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Volumn 9, Issue 4, 2004, Pages 415-422

APP induces neuronal apoptosis through APP-BP1-mediated downregulation of β-catenin

Author keywords

Alzheimer's disease; Apoptosis; APP; NEDD8; Presenilin

Indexed keywords

AMYLOID PRECURSOR PROTEIN; BETA CATENIN;

EID: 3343020091     PISSN: 13608185     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:APPT.0000031447.05354.9f     Document Type: Short Survey
Times cited : (27)

References (91)
  • 1
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner GG, Wong CW. Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun 1984; 120(3): 885-890.
    • (1984) Biochem Biophys Res Commun , vol.120 , Issue.3 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 2
    • 0021207461 scopus 로고
    • Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein
    • Glenner GG, Wong CW. Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein. Biochem Biophys Res Commun 1984; 122(3): 1131-1135.
    • (1984) Biochem Biophys Res Commun , vol.122 , Issue.3 , pp. 1131-1135
    • Glenner, G.G.1    Wong, C.W.2
  • 3
    • 0006876721 scopus 로고
    • Hereditary cerebral hemorrhage with amyloidosis in patients of Dutch origin is related to Alzheimer disease
    • van Duinen SG, Castaño EM, Prelli F, Bots GT, Luyendijk W, Frangione B. Hereditary cerebral hemorrhage with amyloidosis in patients of Dutch origin is related to Alzheimer disease. Proc Natl Acad Sci USA 1987; 84(16): 5991-5994.
    • (1987) Proc Natl Acad Sci USA , vol.84 , Issue.16 , pp. 5991-5994
    • Van Duinen, S.G.1    Castaño, E.M.2    Prelli, F.3    Bots, G.T.4    Luyendijk, W.5    Frangione, B.6
  • 4
    • 0025296269 scopus 로고
    • Mutation of the Alzheimer's disease amyloid gene in hereditary cerebral hemorrhage, Dutch type
    • Levy E, Carman MD, Fernandez-Madrid IJ, et al. Mutation of the Alzheimer's disease amyloid gene in hereditary cerebral hemorrhage, Dutch type. Science 1990; 248(4959): 1124-1126.
    • (1990) Science , vol.248 , Issue.4959 , pp. 1124-1126
    • Levy, E.1    Carman, M.D.2    Fernandez-Madrid, I.J.3
  • 5
    • 0026088977 scopus 로고
    • Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease
    • Goate A, Chartier-Harlin MC, Mullan M, et al. Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease. Nature 1991; 349(6311): 704-706.
    • (1991) Nature , vol.349 , Issue.6311 , pp. 704-706
    • Goate, A.1    Chartier-Harlin, M.C.2    Mullan, M.3
  • 6
    • 0025950987 scopus 로고
    • A mutation in the amyloid precursor protein associated with hereditary Alzheimer's disease
    • Murrell J, Farlow M, Ghetti B, Benson MD. A mutation in the amyloid precursor protein associated with hereditary Alzheimer's disease. Science 1991; 254(5028): 97-99.
    • (1991) Science , vol.254 , Issue.5028 , pp. 97-99
    • Murrell, J.1    Farlow, M.2    Ghetti, B.3    Benson, M.D.4
  • 7
    • 0026075602 scopus 로고
    • Early-onset Alzheimer's disease caused by mutations at codon 717 of the beta-amyloid precursor protein gene
    • Chartier-Harlin MC, Crawford F, Houlden H, et al. Early-onset Alzheimer's disease caused by mutations at codon 717 of the beta-amyloid precursor protein gene. Nature 1991; 353(6347): 844-846.
    • (1991) Nature , vol.353 , Issue.6347 , pp. 844-846
    • Chartier-Harlin, M.C.1    Crawford, F.2    Houlden, H.3
  • 8
    • 0026879650 scopus 로고
    • Presenile dementia and cerebral haemorrhage linked to a mutation at codon 692 of the beta-amyloid precursor protein gene
    • Hendriks L, van Duijn CM, Cras P, et al. Presenile dementia and cerebral haemorrhage linked to a mutation at codon 692 of the beta-amyloid precursor protein gene. Nat Genet 1992; 1(3): 218-221.
    • (1992) Nat Genet , vol.1 , Issue.3 , pp. 218-221
    • Hendriks, L.1    Van Duijn, C.M.2    Cras, P.3
  • 9
    • 0026907151 scopus 로고
    • A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N-terminus of beta-amyloid
    • Mullan M, Crawford F, Axelman K, et al. A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N-terminus of beta-amyloid. Nat Genet 1992; 1(5): 345-347.
    • (1992) Nat Genet , vol.1 , Issue.5 , pp. 345-347
    • Mullan, M.1    Crawford, F.2    Axelman, K.3
  • 10
    • 0026745610 scopus 로고
    • Mutation of the beta-amyloid precursor protein in familial Alzheimer's disease increases beta-protein production
    • Citron M, Oltersdorf T, Haass C, et al. Mutation of the beta-amyloid precursor protein in familial Alzheimer's disease increases beta-protein production. Nature 1992; 360(6405): 672-674.
    • (1992) Nature , vol.360 , Issue.6405 , pp. 672-674
    • Citron, M.1    Oltersdorf, T.2    Haass, C.3
  • 11
    • 0028322017 scopus 로고
    • An increased percentage of long amyloid beta protein secreted by familial amyloid beta protein precursor (beta APP717) mutants
    • Suzuki N, Cheung TT, Cai XD, et al. An increased percentage of long amyloid beta protein secreted by familial amyloid beta protein precursor (beta APP717) mutants. Science 1994; 264(5163): 1336-1340.
    • (1994) Science , vol.264 , Issue.5163 , pp. 1336-1340
    • Suzuki, N.1    Cheung, T.T.2    Cai, X.D.3
  • 12
    • 0026088977 scopus 로고
    • Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease
    • Goate A, Chartier-Harlin MC, Mullan M, et al. Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease. Nature 1991; 349(6311): 704-706.
    • (1991) Nature , vol.349 , Issue.6311 , pp. 704-706
    • Goate, A.1    Chartier-Harlin, M.C.2    Mullan, M.3
  • 13
    • 0034329742 scopus 로고    scopus 로고
    • Apoptosis in neurodegenerative disorders
    • Mattson MP. Apoptosis in neurodegenerative disorders. Nature Rev Mol Cell Biol 2000; 1: 120-129.
    • (2000) Nature Rev Mol Cell Biol , vol.1 , pp. 120-129
    • Mattson, M.P.1
  • 14
    • 0036054030 scopus 로고    scopus 로고
    • Dysregulation of neuronal differentiation and cell cycle control in Alzheimer's disease
    • Arendt T. Dysregulation of neuronal differentiation and cell cycle control in Alzheimer's disease. J Neural Transm Suppl 2002; (62): 77-85.
    • (2002) J Neural Transm Suppl , Issue.62 , pp. 77-85
    • Arendt, T.1
  • 15
    • 0034131044 scopus 로고    scopus 로고
    • Impaired proteasome function in Alzheimer's disease
    • Keller JN, Keith BH, Markesbery WR. Impaired proteasome function in Alzheimer's disease. J Neurochem 2000; 75(1): 436-439.
    • (2000) J Neurochem , vol.75 , Issue.1 , pp. 436-439
    • Keller, J.N.1    Keith, B.H.2    Markesbery, W.R.3
  • 16
    • 0033972037 scopus 로고    scopus 로고
    • Possible involvement of proteasome inhibition in aging: Implications for oxidative stress
    • Keller JN, Hanni KB, Markesbery WR. Possible involvement of proteasome inhibition in aging: Implications for oxidative stress. Mechanisms of Aging and Dev 2000; 113: 61-70.
    • (2000) Mechanisms of Aging and Dev , vol.113 , pp. 61-70
    • Keller, J.N.1    Hanni, K.B.2    Markesbery, W.R.3
  • 17
    • 6844258835 scopus 로고    scopus 로고
    • Frameshift mutants of beta amyloid precursor protein and ubiquitin-B in Alzheimer's and Down patients
    • van Leeuwen FW, de Kleijn DP, van den Hurk HH, et al. Frameshift mutants of beta amyloid precursor protein and ubiquitin-B in Alzheimer's and Down patients. Science 1998; 279(5348): 242-247.
    • (1998) Science , vol.279 , Issue.5348 , pp. 242-247
    • Van Leeuwen, F.W.1    De Kleijn, D.P.2    Van Den Hurk, H.H.3
  • 18
    • 0034730172 scopus 로고    scopus 로고
    • Inhibition of the ubiquitin-proteasome system in Alzheimer's disease
    • Lam YA, Pickart CM, Alban A, et al. Inhibition of the ubiquitin-proteasome system in Alzheimer's disease. Proc Natl Acad Sci USA 2000; 97(18): 9902-9906.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.18 , pp. 9902-9906
    • Lam, Y.A.1    Pickart, C.M.2    Alban, A.3
  • 19
    • 15844408798 scopus 로고    scopus 로고
    • APP-BP1, a novel protein that binds to the carboxyl-termmal region of the amyloid precursor protein
    • Chow N, Korenberg JR, Chen XN, Neve RL. APP-BP1, a novel protein that binds to the carboxyl-termmal region of the amyloid precursor protein. J Biol Chem 1996; 271(19): 11339-11346.
    • (1996) J Biol Chem , vol.271 , Issue.19 , pp. 11339-11346
    • Chow, N.1    Korenberg, J.R.2    Chen, X.N.3    Neve, R.L.4
  • 20
    • 0034708641 scopus 로고    scopus 로고
    • The amyloid precursor protein-binding protein APP-BP1 drives the cell cycle through the S-M checkpoint and causes apoptosis in neurons
    • Chen Y, McPhie DL, Hirschberg J, Neve RL. The amyloid precursor protein-binding protein APP-BP1 drives the cell cycle through the S-M checkpoint and causes apoptosis in neurons. J Biol Chem 2000; 275(12): 8929-8935.
    • (2000) J Biol Chem , vol.275 , Issue.12 , pp. 8929-8935
    • Chen, Y.1    McPhie, D.L.2    Hirschberg, J.3    Neve, R.L.4
  • 21
    • 0032146145 scopus 로고    scopus 로고
    • A new NEDD8-ligating system for cullin-4A
    • Osaka F, Kawasaki H, Aida N, et al. A new NEDD8-ligating system for cullin-4A. Genes Dev 1998; 12(15): 2263-2268.
    • (1998) Genes Dev , vol.12 , Issue.15 , pp. 2263-2268
    • Osaka, F.1    Kawasaki, H.2    Aida, N.3
  • 22
    • 0033597126 scopus 로고    scopus 로고
    • Identification of the activating and conjugating enzymes of the NEDD8 conjugation pathway
    • Gong L, Yeh ET. Identification of the activating and conjugating enzymes of the NEDD8 conjugation pathway. J Biol Chem 1999; 274(17): 12036-12042.
    • (1999) J Biol Chem , vol.274 , Issue.17 , pp. 12036-12042
    • Gong, L.1    Yeh, E.T.2
  • 23
    • 0033581899 scopus 로고    scopus 로고
    • Covalent modification of all members of human cullin family proteins by NEDD8
    • Hori T, Osaka F, Chiba T, et al. Covalent modification of all members of human cullin family proteins by NEDD8. Oncogene 1999; 18(48): 6829-6834.
    • (1999) Oncogene , vol.18 , Issue.48 , pp. 6829-6834
    • Hori, T.1    Osaka, F.2    Chiba, T.3
  • 24
    • 0023623050 scopus 로고
    • Isolation of temperature-sensitive mutants
    • Hirschberg J, Marcus M. Isolation of temperature-sensitive mutants. Methods Enzymol 1987; 151: 145-150.
    • (1987) Methods Enzymol , vol.151 , pp. 145-150
    • Hirschberg, J.1    Marcus, M.2
  • 25
    • 0026460979 scopus 로고
    • The ts41 mutation in Chinese hamster cells leads to successive S phases in the absence of intervening G2, M, and G1
    • Handeli S, Weintraub H. The ts41 mutation in Chinese hamster cells leads to successive S phases in the absence of intervening G2, M, and G1. Cell 1992; 71(4): 599-611.
    • (1992) Cell , vol.71 , Issue.4 , pp. 599-611
    • Handeli, S.1    Weintraub, H.2
  • 26
    • 0035969236 scopus 로고    scopus 로고
    • The NEDD8 system is essential for cell cycle progression and morphogenetic pathway in mice
    • Tateishi K, Omata M, Tanaka K, Chiba T. The NEDD8 system is essential for cell cycle progression and morphogenetic pathway in mice. J Cell Biol 2001; 155(4): 571-579.
    • (2001) J Cell Biol , vol.155 , Issue.4 , pp. 571-579
    • Tateishi, K.1    Omata, M.2    Tanaka, K.3    Chiba, T.4
  • 27
    • 0142059983 scopus 로고    scopus 로고
    • APP-BP1 mediates APP-mduced apoptosis and DNA synthesis and is increased in Alzheimer's disease brain
    • Chen Y, Liu W, McPhie DL, Hassinger L, Neve RL. APP-BP1 mediates APP-mduced apoptosis and DNA synthesis and is increased in Alzheimer's disease brain. J Cell Biol 2003; 163(1): 27-33.
    • (2003) J Cell Biol , vol.163 , Issue.1 , pp. 27-33
    • Chen, Y.1    Liu, W.2    McPhie, D.L.3    Hassinger, L.4    Neve, R.L.5
  • 28
    • 0038673445 scopus 로고    scopus 로고
    • ASPP2 inhibits APP-BP1-mediated NEDD8 conjugation to cullin-1 and decreases APP-BP1-induced cell proliferation and neuronal apoptosis
    • Chen Y, Liu W, Naumovski L, Neve RL. ASPP2 inhibits APP-BP1-mediated NEDD8 conjugation to cullin-1 and decreases APP-BP1-induced cell proliferation and neuronal apoptosis. J Neurochem 2003; 85(3): 801-809.
    • (2003) J Neurochem , vol.85 , Issue.3 , pp. 801-809
    • Chen, Y.1    Liu, W.2    Naumovski, L.3    Neve, R.L.4
  • 29
    • 0033279836 scopus 로고    scopus 로고
    • SCF and Cullin/Ring H2-based ubiquitin ligases
    • Deshaies RJ. SCF and Cullin/Ring H2-based ubiquitin ligases. Annu Rev Cell Dev Biol 1999; 15: 435-467.
    • (1999) Annu Rev Cell Dev Biol , vol.15 , pp. 435-467
    • Deshaies, R.J.1
  • 30
    • 0033666562 scopus 로고    scopus 로고
    • F-box proteins and protein degradation: An emerging theme in cellular regulation
    • del Pozo JC, Estelle M. F-box proteins and protein degradation: An emerging theme in cellular regulation. Plant Mol Biol 2000; 44(2): 123-128.
    • (2000) Plant Mol Biol , vol.44 , Issue.2 , pp. 123-128
    • Del Pozo, J.C.1    Estelle, M.2
  • 31
    • 0029953780 scopus 로고    scopus 로고
    • cul-1 is required for cell cycle exit in C. elegans and identifies a novel gene family
    • Kipreos ET, Lander LE, Wing JP, He WW, Hedgecock EM. cul-1 is required for cell cycle exit in C. elegans and identifies a novel gene family. Cell 1996; 85(6): 829-839.
    • (1996) Cell , vol.85 , Issue.6 , pp. 829-839
    • Kipreos, E.T.1    Lander, L.E.2    Wing, J.P.3    He, W.W.4    Hedgecock, E.M.5
  • 32
    • 0036718539 scopus 로고    scopus 로고
    • Molecular basis of the VHL hereditary cancer syndrome
    • Kaelin WG Jr. Molecular basis of the VHL hereditary cancer syndrome. Nat Rev Cancer 2002; 2(9): 673-682.
    • (2002) Nat Rev Cancer , vol.2 , Issue.9 , pp. 673-682
    • Kaelin Jr., W.G.1
  • 33
    • 0037513423 scopus 로고    scopus 로고
    • Neddylation and deneddylation of CUL-3 is required to target MEI-1/Katanin for degradation at the meiosis-to-mitosis transition in C. elegans
    • Pintard L, Kurz T, Glaser S, Willis JH, Peter M, Bowerman B. Neddylation and deneddylation of CUL-3 is required to target MEI-1/Katanin for degradation at the meiosis-to-mitosis transition in C. elegans. Curr Biol 2003; 13(11): 911-921.
    • (2003) Curr Biol , vol.13 , Issue.11 , pp. 911-921
    • Pintard, L.1    Kurz, T.2    Glaser, S.3    Willis, J.H.4    Peter, M.5    Bowerman, B.6
  • 34
    • 0037967230 scopus 로고    scopus 로고
    • CUL-4 ubiquitin ligase maintains genome stability by restraining DNA-replication licensing
    • Zhong W, Feng H, Santiago FE, Kipreos ET. CUL-4 ubiquitin ligase maintains genome stability by restraining DNA-replication licensing. Nature 2003; 423(6942): 885-889.
    • (2003) Nature , vol.423 , Issue.6942 , pp. 885-889
    • Zhong, W.1    Feng, H.2    Santiago, F.E.3    Kipreos, E.T.4
  • 35
    • 0023105114 scopus 로고
    • The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
    • Kang J, Lemaire HG, Unterbeck A, et al. The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor. Nature 1987; 325(6106): 733-736.
    • (1987) Nature , vol.325 , Issue.6106 , pp. 733-736
    • Kang, J.1    Lemaire, H.G.2    Unterbeck, A.3
  • 36
    • 0141462295 scopus 로고    scopus 로고
    • The amyloid precursor protein of Alzheimer's disease is found on the surface of static but not activity motile portions of neurites
    • Storey E, Spurck T, Pickett-Heaps J, Beyreuther K, Masters CL. The amyloid precursor protein of Alzheimer's disease is found on the surface of static but not activity motile portions of neurites. Brain Res 1996; 735(1): 59-66.
    • (1996) Brain Res , vol.735 , Issue.1 , pp. 59-66
    • Storey, E.1    Spurck, T.2    Pickett-Heaps, J.3    Beyreuther, K.4    Masters, C.L.5
  • 37
    • 0029967005 scopus 로고    scopus 로고
    • Alzheimer's beta-amyloid precursor protein is expressed on the surface of immediately ex vivo brain cells: A flow cytometric study
    • Jung SS, Nalbantoglu J, Cashman NR. Alzheimer's beta-amyloid precursor protein is expressed on the surface of immediately ex vivo brain cells: A flow cytometric study. J Neurosci Res 1996; 46(3): 336-348.
    • (1996) J Neurosci Res , vol.46 , Issue.3 , pp. 336-348
    • Jung, S.S.1    Nalbantoglu, J.2    Cashman, N.R.3
  • 38
    • 0029257190 scopus 로고
    • Cell-surface β-amyloid precursor protein stimulates neunte outgrowth of hippocampal neurons in an isoform-dependent manner
    • Qiu WQ, Ferreira A, Miller C, Koo EH, Selkoe DJ. Cell-surface β-amyloid precursor protein stimulates neunte outgrowth of hippocampal neurons in an isoform-dependent manner. J Neurosci 1995; 15: 2157-2167.
    • (1995) J Neurosci , vol.15 , pp. 2157-2167
    • Qiu, W.Q.1    Ferreira, A.2    Miller, C.3    Koo, E.H.4    Selkoe, D.J.5
  • 39
    • 0031031006 scopus 로고    scopus 로고
    • Trafficking of cell-surface beta-amyloid precursor protein: Evidence that a sorting intermediate participates in synaptic vesicle recycling
    • Marquez-Sterling NR, Lo AC, Sisodia SS, Koo EH. Trafficking of cell-surface beta-amyloid precursor protein: Evidence that a sorting intermediate participates in synaptic vesicle recycling. J Neurosci 1997; 17(1): 140-151.
    • (1997) J Neurosci , vol.17 , Issue.1 , pp. 140-151
    • Marquez-Sterling, N.R.1    Lo, A.C.2    Sisodia, S.S.3    Koo, E.H.4
  • 40
    • 0029950149 scopus 로고    scopus 로고
    • Trafficking of cell-surface amyloid beta-protein precursor. I. Secretion, endocytosis and recycling as detected by labeled monoclonal antibody
    • Koo EH, Squazzo SL, Selkoe DJ, Koo CH. Trafficking of cell-surface amyloid beta-protein precursor. I. Secretion, endocytosis and recycling as detected by labeled monoclonal antibody. J Cell Sci 1996; 109(Pt 5): 991-998.
    • (1996) J Cell Sci , vol.109 , Issue.5 PART , pp. 991-998
    • Koo, E.H.1    Squazzo, S.L.2    Selkoe, D.J.3    Koo, C.H.4
  • 41
    • 0029934134 scopus 로고    scopus 로고
    • Trafficking of cell-surface amyloid beta-protein precursor. II. Endocytosis, recycling and lysosomal targeting detected by immunolocalization
    • Yamazaki T, Koo EH, Selkoe DJ. Trafficking of cell-surface amyloid beta-protein precursor. II. Endocytosis, recycling and lysosomal targeting detected by immunolocalization. J Cell Sci 1996; 109(Pt 5): 999-1008.
    • (1996) J Cell Sci , vol.109 , Issue.5 PART , pp. 999-1008
    • Yamazaki, T.1    Koo, E.H.2    Selkoe, D.J.3
  • 42
    • 0028213567 scopus 로고
    • A heparin-binding domain in the amyloid protein precursor of Alzheimer's disease is involved in the regulation of neurite outgrowth
    • Small DH, Nurcombe V, Reed G, et al. A heparin-binding domain in the amyloid protein precursor of Alzheimer's disease is involved in the regulation of neurite outgrowth. J Neurosci 1994; 14(4): 2117-2127.
    • (1994) J Neurosci , vol.14 , Issue.4 , pp. 2117-2127
    • Small, D.H.1    Nurcombe, V.2    Reed, G.3
  • 44
    • 0030030005 scopus 로고    scopus 로고
    • Regulation of amyloid protein precursor (APP) binding to collagen and mapping of the binding sites on APP and collagen type I
    • Beher D, Hesse L, Masters CL, Multhaup G. Regulation of amyloid protein precursor (APP) binding to collagen and mapping of the binding sites on APP and collagen type I. J Biol Chem 1996; 271(3): 1613-1620.
    • (1996) J Biol Chem , vol.271 , Issue.3 , pp. 1613-1620
    • Beher, D.1    Hesse, L.2    Masters, C.L.3    Multhaup, G.4
  • 45
    • 1842364870 scopus 로고    scopus 로고
    • Interaction between Alzheimer's disease beta A4 precursor protein (APP) and the extracellular matrix: Evidence for the participation of heparan sulfate proteoglycans
    • Caceres J, Brandan E. Interaction between Alzheimer's disease beta A4 precursor protein (APP) and the extracellular matrix: Evidence for the participation of heparan sulfate proteoglycans. J Cell Biochem 1997; 65(2): 145-158.
    • (1997) J Cell Biochem , vol.65 , Issue.2 , pp. 145-158
    • Caceres, J.1    Brandan, E.2
  • 46
    • 0027254060 scopus 로고
    • A metalloproteinase inhibitor domain in Alzheimer amyloid protein precursor
    • Miyazaki K, Hasegawa M, Funahashi K, Umeda M. A metalloproteinase inhibitor domain in Alzheimer amyloid protein precursor. Nature 1993; 362(6423): 839-841.
    • (1993) Nature , vol.362 , Issue.6423 , pp. 839-841
    • Miyazaki, K.1    Hasegawa, M.2    Funahashi, K.3    Umeda, M.4
  • 47
    • 0038052349 scopus 로고    scopus 로고
    • Novel processing of beta-amyloid precursor protein catalyzed by membrane type 1 matrix metalloproteinase releases a fragment lacking the inhibitor domain against gelatinase a
    • Higashi S, Miyazaki K. Novel processing of beta-amyloid precursor protein catalyzed by membrane type 1 matrix metalloproteinase releases a fragment lacking the inhibitor domain against gelatinase A. Biochemistry 2003; 42(21): 6514-6526.
    • (2003) Biochemistry , vol.42 , Issue.21 , pp. 6514-6526
    • Higashi, S.1    Miyazaki, K.2
  • 48
    • 0035823495 scopus 로고    scopus 로고
    • Homodimerization of amyloid precursor protein and its implication in the amyloidogenic pathway of Alzheimer's disease
    • Scheuermann S, Hambsch B, Hesse L, et al. Homodimerization of amyloid precursor protein and its implication in the amyloidogenic pathway of Alzheimer's disease. J Biol Chem 2001; 276(36): 33923-33929.
    • (2001) J Biol Chem , vol.276 , Issue.36 , pp. 33923-33929
    • Scheuermann, S.1    Hambsch, B.2    Hesse, L.3
  • 49
    • 0027447656 scopus 로고
    • Alzheimer amyloid protein precursor complexes with brain GTP-binding protein G(o)
    • Nishimoto I, Okamoto T, Matsuura Y, Okamoto T, Murayama Y, Ogata E. Alzheimer amyloid protein precursor complexes with brain GTP-binding protein G(o). Nature 1993; 362: 75-79.
    • (1993) Nature , vol.362 , pp. 75-79
    • Nishimoto, I.1    Okamoto, T.2    Matsuura, Y.3    Okamoto, T.4    Murayama, Y.5    Ogata, E.6
  • 50
    • 0031717925 scopus 로고    scopus 로고
    • Fe65 and the protein network centered around the cytosolic domain of the Alzheimer's β-amyloid precursor protein
    • Russo T, Faraonio R, Minopoli G, De Candia P, De Renzis S, Zambrano N. Fe65 and the protein network centered around the cytosolic domain of the Alzheimer's β-amyloid precursor protein. FEBS Lett 1998; 434: 1-7.
    • (1998) FEBS Lett , vol.434 , pp. 1-7
    • Russo, T.1    Faraonio, R.2    Minopoli, G.3    De Candia, P.4    De Renzis, S.5    Zambrano, N.6
  • 51
    • 0032955868 scopus 로고    scopus 로고
    • A 127-kDa protein (UV-DDB) binds to the cytoplasmic domain of the Alzheimer's amyloid precursor protein
    • Watanabe T, Sukegawa J, Sukegawa I, et al. A 127-kDa protein (UV-DDB) binds to the cytoplasmic domain of the Alzheimer's amyloid precursor protein. J Neurochem 1999; 72: 549-556.
    • (1999) J Neurochem , vol.72 , pp. 549-556
    • Watanabe, T.1    Sukegawa, J.2    Sukegawa, I.3
  • 52
    • 0035816661 scopus 로고    scopus 로고
    • A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60
    • Cao X, Sudhof TC. A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60. Science 2001; 293(5527): 115-120.
    • (2001) Science , vol.293 , Issue.5527 , pp. 115-120
    • Cao, X.1    Sudhof, T.C.2
  • 53
    • 0036462590 scopus 로고    scopus 로고
    • Jun NH2-terminal kinase (JNK) interacting protein 1 (JIP1) binds the cytoplasmic domain of the Alzheimer's beta-amyloid precursor protein (APP)
    • Scheinfeld MH, Roncarati R, Vito P, Lopez PA, Abdallah M, D'Adamio L. Jun NH2-terminal kinase (JNK) interacting protein 1 (JIP1) binds the cytoplasmic domain of the Alzheimer's beta-amyloid precursor protein (APP). J Biol Chem 2002; 277(5): 3767-3775.
    • (2002) J Biol Chem , vol.277 , Issue.5 , pp. 3767-3775
    • Scheinfeld, M.H.1    Roncarati, R.2    Vito, P.3    Lopez, P.A.4    Abdallah, M.5    D'Adamio, L.6
  • 54
    • 0028988801 scopus 로고
    • Beta-Amyloid precursor protein-deficient mice show reactive gliosis and decreased locomotor activity
    • Zheng H, Jiang M, Trumbauer ME, et al. beta-Amyloid precursor protein-deficient mice show reactive gliosis and decreased locomotor activity. Cell 1995; 81(4): 525-531.
    • (1995) Cell , vol.81 , Issue.4 , pp. 525-531
    • Zheng, H.1    Jiang, M.2    Trumbauer, M.E.3
  • 55
    • 0028295848 scopus 로고
    • Cell cycle-dependent regulation of the phosphorylation and metabolism of the Alzheimer amyloid precursor protein
    • Suzuki T, Oishi M, Marshak DR, Czernik AJ, Nairn AC, Greengard P. Cell cycle-dependent regulation of the phosphorylation and metabolism of the Alzheimer amyloid precursor protein. EMBO J 1994; 13(5): 1114-1122.
    • (1994) EMBO J , vol.13 , Issue.5 , pp. 1114-1122
    • Suzuki, T.1    Oishi, M.2    Marshak, D.R.3    Czernik, A.J.4    Nairn, A.C.5    Greengard, P.6
  • 56
    • 0030935325 scopus 로고    scopus 로고
    • Phosphorylation of Alzheimer beta-amyloid precursor-like proteins
    • Suzuki T, Ando K, Isohara T, et al. Phosphorylation of Alzheimer beta-amyloid precursor-like proteins. Biochemistry 1997; 36(15): 4643-4649.
    • (1997) Biochemistry , vol.36 , Issue.15 , pp. 4643-4649
    • Suzuki, T.1    Ando, K.2    Isohara, T.3
  • 57
    • 0032053984 scopus 로고    scopus 로고
    • Degeneration in vivo of rat hippocampal neurons by wild-type Alzheimer amyloid precursor protein overexpressed by adenovirus-mediated gene transfer
    • Nishimura I, Uetsuki T, Dani SU, et al. Degeneration in vivo of rat hippocampal neurons by wild-type Alzheimer amyloid precursor protein overexpressed by adenovirus-mediated gene transfer. J Neurosci 1998; 18(7): 2387-2398.
    • (1998) J Neurosci , vol.18 , Issue.7 , pp. 2387-2398
    • Nishimura, I.1    Uetsuki, T.2    Dani, S.U.3
  • 58
    • 0034029430 scopus 로고    scopus 로고
    • A monoclonal antibody to amyloid precursor protein induces neuronal apoptosis
    • Rohn TT, Ivins KJ, Bahr BA, Cotman CW, Cribbs DH. A monoclonal antibody to amyloid precursor protein induces neuronal apoptosis. J Neurochem 2000; 74(6): 2331-2342.
    • (2000) J Neurochem , vol.74 , Issue.6 , pp. 2331-2342
    • Rohn, T.T.1    Ivins, K.J.2    Bahr, B.A.3    Cotman, C.W.4    Cribbs, D.H.5
  • 59
    • 0021956826 scopus 로고
    • Occurrence of neuropathological changes and dementia of Alzheimer's disease in Down's syndrome
    • Wisniewski KE, Wisniewski HM, Wen GY. Occurrence of neuropathological changes and dementia of Alzheimer's disease in Down's syndrome. Ann Neurol 1985; 17(3): 278-282.
    • (1985) Ann Neurol , vol.17 , Issue.3 , pp. 278-282
    • Wisniewski, K.E.1    Wisniewski, H.M.2    Wen, G.Y.3
  • 60
    • 0029932417 scopus 로고    scopus 로고
    • Axonal amyloid precursor protein expressed by neurons in vitro is present in a membrane fraction with caveolae-like properties
    • Bouillot C, Prochiantz A, Rougon G, Allinquant B. Axonal amyloid precursor protein expressed by neurons in vitro is present in a membrane fraction with caveolae-like properties. J Biol Chem 1996; 271(13): 7640-7644.
    • (1996) J Biol Chem , vol.271 , Issue.13 , pp. 7640-7644
    • Bouillot, C.1    Prochiantz, A.2    Rougon, G.3    Allinquant, B.4
  • 61
    • 0035928732 scopus 로고    scopus 로고
    • Compartmentalization of beta-secretase (Asp2) into low-buoyant density, noncaveolar lipid rafts
    • Riddell DR, Christie G, Hussam I, Dingwall C. Compartmentalization of beta-secretase (Asp2) into low-buoyant density, noncaveolar lipid rafts. Curr Biol 2001; 11(16): 1288-1293.
    • (2001) Curr Biol , vol.11 , Issue.16 , pp. 1288-1293
    • Riddell, D.R.1    Christie, G.2    Hussam, I.3    Dingwall, C.4
  • 64
    • 0036674082 scopus 로고    scopus 로고
    • Lipid rafts play an important role in a beta biogenesis by regulating the beta-secretase pathway
    • Tun H, Marlow L, Pinnix I, Kinsey R, Sambamurti K. Lipid rafts play an important role in A beta biogenesis by regulating the beta-secretase pathway. J Mol Neurosci 2002; 19(1/2): 31-35.
    • (2002) J Mol Neurosci , vol.19 , Issue.1-2 , pp. 31-35
    • Tun, H.1    Marlow, L.2    Pinnix, I.3    Kinsey, R.4    Sambamurti, K.5
  • 65
    • 0037421206 scopus 로고    scopus 로고
    • Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts
    • Ehehalt R, Keller P, Haass C, Thiele C, Simons K. Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts. J Cell Biol 2003; 160(1): 113-123.
    • (2003) J Cell Biol , vol.160 , Issue.1 , pp. 113-123
    • Ehehalt, R.1    Keller, P.2    Haass, C.3    Thiele, C.4    Simons, K.5
  • 66
    • 0034117282 scopus 로고    scopus 로고
    • Nedd8 modification of cul-1 activates SCF(beta(TrCP))-dependent ubiquitination of IkappaBalpha
    • Read MA, Brownell JE, Gladysheva TB, et al. Nedd8 modification of cul-1 activates SCF(beta(TrCP))-dependent ubiquitination of IkappaBalpha. Mol Cell Biol 2000; 20(7): 2326-2333.
    • (2000) Mol Cell Biol , vol.20 , Issue.7 , pp. 2326-2333
    • Read, M.A.1    Brownell, J.E.2    Gladysheva, T.B.3
  • 67
    • 0036195134 scopus 로고    scopus 로고
    • An intact NEDD8 pathway is required for Cullin-dependent ubiquitylation in mammalian cells
    • Ohh M, Kim WY, Moslehi JJ, et al. An intact NEDD8 pathway is required for Cullin-dependent ubiquitylation in mammalian cells. EMBO Rep 2002; 3(2): 177-182.
    • (2002) EMBO Rep , vol.3 , Issue.2 , pp. 177-182
    • Ohh, M.1    Kim, W.Y.2    Moslehi, J.J.3
  • 68
    • 0037144438 scopus 로고    scopus 로고
    • Fe65, a ligand of the Alzheimer's beta-amyloid precursor protein, blocks cell cycle progression by down-regulating thymidylate synthase expression
    • Bruni P, Minopoli G, Brancaccio T, et al. Fe65, a ligand of the Alzheimer's beta-amyloid precursor protein, blocks cell cycle progression by down-regulating thymidylate synthase expression. J Biol Chem 2002; 277(38): 35481-35488.
    • (2002) J Biol Chem , vol.277 , Issue.38 , pp. 35481-35488
    • Bruni, P.1    Minopoli, G.2    Brancaccio, T.3
  • 69
    • 0032541337 scopus 로고    scopus 로고
    • APLP2, a member of the Alzheimer precursor protein family, is required for correct genomic segregation in dividing mouse cells
    • Rassoulzadegan M, Yang Y, Cuzin F. APLP2, a member of the Alzheimer precursor protein family, is required for correct genomic segregation in dividing mouse cells. EMBO J 1998; 17(16): 4647-4656.
    • (1998) EMBO J , vol.17 , Issue.16 , pp. 4647-4656
    • Rassoulzadegan, M.1    Yang, Y.2    Cuzin, F.3
  • 70
    • 0035943345 scopus 로고    scopus 로고
    • A portrait of Alzheimer secretases-New features and familiar faces
    • Esler WP, Wolfe MS. A portrait of Alzheimer secretases-New features and familiar faces. Science 2001; 293(5534): 1449-1454.
    • (2001) Science , vol.293 , Issue.5534 , pp. 1449-1454
    • Esler, W.P.1    Wolfe, M.S.2
  • 71
    • 1442306058 scopus 로고    scopus 로고
    • Binding of F-spondin to amyloid-{beta} precursor protein: A candidate amyloid-{beta} precursor protein ligand that modulates amyloid-{beta} precursor protein cleavage
    • Ho A, Sudhof TC. Binding of F-spondin to amyloid-{beta} precursor protein: A candidate amyloid-{beta} precursor protein ligand that modulates amyloid-{beta} precursor protein cleavage. Proc Natl Acad Sci USA 2004; 101(8): 2548-2553.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.8 , pp. 2548-2553
    • Ho, A.1    Sudhof, T.C.2
  • 72
    • 0031866596 scopus 로고    scopus 로고
    • Direct association of presenilin-1 with beta-catenin
    • Murayama M, Tanaka S, Palacino J, et al. Direct association of presenilin-1 with beta-catenin. FEBS Lett 1998; 433(1/2): 73-77.
    • (1998) FEBS Lett , vol.433 , Issue.1-2 , pp. 73-77
    • Murayama, M.1    Tanaka, S.2    Palacino, J.3
  • 73
    • 0032568821 scopus 로고    scopus 로고
    • The presenilin 1 protein is a component of a high molecular weight intracellular complex that contains beta-catenin
    • Yu G, Chen F, Levesque G, et al. The presenilin 1 protein is a component of a high molecular weight intracellular complex that contains beta-catenin. J Biol Chem 1998; 273(26): 16470-16475.
    • (1998) J Biol Chem , vol.273 , Issue.26 , pp. 16470-16475
    • Yu, G.1    Chen, F.2    Levesque, G.3
  • 74
    • 1542347695 scopus 로고    scopus 로고
    • Convergence of Wnt, β-catenin, and cadherin pathways
    • Nelson WJ, Nusse R. Convergence of Wnt, β-catenin, and cadherin pathways. Science 2004; 303: 1483-1487.
    • (2004) Science , vol.303 , pp. 1483-1487
    • Nelson, W.J.1    Nusse, R.2
  • 75
    • 0032531793 scopus 로고    scopus 로고
    • Destabilization of beta-catenin by mutations in presenilin-1 potentiates neuronal apoptosis
    • Zhang Z, Hartmann H, Do VM, et al. Destabilization of beta-catenin by mutations in presenilin-1 potentiates neuronal apoptosis. Nature 1998; 395(6703): 698-702.
    • (1998) Nature , vol.395 , Issue.6703 , pp. 698-702
    • Zhang, Z.1    Hartmann, H.2    Do, V.M.3
  • 76
    • 0035845481 scopus 로고    scopus 로고
    • Loss of presenilin 1 is associated with enhanced beta-catenin signaling and skin tumorigenesis
    • Xia X, Qian S, Soriano S, et al. Loss of presenilin 1 is associated with enhanced beta-catenin signaling and skin tumorigenesis. Proc Natl Acad Sci USA 2001; 98(19): 10863-10868.
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.19 , pp. 10863-10868
    • Xia, X.1    Qian, S.2    Soriano, S.3
  • 77
    • 0141429160 scopus 로고    scopus 로고
    • A CBP binding transcriptional repressor produced by the PS1/epsilon-cleavage of N-cadherin is inhibited by PS1 FAD mutations
    • Marambaud P, Wen PH, Dutt A, et al. A CBP binding transcriptional repressor produced by the PS1/epsilon-cleavage of N-cadherin is inhibited by PS1 FAD mutations. Cell 2003; 114(5): 635-645.
    • (2003) Cell , vol.114 , Issue.5 , pp. 635-645
    • Marambaud, P.1    Wen, P.H.2    Dutt, A.3
  • 78
    • 0035930522 scopus 로고    scopus 로고
    • Presenilin 1 independently regulates β-catenin stability and transcriptional activity
    • Killick R, Pollard CC, Asuni AA, et al. Presenilin 1 independently regulates β-catenin stability and transcriptional activity. J Biol Chem 2001; 276(51): 48554-48561.
    • (2001) J Biol Chem , vol.276 , Issue.51 , pp. 48554-48561
    • Killick, R.1    Pollard, C.C.2    Asuni, A.A.3
  • 79
    • 0037145062 scopus 로고    scopus 로고
    • Presenilin couples the paired phosphorylation of beta-catenin independent of axin: Implications for beta-catenin activation in tumorigenesis
    • Kang DE, Soriano S, Xia X, et al. Presenilin couples the paired phosphorylation of beta-catenin independent of axin: Implications for beta-catenin activation in tumorigenesis. Cell 2002; 110(6): 751-762.
    • (2002) Cell , vol.110 , Issue.6 , pp. 751-762
    • Kang, D.E.1    Soriano, S.2    Xia, X.3
  • 80
    • 0035933518 scopus 로고    scopus 로고
    • Presenilin 1 mutations increase amyloid precursor protein production and proteolysis in Xenopus laevis oocytes
    • Heyn SN, Vulliet PR. Presenilin 1 mutations increase amyloid precursor protein production and proteolysis in Xenopus laevis oocytes. Brain Res 2001; 904(2): 189-198.
    • (2001) Brain Res , vol.904 , Issue.2 , pp. 189-198
    • Heyn, S.N.1    Vulliet, P.R.2
  • 81
    • 0025369198 scopus 로고
    • Amyloid beta protein precursor gene and hereditary cerebral hemorrhage with amyloidosis (Dutch)
    • van Broeckhoven C, Haan J, Bakker E, et al. Amyloid beta protein precursor gene and hereditary cerebral hemorrhage with amyloidosis (Dutch). Science 1990; 248(4959): 1120-1122.
    • (1990) Science , vol.248 , Issue.4959 , pp. 1120-1122
    • Van Broeckhoven, C.1    Haan, J.2    Bakker, E.3
  • 82
    • 0034982951 scopus 로고    scopus 로고
    • Novel amyloid precursor protein mutation in an Iowa family with dementia and severe cerebral amyloid angiopathy
    • Grabowski TJ, Cho HS, Vonsattel JP, Rebeck GW, Greenberg SM. Novel amyloid precursor protein mutation in an Iowa family with dementia and severe cerebral amyloid angiopathy. Ann Neurol 2001; 49(6): 697-705.
    • (2001) Ann Neurol , vol.49 , Issue.6 , pp. 697-705
    • Grabowski, T.J.1    Cho, H.S.2    Vonsattel, J.P.3    Rebeck, G.W.4    Greenberg, S.M.5
  • 83
    • 0033588412 scopus 로고    scopus 로고
    • The role of beta-catenin stability in mutant PS1-associated apoptosis
    • Weihl CC, Miller RJ, Roos RP. The role of beta-catenin stability in mutant PS1-associated apoptosis. Neuroreport 1999; 10(12): 2527-2532.
    • (1999) Neuroreport , vol.10 , Issue.12 , pp. 2527-2532
    • Weihl, C.C.1    Miller, R.J.2    Roos, R.P.3
  • 84
    • 0344668728 scopus 로고    scopus 로고
    • Fine mapping of the alpha-T catenin gene to a quantitative trait locus on chromosome 10 in late-onset Alzheimer's disease pedigrees
    • Ertekin-Taner N, Ronald J, Asahara H, et al. Fine mapping of the alpha-T catenin gene to a quantitative trait locus on chromosome 10 in late-onset Alzheimer's disease pedigrees. Hum Mol Genet 2003; 12(23): 3133-3143.
    • (2003) Hum Mol Genet , vol.12 , Issue.23 , pp. 3133-3143
    • Ertekin-Taner, N.1    Ronald, J.2    Asahara, H.3
  • 85
    • 0035936807 scopus 로고    scopus 로고
    • Hyper-prohferation and defects in epithelial polarity upon conditional ablation of alpha-catenin in skin
    • Vasioukhin V, Bauer C, Degenstein L, Wise B, Fuchs E. Hyper-prohferation and defects in epithelial polarity upon conditional ablation of alpha-catenin in skin. Cell 2001; 104(4): 605-617.
    • (2001) Cell , vol.104 , Issue.4 , pp. 605-617
    • Vasioukhin, V.1    Bauer, C.2    Degenstein, L.3    Wise, B.4    Fuchs, E.5
  • 86
    • 0038359353 scopus 로고    scopus 로고
    • Caught up in a Wnt storm: Wnt signaling in cancer
    • Giles RH, van Es JH, Clevers H. Caught up in a Wnt storm: Wnt signaling in cancer. Biochim Biophys Acta 2003; 1653(1): 1-24.
    • (2003) Biochim Biophys Acta , vol.1653 , Issue.1 , pp. 1-24
    • Giles, R.H.1    Van Es, J.H.2    Clevers, H.3
  • 87
    • 0037135177 scopus 로고    scopus 로고
    • Regulation of cerebral cortical size by control of cell cycle exit in neural precursors
    • Chenn A, Walsh CA. Regulation of cerebral cortical size by control of cell cycle exit in neural precursors. Science 2002; 297(5580): 365-369.
    • (2002) Science , vol.297 , Issue.5580 , pp. 365-369
    • Chenn, A.1    Walsh, C.A.2
  • 88
    • 0035034474 scopus 로고    scopus 로고
    • Ontogenetic changes in protein level of amyloid precursor protein (APP) in growth cones and synaptosomes from rat brain and prenatal expression pattern of APP mRNA isoforms in developing rat embryo
    • Kirazov E, Kirazov L, Bigl V, Schliebs R. Ontogenetic changes in protein level of amyloid precursor protein (APP) in growth cones and synaptosomes from rat brain and prenatal expression pattern of APP mRNA isoforms in developing rat embryo. Int J Dev Neurosci 2001; 19(3): 287-296.
    • (2001) Int J Dev Neurosci , vol.19 , Issue.3 , pp. 287-296
    • Kirazov, E.1    Kirazov, L.2    Bigl, V.3    Schliebs, R.4
  • 89
    • 0037106090 scopus 로고    scopus 로고
    • Stem cell biology of the central nervous system
    • Okano H. Stem cell biology of the central nervous system. J Neurosci Res 2002; 69: 698-707.
    • (2002) J Neurosci Res , vol.69 , pp. 698-707
    • Okano, H.1
  • 90
    • 0043135185 scopus 로고    scopus 로고
    • DNA synthesis and neuronal apoptosis caused by familia Alzheimer disease mutants of the amyloid precursor protein are mediated by the p21 activated kinase PAK3
    • McPhie DL, Coopersmith R, Hines-Peratta A, Chen Ivins KJ, Manly SP, Kozlowski MR, Neve KA, Neve RL. DNA synthesis and neuronal apoptosis caused by familia Alzheimer disease mutants of the amyloid precursor protein are mediated by the p21 activated kinase PAK3. J Neurosci 2003; 23: 6914-6927.
    • (2003) J Neurosci , vol.23 , pp. 6914-6927
    • McPhie, D.L.1    Coopersmith, R.2    Hines-Peratta, A.3    Chen Ivins, K.J.4    Manly, S.P.5    Kozlowski, M.R.6    Neve, K.A.7    Neve, R.L.8
  • 91
    • 0029003699 scopus 로고
    • Cell adhesion and signal transduction: The Armadillo connection
    • Peifer M. Cell adhesion and signal transduction: The Armadillo connection. Trends Cell Biol 1995; 5: 224-229.
    • (1995) Trends Cell Biol , vol.5 , pp. 224-229
    • Peifer, M.1


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