, H.A.4
  • 102
    • 0345687495 scopus 로고    scopus 로고
    • Modulation of L-type voltage-gated calcium channels by recombinant prion protein
    • Korte, S., Vassallo, N., Kramer, M. L., Kretzschmar, H. A. and Herms, J. Modulation of L-type voltage-gated calcium channels by recombinant prion protein. J. Neurochem. 87 (2003) 1037-1042.
    • (2003) J. Neurochem. , vol.87 , pp. 1037-1042
    • Korte, S.1    Vassallo, N.2    Kramer, M.L.3    Kretzschmar, H.A.4    Herms, J.5
  • 103
    • 43049180250 scopus 로고    scopus 로고
    • Alterations in Ca2+-buffering in prion-null mice: association with reduced afterhyperpolarizations in CA1 hippocampal neurons
    • Powell, A. D., Toescu, E. C., Collinge, J. and Jefferys, J. G. Alterations in Ca2+-buffering in prion-null mice: association with reduced afterhyperpolarizations in CA1 hippocampal neurons. J. Neurosci. 28 (2008) 3877-3886.
    • (2008) J. Neurosci. , vol.28 , pp. 3877-3886
    • Powell, A.D.1    Toescu, E.C.2    Collinge, J.3    Jefferys, J.G.4
  • 104
    • 79851481136 scopus 로고    scopus 로고
    • Cellular prion protein is implicated in the regulation of local Ca2+ movements in cerebellar granule neurons
    • Lazzari, C., Peggion, C., Stella, R., Massimino, M. L., Lim, D., Bertoli, A. and Sorgato, M. C. Cellular prion protein is implicated in the regulation of local Ca2+ movements in cerebellar granule neurons. J. Neurochem. 116 (2011) 881-890.
    • (2011) J. Neurochem. , vol.116 , pp. 881-890
    • Lazzari, C.1    Peggion, C.2    Stella, R.3    Massimino, M.L.4    Lim, D.5    Bertoli, A.6    Sorgato, M.C.7
  • 105
    • 34249092704 scopus 로고    scopus 로고
    • Calcium and neurodegeneration
    • Mattson, M. P. Calcium and neurodegeneration. Aging Cell6 (2007) 337-350.
    • (2007) Aging Cell , vol.6 , pp. 337-350
    • Mattson, M.P.1
  • 107
    • 0032701489 scopus 로고    scopus 로고
    • Intrinsic physiological and morphological properties of principal cells of the hippocampus and neocortex in hamsters infected with scrapie
    • Barrow, P. A., Holmgren, C. D., Tapper, A. J. and Jefferys, J. G. Intrinsic physiological and morphological properties of principal cells of the hippocampus and neocortex in hamsters infected with scrapie. Neurobiol. Dis. 6 (1999) 406-423.
    • (1999) Neurobiol. Dis. , vol.6 , pp. 406-423
    • Barrow, P.A.1    Holmgren, C.D.2    Tapper, A.J.3    Jefferys, J.G.4
  • 108
    • 0032101845 scopus 로고    scopus 로고
    • Alterations in potassium currents may trigger neurodegeneration in murine scrapie
    • Johnston, A. R., Fraser, J. R., Jeffrey, M. and MacLeod, N. Alterations in potassium currents may trigger neurodegeneration in murine scrapie. Exp. Neurol. 151 (1998) 326-333.
    • (1998) Exp. Neurol. , vol.151 , pp. 326-333
    • Johnston, A.R.1    Fraser, J.R.2    Jeffrey, M.3    MacLeod, N.4
  • 109
    • 0032213349 scopus 로고    scopus 로고
    • Prion protein fragment 106-126 induces apoptotic cell death and impairment of L-type voltage-sensitive calcium channel activity in the GH3 cell line
    • Florio, T., Thellung, S., Amico, C., Robello, M., Salmona, M., Bugiani, O., Tagliavini, F., Forloni, G. and Schettini, G. Prion protein fragment 106-126 induces apoptotic cell death and impairment of L-type voltage-sensitive calcium channel activity in the GH3 cell line. J. Neurosci. Res. 54 (1998) 341-352.
    • (1998) J. Neurosci. Res. , vol.54 , pp. 341-352
    • Florio, T.1    Thellung, S.2    Amico, C.3    Robello, M.4    Salmona, M.5    Bugiani, O.6    Tagliavini, F.7    Forloni, G.8    Schettini, G.9
  • 111
    • 1642578920 scopus 로고    scopus 로고
    • Scrapieinfected GT1-1 cells show impaired function of voltage-gated N-type calcium channels (Ca(v) 2.2) which is ameliorated by quinacrine treatment
    • Sandberg, M. K., Wallen, P., Wikstrom, M. A. and Kristensson, K. Scrapieinfected GT1-1 cells show impaired function of voltage-gated N-type calcium channels (Ca(v) 2. 2) which is ameliorated by quinacrine treatment. Neurobiol. Dis. 15 (2004) 143-151.
    • (2004) Neurobiol. Dis. , vol.15 , pp. 143-151
    • Sandberg, M.K.1    Wallen, P.2    Wikstrom, M.A.3    Kristensson, K.4
  • 112
    • 78650843400 scopus 로고    scopus 로고
    • Prion protein misfolding affects calcium homeostasis and sensitizes cells to endoplasmic reticulum stress
    • Torres, M., Castillo, K., Armisen, R., Stutzin, A., Soto, C. and Hetz, C. Prion protein misfolding affects calcium homeostasis and sensitizes cells to endoplasmic reticulum stress. PLOS One5 (2010) e15658.
    • (2010) PLOS One , vol.5
    • Torres, M.1    Castillo, K.2    Armisen, R.3    Stutzin, A.4    Soto, C.5    Hetz, C.6
  • 114
    • 0036154536 scopus 로고    scopus 로고
    • MHC and MHCrelated proteins as pleiotropic signal molecules
    • Ojcius, D. M., Delarbre, C., Kourilsky, P. and Gachelin, G. MHC and MHCrelated proteins as pleiotropic signal molecules. FASEB J. 16 (2002) 202-206.
    • (2002) FASEB J. , vol.16 , pp. 202-206
    • Ojcius, D.M.1    Delarbre, C.2    Kourilsky, P.3    Gachelin, G.4


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