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Volumn 287, Issue 7, 2012, Pages 5021-5032

α-secretase-derived fragment of cellular prion, N1, protects against monomeric and oligomeric amyloid β(Aβ)-associated cell death

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMER; ALZHEIMER DISEASE; AMYLOID PRECURSOR PROTEINS; BRAIN TISSUE; CASPASE-3 ACTIVATION; CELLULAR PRION; CHO CELL; CONDITIONED MEDIUM; CULTURED NEURONS; HUMAN CELLS; IN-VITRO; N-TERMINALS; OVER-EXPRESSION; PHYSIOLOGICAL CONDITION; SECRETASES; TRANSACTIVATION;

EID: 84856845217     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.323626     Document Type: Article
Times cited : (79)

References (69)
  • 1
    • 0032076463 scopus 로고    scopus 로고
    • Prion protein biology
    • DOI 10.1016/S0092-8674(00)81163-0
    • Prusiner, S. B., Scott, M. R., DeArmond, S. J., and Cohen, F. E. (1998) Prion protein biology. Cell 93, 337-348 (Pubitemid 28232079)
    • (1998) Cell , vol.93 , Issue.3 , pp. 337-348
    • Prusiner, S.B.1    Scott, M.R.2    DeArmond, S.J.3    Cohen, F.E.4
  • 2
    • 0027333557 scopus 로고
    • Cellular processing of β-amyloid precursor protein and the genesis of amyloid β-peptide
    • Haass, C., and Selkoe, D. J. (1993) Cellular processing of β-amyloid precursor protein and the genesis of amyloid β-peptide. Cell 75, 1039-1042
    • (1993) Cell , vol.75 , pp. 1039-1042
    • Haass, C.1    Selkoe, D.J.2
  • 3
    • 0029379605 scopus 로고
    • Processing of the β-amyloid precursor protein and its regulation in Alzheimer's disease
    • Checler, F. (1995) Processing of the β-amyloid precursor protein and its regulation in Alzheimer's disease. J. Neurochem. 65, 1431-1444
    • (1995) J. Neurochem. , vol.65 , pp. 1431-1444
    • Checler, F.1
  • 4
    • 0027478347 scopus 로고
    • Evidence for excitoprotective and intraneuronal calcium-regulating roles for secreted forms of the β-amyloid precursor protein
    • DOI 10.1016/0896-6273(93)90315-I
    • Mattson, M. P., Cheng, B., Culwell, A. R., Esch, F. S., Lieberburg, I., and Rydel, R. E. (1993) Evidence for excitoprotective and intraneuronal calcium-regulating roles for secreted forms of the β-amyloid precursor protein. Neuron 10, 243-254 (Pubitemid 23079546)
    • (1993) Neuron , vol.10 , Issue.2 , pp. 243-254
    • Mattson, M.P.1    Cheng, B.2    Culwell, A.R.3    Esch, F.S.4    Lieberburg, I.5    Rydel, R.E.6
  • 5
    • 0028169905 scopus 로고
    • Secreted forms of β-amyloid precursor protein protect hippocampal neurons against amyloid β-peptide-induced oxidative injury
    • Goodman, Y., and Mattson, M. P. (1994) Secreted forms of β-amyloid precursor protein protect hippocampal neurons against amyloid β-peptide-induced oxidative injury. Exp. Neurol. 128, 1-12
    • (1994) Exp. Neurol. , vol.128 , pp. 1-12
    • Goodman, Y.1    Mattson, M.P.2
  • 6
    • 0030763739 scopus 로고    scopus 로고
    • Synaptic β-amyloid precursor proteins increase with learning capacity in rats
    • DOI 10.1016/S0306-4522(97)00120-6, PII S0306452297001206
    • Huber, G., Bailly, Y., Martin, J. R., Mariani, J., and Brugg, B. (1997) Synaptic β-amyloid precursor proteins increase with learning capacity in rats. Neuroscience 80, 313-320 (Pubitemid 27334583)
    • (1997) Neuroscience , vol.80 , Issue.2 , pp. 313-320
    • Huber, G.1    Bailly, Y.2    Martin, J.R.3    Mariani, J.4    Brugg, B.5
  • 9
    • 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
  • 10
    • 0028297994 scopus 로고
    • A glycosylphosphatidylinositol (GPI)-negative phenotype produced in Leishmania major by GPI phospholipase C from Trypanosoma brucei: Topography of two GPI pathways
    • Mensa-Wilmot, K., LeBowitz, J. H., Chang, K. P., al-Qahtani, A., McGwire, B. S., Tucker, S., and Morris, J. C. (1994) A glycosylphosphatidylinositol (GPI)-negative phenotype produced in Leishmania major by GPI phospholipase C from Trypanosoma brucei: topography of two GPI pathways. J. Cell Biol. 124, 935-947 (Pubitemid 24109396)
    • (1994) Journal of Cell Biology , vol.124 , Issue.6 , pp. 935-947
    • Mensa-Wilmot, K.1    LeBowitz, J.H.2    Chang, K.-P.3    Al-Qahtani, A.4    McGwire, B.S.5    Tucker, S.6    Morris, J.C.7
  • 11
    • 0034634655 scopus 로고    scopus 로고
    • Phorbol ester-regulated cleavage of normal prion protein in HEK293 human cells and murine neurons
    • Vincent, B., Paitel, E., Frobert, Y., Lehmann, S., Grassi, J., and Checler, F. (2000) Phorbol ester-regulated cleavage of normal prion protein in HEK293 human cells and murine neurons. J. Biol. Chem. 275, 35612-35616
    • (2000) J. Biol. Chem. , vol.275 , pp. 35612-35616
    • Vincent, B.1    Paitel, E.2    Frobert, Y.3    Lehmann, S.4    Grassi, J.5    Checler, F.6
  • 12
    • 0035851151 scopus 로고    scopus 로고
    • The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein
    • Vincent, B., Paitel, E., Saftig, P., Frobert, Y., Hartmann, D., De Strooper, B., Grassi, J., Lopez-Perez, E., and Checler, F. (2001) The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein. J. Biol. Chem. 276, 37743-37746
    • (2001) J. Biol. Chem. , vol.276 , pp. 37743-37746
    • Vincent, B.1    Paitel, E.2    Saftig, P.3    Frobert, Y.4    Hartmann, D.5    De Strooper, B.6    Grassi, J.7    Lopez-Perez, E.8    Checler, F.9
  • 13
    • 42149140619 scopus 로고    scopus 로고
    • c cleavage by α-secretase: Mechanistic and therapeutic perspectives
    • DOI 10.2174/156720508783954749
    • Vincent, B., Cisse, M. A., Sunyach, C., Guillot-Sestier, M. V., and Checler, F. (2008) Regulation of βAPP and PrPc cleavage by α-secretase: mechanistic and therapeutic perspectives. Curr. Alzheimer Res. 5, 202-211 (Pubitemid 351536345)
    • (2008) Current Alzheimer Research , vol.5 , Issue.2 , pp. 202-211
    • Vincent, B.1    Cisse, M.A.2    Sunyach, C.3    Guillot-Sestier, M.-V.4    Checler, F.5
  • 15
    • 34247115682 scopus 로고    scopus 로고
    • 3 muscarinic receptors control physiological processing of cellular prion by modulating ADAM17 phosphorylation and activity
    • DOI 10.1523/JNEUROSCI.5293-06.2007
    • Alfa Cissé, M., Sunyach, C., Slack, B. E., Fisher, A., Vincent, B., and Checler, F. (2007) M1 and M3 muscarinic receptors control physiological processing of cellular prion by modulating ADAM17 phosphorylation and activity. J. Neurosci. 27, 4083-4092 (Pubitemid 46597172)
    • (2007) Journal of Neuroscience , vol.27 , Issue.15 , pp. 4083-4092
    • Cisse, M.A.1    Sunyach, C.2    Slack, B.E.3    Fisher, A.4    Vincent, B.5    Checler, F.6
  • 16
    • 80051685988 scopus 로고    scopus 로고
    • The extracellular regulated kinase-1 (ERK1) controls regulated α-secretase-mediated processing, promoter transactivation, and mRNA levels of the cellular prion protein
    • Cissé, M., Duplan, E., Guillot-Sestier, M. V., Rumigny, J., Bauer, C., Pagès, G., Orzechowski, H. D., Slack, B. E., Checler, F., and Vincent, B. (2011) The extracellular regulated kinase-1 (ERK1) controls regulated α-secretase-mediated processing, promoter transactivation, and mRNA levels of the cellular prion protein. J. Biol. Chem. 286, 29192-29206
    • (2011) J. Biol. Chem. , vol.286 , pp. 29192-29206
    • Cissé, M.1    Duplan, E.2    Guillot-Sestier, M.V.3    Rumigny, J.4    Bauer, C.5    Pagès, G.6    Orzechowski, H.D.7    Slack, B.E.8    Checler, F.9    Vincent, B.10
  • 17
    • 79957646992 scopus 로고    scopus 로고
    • ERK1-independent α-secretase cut of β-amyloid precursor protein via M1 muscarinic receptors and PKCα/ε
    • Cisse, M., Braun, U., Leitges, M., Fisher, A., Pages, G., Checler, F., and Vincent, B. (2011) ERK1-independent α-secretase cut of β-amyloid precursor protein via M1 muscarinic receptors and PKCα/ε. Mol. Cell. Neurosci. 47, 223-232
    • (2011) Mol. Cell. Neurosci. , vol.47 , pp. 223-232
    • Cisse, M.1    Braun, U.2    Leitges, M.3    Fisher, A.4    Pages, G.5    Checler, F.6    Vincent, B.7
  • 18
    • 72149127389 scopus 로고    scopus 로고
    • The β-secretase-derived N-terminal product of cellular prion, N1, displays neuroprotective function in vitro and in vivo
    • Guillot-Sestier, M. V., Sunyach, C., Druon, C., Scarzello, S., and Checler, F. (2009) The β-secretase-derived N-terminal product of cellular prion, N1, displays neuroprotective function in vitro and in vivo. J. Biol. Chem. 284, 35973-35986
    • (2009) J. Biol. Chem. , vol.284 , pp. 35973-35986
    • Guillot-Sestier, M.V.1    Sunyach, C.2    Druon, C.3    Scarzello, S.4    Checler, F.5
  • 20
    • 0035736326 scopus 로고    scopus 로고
    • Endogenous β-amyloid production in presenilin-deficient embryonic mouse fibroblasts
    • DOI 10.1038/ncb1101-1030
    • Armogida, M., Petit, A., Vincent, B., Scarzello, S., da Costa, C. A., and Checler, F. (2001) Endogenous β-amyloid production in presenilin-deficient embryonic mouse fibroblasts. Nat. Cell Biol. 3, 1030-1033 (Pubitemid 34428750)
    • (2001) Nature Cell Biology , vol.3 , Issue.11 , pp. 1030-1033
    • Armogida, M.1    Petit, A.2    Vincent, B.3    Scarzello, S.4    Da, C.C.A.5    Checler, F.6
  • 24
    • 33846024069 scopus 로고    scopus 로고
    • The low density lipoprotein receptor-related protein functions as an endocytic receptor for decorin
    • DOI 10.1074/jbc.M602919200
    • Brandan, E., Retamal, C., Cabello-Verrugio, C., and Marzolo, M. P. (2006) The low density lipoprotein receptor-related protein functions as an endocytic receptor for decorin. J. Biol. Chem. 281, 31562-31571 (Pubitemid 46041422)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.42 , pp. 31562-31571
    • Brandan, E.1    Retamal, C.2    Cabello-Verrugio, C.3    Marzolo, M.-P.4
  • 25
    • 0029781361 scopus 로고    scopus 로고
    • Distinct properties of neuronal and astrocytic endopeptidase 3.4.24.16: A study on differentiation, subcellular distribution, and secretion processes
    • Vincent, B., Beaudet, A., Dauch, P., Vincent, J. P., and Checler, F. (1996) Distinct properties of neuronal and astrocytic endopeptidase 3.4.24.16: a study on differentiation, subcellular distribution, and secretion processes. J. Neurosci. 16, 5049-5059 (Pubitemid 26269665)
    • (1996) Journal of Neuroscience , vol.16 , Issue.16 , pp. 5049-5059
    • Vincent, B.1    Beaudet, A.2    Dauch, P.3    Vincent, J.-P.4    Checler, F.5
  • 27
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
    • DOI 10.1038/416535a
    • Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., and Selkoe, D. J. (2002) Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416, 535-539 (Pubitemid 34288854)
    • (2002) Nature , vol.416 , Issue.6880 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6    Rowan, M.J.7    Selkoe, D.J.8
  • 29
    • 0036932412 scopus 로고    scopus 로고
    • Solution studies and structural model of the extracellular domain of the human amyloid precursor protein
    • Gralle, M., Botelho, M. M., de Oliveira, C. L., Torriani, I., and Ferreira, S. T. (2002) Solution studies and structural model of the extracellular domain of the human amyloid precursor protein. Biophys. J. 83, 3513-3524 (Pubitemid 36041968)
    • (2002) Biophysical Journal , vol.83 , Issue.6 , pp. 3513-3524
    • Gralle, M.1    Botelho, M.M.2    De Oliveira, C.L.P.3    Torriani, I.4    Ferreira, S.T.5
  • 30
    • 0031194489 scopus 로고    scopus 로고
    • Expression of human amyloid precursor protein ectodomains in pichia pastoris: Analysis of culture conditions, purification, and characterization
    • DOI 10.1006/prep.1997.0748
    • Henry, A., Masters, C. L., Beyreuther, K., and Cappai, R. (1997) Expression of human amyloid precursor protein ectodomains in Pichia pastoris: analysis of culture conditions, purification, and characterization. Protein Expr. Purif. 10, 283-291 (Pubitemid 27288793)
    • (1997) Protein Expression and Purification , vol.10 , Issue.2 , pp. 283-291
    • Henry, A.1    Masters, C.L.2    Beyreuther, K.3    Cappai, R.4
  • 31
    • 67449110951 scopus 로고    scopus 로고
    • Pharmacological evidences for DFK167-sensitive presenilin-independent γ-secretase-like activity
    • Sevalle, J., Ayral, E., Hernandez, J. F., Martinez, J., and Checler, F. (2009) Pharmacological evidences for DFK167-sensitive presenilin-independent γ-secretase-like activity. J. Neurochem. 110, 275-283
    • (2009) J. Neurochem. , vol.110 , pp. 275-283
    • Sevalle, J.1    Ayral, E.2    Hernandez, J.F.3    Martinez, J.4    Checler, F.5
  • 32
    • 84934441666 scopus 로고    scopus 로고
    • Isolation of low-n amyloid β-protein oligomers from cultured cells, CSF, and brain
    • Shankar, G. M., Welzel, A. T., McDonald, J. M., Selkoe, D. J., and Walsh, D. M. (2011) Isolation of low-n amyloid β-protein oligomers from cultured cells, CSF, and brain. Methods Mol. Biol. 670, 33-44
    • (2011) Methods Mol. Biol. , vol.670 , pp. 33-44
    • Shankar, G.M.1    Welzel, A.T.2    McDonald, J.M.3    Selkoe, D.J.4    Walsh, D.M.5
  • 33
    • 14444267540 scopus 로고    scopus 로고
    • Characterization of new polyclonal antibodies specific for 40 and 42 amino acid-long amyloid β peptides: Their use to examine the cell biology of presenilins and the immunohistochemistry of sporadic Alzheimer's disease and cerebral amyloid angiopathy cases
    • Barelli, H., Lebeau, A., Vizzavona, J., Delaere, P., Chevallier, N., Drouot, C., Marambaud, P., Ancolio, K., Buxbaum, J. D., Khorkova, O., Heroux, J., Sahasrabudhe, S., Martinez, J., Warter, J. M., Mohr, M., and Checler, F. (1997) Characterization of new polyclonal antibodies specific for 40 and 42 amino acid-long amyloid β peptides: their use to examine the cell biology of presenilins and the immunohistochemistry of sporadic Alzheimer's disease and cerebral amyloid angiopathy cases. Mol. Med. 3, 695-707 (Pubitemid 28008375)
    • (1997) Molecular Medicine , vol.3 , Issue.10 , pp. 695-707
    • Barelli, H.1    Lebeau, A.2    Vizzavona, J.3    Delaere, P.4    Chevallier, N.5    Drouot, C.6    Marambaud, P.7    Ancolio, K.8    Buxbaum, J.D.9    Khorkova, O.10    Heroux, J.11    Sahasrabudhe, S.12    Martinez, J.13    Warter, J.-M.14    Mohr, M.15    Checler, F.16
  • 35
    • 0037830752 scopus 로고    scopus 로고
    • BACE1- and BACE2-expressing human cells: Characterization of β-amyloid precursor protein-derived catabolites, design of a novel fluorimetric assay, and identification of new in vitro inhibitors
    • DOI 10.1074/jbc.M302622200
    • Andrau, D., Dumanchin-Njock, C., Ayral, E., Vizzavona, J., Farzan, M., Boisbrun, M., Fulcrand, P., Hernandez, J. F., Martinez, J., Lefranc-Jullien, S., and Checler, F. (2003) BACE1- and BACE2-expressing human cells: characterization of β-amyloid precursor protein-derived catabolites, design of a novel fluorimetric assay, and identification of new in vitro inhibitors. J. Biol. Chem. 278, 25859-25866 (Pubitemid 36835346)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.28 , pp. 25859-25866
    • Andrau, D.1    Dumanchin-Njock, C.2    Ayral, E.3    Vizzavona, J.4    Farzan, M.5    Boisbrun, M.6    Fulcrand, P.7    Hernandez, J.-F.8    Martinez, J.9    Lefranc-Jullien, S.10    Checler, F.11
  • 37
    • 0034604583 scopus 로고    scopus 로고
    • Wild-type but not Parkinson's disease-related Ala-53 → Thr mutant α-Synuclein protects neuronal cells from apoptotic stimuli
    • DOI 10.1074/jbc.M002413200
    • da Costa, C. A., Ancolio, K., and Checler, F. (2000) Wild-type but not Parkinson's disease-related Ala-53 → Thr mutant α-synuclein protects neuronal cells from apoptotic stimuli. J. Biol. Chem. 275, 24065-24069 (Pubitemid 30624697)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.31 , pp. 24065-24069
    • Da, C.C.A.1    Ancolio, K.2    Checler, F.3
  • 39
    • 0347683432 scopus 로고    scopus 로고
    • Primary Cultured Neurons Devoid of Cellular Prion Display Lower Responsiveness to Staurosporine through the Control of p53 at Both Transcriptional and Post-transcriptional Levels
    • DOI 10.1074/jbc.M310453200
    • Paitel, E., Sunyach, C., Alves da Costa, C., Bourdon, J. C., Vincent, B., and Checler, F. (2004) Primary cultured neurons devoid of cellular prion display lower responsiveness to staurosporine through the control of p53 at both transcriptional and post-transcriptional levels. J. Biol. Chem. 279, 612-618 (Pubitemid 38044865)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.1 , pp. 612-618
    • Paitel, E.1    Sunyach, C.2    Da, C.C.A.3    Bourdon, J.-C.4    Vincent, B.5    Checler, F.6
  • 40
    • 33847299070 scopus 로고    scopus 로고
    • The C-terminal products of cellular prion protein processing, C1 and C2, exert distinct influence on p53-dependent staurosporine-induced caspase-3 activation
    • DOI 10.1074/jbc.M609663200
    • Sunyach, C., Cisse, M. A., da Costa, C. A., Vincent, B., and Checler, F. (2007) The C-terminal products of cellular prion protein processing, C1 and C2, exert distinct influence on p53-dependent staurosporine-induced caspase-3 activation. J. Biol. Chem. 282, 1956-1963 (Pubitemid 47076732)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.3 , pp. 1956-1963
    • Sunyach, C.1    Cisse, M.A.2    Da, C.C.A.3    Vincent, B.4    Checler, F.5
  • 43
    • 33846953615 scopus 로고    scopus 로고
    • The low-density lipoprotein receptor-related protein 1 (LRP1) mediates the endocytosis of the cellular prion protein
    • Taylor, D. R., and Hooper, N. M. (2007) The low-density lipoprotein receptor-related protein 1 (LRP1) mediates the endocytosis of the cellular prion protein. Biochem. J. 402, 17-23
    • (2007) Biochem. J. , vol.402 , pp. 17-23
    • Taylor, D.R.1    Hooper, N.M.2
  • 45
    • 71749107981 scopus 로고    scopus 로고
    • Low density lipoprotein receptor-related protein 1 promotes anti-apoptotic signaling in neurons by activating Akt survival pathway
    • Fuentealba, R. A., Liu, Q., Kanekiyo, T., Zhang, J., and Bu, G. (2009) Low density lipoprotein receptor-related protein 1 promotes anti-apoptotic signaling in neurons by activating Akt survival pathway. J. Biol. Chem. 284, 34045-34053
    • (2009) J. Biol. Chem. , vol.284 , pp. 34045-34053
    • Fuentealba, R.A.1    Liu, Q.2    Kanekiyo, T.3    Zhang, J.4    Bu, G.5
  • 46
    • 2942604376 scopus 로고    scopus 로고
    • The γ-secretase complex: Machinery for intramembrane proteolysis
    • Iwatsubo, T. (2004) The γ-secretase complex: machinery for intramembrane proteolysis. Curr. Opin. Neurobiol. 14, 379-383
    • (2004) Curr. Opin. Neurobiol. , vol.14 , pp. 379-383
    • Iwatsubo, T.1
  • 50
    • 82355192272 scopus 로고    scopus 로고
    • The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer's disease
    • Ferreira, S. T., and Klein, W. L. (2011) The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer's disease. Neurobiol. Learn. Mem. 96, 529-543
    • (2011) Neurobiol. Learn. Mem. , vol.96 , pp. 529-543
    • Ferreira, S.T.1    Klein, W.L.2
  • 51
    • 34248190279 scopus 로고    scopus 로고
    • Aβ oligomers - A decade of discovery
    • Walsh, D. M., and Selkoe, D. J. (2007) Aβ oligomers - a decade of discovery. J. Neurochem. 101, 1172-1184
    • (2007) J. Neurochem. , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 52
    • 0037017399 scopus 로고    scopus 로고
    • 1-42 through p53 and Bax in cultured primary human neurons
    • DOI 10.1083/jcb.200110119
    • Zhang, Y., McLaughlin, R., Goodyer, C., and LeBlanc, A. (2002) Selective cytotoxicity of intracellular amyloid β peptide1-42 through p53 and Bax in cultured primary human neurons. J. Cell Biol. 156, 519-529 (Pubitemid 34839899)
    • (2002) Journal of Cell Biology , vol.156 , Issue.3 , pp. 519-529
    • Zhang, Y.1    McLaughlin, R.2    Goodyer, C.3    LeBlanc, A.4
  • 53
    • 69749122264 scopus 로고    scopus 로고
    • Evidence of molecular links between PKR and mTOR signalling pathways in Aβ neurotoxicity: Role of p53, Redd1 and TSC2
    • Morel, M., Couturier, J., Pontcharraud, R., Gil, R., Fauconneau, B., Paccalin, M., and Page, G. (2009) Evidence of molecular links between PKR and mTOR signalling pathways in Aβ neurotoxicity: role of p53, Redd1 and TSC2. Neurobiol. Dis. 36, 151-161
    • (2009) Neurobiol. Dis. , vol.36 , pp. 151-161
    • Morel, M.1    Couturier, J.2    Pontcharraud, R.3    Gil, R.4    Fauconneau, B.5    Paccalin, M.6    Page, G.7
  • 55
    • 0036285116 scopus 로고    scopus 로고
    • Phosphatidylinositol-3-kinase-Akt kinase and p42/p44 mitogen-activated protein kinases mediate neurotrophic and excitoprotective actions of a secreted form of amyloid precursor protein
    • DOI 10.1006/exnr.2002.7920
    • Cheng, G., Yu, Z., Zhou, D., and Mattson, M. P. (2002) Phosphatidylinositol-3-kinase-Akt kinase and p42/p44 mitogen-activated protein kinases mediate neurotrophic and excitoprotective actions of a secreted form of amyloid precursor protein. Exp. Neurol. 175, 407-414 (Pubitemid 34634294)
    • (2002) Experimental Neurology , vol.175 , Issue.2 , pp. 407-414
    • Cheng, G.1    Yu, Z.2    Zhou, D.3    Mattson, M.P.4
  • 56
    • 79956320988 scopus 로고    scopus 로고
    • Age-dependent accumulation of soluble amyloid β (Aβ) oligomers reverses the neuroprotective effect of soluble amyloid precursor protein-α (sAPPα) by modulating phosphatidylinositol 3-kinase (PI3K)/Akt-GSK- 3β pathway in Alzheimer mouse model
    • Jimenez, S., Torres, M., Vizuete, M., Sanchez-Varo, R., Sanchez-Mejias, E., Trujillo-Estrada, L., Carmona-Cuenca, I., Caballero, C., Ruano, D., Gutierrez, A., and Vitorica, J. (2011) Age-dependent accumulation of soluble amyloid β (Aβ) oligomers reverses the neuroprotective effect of soluble amyloid precursor protein-α (sAPPα) by modulating phosphatidylinositol 3-kinase (PI3K)/Akt-GSK-3β pathway in Alzheimer mouse model. J. Biol. Chem. 286, 18414-18425
    • (2011) J. Biol. Chem. , vol.286 , pp. 18414-18425
    • Jimenez, S.1    Torres, M.2    Vizuete, M.3    Sanchez-Varo, R.4    Sanchez-Mejias, E.5    Trujillo-Estrada, L.6    Carmona-Cuenca, I.7    Caballero, C.8    Ruano, D.9    Gutierrez, A.10    Vitorica, J.11
  • 57
    • 0029128232 scopus 로고
    • LDL receptor-related protein, a multifunctional ApoE receptor, binds secreted β-amyloid precursor protein and mediates its degradation
    • Kounnas, M. Z., Moir, R. D., Rebeck, G. W., Bush, A. I., Argraves, W. S., Tanzi, R. E., Hyman, B. T., and Strickland, D. K. (1995) LDL receptor-related protein, a multifunctional ApoE receptor, binds secreted β-amyloid precursor protein and mediates its degradation. Cell 82, 331-340
    • (1995) Cell , vol.82 , pp. 331-340
    • Kounnas, M.Z.1    Moir, R.D.2    Rebeck, G.W.3    Bush, A.I.4    Argraves, W.S.5    Tanzi, R.E.6    Hyman, B.T.7    Strickland, D.K.8
  • 59
    • 61349201380 scopus 로고    scopus 로고
    • Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers
    • Laurén, J., Gimbel, D. A., Nygaard, H. B., Gilbert, J. W., and Strittmatter, S. M. (2009) Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers. Nature 457, 1128-1132
    • (2009) Nature , vol.457 , pp. 1128-1132
    • Laurén, J.1    Gimbel, D.A.2    Nygaard, H.B.3    Gilbert, J.W.4    Strittmatter, S.M.5
  • 60
    • 70449629657 scopus 로고    scopus 로고
    • Cellular prion protein mediates the toxicity of β-amyloid oligomers: Implications for Alzheimer disease
    • Nygaard, H. B., and Strittmatter, S. M. (2009) Cellular prion protein mediates the toxicity of β-amyloid oligomers: implications for Alzheimer disease. Arch. Neurol. 66, 1325-1328
    • (2009) Arch. Neurol. , vol.66 , pp. 1325-1328
    • Nygaard, H.B.1    Strittmatter, S.M.2
  • 61
    • 77956965281 scopus 로고    scopus 로고
    • Prion protein in Alzheimer's pathogenesis: A hot and controversial issue
    • Benilova, I., and De Strooper, B. (2010) Prion protein in Alzheimer's pathogenesis: a hot and controversial issue. EMBO Mol. Med. 2, 289-290
    • (2010) EMBO Mol. Med. , vol.2 , pp. 289-290
    • Benilova, I.1    De Strooper, B.2
  • 63
    • 79960660843 scopus 로고    scopus 로고
    • Ablation of cellular prion protein does not ameliorate abnormal neural network activity or cognitive dysfunction in the J20 line of human amyloid precursor protein transgenic mice
    • Cissé, M., Sanchez, P. E., Kim, D. H., Ho, K., Yu, G. Q., and Mucke, L. (2011) Ablation of cellular prion protein does not ameliorate abnormal neural network activity or cognitive dysfunction in the J20 line of human amyloid precursor protein transgenic mice. J. Neurosci. 31, 10427-10431
    • (2011) J. Neurosci. , vol.31 , pp. 10427-10431
    • Cissé, M.1    Sanchez, P.E.2    Kim, D.H.3    Ho, K.4    Yu, G.Q.5    Mucke, L.6
  • 64
    • 77955617917 scopus 로고    scopus 로고
    • The prion protein as a receptor for amyloid-β
    • discussion E4-E5
    • Kessels, H. W., Nguyen, L. N., Nabavi, S., and Malinow, R. (2010) The prion protein as a receptor for amyloid-β. Nature 466, E3-E4; discussion E4-E5
    • (2010) Nature , vol.466
    • Kessels, H.W.1    Nguyen, L.N.2    Nabavi, S.3    Malinow, R.4
  • 65
    • 77956197815 scopus 로고    scopus 로고
    • Interaction between human prion protein and amyloid-β (Aβ) oligomers: Role of N-terminal residues
    • Chen, S., Yadav, S. P., and Surewicz, W. K. (2010) Interaction between human prion protein and amyloid-β (Aβ) oligomers: role of N-terminal residues. J. Biol. Chem. 285, 26377-26383
    • (2010) J. Biol. Chem. , vol.285 , pp. 26377-26383
    • Chen, S.1    Yadav, S.P.2    Surewicz, W.K.3
  • 67
    • 33344458827 scopus 로고    scopus 로고
    • M1 receptors play a central role in modulating AD-like pathology in transgenic mice
    • DOI 10.1016/j.neuron.2006.01.020, PII S0896627306000730
    • Caccamo, A., Oddo, S., Billings, L. M., Green, K. N., Martinez-Coria, H., Fisher, A., and LaFerla, F. M. (2006) M1 receptors play a central role in modulating AD-like pathology in transgenic mice. Neuron 49, 671-682 (Pubitemid 43290127)
    • (2006) Neuron , vol.49 , Issue.5 , pp. 671-682
    • Caccamo, A.1    Oddo, S.2    Billings, L.M.3    Green, K.N.4    Martinez-Coria, H.5    Fisher, A.6    LaFerla, F.M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.