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Volumn 1471, Issue , 2012, Pages 102-117

Dopamine induces apoptosis in APPswe-expressing Neuro2A cells following Pepstatin-sensitive proteolysis of APP in acid compartments

Author keywords

Alzheimer's disease; Chloroquine; Lysosome; Parkinson's disease; Pepstatin A

Indexed keywords

AMYLOID PRECURSOR PROTEIN; DOPAMINE; GAMMA SECRETASE INHIBITOR; PEPSTATIN; PHORBOL ESTER;

EID: 84864684593     PISSN: 00068993     EISSN: 18726240     Source Type: Journal    
DOI: 10.1016/j.brainres.2012.06.025     Document Type: Article
Times cited : (17)

References (63)
  • 1
    • 67949118809 scopus 로고    scopus 로고
    • Effect of dioxins on regulation of tyrosine hydroxylase gene expression by aryl hydrocarbon receptor: A neurotoxicology study
    • E. Akahoshi, S. Yoshimura, and S. Uruno Effect of dioxins on regulation of tyrosine hydroxylase gene expression by aryl hydrocarbon receptor: a neurotoxicology study Environ. Health 8 2009 24
    • (2009) Environ. Health , vol.8 , pp. 24
    • Akahoshi, E.1    Yoshimura, S.2    Uruno, S.3
  • 3
    • 0032515813 scopus 로고    scopus 로고
    • Hydroxychloroquine and retinal safety
    • J.A. Block Hydroxychloroquine and retinal safety Lancet 351 1998 771 (Pubitemid 28112335)
    • (1998) Lancet , vol.351 , Issue.9105 , pp. 771
    • Block, J.A.1
  • 4
    • 17644392127 scopus 로고    scopus 로고
    • The pathology of the substantia nigra in Alzheimer disease with extrapyramidal signs
    • J.M. Burns, J.E. Galvin, and C.M. Roe The pathology of the substantia nigra in Alzheimer disease with extrapyramidal signs Neurology 64 2005 1397 1403 (Pubitemid 40570508)
    • (2005) Neurology , vol.64 , Issue.8 , pp. 1397-1403
    • Burns, J.M.1    Galvin, J.E.2    Roe, C.M.3    Morris, J.C.4    McKeel, D.W.5
  • 6
    • 0026589836 scopus 로고
    • Chloroquine inhibits intracellular degradation but not secretion of Alzheimer beta/A4 amyloid precursor protein
    • G.L. Caporaso, S.E. Gandy, and J.D. Buxbaum Chloroquine inhibits intracellular degradation but not secretion of Alzheimer beta/A4 amyloid precursor protein Proc. Natl. Acad. Sci. U.S.A. 89 1992 2252 2256
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 2252-2256
    • Caporaso, G.L.1    Gandy, S.E.2    Buxbaum, J.D.3
  • 7
    • 0028351791 scopus 로고
    • Morphologic and biochemical analysis of the intracellular trafficking of the Alzheimer beta/A4 amyloid precursor protein
    • G.L. Caporaso, K. Takei, and S.E. Gandy Morphologic and biochemical analysis of the intracellular trafficking of the Alzheimer beta/A4 amyloid precursor protein J. Neurosci. 14 1994 3122 3138
    • (1994) J. Neurosci. , vol.14 , pp. 3122-3138
    • Caporaso, G.L.1    Takei, K.2    Gandy, S.E.3
  • 8
    • 77955865105 scopus 로고    scopus 로고
    • Inhibition of PI3k class III-dependent autophagy prevents apoptosis and necrosis by oxidative stress in dopaminergic neuroblastoma cells
    • R. Castino, N. Bellio, and C. Follo Inhibition of PI3k class III-dependent autophagy prevents apoptosis and necrosis by oxidative stress in dopaminergic neuroblastoma cells Toxicol. Sci. 117 2010 152 162
    • (2010) Toxicol. Sci. , vol.117 , pp. 152-162
    • Castino, R.1    Bellio, N.2    Follo, C.3
  • 10
    • 20444493589 scopus 로고    scopus 로고
    • Autophagy-dependent cell survival and cell death in an autosomal dominant familial neurohypophyseal diabetes insipidus in vitro model
    • DOI 10.1096/fj.04-3163fje
    • R. Castino, C. Isidoro, and D. Murphy Autophagy-dependent cell survival and cell death in an autosomal dominant familial neurohypophyseal diabetes insipidus in vitro model FASEB J. 19 2005 1024 1026 (Pubitemid 40827739)
    • (2005) FASEB Journal , vol.19 , Issue.8 , pp. 1024-1026
    • Castino, R.1    Isidoro, C.2    Murphy, D.3
  • 12
    • 77952515576 scopus 로고    scopus 로고
    • An overview of APP processing enzymes and products
    • V.W. Chow, M.P. Mattson, and P.C. Wong An overview of APP processing enzymes and products Neuromol. Med. 12 2010 1 12
    • (2010) Neuromol. Med. , vol.12 , pp. 1-12
    • Chow, V.W.1    Mattson, M.P.2    Wong, P.C.3
  • 13
    • 0028352254 scopus 로고
    • Extrapyramidal signs and psychiatric symptoms predict faster cognitive decline in Alzheimer's disease
    • H.C. Chui, S.A. Lyness, and E. Sobel Extrapyramidal signs and psychiatric symptoms predict faster cognitive decline in Alzheimer's disease Arch. Neurol. 51 1994 676 681 (Pubitemid 24201886)
    • (1994) Archives of Neurology , vol.51 , Issue.7 , pp. 676-681
    • Chui, H.C.1    Lyness, S.A.2    Sobel, E.3    Schneider, L.S.4
  • 14
    • 0033785510 scopus 로고    scopus 로고
    • The lysosomal protease cathepsin D is efficiently sorted to and secreted from regulated secretory compartments in the rat basophilic/mast cell line RBL
    • A. Dragonetti, M. Baldassarre, and R. Castino The lysosomal protease cathepsin D is efficiently sorted to and secreted from regulated secretory compartments in the rat basophilic/mast cell line RBL J. Cell Sci. 113 2000 3289 3298
    • (2000) J. Cell Sci. , vol.113 , pp. 3289-3298
    • Dragonetti, A.1    Baldassarre, M.2    Castino, R.3
  • 15
    • 0024353924 scopus 로고
    • Characterization of muscarinic receptors: Type M2 (subtype B) on neuro-2A neuroblastoma cells
    • A. Edwards, M. Gillard, and E. Merler Characterization of muscarinic receptors: type M2 (subtype B) on neuro-2A neuroblastoma cells J. Recept. Res. 9 1989 259 270 (Pubitemid 19201669)
    • (1989) Journal of Receptor Research , vol.9 , Issue.3 , pp. 259-270
    • Edwards, A.1    Gillard, M.2    Merler, E.3
  • 16
    • 0037421206 scopus 로고    scopus 로고
    • Amyloidogenic processing of the Alzheimer β-amyloid precursor protein depends on lipid rafts
    • DOI 10.1083/jcb.200207113
    • R. Ehehalt, P. Keller, and C. Haass Amyloidogenic processing of the Alzheimer β-amyloid precursor protein depends on lipid rafts J. Cell Biol. 160 2003 113 123 (Pubitemid 36091721)
    • (2003) Journal of Cell Biology , vol.160 , Issue.1 , pp. 113-123
    • Ehehalt, R.1    Keller, P.2    Haass, C.3    Thiele, C.4    Simons, K.5
  • 17
    • 84864715995 scopus 로고    scopus 로고
    • Labeling and exocytosis of secretory compartments in RBL mastocytes by polystyrene and mesoporous silica nanoparticles
    • 2012
    • M. Ekkapongpisit, A. Giovia, and G. Nicotra Labeling and exocytosis of secretory compartments in RBL mastocytes by polystyrene and mesoporous silica nanoparticles Int. J. Nanomed. 7 2012 1829 1840 2012
    • (2012) Int. J. Nanomed. , vol.7 , pp. 1829-1840
    • Ekkapongpisit, M.1    Giovia, A.2    Nicotra, G.3
  • 19
    • 33645937614 scopus 로고    scopus 로고
    • Presenilin-dependent gamma-secretase on plasma membrane and endosomes is functionally distinct
    • A. Fukumori, M. Okochi, and S. Tagami Presenilin-dependent gamma-secretase on plasma membrane and endosomes is functionally distinct Biochemistry 45 2006 4907 4914
    • (2006) Biochemistry , vol.45 , pp. 4907-4914
    • Fukumori, A.1    Okochi, M.2    Tagami, S.3
  • 20
    • 0020420034 scopus 로고
    • Lethality and behavioral side effects of chloroquine
    • DOI 10.1097/00004714-198202000-00005
    • M.I. Good, and R.I. Shader Lethality and behavioral side effects of chloroquine J. Clin. Psychopharmacol. 2 1982 40 47 (Pubitemid 13245188)
    • (1982) Journal of Clinical Psychopharmacology , vol.2 , Issue.1 , pp. 40-47
    • Good, M.I.1    Shader, R.I.2
  • 21
    • 0028866435 scopus 로고
    • The Swedish mutation causes early-onset Alzheimer's disease by beta-secretase cleavage within the secretory pathway
    • C. Haass, C.A. Lemere, and A. Capell The Swedish mutation causes early-onset Alzheimer's disease by beta-secretase cleavage within the secretory pathway Nat. Med. 1 1995 1291 1296
    • (1995) Nat. Med. , vol.1 , pp. 1291-1296
    • Haass, C.1    Lemere, C.A.2    Capell, A.3
  • 23
    • 67649656100 scopus 로고    scopus 로고
    • Genetic cathepsin B deficiency reduces beta-amyloid in transgenic mice expressing human wild-type amyloid precursor protein
    • V.Y. Hook, M. Kindy, and T. Reinheckel Genetic cathepsin B deficiency reduces beta-amyloid in transgenic mice expressing human wild-type amyloid precursor protein Biochem. Biophys. Res. Commun. 386 2009 284 288
    • (2009) Biochem. Biophys. Res. Commun. , vol.386 , pp. 284-288
    • Hook, V.Y.1    Kindy, M.2    Reinheckel, T.3
  • 24
    • 0026079092 scopus 로고
    • Differential segregation of human and hamster cathepsin D in transfected baby-hamster kidney cells
    • C. Isidoro, M. Horst, and F.M. Baccino Differential segregation of human and hamster cathepsin D in transfected baby-hamster kidney cells Biochem. J. 273 1991 363 367
    • (1991) Biochem. J. , vol.273 , pp. 363-367
    • Isidoro, C.1    Horst, M.2    Baccino, F.M.3
  • 25
    • 0042974099 scopus 로고    scopus 로고
    • α-Synuclein pathology in Parkinson's and Alzheimer's disease brain: Incidence and topographic distribution - A pilot study
    • DOI 10.1007/s00401-003-0725-y
    • K.A. Jellinger Alpha-synuclein pathology in Parkinson's and Alzheimer's disease brain: incidence and topographic distribution - a pilot study Acta Neuropathol. 106 2003 191 201 (Pubitemid 37021251)
    • (2003) Acta Neuropathologica , vol.106 , Issue.3 , pp. 191-201
    • Jellinger, K.A.1
  • 26
    • 0025014702 scopus 로고
    • 695 mRNA is predominantly produced in rat and human brain
    • DOI 10.1016/0006-291X(90)90992-V
    • J. Kang, and B. Müller-Hill Differential splicing of Alzheimer's disease amyloid A4 precursor RNA in rat tissues: PreA4(695) mRNA is predominantly produced in rat and human brain Biochem. Biophys. Res. Commun. 166 1990 1192 1200 (Pubitemid 20068966)
    • (1990) Biochemical and Biophysical Research Communications , vol.166 , Issue.3 , pp. 1192-1200
    • Kang, J.1    Muller-Hill, B.2
  • 27
    • 0042887148 scopus 로고    scopus 로고
    • Demonstration by FRET of BACE interaction with the amyloid precursor protein at the cell surface and in early endosomes
    • DOI 10.1242/jcs.00643
    • A. Kinoshita, H. Fukumoto, and T. Shah Demonstration by FRET of BACE interaction with the amyloid precursor protein at the cell surface and in early endosomes J. Cell Sci. 116 2003 3339 3346 (Pubitemid 37038982)
    • (2003) Journal of Cell Science , vol.116 , Issue.16 , pp. 3339-3346
    • Kinoshita, A.1    Fukumoto, H.2    Shah, T.3    Whelan, C.M.4    Irizarry, M.C.5    Hyman, B.T.6
  • 28
    • 0027970181 scopus 로고
    • Induction of cholinergic differentiation with neurite sprouting by de novo biosynthesis and expression of GD3 and b-series gangliosides in Neuro2a cells
    • N. Kojima, N. Kurosawa, and T. Nishi Induction of cholinergic differentiation with neurite sprouting by de novo biosynthesis and expression of GD3 and b-series gangliosides in Neuro2a cells J. Biol. Chem. 269 1994 30451 30456 (Pubitemid 24376524)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.48 , pp. 30451-30456
    • Kojima, N.1    Kurosawa, N.2    Nishi, T.3    Hanai, N.4    Tsuji, S.5
  • 29
    • 0028276801 scopus 로고
    • Evidence that production and release of amyloid β-protein involves the endocytic pathway
    • E.H. Koo, and S.L. Squazzo Evidence that production and release of amyloid beta-protein involves the endocytic pathway J. Biol. Chem. 269 1994 17386 17389 (Pubitemid 24218009)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.26 , pp. 17386-17389
    • Koo, E.H.1    Squazzo, S.L.2
  • 30
    • 0029950149 scopus 로고    scopus 로고
    • Trafficking of cell-surface amyloid beta-protein precursor. I. Secretion, endocytosis and recycling as detected by labeled monoclonal antibody
    • E.H. Koo, S.L. Squazzo, and D.J. Selkoe Trafficking of cell-surface amyloid beta-protein precursor. I. Secretion, endocytosis and recycling as detected by labeled monoclonal antibody J. Cell Sci. 109 1996 991 998
    • (1996) J. Cell Sci. , vol.109 , pp. 991-998
    • Koo, E.H.1    Squazzo, S.L.2    Selkoe, D.J.3
  • 31
    • 77953782590 scopus 로고    scopus 로고
    • Membrane localization of beta-amyloid 1-42 in lysosomes: A possible mechanism for lysosome labilization
    • R.Q. Liu, Q.H. Zhou, and S.R. Ji Membrane localization of beta-amyloid 1-42 in lysosomes: a possible mechanism for lysosome labilization J. Biol. Chem. 285 2010 19986 19996
    • (2010) J. Biol. Chem. , vol.285 , pp. 19986-19996
    • Liu, R.Q.1    Zhou, Q.H.2    Ji, S.R.3
  • 32
    • 0028172238 scopus 로고
    • Metabolism of the Swedish amyloid precursor protein variant in Madin-Darby canine kidney cells
    • A.C. Lo, C. Haass, and S.L. Wagner Metabolism of the Swedish amyloid precursor protein variant in Madin-Darby canine kidney cells J. Biol. Chem. 269 1994 30966 30973
    • (1994) J. Biol. Chem. , vol.269 , pp. 30966-30973
    • Lo, A.C.1    Haass, C.2    Wagner, S.L.3
  • 33
    • 77952530222 scopus 로고    scopus 로고
    • Rapid and direct transport of cell surface APP to the lysosome defines a novel selective pathway
    • A. Lorenzen, J. Samosh, and K. Vandewark Rapid and direct transport of cell surface APP to the lysosome defines a novel selective pathway Mol. Brain 3 2011 11
    • (2011) Mol. Brain , vol.3 , pp. 11
    • Lorenzen, A.1    Samosh, J.2    Vandewark, K.3
  • 35
    • 0026784959 scopus 로고
    • Predictors of cognitive and functional progression in patients with probable Alzheimer's disease
    • J.A. Mortimer, B. Ebbitt, and S.P. Jun Predictors of cognitive and functional progression in patients with probable Alzheimer's disease Neurology 42 1992 1689 1696
    • (1992) Neurology , vol.42 , pp. 1689-1696
    • Mortimer, J.A.1    Ebbitt, B.2    Jun, S.P.3
  • 37
    • 79959886270 scopus 로고    scopus 로고
    • Amyloid precursor protein processing and Alzheimer's disease
    • R.J. O'Brien, and P.C. Wong Amyloid precursor protein processing and Alzheimer's disease Annu. Rev. Neurosci. 34 2011 185 204
    • (2011) Annu. Rev. Neurosci. , vol.34 , pp. 185-204
    • O'Brien, R.J.1    Wong, P.C.2
  • 39
    • 1842532328 scopus 로고    scopus 로고
    • The role of the endosomal/lysosomal system in amyloid-beta production and the pathophysiology of Alzheimer's disease: Reexamining the spatial paradox from a lysosomal perspective
    • S.H. Pasternak, J.W. Callahan, and D.J. Mahuran The role of the endosomal/lysosomal system in amyloid-beta production and the pathophysiology of Alzheimer's disease: reexamining the spatial paradox from a lysosomal perspective J. Alzheimers Dis. 6 2004 53 65 (Pubitemid 38418558)
    • (2004) Journal of Alzheimer's Disease , vol.6 , Issue.1 , pp. 53-65
    • Pasternak, S.H.1    Callahan, J.W.2    Mahuran, D.J.3
  • 40
    • 61849088987 scopus 로고    scopus 로고
    • Elucidation of O-glycosylation structures of the beta-amyloid precursor protein by liquid chromatography-mass spectrometry using electron transfer dissociation and collision induced dissociation
    • I. Perdivara, R. Petrovich, and B. Allinquant Elucidation of O-glycosylation structures of the beta-amyloid precursor protein by liquid chromatography-mass spectrometry using electron transfer dissociation and collision induced dissociation J. Proteome Res. 8 2009 631 642
    • (2009) J. Proteome Res. , vol.8 , pp. 631-642
    • Perdivara, I.1    Petrovich, R.2    Allinquant, B.3
  • 42
    • 80051553765 scopus 로고    scopus 로고
    • Alzheimer's disease neuroimaging initiative. The dynamics of cortical and hippocampal atrophy in Alzheimer disease
    • M.R. Sabuncu, R.S. Desikan, and J. Sepulcre Alzheimer's disease neuroimaging initiative. The dynamics of cortical and hippocampal atrophy in Alzheimer disease Arch. Neurol. 68 2011 1040 1048
    • (2011) Arch. Neurol. , vol.68 , pp. 1040-1048
    • Sabuncu, M.R.1    Desikan, R.S.2    Sepulcre, J.3
  • 46
    • 40149084036 scopus 로고    scopus 로고
    • Kinetic properties of cathepsin D and BACE 1 indicate the need to search for additional β-secretase candidate(s)
    • DOI 10.1515/BC.2008.025
    • I. Schechter, and E. Ziv Kinetic properties of cathepsin D and BACE 1 indicate the need to search for additional beta-secretase candidate(s) Biol. Chem. 389 2008 313 320 (Pubitemid 351329023)
    • (2008) Biological Chemistry , vol.389 , Issue.3 , pp. 313-320
    • Schechter, I.1    Ziv, E.2
  • 48
    • 0029972129 scopus 로고    scopus 로고
    • Effect of alkalizing agents on the processing of the β-amyloid precursor protein
    • DOI 10.1016/0006-8993(96)00002-9
    • G. Schrader-Fischer, and P.A. Paganetti Effect of alkalizing agents on the processing of the beta-amyloid precursor protein Brain Res. 716 1996 91 100 (Pubitemid 26155223)
    • (1996) Brain Research , vol.716 , Issue.1-2 , pp. 91-100
    • Schrader-Fischer, G.1    Paganetti, P.A.2
  • 50
    • 57649221135 scopus 로고    scopus 로고
    • Amyloid precursor protein trafficking, processing, and function
    • G. Thinakaran, and E.H. Koo Amyloid precursor protein trafficking, processing, and function J. Biol. Chem. 283 2008 29615 29619
    • (2008) J. Biol. Chem. , vol.283 , pp. 29615-29619
    • Thinakaran, G.1    Koo, E.H.2
  • 51
    • 0029942495 scopus 로고    scopus 로고
    • Metabolism of the Swedish amyloid precursor protein variant in neuro2a (N2a) cells. Evidence that cleavage at the beta-secretase site occurs in the golgi apparatus
    • G. Thinakaran, D.B. Teplow, and R. Siman Metabolism of the Swedish amyloid precursor protein variant in neuro2a (N2a) cells. Evidence that cleavage at the beta-secretase site occurs in the golgi apparatus J. Biol. Chem. 271 1996 9390 9397
    • (1996) J. Biol. Chem. , vol.271 , pp. 9390-9397
    • Thinakaran, G.1    Teplow, D.B.2    Siman, R.3
  • 53
    • 40549085336 scopus 로고    scopus 로고
    • Resveratrol-induced apoptosis depends on the lipid kinase activity of Vps34 and on the formation of autophagolysosomes
    • DOI 10.1093/carcin/bgm271
    • N.F. Trincheri, C. Follo, and G. Nicotra Resveratrol-induced apoptosis depends on the lipid kinase activity of Vps34 and on the formation of autophagolysosomes Carcinogenesis 29 2008 381 389 (Pubitemid 351359678)
    • (2008) Carcinogenesis , vol.29 , Issue.2 , pp. 381-389
    • Trincheri, N.F.1    Follo, C.2    Nicotra, G.3    Peracchio, C.4    Castino, R.5    Isidoro, C.6
  • 54
    • 34447100874 scopus 로고    scopus 로고
    • Resveratrol induces cell death in colorectal cancer cells by a novel pathway involving lysosomal cathepsin D
    • DOI 10.1093/carcin/bgl223
    • N.F. Trincheri, G. Nicotra, and C. Follo Resveratrol induces cell death in colorectal cancer cells by a novel pathway involving lysosomal cathepsin D Carcinogenesis 28 2007 922 931 (Pubitemid 47072174)
    • (2007) Carcinogenesis , vol.28 , Issue.5 , pp. 922-931
    • Trincheri, N.F.1    Nicotra, G.2    Follo, C.3    Castino, R.4    Isidoro, C.5
  • 55
    • 0035845325 scopus 로고    scopus 로고
    • Effect of hydroxychloroquine on progression of dementia in early Alzheimer's disease: An 18-month randomised, double-blind, placebo-controlled study
    • DOI 10.1016/S0140-6736(01)05623-9
    • W.A. Van Gool, H.C. Weinstein, and P. Scheltens Effect of hydroxychloroquine on progression of dementia in early Alzheimer's disease: an 18-month randomised, double-blind, placebo-controlled study Lancet 358 2001 455 460 (Pubitemid 32769852)
    • (2001) Lancet , vol.358 , Issue.9280 , pp. 455-460
    • Van Gool, W.A.1    Weinstein, H.C.2    Scheltens, P.K.3    Walstra, G.J.M.4
  • 56
    • 0033595706 scopus 로고    scopus 로고
    • Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE
    • R. Vassar, B.D. Bennett, and S. Babu-Khan Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE Science 286 1999 735 741
    • (1999) Science , vol.286 , pp. 735-741
    • Vassar, R.1    Bennett, B.D.2    Babu-Khan, S.3
  • 57
    • 77957684047 scopus 로고    scopus 로고
    • Retrieval of the Alzheimer's amyloid precursor protein from the endosome to the TGN is S655 phosphorylation state-dependent and retromer-mediated
    • S.I. Vieira, S. Rebelo, and H. Esselmann Retrieval of the Alzheimer's amyloid precursor protein from the endosome to the TGN is S655 phosphorylation state-dependent and retromer-mediated Mol. Neurodegener. 5 2010 40
    • (2010) Mol. Neurodegener. , vol.5 , pp. 40
    • Vieira, S.I.1    Rebelo, S.2    Esselmann, H.3
  • 58
    • 79955655453 scopus 로고    scopus 로고
    • Activation of the α-secretase processing of AβPP as a therapeutic approach in Alzheimer's disease
    • B. Vincent, and P. Govitrapong Activation of the α-secretase processing of AβPP as a therapeutic approach in Alzheimer's disease J. Alzheimers Dis. 24 2 2011 75 94
    • (2011) J. Alzheimers Dis. , vol.24 , Issue.2 , pp. 75-94
    • Vincent, B.1    Govitrapong, P.2
  • 60
    • 0035937153 scopus 로고    scopus 로고
    • The role of presenilins in gamma-secretase activity
    • M.S. Wolfe, and C. Haass The role of presenilins in gamma-secretase activity J. Biol. Chem. 276 2001 5413 5416
    • (2001) J. Biol. Chem. , vol.276 , pp. 5413-5416
    • Wolfe, M.S.1    Haass, C.2
  • 62
    • 0029934134 scopus 로고    scopus 로고
    • Trafficking of cell-surface amyloid β-protein precursor: II. Endocytosis, recycling, and lysosomal targeting detected by immunolocalization
    • T. Yamazaki, E.H. Koo, and D.J. Selkoe Trafficking of cell-surface amyloid beta-protein precursor. II. Endocytosis, recycling and lysosomal targeting detected by immunolocalization J. Cell Sci. 109 1996 999 1008 (Pubitemid 126477168)
    • (1996) Journal of Cell Science , vol.109 , Issue.5 , pp. 999-1008
    • Yamazaki, T.1    Koo, E.H.2    Selkoe, D.J.3
  • 63
    • 78650944520 scopus 로고    scopus 로고
    • APP processing in Alzheimer's disease
    • Y.W. Zhang, R. Thompson, and H. Zhang APP processing in Alzheimer's disease Mol. Brain 4 2011 3
    • (2011) Mol. Brain , vol.4 , pp. 3
    • Zhang, Y.W.1    Thompson, R.2    Zhang, H.3


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