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Volumn 80, Issue 2, 2005, Pages 151-159

Cytoplasmic domain of the β-amyloid protein precursor of Alzheimer's disease: Function, regulation of proteolysis, and implications for drug development

Author keywords

amyloid; secretase; 20S proteasome; Adaptor protein; Alzheimer's disease; Amyloid protein precursor

Indexed keywords

A DISINTEGRIN AND METALLOPROTEASE 10; AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; BETA SECRETASE; GAMMA SECRETASE; METALLOPROTEINASE; PROTEASOME; TUMOR NECROSIS FACTOR ALPHA CONVERTING ENZYME; UNCLASSIFIED DRUG;

EID: 18744405422     PISSN: 03604012     EISSN: None     Source Type: Journal    
DOI: 10.1002/jnr.20408     Document Type: Short Survey
Times cited : (38)

References (113)
  • 1
    • 0035955712 scopus 로고    scopus 로고
    • Phosphorylation-dependent regulation of the interaction of amyloid precursor protein with Fe65 affects the production of beta-amyloid
    • Ando K, Iijima KI, Elliott JI, Kirino Y, Suzuki T. 2001. Phosphorylation-dependent regulation of the interaction of amyloid precursor protein with Fe65 affects the production of beta-amyloid. J Biol Chem 276:40353-40361.
    • (2001) J Biol Chem , vol.276 , pp. 40353-40361
    • Ando, K.1    Iijima, K.I.2    Elliott, J.I.3    Kirino, Y.4    Suzuki, T.5
  • 4
    • 0036696444 scopus 로고    scopus 로고
    • The endocytic protein alpha-adaptin is required for numb-mediated asymmetric cell division in Drosophila
    • Berdnik D, Torok T, Gonzalez-Gaitan M, Knoblich JA. 2002. The endocytic protein alpha-adaptin is required for numb-mediated asymmetric cell division in Drosophila. Dev Cell 3:221-231.
    • (2002) Dev Cell , vol.3 , pp. 221-231
    • Berdnik, D.1    Torok, T.2    Gonzalez-Gaitan, M.3    Knoblich, J.A.4
  • 6
    • 0029805132 scopus 로고    scopus 로고
    • The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein
    • Borg JP, Ooi J, Levy E, Margolis B. 1996. The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein. Mol Cell Biol 16:6229-6241.
    • (1996) Mol Cell Biol , vol.16 , pp. 6229-6241
    • Borg, J.P.1    Ooi, J.2    Levy, E.3    Margolis, B.4
  • 7
    • 0032510834 scopus 로고    scopus 로고
    • The X11alpha protein slows cellular amyloid precursor protein processing and reduces Abeta 40 and Abeta 42 secretion
    • Borg JP, Yang Y, De Taddeo-Borg M, Margolis B, Turner RS. 1998. The X11alpha protein slows cellular amyloid precursor protein processing and reduces Abeta 40 and Abeta 42 secretion. J Biol Chem 273:14761-14766.
    • (1998) J Biol Chem , vol.273 , pp. 14761-14766
    • Borg, J.P.1    Yang, Y.2    De Taddeo-Borg, M.3    Margolis, B.4    Turner, R.S.5
  • 8
    • 0025965521 scopus 로고
    • Beta amyloid precursor protein mediates neuronal cell-cell and cell-surface adhesion
    • Breen KC, Bruce M, Anderton BH. 1991. Beta amyloid precursor protein mediates neuronal cell-cell and cell-surface adhesion. J Neurosci Res 28:90-100.
    • (1991) J Neurosci Res , vol.28 , pp. 90-100
    • Breen, K.C.1    Bruce, M.2    Anderton, B.H.3
  • 9
    • 0031695197 scopus 로고    scopus 로고
    • Projections of Alzheimer's disease in the United States and the public health impact of delaying disease onset
    • Brookmeyer R, Gray S, Kawas C. 1998. Projections of Alzheimer's disease in the United States and the public health impact of delaying disease onset. Am J Public Health 88:1337-1342.
    • (1998) Am J Public Health , vol.88 , pp. 1337-1342
    • Brookmeyer, R.1    Gray, S.2    Kawas, C.3
  • 11
    • 0035816661 scopus 로고    scopus 로고
    • A transcriptively active complex of APP with Fe65 and histone acetyltransferase Tip60
    • Cao X, Sudhof TC. 2001. A transcriptively active complex of APP with Fe65 and histone acetyltransferase Tip60. Science 293:115-120.
    • (2001) Science , vol.293 , pp. 115-120
    • Cao, X.1    Sudhof, T.C.2
  • 12
    • 2642582435 scopus 로고    scopus 로고
    • Dissection of APP-dependent transcriptional transactivation
    • Cao X, Sudhof TC. 2004. Dissection of APP-dependent transcriptional transactivation. J Biol Chem 279:24601-24611.
    • (2004) J Biol Chem , vol.279 , pp. 24601-24611
    • Cao, X.1    Sudhof, T.C.2
  • 13
    • 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, Tesco G, Jeong WJ, Lindsley L, Eckman EA, Eckman CB, Tanzi RE, Gueriette SY. 2003. Generation of the beta-amyloid peptide and the amyloid precursor protein C-terminal fragment gamma are potentiated by FE65L1. J Biol Chem 278:51100-51107.
    • (2003) J Biol Chem , vol.278 , pp. 51100-51107
    • Chang, Y.1    Tesco, G.2    Jeong, W.J.3    Lindsley, L.4    Eckman, E.A.5    Eckman, C.B.6    Tanzi, R.E.7    Gueriette, S.Y.8
  • 14
    • 0025250145 scopus 로고
    • NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor
    • Chen WJ, Goldstein JL, Brown MS. 1990. NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor. J Biol Chem 265:3116-3123.
    • (1990) J Biol Chem , vol.265 , pp. 3116-3123
    • Chen, W.J.1    Goldstein, J.L.2    Brown, M.S.3
  • 15
    • 0142059983 scopus 로고    scopus 로고
    • APP-BP1 mediates APP-induced apoptosis and DNA synthesis and is increased in Alzheimer's disease brain
    • Chen Y, Liu W, McPhie DL, Hassinger L, Neve RL. 2003. APP-BP1 mediates APP-induced apoptosis and DNA synthesis and is increased in Alzheimer's disease brain. J Cell Biol 163:27-33.
    • (2003) J Cell Biol , vol.163 , pp. 27-33
    • Chen, Y.1    Liu, W.2    McPhie, D.L.3    Hassinger, L.4    Neve, R.L.5
  • 16
    • 15844408798 scopus 로고    scopus 로고
    • APP-BP1, a novel protein that binds to the carboxyl-terminal region of the amyloid precursor protein
    • Chow N, Korenberg JR, Chen XN, Neve RL. 1996. APP-BP1, a novel protein that binds to the carboxyl-terminal region of the amyloid precursor protein. J Biol Chem 271:11339-11346.
    • (1996) J Biol Chem , vol.271 , pp. 11339-11346
    • Chow, N.1    Korenberg, J.R.2    Chen, X.N.3    Neve, R.L.4
  • 18
    • 0032519711 scopus 로고    scopus 로고
    • Fe65L2: A new member of the Fe65 protein family interacting with the intracellular domain of the Alzheimer's beta-amyloid precursor protein
    • Duilio A, Faraonio R, Minopoli G, Zambrano N, Russo T. 1998. Fe65L2: a new member of the Fe65 protein family interacting with the intracellular domain of the Alzheimer's beta-amyloid precursor protein. Biochem J 330:513-519.
    • (1998) Biochem J , vol.330 , pp. 513-519
    • Duilio, A.1    Faraonio, R.2    Minopoli, G.3    Zambrano, N.4    Russo, T.5
  • 21
    • 0027076090 scopus 로고
    • Normal processing of the Alzheimer's disease amyloid beta protein precursor generates potentially amyloidogenic carboxyl-terminal derivatives
    • Estus S, Golde TE, Younkin SG. 1992. Normal processing of the Alzheimer's disease amyloid beta protein precursor generates potentially amyloidogenic carboxyl-terminal derivatives. Ann N Y Acad Sci 674:138-148.
    • (1992) Ann N Y Acad Sci , vol.674 , pp. 138-148
    • Estus, S.1    Golde, T.E.2    Younkin, S.G.3
  • 22
    • 0034662929 scopus 로고    scopus 로고
    • BACE2, a beta-secretase homolog, cleaves at the beta site and within the amyloid-beta region of the amyloid-beta precursor protein
    • Farzan M, Schnitzler CE, Vasilieva N, Leung D, Choe H. 2000. BACE2, a beta-secretase homolog, cleaves at the beta site and within the amyloid-beta region of the amyloid-beta precursor protein. Proc Natl Acad Sci USA 97:9712-9717.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 9712-9717
    • Farzan, M.1    Schnitzler, C.E.2    Vasilieva, N.3    Leung, D.4    Choe, H.5
  • 23
    • 0029598484 scopus 로고
    • The regions of the Fe65 protein homologous to the phosphotyrosine interaction/phosphotyrosine binding domain of shc bind the intracellular domain of the Alzheimer's amyloid precursor protein
    • Fiore F, Zambrano N, Minopoli G, Donini V, Duilio A, Russo T. 1995. The regions of the Fe65 protein homologous to the phosphotyrosine interaction/phosphotyrosine binding domain of shc bind the intracellular domain of the Alzheimer's amyloid precursor protein. J Biol Chem 270:30853-30856.
    • (1995) J Biol Chem , vol.270 , pp. 30853-30856
    • Fiore, F.1    Zambrano, N.2    Minopoli, G.3    Donini, V.4    Duilio, A.5    Russo, T.6
  • 25
    • 0026070054 scopus 로고
    • Effects of injected Alzheimer beta-amyloid cores in rat brain
    • Frautschy SA, Baird A, Cole GM. 1991. Effects of injected Alzheimer beta-amyloid cores in rat brain. Proc Natl Acad Sci U S A 88:8362-8366.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 8362-8366
    • Frautschy, S.A.1    Baird, A.2    Cole, G.M.3
  • 27
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner GG, Wong CW. 1984. Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun 120:885-890.
    • (1984) Biochem Biophys Res Commun , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 28
    • 0029746156 scopus 로고    scopus 로고
    • Association of a novel human FE65-like protein with the cytoplasmic domain of the beta-amyloid precursor protein
    • Guenette SY, Chen J, Jondro PD, Tanzi RE. 1996. Association of a novel human FE65-like protein with the cytoplasmic domain of the beta-amyloid precursor protein. Proc Natl Acad Sci U S A 93:10832-10837.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 10832-10837
    • Guenette, S.Y.1    Chen, J.2    Jondro, P.D.3    Tanzi, R.E.4
  • 31
    • 0028985176 scopus 로고
    • Polarized sorting of beta-amyloid precursor protein and its proteolytic products in MDCK cells is regulated by two independent signals
    • Haass C, Koo EH, Capell A, Teplow DB, Selkoe DJ. 1995. Polarized sorting of beta-amyloid precursor protein and its proteolytic products in MDCK cells is regulated by two independent signals. J Cell Biol 128:537-547.
    • (1995) J Cell Biol , vol.128 , pp. 537-547
    • Haass, C.1    Koo, E.H.2    Capell, A.3    Teplow, D.B.4    Selkoe, D.J.5
  • 32
    • 0037113960 scopus 로고    scopus 로고
    • ARH is a modular adaptor protein that interacts with the LDL receptor, clathrin, and AP-2
    • He G, Gupta S, Yi M, Michaely P, Hobbs HH, Cohen JC. 2002. ARH is a modular adaptor protein that interacts with the LDL receptor, clathrin, and AP-2. J Biol Chem 277:44044-44049.
    • (2002) J Biol Chem , vol.277 , pp. 44044-44049
    • He, G.1    Gupta, S.2    Yi, M.3    Michaely, P.4    Hobbs, H.H.5    Cohen, J.C.6
  • 33
    • 8144230876 scopus 로고    scopus 로고
    • Cortical dysplasia resembling human type 2 lissencephaly in mice lacking all three APP family members
    • Herms J, Anliker B, Heber S, Ring S, Fuhrmann M, Kretzschmar H, Sisodia S, Muller U. 2004. Cortical dysplasia resembling human type 2 lissencephaly in mice lacking all three APP family members. EMBO J 23:4106-4115.
    • (2004) EMBO J , vol.23 , pp. 4106-4115
    • Herms, J.1    Anliker, B.2    Heber, S.3    Ring, S.4    Fuhrmann, M.5    Kretzschmar, H.6    Sisodia, S.7    Muller, U.8
  • 34
    • 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. 2004. 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 U S A 101:2548-2553.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 2548-2553
    • Ho, A.1    Sudhof, T.C.2
  • 35
    • 0033198295 scopus 로고    scopus 로고
    • Disabled-1 binds to the cytoplasmic domain of amyloid precursor-like protein 1
    • Homayouni R, Rice DS, Sheldon M, Curran T. 1999. Disabled-1 binds to the cytoplasmic domain of amyloid precursor-like protein 1. J Neurosci 19:7507-7515.
    • (1999) J Neurosci , vol.19 , pp. 7507-7515
    • Homayouni, R.1    Rice, D.S.2    Sheldon, M.3    Curran, T.4
  • 36
    • 0031035703 scopus 로고    scopus 로고
    • Mouse disabled (mDab1): A Src binding protein implicated in neuronal development
    • Howell BW, Gerder FB, Cooper JA. 1997. Mouse disabled (mDab1): a Src binding protein implicated in neuronal development. EMBO J 16:121-132.
    • (1997) EMBO J , vol.16 , pp. 121-132
    • Howell, B.W.1    Gerder, F.B.2    Cooper, J.A.3
  • 37
    • 0033066680 scopus 로고    scopus 로고
    • The Disabled 1 phosphotyrosine-binding domain binds to the internalization signals of transmembrane glycoproteins and to phospholipids
    • Howell BW, Lanier LM, Frank R, Gertler FB, Cooper JA. 1999. The Disabled 1 phosphotyrosine-binding domain binds to the internalization signals of transmembrane glycoproteins and to phospholipids. Mol Cell Biol 19:5179-5188.
    • (1999) Mol Cell Biol , vol.19 , pp. 5179-5188
    • Howell, B.W.1    Lanier, L.M.2    Frank, R.3    Gertler, F.B.4    Cooper, J.A.5
  • 39
    • 0038603918 scopus 로고    scopus 로고
    • A scaffold protein JIP-1b enhances amyloid precursor protein phosphorylation by JNK and its association with kinesin light chain 1
    • Inomata H, Nakamura Y, Hayakawa A, Takata H, Suzuki T, Miyazawa K, Kitamura N. 2003. A scaffold protein JIP-1b enhances amyloid precursor protein phosphorylation by JNK and its association with kinesin light chain 1. J Biol Chem 278:22946-22955.
    • (2003) J Biol Chem , vol.278 , pp. 22946-22955
    • Inomata, H.1    Nakamura, Y.2    Hayakawa, A.3    Takata, H.4    Suzuki, T.5    Miyazawa, K.6    Kitamura, N.7
  • 40
    • 0032054723 scopus 로고    scopus 로고
    • Signal transduction by the c-Jun N-terminal kinase (JNK) - From inflammation to development
    • Ip YT, Davis RJ. 1998. Signal transduction by the c-Jun N-terminal kinase (JNK) - from inflammation to development. Curr Opin Cell Biol 10:205-219.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 205-219
    • Ip, Y.T.1    Davis, R.J.2
  • 41
    • 0033636136 scopus 로고    scopus 로고
    • Axonal transport of amyloid precursor protein is mediated by direct binding to the kinesin light chain subunit of kinesin-I
    • Kamal A, Stokin GB, Yang Z, Xia CH, Goldstein LSB. 2000. Axonal transport of amyloid precursor protein is mediated by direct binding to the kinesin light chain subunit of kinesin-I. Neuron 28:449-459.
    • (2000) Neuron , vol.28 , pp. 449-459
    • Kamal, A.1    Stokin, G.B.2    Yang, Z.3    Xia, C.H.4    Goldstein, L.S.B.5
  • 43
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: The control of NF-kappaB activity
    • Karin M, Ben-Neriah Y. 2000. Phosphorylation meets ubiquitination: the control of NF-kappaB activity. Annu Rev Immunol 18:621-663.
    • (2000) Annu Rev Immunol , vol.18 , pp. 621-663
    • Karin, M.1    Ben-Neriah, Y.2
  • 45
    • 0035955693 scopus 로고    scopus 로고
    • The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a Notch-like manner
    • Kimberly WT, Zheng JB, Guenette SY, Selkoe DJ. 2001. The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a Notch-like manner. J Biol Chem 276:40288-40292.
    • (2001) J Biol Chem , vol.276 , pp. 40288-40292
    • Kimberly, W.T.1    Zheng, J.B.2    Guenette, S.Y.3    Selkoe, D.J.4
  • 46
    • 0037827785 scopus 로고    scopus 로고
    • X11alpha modulates secretory and endocytic trafficking and metabolism of amyloid precursor protein: Mutational analysis of the YENPTY sequence
    • King GD, Perez RG, Steinhilb ML, Gaut JR, Turner RS. 2003. X11alpha modulates secretory and endocytic trafficking and metabolism of amyloid precursor protein: mutational analysis of the YENPTY sequence. Neuroscience 120:143-154.
    • (2003) Neuroscience , vol.120 , pp. 143-154
    • King, G.D.1    Perez, R.G.2    Steinhilb, M.L.3    Gaut, J.R.4    Turner, R.S.5
  • 47
    • 0346435147 scopus 로고    scopus 로고
    • X11alpha impairs gamma- but not beta-cleavage of amyloid precursor protein
    • King GD, Cherian K, Turner RS. 2004. X11alpha impairs gamma- but not beta-cleavage of amyloid precursor protein. J Neurochem 88:971-982.
    • (2004) J Neurochem , vol.88 , pp. 971-982
    • King, G.D.1    Cherian, K.2    Turner, R.S.3
  • 48
    • 0028276801 scopus 로고
    • Evidence that production and release of amyloid beta-protein involves the endocytic pathway
    • Koo EH, Squazzo SL. 1994. Evidence that production and release of amyloid beta-protein involves the endocytic pathway. J Biol Chem 269:17386-17389.
    • (1994) J Biol Chem , vol.269 , pp. 17386-17389
    • Koo, E.H.1    Squazzo, S.L.2
  • 52
    • 0027943816 scopus 로고
    • Production of Alzheimer 4kDa beta-amyloid peptide requires the C-terminal cytosolic domain of the amyloid precursor protein
    • LeBlanc AC, Gambetti P. 1994. Production of Alzheimer 4kDa beta-amyloid peptide requires the C-terminal cytosolic domain of the amyloid precursor protein. Biochem Biophys Res Commun 204:1371-1380.
    • (1994) Biochem Biophys Res Commun , vol.204 , pp. 1371-1380
    • LeBlanc, A.C.1    Gambetti, P.2
  • 54
    • 0034652309 scopus 로고    scopus 로고
    • Human aspartic protease memapsin 2 cleaves the beta-secretase site of beta-amyloid precursor protein
    • Lin X, Koelsch G, Wu S, Downs D, Dashti A, Tang J. 2000. Human aspartic protease memapsin 2 cleaves the beta-secretase site of beta-amyloid precursor protein. Proc Natl Acad Sci USA 97:1456-1460.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 1456-1460
    • Lin, X.1    Koelsch, G.2    Wu, S.3    Downs, D.4    Dashti, A.5    Tang, J.6
  • 58
    • 0026570528 scopus 로고
    • β-amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity
    • Mattson MP, Cheng B, Davis D, Bryant K, Lieberburg I, Rydel RE. 1992. β-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity. J Neurosci 12:376-389.
    • (1992) J Neurosci , vol.12 , pp. 376-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3    Bryant, K.4    Lieberburg, I.5    Rydel, R.E.6
  • 59
    • 0026663993 scopus 로고
    • The amyloid protein precursor of Alzheimer's disease is a mediator of the effects of nerve growth factor on neurite outgrowth
    • Milward EA, Papadopoulos R, Fuller SJ, Moir RD, Small D, Beyreuther K, Masters CL. 1992. The amyloid protein precursor of Alzheimer's disease is a mediator of the effects of nerve growth factor on neurite outgrowth. Neuron 9:129-137.
    • (1992) Neuron , vol.9 , pp. 129-137
    • Milward, E.A.1    Papadopoulos, R.2    Fuller, S.J.3    Moir, R.D.4    Small, D.5    Beyreuther, K.6    Masters, C.L.7
  • 61
    • 0037059006 scopus 로고    scopus 로고
    • The autosomal recessive hypercholesterolemia (ARH) protein interfaces directly with the clathrin-coat machinery
    • Mishra SK, Watkins SC, Traub LM. 2002b. The autosomal recessive hypercholesterolemia (ARH) protein interfaces directly with the clathrin-coat machinery. Proc Natl Acad Sci U S A 99:16099-16104.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 16099-16104
    • Mishra, S.K.1    Watkins, S.C.2    Traub, L.M.3
  • 62
  • 63
    • 0042357124 scopus 로고    scopus 로고
    • Autosomal recessive hypercholesterolemia protein interacts with and regulates the cell surface level of Alzheimer's amyloid-beta precursor protein
    • Noviello C, Vito P, Lopez P, Abdallah M, D'Adamio L. 2003. Autosomal recessive hypercholesterolemia protein interacts with and regulates the cell surface level of Alzheimer's amyloid-beta precursor protein. J Biol Chem 278:31843-31847.
    • (2003) J Biol Chem , vol.278 , pp. 31843-31847
    • Noviello, C.1    Vito, P.2    Lopez, P.3    Abdallah, M.4    D'Adamio, L.5
  • 64
    • 0034644836 scopus 로고    scopus 로고
    • Regulation of APP cleavage by alpha-, beta- and gamma-secretases
    • Nunan J, Small DH. 2000. Regulation of APP cleavage by alpha-, beta- and gamma-secretases. FEBS Lett 483:6-10.
    • (2000) FEBS Lett , vol.483 , pp. 6-10
    • Nunan, J.1    Small, D.H.2
  • 65
    • 0034797234 scopus 로고    scopus 로고
    • The C-terminal fragment of the Alzheimer's disease amyloid protein precursor is degraded by a proteasome-dependent mechanism distinct from gamma-secretase
    • Nunan J, Shearman MS, Checler F, Cappai R, Evin G, Beyreuther K, Masters CL, Small DH. 2001. The C-terminal fragment of the Alzheimer's disease amyloid protein precursor is degraded by a proteasome-dependent mechanism distinct from gamma-secretase. Eur J Biochem 268:5329-5336.
    • (2001) Eur J Biochem , vol.268 , pp. 5329-5336
    • Nunan, J.1    Shearman, M.S.2    Checler, F.3    Cappai, R.4    Evin, G.5    Beyreuther, K.6    Masters, C.L.7    Small, D.H.8
  • 66
    • 0242330370 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of the C-terminus of the Alzheimer's disease beta-amyloid protein precursor: Effect of C-terminal truncation on production of beta-amyloid protein
    • Nunan J, Williamson NA, Hill AF, Sernee MF, Masters CL, Small DH. 2003. Proteasome-mediated degradation of the C-terminus of the Alzheimer's disease beta-amyloid protein precursor: effect of C-terminal truncation on production of beta-amyloid protein. J Neurosci Res 74:378-385.
    • (2003) J Neurosci Res , vol.74 , pp. 378-385
    • Nunan, J.1    Williamson, N.A.2    Hill, A.F.3    Sernee, M.F.4    Masters, C.L.5    Small, D.H.6
  • 67
    • 0029008666 scopus 로고
    • The reeler gene-associated antigen on Cajal-Retzius neurons is a crucial molecule for laminar organization of cortical neurons
    • Ogawa M, Miyata T, Nakajima K, Yagyu K, Seike M, Ikenaka K, Yamamoto H, Mikoshiba K. 1995. The reeler gene-associated antigen on Cajal-Retzius neurons is a crucial molecule for laminar organization of cortical neurons. Neuron 14:899-912.
    • (1995) Neuron , vol.14 , pp. 899-912
    • Ogawa, M.1    Miyata, T.2    Nakajima, K.3    Yagyu, K.4    Seike, M.5    Ikenaka, K.6    Yamamoto, H.7    Mikoshiba, K.8
  • 68
    • 0031736233 scopus 로고    scopus 로고
    • Mint 3: A ubiquitous mint isoform that does not bind to munc18-1 or -2
    • Okamoto M, Sudhof TC. 1998. Mint 3: a ubiquitous mint isoform that does not bind to munc18-1 or -2. Eur J Cell Biol 77:161-165.
    • (1998) Eur J Cell Biol , vol.77 , pp. 161-165
    • Okamoto, M.1    Sudhof, T.C.2
  • 69
    • 0033516554 scopus 로고    scopus 로고
    • Mutagenesis identifies new signals for beta-amyloid precursor protein endocytosis, turnover, and the generation of secreted fragments, including Abeta42
    • Perez RG, Soriano S, Hayes JD, Ostaszewski B, Xia W, Selkoe DJ, Chen X, Stokin GB, Koo EH. 1999. Mutagenesis identifies new signals for beta-amyloid precursor protein endocytosis, turnover, and the generation of secreted fragments, including Abeta42. J Biol Chem 274:18851-18856.
    • (1999) J Biol Chem , vol.274 , pp. 18851-18856
    • Perez, R.G.1    Soriano, S.2    Hayes, J.D.3    Ostaszewski, B.4    Xia, W.5    Selkoe, D.J.6    Chen, X.7    Stokin, G.B.8    Koo, E.H.9
  • 70
    • 3242811966 scopus 로고    scopus 로고
    • Functional reconstitution of γ-secretase through coordinated expression of presenilin, nicastrin, aph-1 and pen-2
    • Periz G, Fortini ME. 2004. Functional reconstitution of γ-secretase through coordinated expression of presenilin, nicastrin, aph-1 and pen-2. J Neurosci Res 77:309-322.
    • (2004) J Neurosci Res , vol.77 , pp. 309-322
    • Periz, G.1    Fortini, M.E.2
  • 71
    • 2542423595 scopus 로고    scopus 로고
    • The c-Abl tyrosine kinase phosphorylates the Fe65 adaptor protein to stimulate Fe65/amyloid precursor protein nuclear signaling
    • Perkinton MS, Standen CL, Lau KF, Kesavapany S, Byers HL, Ward M, McLoughlin DM, Miller CC. 2004. The c-Abl tyrosine kinase phosphorylates the Fe65 adaptor protein to stimulate Fe65/amyloid precursor protein nuclear signaling. J Biol Chem 279:22084-22091.
    • (2004) J Biol Chem , vol.279 , pp. 22084-22091
    • Perkinton, M.S.1    Standen, C.L.2    Lau, K.F.3    Kesavapany, S.4    Byers, H.L.5    Ward, M.6    McLoughlin, D.M.7    Miller, C.C.8
  • 72
    • 1542344435 scopus 로고    scopus 로고
    • Proteasomes and their kin: Proteases in the machine age
    • Pickart CM, Cohen RE. 2004. Proteasomes and their kin: proteases in the machine age. Nat Rev Mol Cell Biol 5:177-187.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 177-187
    • Pickart, C.M.1    Cohen, R.E.2
  • 73
    • 2442498577 scopus 로고    scopus 로고
    • FE65 constitutes the functional link between the low-density lipoprotein receptor-related protein and the amyloid precursor protein
    • Pietrzik CU, Yoon IS, Jaeger S, Busse T, Weggen S, Koo EH. 2004. FE65 constitutes the functional link between the low-density lipoprotein receptor-related protein and the amyloid precursor protein. J Neurosci 24:4259-4265.
    • (2004) J Neurosci , vol.24 , pp. 4259-4265
    • Pietrzik, C.U.1    Yoon, I.S.2    Jaeger, S.3    Busse, T.4    Weggen, S.5    Koo, E.H.6
  • 76
    • 0026181909 scopus 로고
    • Alzheimer's disease: A description of the structural lesions
    • Probst A, Langui D, Ulrich J. 1991. Alzheimer's disease: a description of the structural lesions. Brain Pathol 1:229-239.
    • (1991) Brain Pathol , vol.1 , pp. 229-239
    • Probst, A.1    Langui, D.2    Ulrich, J.3
  • 77
    • 0029257190 scopus 로고
    • Cell-surface beta-amyloid precursor protein stimulates neurite outgrowth of hippocampal neurons in an isoform-dependent manner
    • Qiu WQ, Ferreira A, Miller C, Koo EH, Selkoe DJ. 1995. Cell-surface beta-amyloid precursor protein stimulates neurite outgrowth of hippocampal neurons in an isoform-dependent manner. J Neurosci 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
  • 80
    • 0027936838 scopus 로고
    • Apolipoprotein E affects the rate of Alzheimer disease expression: β-amyloid burden is a secondary consequence dependent on APOE genotype and duration of disease
    • Roses AD. 1994. Apolipoprotein E affects the rate of Alzheimer disease expression: β-amyloid burden is a secondary consequence dependent on APOE genotype and duration of disease. J Neuropathol Exp Neurol 53:429-437.
    • (1994) J Neuropathol Exp Neurol , vol.53 , pp. 429-437
    • Roses, A.D.1
  • 83
    • 0032575559 scopus 로고    scopus 로고
    • X11 interaction with beta-amyloid precursor protein modulates its cellular stabilization and reduces amyloid beta-protein secretion
    • Sastre M, Turner RS, Levy E. 1998. X11 interaction with beta-amyloid precursor protein modulates its cellular stabilization and reduces amyloid beta-protein secretion. J Biol Chem 273:22351-22357.
    • (1998) J Biol Chem , vol.273 , pp. 22351-22357
    • Sastre, M.1    Turner, R.S.2    Levy, E.3
  • 84
    • 0030957355 scopus 로고    scopus 로고
    • Clathrin-coated vesicle formation and protein sorting: An integrated process
    • Schmid SL. 1997. Clathrin-coated vesicle formation and protein sorting: an integrated process. Annu Rev Biochem 66:511-548.
    • (1997) Annu Rev Biochem , vol.66 , pp. 511-548
    • Schmid, S.L.1
  • 85
    • 0024810385 scopus 로고
    • The regulation of amyloid beta protein precursor secretion and its modulatory role in cell adhesion
    • Schubert D, Jin LW, Saitoh T, Cole G. 1989. The regulation of amyloid beta protein precursor secretion and its modulatory role in cell adhesion. Neuron 3:689-694.
    • (1989) Neuron , vol.3 , pp. 689-694
    • Schubert, D.1    Jin, L.W.2    Saitoh, T.3    Cole, G.4
  • 86
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe DJ. 2001. Alzheimer's disease: genes, proteins, and therapy. Physiol Rev 81:741-766.
    • (2001) Physiol Rev , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 90
    • 0034142022 scopus 로고    scopus 로고
    • A distinct ER/IC gamma-secretase competes with the proteasome for cleavage of APP
    • Skovronsky DM, Pijak DS, Doms RW, Lee VM. 2000. A distinct ER/IC gamma-secretase competes with the proteasome for cleavage of APP. Biochemistry 39:810-817.
    • (2000) Biochemistry , vol.39 , pp. 810-817
    • Skovronsky, D.M.1    Pijak, D.S.2    Doms, R.W.3    Lee, V.M.4
  • 91
    • 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, Clarris H, Moir R, Beyreuther K, Masters CL. 1994. A heparin-binding domain in the amyloid protein precursor of Alzheimer's disease is involved in the regulation of neurite outgrowth. J Neurosci 14:2117-2127.
    • (1994) J Neurosci , vol.14 , pp. 2117-2127
    • Small, D.H.1    Nurcombe, V.2    Reed, G.3    Clarris, H.4    Moir, R.5    Beyreuther, K.6    Masters, C.L.7
  • 92
    • 0035433962 scopus 로고    scopus 로고
    • Alzheimer's disease and Abeta toxicity: From top to bottom
    • Small DH, Mok SS, Bornstein JC. 2001. Alzheimer's disease and Abeta toxicity: from top to bottom. Nat Rev Neurosci 2:595-598.
    • (2001) Nat Rev Neurosci , vol.2 , pp. 595-598
    • Small, D.H.1    Mok, S.S.2    Bornstein, J.C.3
  • 94
    • 0033599341 scopus 로고    scopus 로고
    • X11L2, a new member of the X11 protein family, interacts with Alzheimer's beta-amyloid precursor protein
    • Tanahashi H, Tabira T. 1999. X11L2, a new member of the X11 protein family, interacts with Alzheimer's beta-amyloid precursor protein. Biochem Biophys Res Commun 255:663-667.
    • (1999) Biochem Biophys Res Commun , vol.255 , pp. 663-667
    • Tanahashi, H.1    Tabira, T.2
  • 95
    • 0036844981 scopus 로고    scopus 로고
    • Characterization of an amyloid precursor protein-binding protein Fe65L2 and its novel isoforms lacking phosphotyrosine-interaction domains
    • Tanahashi H, Tabira T. 2002. Characterization of an amyloid precursor protein-binding protein Fe65L2 and its novel isoforms lacking phosphotyrosine-interaction domains. Biochem J 367:687-695.
    • (2002) Biochem J , vol.367 , pp. 687-695
    • Tanahashi, H.1    Tabira, T.2
  • 96
    • 0037205493 scopus 로고    scopus 로고
    • Interaction of Alzheimer's beta-amyloid precursor family proteins with scaffold proteins of the JNK signaling cascade
    • Taru H, Iijima K, Hase M, Kirino Y, Yagi Y, Suzuki T. 2002a. Interaction of Alzheimer's beta-amyloid precursor family proteins with scaffold proteins of the JNK signaling cascade. J Biol Chem 277:20070-20078.
    • (2002) J Biol Chem , vol.277 , pp. 20070-20078
    • Taru, H.1    Iijima, K.2    Hase, M.3    Kirino, Y.4    Yagi, Y.5    Suzuki, T.6
  • 97
    • 0037178872 scopus 로고    scopus 로고
    • Differential roles of JIP scaffold proteins in the modulation of amyloid precursor protein metabolism
    • Taru H, Kirino Y, Suzuki T. 2002b. Differential roles of JIP scaffold proteins in the modulation of amyloid precursor protein metabolism. J Biol Chem 277:27567-27574.
    • (2002) J Biol Chem , vol.277 , pp. 27567-27574
    • Taru, H.1    Kirino, Y.2    Suzuki, T.3
  • 98
  • 99
    • 0032509346 scopus 로고    scopus 로고
    • Interaction of cytosolic adaptor proteins with neuronal apolipoprotein E receptors and the amyloid precursor protein
    • Trommsdorff M, Borg JP, Margolis B, Herz J. 1998. Interaction of cytosolic adaptor proteins with neuronal apolipoprotein E receptors and the amyloid precursor protein. J Biol Chem 273:33556-33560.
    • (1998) J Biol Chem , vol.273 , pp. 33556-33560
    • Trommsdorff, M.1    Borg, J.P.2    Margolis, B.3    Herz, J.4
  • 101
    • 5444275067 scopus 로고    scopus 로고
    • The APP intracellular domain forms nuclear multiprotein complexes and regulates the transcription of its own precursor
    • von Rotz RC, Kohli BM, Bosset J, Meier M, Suzuki T, Nitsch RM, Konietzko U. 2004. The APP intracellular domain forms nuclear multiprotein complexes and regulates the transcription of its own precursor. J Cell Sci 117:4435-4448.
    • (2004) J Cell Sci , vol.117 , pp. 4435-4448
    • Von Rotz, R.C.1    Kohli, B.M.2    Bosset, J.3    Meier, M.4    Suzuki, T.5    Nitsch, R.M.6    Konietzko, U.7
  • 103
    • 0024550204 scopus 로고
    • Identification, biogenesis, and localization of precursors of Alzheimer's disease A4 amyloid protein
    • Weidemann A, Konig G, Bunke D, Fischer P, Salbaum JM, Masters CL, Beyreuther K. 1989. Identification, biogenesis, and localization of precursors of Alzheimer's disease A4 amyloid protein. Cell 57:115-126.
    • (1989) Cell , vol.57 , pp. 115-126
    • Weidemann, A.1    Konig, G.2    Bunke, D.3    Fischer, P.4    Salbaum, J.M.5    Masters, C.L.6    Beyreuther, K.7
  • 109
    • 0033605588 scopus 로고    scopus 로고
    • Calpain inhibitor I increases beta-amyloid peptide production by inhibiting the degradation of the substrate of gamma-secretase
    • Zhang L, Song L, Parker EM. 1999. Calpain inhibitor I increases beta-amyloid peptide production by inhibiting the degradation of the substrate of gamma-secretase. J Biol Chem 274:8966-8972.
    • (1999) J Biol Chem , vol.274 , pp. 8966-8972
    • Zhang, L.1    Song, L.2    Parker, E.M.3
  • 110
    • 0030723614 scopus 로고    scopus 로고
    • Sequence-specific recognition of the internalization motif of the Alzheimer's amyloid precursor protein by the X11 PTB domain
    • Zhang Z, Lee CH, Mandiyan V, Borg JP, Margolis B, Schlessinger J, Kuriyan J. 1997. Sequence-specific recognition of the internalization motif of the Alzheimer's amyloid precursor protein by the X11 PTB domain. EMBO J 16:6141-6150.
    • (1997) EMBO J , vol.16 , pp. 6141-6150
    • Zhang, Z.1    Lee, C.H.2    Mandiyan, V.3    Borg, J.P.4    Margolis, B.5    Schlessinger, J.6    Kuriyan, J.7
  • 111
    • 0033779635 scopus 로고    scopus 로고
    • Presenilins are required for gamma-secretase cleavage of beta-APP and transmembrane cleavage of Notch-1
    • Zhang Z, Nadeau P, Song W, Donoviel D, Yuan M, Bernstein A, Yankner BA. 2000. Presenilins are required for gamma-secretase cleavage of beta-APP and transmembrane cleavage of Notch-1. Nat Cell Biol 2:463-465.
    • (2000) Nat Cell Biol , vol.2 , pp. 463-465
    • Zhang, Z.1    Nadeau, P.2    Song, W.3    Donoviel, D.4    Yuan, M.5    Bernstein, A.6    Yankner, B.A.7
  • 113
    • 0032410747 scopus 로고    scopus 로고
    • PAT1, a microtubule-interacting protein, recognizes the basolateral sorting signal of amyloid precursor protein
    • Zheng P, Eastman J, Vande Pol S, Pimplikar SW. 1998. PAT1, a microtubule-interacting protein, recognizes the basolateral sorting signal of amyloid precursor protein. Proc Natl Acad Sci U S A 95:14745-14750.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 14745-14750
    • Zheng, P.1    Eastman, J.2    Vande Pol, S.3    Pimplikar, S.W.4


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