메뉴 건너뛰기




Volumn 30, Issue 2, 2008, Pages 243-254

Fibrillar prion peptide PrP(106-126) treatment induces Dab1 phosphorylation and impairs APP processing and Aβ production in cortical neurons

Author keywords

Amyloidoses; Intracellular kinases; Mouse disabled 1; Neuropathology; Oxidative stress; Prion

Indexed keywords

2,3 DIHYDRO 2 OXO 3 (4,5,6,7 TETRAHYDRO 1H INDOL 2 YLMETHYLENE) 1H INDOLE 5 SULFONIC ACID DIMETHYLAMIDE; 4 AMINO 7 TERT BUTYL 5 (4 CHLOROPHENYL)PYRAZOLO[3,4 D]PYRIMIDINE; ACETYLCYSTEINE; ADAPTOR PROTEIN; AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; DAB1 PROTEIN; DIPHENYLIODONIUM SALT; FIBRILLAR PRION PEPTIDE; HERBIMYCIN A; PRION PROTEIN; PROTEIN TYROSINE KINASE; TYROSINE;

EID: 42649101642     PISSN: 09699961     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.nbd.2008.02.001     Document Type: Article
Times cited : (15)

References (57)
  • 1
    • 20344406271 scopus 로고    scopus 로고
    • Cell biology. Prion toxicity: all sail and no anchor
    • Aguzzi A. Cell biology. Prion toxicity: all sail and no anchor. Science 308 (2005) 1420-1421
    • (2005) Science , vol.308 , pp. 1420-1421
    • Aguzzi, A.1
  • 2
    • 0344197741 scopus 로고    scopus 로고
    • Regulation of protein tyrosine kinase signaling by substrate degradation during brain development
    • Arnaud L., et al. Regulation of protein tyrosine kinase signaling by substrate degradation during brain development. Mol. Cell. Biol. 23 (2003) 9293-9302
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 9293-9302
    • Arnaud, L.1
  • 3
    • 0345317906 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of Disabled-1 is essential for Reelin-stimulated activation of Akt and Src family kinases
    • Ballif B.A., et al. Tyrosine phosphorylation of Disabled-1 is essential for Reelin-stimulated activation of Akt and Src family kinases. Brain Res. Mol. Brain Res. 117 (2003) 152-159
    • (2003) Brain Res. Mol. Brain Res. , vol.117 , pp. 152-159
    • Ballif, B.A.1
  • 4
    • 33746304427 scopus 로고    scopus 로고
    • Delineating common molecular mechanisms in Alzheimer's and prion diseases
    • Barnham K.J., et al. Delineating common molecular mechanisms in Alzheimer's and prion diseases. Trends Biochem. Sci. 31 (2006) 465-472
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 465-472
    • Barnham, K.J.1
  • 5
    • 0037425581 scopus 로고    scopus 로고
    • Reelin activates SRC family tyrosine kinases in neurons
    • Bock H.H., and Herz J. Reelin activates SRC family tyrosine kinases in neurons. Curr. Biol. 13 (2003) 18-26
    • (2003) Curr. Biol. , vol.13 , pp. 18-26
    • Bock, H.H.1    Herz, J.2
  • 6
    • 0027319326 scopus 로고
    • Mice devoid of PrP are resistant to scrapie
    • Bueler H., et al. Mice devoid of PrP are resistant to scrapie. Cell 73 (1993) 1339-1347
    • (1993) Cell , vol.73 , pp. 1339-1347
    • Bueler, H.1
  • 7
    • 3142717640 scopus 로고    scopus 로고
    • The low density lipoprotein receptor-related protein 1B retains beta-amyloid precursor protein at the cell surface and reduces amyloid-beta peptide production
    • Cam J.A., et al. The low density lipoprotein receptor-related protein 1B retains beta-amyloid precursor protein at the cell surface and reduces amyloid-beta peptide production. J. Biol. Chem. 279 28 (2004) 29639-29646
    • (2004) J. Biol. Chem. , vol.279 , Issue.28 , pp. 29639-29646
    • Cam, J.A.1
  • 8
    • 1242272011 scopus 로고    scopus 로고
    • Oxidative stress activates both Src-kinases and their negative regulator Csk and induces phosphorylation of two targeting proteins for Csk: caveolin-1 and paxillin
    • Cao H., et al. Oxidative stress activates both Src-kinases and their negative regulator Csk and induces phosphorylation of two targeting proteins for Csk: caveolin-1 and paxillin. Exp. Cell Res. 294 (2004) 159-171
    • (2004) Exp. Cell Res. , vol.294 , pp. 159-171
    • Cao, H.1
  • 9
    • 0036270446 scopus 로고    scopus 로고
    • Hydrogen peroxide-mediated phosphorylation of ERK1/2, Akt/PKB and JNK in cortical neurones: dependence on Ca(2+) and PI3-kinase
    • Crossthwaite A.J., et al. Hydrogen peroxide-mediated phosphorylation of ERK1/2, Akt/PKB and JNK in cortical neurones: dependence on Ca(2+) and PI3-kinase. J. Neurochem. 80 (2002) 24-35
    • (2002) J. Neurochem. , vol.80 , pp. 24-35
    • Crossthwaite, A.J.1
  • 10
    • 0346435103 scopus 로고    scopus 로고
    • Generation of the beta-amyloid peptide and the amyloid precursor protein C-terminal fragment gamma are potentiated by FE65L1
    • Chang Y., et al. Generation of the beta-amyloid peptide and the amyloid precursor protein C-terminal fragment gamma are potentiated by FE65L1. J. Biol. Chem. 278 (2003) 51100-51107
    • (2003) J. Biol. Chem. , vol.278 , pp. 51100-51107
    • Chang, Y.1
  • 11
    • 0029379605 scopus 로고
    • Processing of the beta-amyloid precursor protein and its regulation in Alzheimer's disease
    • Checler F. Processing of the beta-amyloid precursor protein and its regulation in Alzheimer's disease. J. Neurochem. 65 (1995) 1431-1444
    • (1995) J. Neurochem. , vol.65 , pp. 1431-1444
    • Checler, F.1
  • 12
    • 0036890486 scopus 로고    scopus 로고
    • Alzheimer's and prion diseases: distinct pathologies, common proteolytic denominators
    • Checler F., and Vincent B. Alzheimer's and prion diseases: distinct pathologies, common proteolytic denominators. Trends Neurosci. 25 (2002) 616-620
    • (2002) Trends Neurosci. , vol.25 , pp. 616-620
    • Checler, F.1    Vincent, B.2
  • 13
    • 20344394154 scopus 로고    scopus 로고
    • Anchorless prion protein results in infectious amyloid disease without clinical scrapie
    • Chesebro B., et al. Anchorless prion protein results in infectious amyloid disease without clinical scrapie. Science 308 (2005) 1435-1439
    • (2005) Science , vol.308 , pp. 1435-1439
    • Chesebro, B.1
  • 14
    • 14244268498 scopus 로고    scopus 로고
    • Gamma-secretase exists on the plasma membrane as an intact complex that accepts substrates and effects intramembrane cleavage
    • Chyung J.H., et al. Gamma-secretase exists on the plasma membrane as an intact complex that accepts substrates and effects intramembrane cleavage. J. Biol. Chem. 280 (2005) 4383-4392
    • (2005) J. Biol. Chem. , vol.280 , pp. 4383-4392
    • Chyung, J.H.1
  • 15
    • 0345803941 scopus 로고    scopus 로고
    • Inhibition of receptor-mediated endocytosis demonstrates generation of amyloid beta-protein at the cell surface
    • Chyung J.H., and Selkoe D.J. Inhibition of receptor-mediated endocytosis demonstrates generation of amyloid beta-protein at the cell surface. J. Biol. Chem. 278 (2003) 51035-51043
    • (2003) J. Biol. Chem. , vol.278 , pp. 51035-51043
    • Chyung, J.H.1    Selkoe, D.J.2
  • 16
    • 18844453149 scopus 로고    scopus 로고
    • Interaction of the 106-126 prion peptide with lipid membranes and potential implication for neurotoxicity
    • Dupiereux I., et al. Interaction of the 106-126 prion peptide with lipid membranes and potential implication for neurotoxicity. Biochem. Biophys. Res. Commun. 331 (2005) 894-901
    • (2005) Biochem. Biophys. Res. Commun. , vol.331 , pp. 894-901
    • Dupiereux, I.1
  • 17
    • 0035141524 scopus 로고    scopus 로고
    • Prion protein expression in senile plaques in Alzheimer's disease
    • Ferrer I., et al. Prion protein expression in senile plaques in Alzheimer's disease. Acta Neuropathol. (Berl.). 101 (2001) 49-56
    • (2001) Acta Neuropathol. (Berl.). , vol.101 , pp. 49-56
    • Ferrer, I.1
  • 18
    • 10644226077 scopus 로고    scopus 로고
    • The neurotoxicity of prion protein (PrP) peptide 106-126 is independent of the expression level of PrP and is not mediated by abnormal PrP species
    • Fioriti L., et al. The neurotoxicity of prion protein (PrP) peptide 106-126 is independent of the expression level of PrP and is not mediated by abnormal PrP species. Mol. Cell. Neurosci. 28 (2005) 165-176
    • (2005) Mol. Cell. Neurosci. , vol.28 , pp. 165-176
    • Fioriti, L.1
  • 19
    • 0030469956 scopus 로고    scopus 로고
    • Neurotoxicity of beta-amyloid and prion peptides
    • Forloni G. Neurotoxicity of beta-amyloid and prion peptides. Curr. Opin. Neurol. 9 (1996) 492-500
    • (1996) Curr. Opin. Neurol. , vol.9 , pp. 492-500
    • Forloni, G.1
  • 20
    • 22544439039 scopus 로고    scopus 로고
    • PrP(106-126) activates neuronal intracellular kinases and Egr1 synthesis through activation of NADPH-oxidase independently of PrPc
    • Gavin R., et al. PrP(106-126) activates neuronal intracellular kinases and Egr1 synthesis through activation of NADPH-oxidase independently of PrPc. FEBS Lett. 579 (2005) 4099-4106
    • (2005) FEBS Lett. , vol.579 , pp. 4099-4106
    • Gavin, R.1
  • 21
    • 33846597049 scopus 로고    scopus 로고
    • Decreased cell surface prion protein in mouse models of prion disease
    • Griffin J.K., et al. Decreased cell surface prion protein in mouse models of prion disease. NeuroReport 18 (2007) 1-6
    • (2007) NeuroReport , vol.18 , pp. 1-6
    • Griffin, J.K.1
  • 22
    • 0036677899 scopus 로고    scopus 로고
    • Low-density lipoprotein receptor-related protein levels and endocytic function are reduced by overexpression of the FE65 adaptor protein, FE65L1
    • Guenette S.Y., et al. Low-density lipoprotein receptor-related protein levels and endocytic function are reduced by overexpression of the FE65 adaptor protein, FE65L1. J. Neurochem. 82 (2002) 755-762
    • (2002) J. Neurochem. , vol.82 , pp. 755-762
    • Guenette, S.Y.1
  • 23
    • 0031847332 scopus 로고    scopus 로고
    • Coexistence of Alzheimer-type neuropathology in Creutzfeldt-Jakob disease
    • Hainfellner J.A., et al. Coexistence of Alzheimer-type neuropathology in Creutzfeldt-Jakob disease. Acta Neuropathol. (Berl.) 96 (1998) 116-122
    • (1998) Acta Neuropathol. (Berl.) , vol.96 , pp. 116-122
    • Hainfellner, J.A.1
  • 24
    • 0032823769 scopus 로고    scopus 로고
    • Antioxidant defence mechanisms: from the beginning to the end (of the beginning)
    • Halliwell B. Antioxidant defence mechanisms: from the beginning to the end (of the beginning). Free Radic. Res. 31 (1999) 261-272
    • (1999) Free Radic. Res. , vol.31 , pp. 261-272
    • Halliwell, B.1
  • 25
    • 0027439062 scopus 로고
    • Amyloid-like properties of peptides flanking the epitope of amyloid precursor protein-specific monoclonal antibody 22C11
    • Hilbich C., et al. Amyloid-like properties of peptides flanking the epitope of amyloid precursor protein-specific monoclonal antibody 22C11. J. Biol. Chem. 268 (1993) 26571-26577
    • (1993) J. Biol. Chem. , vol.268 , pp. 26571-26577
    • Hilbich, C.1
  • 26
    • 33845925306 scopus 로고    scopus 로고
    • Dab1 and Reelin effects on APP and ApoEr2 trafficking and processing
    • Hoe H.S., et al. Dab1 and Reelin effects on APP and ApoEr2 trafficking and processing. J. Biol. Chem. 281 (2006) 35176-35185
    • (2006) J. Biol. Chem. , vol.281 , pp. 35176-35185
    • Hoe, H.S.1
  • 27
    • 0033198295 scopus 로고    scopus 로고
    • Disabled-1 binds to the cytoplasmic domain of amyloid precursor-like protein 1
    • Homayouni R., et al. Disabled-1 binds to the cytoplasmic domain of amyloid precursor-like protein 1. J. Neurosci. 19 (1999) 7507-7515
    • (1999) J. Neurosci. , vol.19 , pp. 7507-7515
    • Homayouni, R.1
  • 28
    • 0031035703 scopus 로고    scopus 로고
    • Mouse disabled (mDab1): a Src binding protein implicated in neuronal development
    • Howell B.W., et al. Mouse disabled (mDab1): a Src binding protein implicated in neuronal development. EMBO J. 16 (1997) 121-132
    • (1997) EMBO J. , vol.16 , pp. 121-132
    • Howell, B.W.1
  • 29
    • 0033559054 scopus 로고    scopus 로고
    • Reelin-induced tyrosine phosphorylation of disabled 1 during neuronal positioning
    • Howell B.W., et al. Reelin-induced tyrosine phosphorylation of disabled 1 during neuronal positioning. Genes Dev. 13 (1999) 643-648
    • (1999) Genes Dev. , vol.13 , pp. 643-648
    • Howell, B.W.1
  • 30
    • 0033066680 scopus 로고    scopus 로고
    • The disabled 1 phosphotyrosine-binding domain binds to the internalization signals of transmembrane glycoproteins and to phospholipids
    • Howell B.W., et al. The disabled 1 phosphotyrosine-binding domain binds to the internalization signals of transmembrane glycoproteins and to phospholipids. Mol. Cell. Biol. 19 (1999) 5179-5188
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5179-5188
    • Howell, B.W.1
  • 31
    • 0035844278 scopus 로고    scopus 로고
    • Identification of reelin-induced sites of tyrosyl phosphorylation on disabled 1
    • Keshvara L., et al. Identification of reelin-induced sites of tyrosyl phosphorylation on disabled 1. J. Biol. Chem. 276 (2001) 16008-16014
    • (2001) J. Biol. Chem. , vol.276 , pp. 16008-16014
    • Keshvara, L.1
  • 32
    • 0035950434 scopus 로고    scopus 로고
    • Mechanisms of prion-induced modifications in membrane transport properties: implications for signal transduction and neurotoxicity
    • Kourie J.I. Mechanisms of prion-induced modifications in membrane transport properties: implications for signal transduction and neurotoxicity. Chem. Biol. Interact 138 (2001) 1-26
    • (2001) Chem. Biol. Interact , vol.138 , pp. 1-26
    • Kourie, J.I.1
  • 33
    • 0035253564 scopus 로고    scopus 로고
    • The neurotoxic prion peptide fragment PrP(106-126) is a chemotactic agonist for the G protein-coupled receptor formyl peptide receptor-like 1
    • Le Y., et al. The neurotoxic prion peptide fragment PrP(106-126) is a chemotactic agonist for the G protein-coupled receptor formyl peptide receptor-like 1. J. Immunol. 166 (2001) 1448-1451
    • (2001) J. Immunol. , vol.166 , pp. 1448-1451
    • Le, Y.1
  • 34
    • 0037070220 scopus 로고    scopus 로고
    • Cellular prion protein: on the road for functions
    • Martins V.R., et al. Cellular prion protein: on the road for functions. FEBS Lett. 512 (2002) 25-28
    • (2002) FEBS Lett. , vol.512 , pp. 25-28
    • Martins, V.R.1
  • 35
    • 0027367765 scopus 로고
    • beta-Amyloid precursor protein metabolites and loss of neuronal Ca2+ homeostasis in Alzheimer's disease
    • Mattson M.P., et al. beta-Amyloid precursor protein metabolites and loss of neuronal Ca2+ homeostasis in Alzheimer's disease. Trends Neurosci. 16 (1993) 409-414
    • (1993) Trends Neurosci. , vol.16 , pp. 409-414
    • Mattson, M.P.1
  • 36
    • 0026559760 scopus 로고
    • Colocalization of prion protein and beta protein in the same amyloid plaques in patients with Gerstmann-Straussler syndrome
    • Miyazono M., et al. Colocalization of prion protein and beta protein in the same amyloid plaques in patients with Gerstmann-Straussler syndrome. Acta Neuropathol. (Berl.) 83 (1992) 333-339
    • (1992) Acta Neuropathol. (Berl.) , vol.83 , pp. 333-339
    • Miyazono, M.1
  • 37
    • 0034665847 scopus 로고    scopus 로고
    • Signal transduction through prion protein
    • Moulliet-Richard S., et al. Signal transduction through prion protein. Science 289 (2000) 1925-1928
    • (2000) Science , vol.289 , pp. 1925-1928
    • Moulliet-Richard, S.1
  • 38
    • 33845542144 scopus 로고    scopus 로고
    • Activation of beta2-adrenergic receptor stimulates gamma-secretase activity and accelerates amyloid plaque formation
    • Ni Y., et al. Activation of beta2-adrenergic receptor stimulates gamma-secretase activity and accelerates amyloid plaque formation. Nat. Med. 12 (2006) 1390-1396
    • (2006) Nat. Med. , vol.12 , pp. 1390-1396
    • Ni, Y.1
  • 39
    • 33846651249 scopus 로고    scopus 로고
    • Expression of mDab1 promotes the stability and processing of amyloid precursor protein and this effect is counteracted by X11alpha
    • Parisiadou L., and Efthimiopoulos S. Expression of mDab1 promotes the stability and processing of amyloid precursor protein and this effect is counteracted by X11alpha. Neurobiol. Aging 28 (2007) 377-388
    • (2007) Neurobiol. Aging , vol.28 , pp. 377-388
    • Parisiadou, L.1    Efthimiopoulos, S.2
  • 40
    • 34547400403 scopus 로고    scopus 로고
    • Cellular prion protein regulates beta-secretase cleavage of the Alzheimer's amyloid precursor protein
    • Parkin E.T., et al. Cellular prion protein regulates beta-secretase cleavage of the Alzheimer's amyloid precursor protein. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 11062-11067
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 11062-11067
    • Parkin, E.T.1
  • 41
    • 0038292054 scopus 로고    scopus 로고
    • Prion peptide induces neuronal cell death through a pathway involving glycogen synthase kinase 3
    • Perez M., et al. Prion peptide induces neuronal cell death through a pathway involving glycogen synthase kinase 3. Biochem. J. 372 (2003) 129-136
    • (2003) Biochem. J. , vol.372 , pp. 129-136
    • Perez, M.1
  • 42
    • 33748776269 scopus 로고    scopus 로고
    • Overstimulation of PrPC signaling pathways by prion peptide 106-126 causes oxidative injury of bioaminergic neuronal cells
    • Pietri M., et al. Overstimulation of PrPC signaling pathways by prion peptide 106-126 causes oxidative injury of bioaminergic neuronal cells. J. Biol. Chem. 281 (2006) 28470-28479
    • (2006) J. Biol. Chem. , vol.281 , pp. 28470-28479
    • Pietri, M.1
  • 44
    • 0030719529 scopus 로고    scopus 로고
    • A neurotoxic and gliotrophic fragment of the prion protein increases plasma membrane microviscosity
    • Salmona M., et al. A neurotoxic and gliotrophic fragment of the prion protein increases plasma membrane microviscosity. Neurobiol. Dis. 4 (1997) 47-57
    • (1997) Neurobiol. Dis. , vol.4 , pp. 47-57
    • Salmona, M.1
  • 45
    • 0033120504 scopus 로고    scopus 로고
    • Redox metals and neurodegenerative disease
    • Sayre L.M., et al. Redox metals and neurodegenerative disease. Curr. Opin. Chem. Biol. 3 (1999) 220-225
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 220-225
    • Sayre, L.M.1
  • 46
    • 2542583141 scopus 로고    scopus 로고
    • Time-controlled transcardiac perfusion cross-linking for the study of protein interactions in complex tissues
    • Schmitt-Ulms G., et al. Time-controlled transcardiac perfusion cross-linking for the study of protein interactions in complex tissues. Nat. Biotechnol. 22 (2004) 724-731
    • (2004) Nat. Biotechnol. , vol.22 , pp. 724-731
    • Schmitt-Ulms, G.1
  • 47
    • 19444386089 scopus 로고    scopus 로고
    • Prion protein (PrPc) promotes beta-amyloid plaque formation
    • Schwarze-Eicker K., et al. Prion protein (PrPc) promotes beta-amyloid plaque formation. Neurobiol. Aging 26 (2005) 1177-1182
    • (2005) Neurobiol. Aging , vol.26 , pp. 1177-1182
    • Schwarze-Eicker, K.1
  • 48
    • 0028170818 scopus 로고
    • Cell biology of the amyloid beta-protein precursor and the mechanism of Alzheimer's disease
    • Selkoe D.J. Cell biology of the amyloid beta-protein precursor and the mechanism of Alzheimer's disease. Annu. Rev. Cell Biol. 10 (1994) 373-403
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 373-403
    • Selkoe, D.J.1
  • 49
    • 33846026714 scopus 로고    scopus 로고
    • Reelin induces the detachment of postnatal subventricular zone cells and the expression of the Egr-1 through Erk1/2 activation
    • Simo S., et al. Reelin induces the detachment of postnatal subventricular zone cells and the expression of the Egr-1 through Erk1/2 activation. Cereb. Cortex 17 (2007) 294-303
    • (2007) Cereb. Cortex , vol.17 , pp. 294-303
    • Simo, S.1
  • 50
    • 0036176506 scopus 로고    scopus 로고
    • p38 MAP kinase mediates the cell death induced by PrP106-126 in the SH-SY5Y neuroblastoma cells
    • Thellung S., et al. p38 MAP kinase mediates the cell death induced by PrP106-126 in the SH-SY5Y neuroblastoma cells. Neurobiol. Dis. 9 (2002) 69-81
    • (2002) Neurobiol. Dis. , vol.9 , pp. 69-81
    • Thellung, S.1
  • 51
    • 42649083005 scopus 로고    scopus 로고
    • Tortosa, R., et al., in press. Stress response in the central nervous system of a transgenic mouse model of bovine spongiform encephalopathy. Vet. J.
    • Tortosa, R., et al., in press. Stress response in the central nervous system of a transgenic mouse model of bovine spongiform encephalopathy. Vet. J.
  • 52
    • 0032509346 scopus 로고    scopus 로고
    • Interaction of cytosolic adaptor proteins with neuronal apolipoprotein E receptors and the amyloid precursor protein
    • Trommsdorff M., et al. Interaction of cytosolic adaptor proteins with neuronal apolipoprotein E receptors and the amyloid precursor protein. J. Biol. Chem. 273 (1998) 33556-33560
    • (1998) J. Biol. Chem. , vol.273 , pp. 33556-33560
    • Trommsdorff, M.1
  • 53
    • 0035029801 scopus 로고    scopus 로고
    • Sublethal concentrations of prion peptide PrP106-126 or the amyloid beta peptide of Alzheimer's disease activates expression of proapoptotic markers in primary cortical neurons
    • White A.R., et al. Sublethal concentrations of prion peptide PrP106-126 or the amyloid beta peptide of Alzheimer's disease activates expression of proapoptotic markers in primary cortical neurons. Neurobiol. Dis. 8 (2001) 299-316
    • (2001) Neurobiol. Dis. , vol.8 , pp. 299-316
    • White, A.R.1
  • 54
    • 0037459782 scopus 로고    scopus 로고
    • Diverse fibrillar peptides directly bind the Alzheimer's amyloid precursor protein and amyloid precursor-like protein 2 resulting in cellular accumulation
    • White A.R., et al. Diverse fibrillar peptides directly bind the Alzheimer's amyloid precursor protein and amyloid precursor-like protein 2 resulting in cellular accumulation. Brain Res. 966 (2003) 231-244
    • (2003) Brain Res. , vol.966 , pp. 231-244
    • White, A.R.1
  • 55
    • 36349036676 scopus 로고    scopus 로고
    • Fe65 stimulates proteolytic liberation of the beta-amyloid precursor protein intracellular domain
    • Wiley J.C., et al. Fe65 stimulates proteolytic liberation of the beta-amyloid precursor protein intracellular domain. J. Biol. Chem. 282 (2007) 33313-33325
    • (2007) J. Biol. Chem. , vol.282 , pp. 33313-33325
    • Wiley, J.C.1
  • 56
    • 0030940607 scopus 로고    scopus 로고
    • Identification of candidate proteins binding to prion protein
    • Yehiely F., et al. Identification of candidate proteins binding to prion protein. Neurobiol. Dis. 3 (1997) 339-355
    • (1997) Neurobiol. Dis. , vol.3 , pp. 339-355
    • Yehiely, F.1
  • 57
    • 1942533538 scopus 로고    scopus 로고
    • Fe65 is not involved in the platelet-derived growth factor-induced processing of Alzheimer's amyloid precursor protein, which activates its caspase-directed cleavage
    • Zambrano N., et al. Fe65 is not involved in the platelet-derived growth factor-induced processing of Alzheimer's amyloid precursor protein, which activates its caspase-directed cleavage. J. Biol. Chem. 279 (2004) 16161-16169
    • (2004) J. Biol. Chem. , vol.279 , pp. 16161-16169
    • Zambrano, N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.