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Volumn 185, Issue 2, 2004, Pages 208-219

Adaptor protein interactions: Modulators of amyloid precursor protein metabolism and Alzheimer's disease risk?

Author keywords

Adaptor proteins; Alzheimer's disease; Amyloid precursor protein; A ; Fe65; JIP; Mint; PTB domain; X11; Secretase; Secretase

Indexed keywords

ADAPTOR PROTEIN; ADAPTOR PROTEIN X11; ALPHA SECRETASE; AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; BETA SECRETASE; CYCLOSPORIN; FUSICOCCIN; GAMMA SECRETASE; PHOSPHOTYROSINE; PROTEIN FE65; PROTEIN INHIBITOR; PROTEINASE INHIBITOR; RAPAMYCIN; STRESS ACTIVATED PROTEIN KINASE; TACROLIMUS; UNCLASSIFIED DRUG;

EID: 0345743462     PISSN: 00144886     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.expneurol.2003.10.011     Document Type: Review
Times cited : (141)

References (154)
  • 2
    • 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 K., Elliott J.I., Kirino Y., Suzuki T. Phosphorylation-dependent regulation of the interaction of amyloid precursor protein with Fe65 affects the production of beta-amyloid. J. Biol. Chem. 276:2001;40353-40361.
    • (2001) J. Biol. Chem. , vol.276 , pp. 40353-40361
    • Ando, K.1    Iijima, K.2    Elliott, J.I.3    Kirino, Y.4    Suzuki, T.5
  • 3
    • 1542782550 scopus 로고    scopus 로고
    • Novel cadherin-related membrane proteins, Alcadeins, enhance the X11-like protein-mediated stabilization of amyloid beta-protein precursor metabolism
    • (in press)
    • Araki Y., Tomita S., Yamaguchi H., Miyagi N., Sumioka A., Kirino Y., Suzuki T. Novel cadherin-related membrane proteins, Alcadeins, enhance the X11-like protein-mediated stabilization of amyloid beta-protein precursor metabolism. J. Biol. Chem. 2003;. (in press).
    • (2003) J. Biol. Chem.
    • Araki, Y.1    Tomita, S.2    Yamaguchi, H.3    Miyagi, N.4    Sumioka, A.5    Kirino, Y.6    Suzuki, T.7
  • 4
    • 0032760270 scopus 로고    scopus 로고
    • It all sticks together - The APP-related family of proteins and Alzheimer's disease
    • Bayer T.A., Cappai R., Masters C.L., Beyreuther K., Multhaup G. It all sticks together - The APP-related family of proteins and Alzheimer's disease. Mol. Psychiatry. 4:1999;524-528.
    • (1999) Mol. Psychiatry , vol.4 , pp. 524-528
    • Bayer, T.A.1    Cappai, R.2    Masters, C.L.3    Beyreuther, K.4    Multhaup, G.5
  • 6
    • 0034704089 scopus 로고    scopus 로고
    • Mints as adaptors - Direct binding to neurexins and recruitment of Munc18
    • Biederer T., Sudhof T.C. Mints as adaptors - Direct binding to neurexins and recruitment of Munc18. J. Biol. Chem. 275:2000;39803-39806.
    • (2000) J. Biol. Chem. , vol.275 , pp. 39803-39806
    • Biederer, T.1    Sudhof, T.C.2
  • 7
    • 0036759068 scopus 로고    scopus 로고
    • Regulation of APP-dependent transcription complexes by Mint/X11s: Differential functions of mint isoforms
    • Biederer T., Cao X.W., Sudhof T.C., Liu X.R. Regulation of APP-dependent transcription complexes by Mint/X11s: differential functions of mint isoforms. J. Neurosci. 22:2002;7340-7351.
    • (2002) J. Neurosci. , vol.22 , pp. 7340-7351
    • Biederer, T.1    Cao, X.W.2    Sudhof, T.C.3    Liu, X.R.4
  • 10
    • 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 J.P., Ooi J., Levy E., Margolis B. The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein. Mol. Cell. Biol. 16:1996;6229-6241.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6229-6241
    • Borg, J.P.1    Ooi, J.2    Levy, E.3    Margolis, B.4
  • 12
    • 0032510834 scopus 로고    scopus 로고
    • The X11alpha protein slows cellular amyloid precursor protein processing and reduces Abeta40 and Abeta42 secretion
    • Borg J.P., Yang Y., De Taddeo-Borg M., Margolis B., Turner R.S. The X11alpha protein slows cellular amyloid precursor protein processing and reduces Abeta40 and Abeta42 secretion. J. Biol. Chem. 273:1998;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
  • 14
    • 0025965521 scopus 로고
    • Beta-Amyloid precursor protein mediates neuronal cell-cell and cell-surface adhesion
    • Breen K.C., Bruce M., Anderton B.H. Beta-Amyloid precursor protein mediates neuronal cell-cell and cell-surface adhesion. J. Neurosci. Res. 28:1991;90-100.
    • (1991) J. Neurosci. Res. , vol.28 , pp. 90-100
    • Breen, K.C.1    Bruce, M.2    Anderton, B.H.3
  • 15
    • 10144251747 scopus 로고    scopus 로고
    • CDNA cloning and chromosome mapping of the human Fe65 gene: Interaction of the conserved cytoplasmic domains of the human beta-amyloid precursor protein and its homologues with the mouse Fe65 protein
    • Bressler S.L., Gray M.D., Sopher B.L., Hu Q.B., Hearn M.G., Pham D.G., Dinulos M.B., Fukuchi K.I., Sisodia S.S., Miller M.A., Disteche C.M., Martin G.M. cDNA cloning and chromosome mapping of the human Fe65 gene: interaction of the conserved cytoplasmic domains of the human beta-amyloid precursor protein and its homologues with the mouse Fe65 protein. Human Mol. Genet. 5:1996;1589-1598.
    • (1996) Human Mol. Genet. , vol.5 , pp. 1589-1598
    • Bressler, S.L.1    Gray, M.D.2    Sopher, B.L.3    Hu, Q.B.4    Hearn, M.G.5    Pham, D.G.6    Dinulos, M.B.7    Fukuchi, K.I.8    Sisodia, S.S.9    Miller, M.A.10    Disteche, C.M.11    Martin, G.M.12
  • 16
    • 0033103343 scopus 로고    scopus 로고
    • The amyloid precursor protein interacts with Go heterotrimeric protein within a cell compartment specialized for signal transduction
    • Brouillet E., Trembleau A., Galanaud D., Volovitch M., Bouillot C., Valenza C., Prochiantz A., Allinquant B. The amyloid precursor protein interacts with Go heterotrimeric protein within a cell compartment specialized for signal transduction. J. Neurosci. 19:1999;1717-1727.
    • (1999) J. Neurosci. , vol.19 , pp. 1717-1727
    • Brouillet, E.1    Trembleau, A.2    Galanaud, D.3    Volovitch, M.4    Bouillot, C.5    Valenza, C.6    Prochiantz, A.7    Allinquant, B.8
  • 17
    • 0032544613 scopus 로고    scopus 로고
    • A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain
    • Butz S., Okamoto M., Sudhof T.C. A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Cell. 94:1998;773-782.
    • (1998) Cell , vol.94 , pp. 773-782
    • Butz, S.1    Okamoto, M.2    Sudhof, T.C.3
  • 19
    • 17944372928 scopus 로고    scopus 로고
    • A transcriptively active complex of APP with Fe65 and histone acetyltransferase Tip60
    • Cao X., Sudhof T.C. A transcriptively active complex of APP with Fe65 and histone acetyltransferase Tip60. Science. 293:2001;1436.
    • (2001) Science , vol.293 , pp. 1436
    • Cao, X.1    Sudhof, T.C.2
  • 20
    • 0033953961 scopus 로고    scopus 로고
    • Increased generation of alternatively cleaved beta-amyloid peptides in cells expressing mutants of the amyloid precursor protein defective in endocytosis
    • Cescato R., Dumermuth E., Spiess M., Paganetti P.A. Increased generation of alternatively cleaved beta-amyloid peptides in cells expressing mutants of the amyloid precursor protein defective in endocytosis. J. Neurochem. 74:2000;1131-1139.
    • (2000) J. Neurochem. , vol.74 , pp. 1131-1139
    • Cescato, R.1    Dumermuth, E.2    Spiess, M.3    Paganetti, P.A.4
  • 22
    • 0025759161 scopus 로고
    • An antibody to beta-Amyloid and the Amyloid Precursor Protein inhibits cell-substratum adhesion in many mammalian-cell types
    • Chen M., Yankner B.A. An antibody to beta-Amyloid and the Amyloid Precursor Protein inhibits cell-substratum adhesion in many mammalian-cell types. Neurosci. Lett. 125:1991;223-226.
    • (1991) Neurosci. Lett. , vol.125 , pp. 223-226
    • Chen, M.1    Yankner, B.A.2
  • 23
    • 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 W.J., Goldstein J.L., Brown M.S. NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor. J. Biol. Chem. 265:1990;3116-3123.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3116-3123
    • Chen, W.J.1    Goldstein, J.L.2    Brown, M.S.3
  • 24
    • 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.Z., McPhie D.L., Hirschberg J., Neve R.L. 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. 275:2000;8929-8935.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8929-8935
    • Chen, Y.Z.1    McPhie, D.L.2    Hirschberg, J.3    Neve, R.L.4
  • 25
    • 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 D.L., Hassinger L., Neve R. APP-BP1 mediates APP-induced apoptosis and DNA synthesis and is increased in Alzheimer's disease brain. J. Cell Biol. 163:2003;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.5
  • 26
    • 0029842109 scopus 로고    scopus 로고
    • Structure of the FKBP12-rapamycin complex interacting with binding domain of human FRAP
    • Choi J., Chen J., Schreiber S.L., Clardy J. Structure of the FKBP12-rapamycin complex interacting with binding domain of human FRAP. Science. 273:1996;239.
    • (1996) Science , vol.273 , pp. 239
    • Choi, J.1    Chen, J.2    Schreiber, S.L.3    Clardy, J.4
  • 27
    • 15844408798 scopus 로고    scopus 로고
    • APP-BP1, a novel protein that binds to the carboxy-terminal region of the amyloid precursor protein
    • Chow N., Korenberg J.R., Chen X.-N., Neve R.L. APP-BP1, a novel protein that binds to the carboxy-terminal region of the amyloid precursor protein. J. Biol. Chem. 271:1996;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
  • 28
    • 0036861132 scopus 로고    scopus 로고
    • Emerging Alzheimer's disease therapies: Inhibition of beta-secretase
    • Citron M. Emerging Alzheimer's disease therapies: inhibition of beta-secretase. Neurobiol. Aging. 23:2002;1017-1022.
    • (2002) Neurobiol. Aging , vol.23 , pp. 1017-1022
    • Citron, M.1
  • 29
    • 0025635559 scopus 로고
    • Tranferrin receptor internalization sequence YXRF implicates a tight turn as the structural recognition motif for endocytosis
    • Collawn J.F., Stangel M., Kuhn L.A., Esekogwu V., Jing S.Q., Trowbridge I.S., Tainer J.A. Tranferrin receptor internalization sequence YXRF implicates a tight turn as the structural recognition motif for endocytosis. Cell. 63:1990;1061-1072.
    • (1990) Cell , vol.63 , pp. 1061-1072
    • Collawn, J.F.1    Stangel, M.2    Kuhn, L.A.3    Esekogwu, V.4    Jing, S.Q.5    Trowbridge, I.S.6    Tainer, J.A.7
  • 31
    • 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. Fe65L2: a new member of the Fe65 protein family interacting with the intracellular domain of the Alzheimer's beta-amyloid precursor protein. Biochem. J. 330:1998;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
  • 33
    • 0031451149 scopus 로고    scopus 로고
    • The WW domain of neural protein Fe65 interacts with proline-rich motifs in Mena, the mammalian homolog of Drosophila enabled
    • Ermekova K.S., Zambrano N., Linn H., Minopoli G., Gertler F., Russo T., Sudol M. The WW domain of neural protein Fe65 interacts with proline-rich motifs in Mena, the mammalian homolog of Drosophila enabled. J. Biol. Chem. 272:1997;32869-32877.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32869-32877
    • Ermekova, K.S.1    Zambrano, N.2    Linn, H.3    Minopoli, G.4    Gertler, F.5    Russo, T.6    Sudol, M.7
  • 35
    • 0030044888 scopus 로고    scopus 로고
    • Missense mutations associated with familial Alzheimer's disease in Sweden lead to the production of the amyloid peptide without internalization of its precursor
    • Essalmani R., Macq A.F., Mercken L., Octave J.N. Missense mutations associated with familial Alzheimer's disease in Sweden lead to the production of the amyloid peptide without internalization of its precursor. Biochem. Biophys. Res. Commun. 218:1996;89-96.
    • (1996) Biochem. Biophys. Res. Commun. , vol.218 , pp. 89-96
    • Essalmani, R.1    MacQ, A.F.2    Mercken, L.3    Octave, J.N.4
  • 36
    • 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. 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. 270:1995;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
  • 38
    • 0027082156 scopus 로고
    • A 109-Amino-Acid C-Terminal fragment of Alzheimer's disease amyloid precursor protein contains a sequence, -RHDS-, that promotes cell-adhesion
    • Ghiso J., Rostagno A., Gardella J.E., Liem L., Gorevic P.D., Frangione B. A 109-Amino-Acid C-Terminal fragment of Alzheimer's disease amyloid precursor protein contains a sequence, -RHDS-, that promotes cell-adhesion. Biochem. J. 288:1992;1053-1059.
    • (1992) Biochem. J. , vol.288 , pp. 1053-1059
    • Ghiso, J.1    Rostagno, A.2    Gardella, J.E.3    Liem, L.4    Gorevic, P.D.5    Frangione, B.6
  • 43
    • 0036677899 scopus 로고    scopus 로고
    • Low-density lipoprotein receptor-related protein levels and endocytic function are reduced by overexpression of the FE65 adaptor protein, FE65L1
    • Guenette S.Y., Chang Y., Hyman B.T., Tanzi R.E., Rebeck G.W. Low-density lipoprotein receptor-related protein levels and endocytic function are reduced by overexpression of the FE65 adaptor protein, FE65L1. J. Neurochem. 82:2002;755-762.
    • (2002) J. Neurochem. , vol.82 , pp. 755-762
    • Guenette, S.Y.1    Chang, Y.2    Hyman, B.T.3    Tanzi, R.E.4    Rebeck, G.W.5
  • 45
    • 0026546599 scopus 로고
    • An anatomical cascade hypothesis for Alzheimers disease
    • Hardy J. An anatomical cascade hypothesis for Alzheimers disease. Trends Neurosci. 15:1992;200-201.
    • (1992) Trends Neurosci. , vol.15 , pp. 200-201
    • Hardy, J.1
  • 50
    • 0141481046 scopus 로고    scopus 로고
    • Munc 18 interacting (MINT) proteins: Arf-dependent coat proteins that regulate traffic of the Alzheimer's precursor protein (beta-APP)
    • Hill K., Li Y., Bennett M., McKay M., Zhu X., Shern J., Torre E., Lah J.J., Levey A.I., Kahn R.A. Munc 18 interacting (MINT) proteins: Arf-dependent coat proteins that regulate traffic of the Alzheimer's precursor protein (beta-APP). J. Biol. Chem. 2003.
    • (2003) J. Biol. Chem.
    • Hill, K.1    Li, Y.2    Bennett, M.3    McKay, M.4    Zhu, X.5    Shern, J.6    Torre, E.7    Lah, J.J.8    Levey, A.I.9    Kahn, R.A.10
  • 51
  • 52
    • 0037417897 scopus 로고    scopus 로고
    • A role for Mints in transmitter release: Mint 1 knockout mice exhibit impaired GABAergic synaptic transmission
    • Ho A., Morishita W., Hammer R.E., Malenka R.C., Sudhof T.C. A role for Mints in transmitter release: mint 1 knockout mice exhibit impaired GABAergic synaptic transmission. Proc. Natl. Acad. Sci. U. S. A. 100:2003;1409-1414.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 1409-1414
    • Ho, A.1    Morishita, W.2    Hammer, R.E.3    Malenka, R.C.4    Sudhof, T.C.5
  • 53
    • 0033198295 scopus 로고    scopus 로고
    • Disabled-1 binds to the cytoplasmic domain of amyloid precursor-like protein 1
    • Homayouni R., Rice D.S., Sheldon M., Curran T. Disabled-1 binds to the cytoplasmic domain of amyloid precursor-like protein 1. J. Neurosci. 19:1999;7507-7515.
    • (1999) J. Neurosci. , vol.19 , pp. 7507-7515
    • Homayouni, R.1    Rice, D.S.2    Sheldon, M.3    Curran, T.4
  • 54
    • 0030067804 scopus 로고    scopus 로고
    • The C. elegans vulval induction gene lin-2 encodes a member of the MAGUK family of cell junction proteins
    • Hoskins R., Hajnal A.F., Harp S.A., Kim S.K. The C. elegans vulval induction gene lin-2 encodes a member of the MAGUK family of cell junction proteins. Development. 122:1996;97-111.
    • (1996) Development , vol.122 , pp. 97-111
    • Hoskins, R.1    Hajnal, A.F.2    Harp, S.A.3    Kim, S.K.4
  • 55
    • 0033066680 scopus 로고    scopus 로고
    • The disabled 1 phosphotyrosine-binding domain binds to the internalization signals of transmembrane glycoproteins and to phospholipids
    • Howell B.W., Lanier L.M., Frank R., Gertler F.B., Cooper J.A. The disabled 1 phosphotyrosine-binding domain binds to the internalization signals of transmembrane glycoproteins and to phospholipids. Mol. Cell. Biol. 19:1999;5179-5188.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5179-5188
    • Howell, B.W.1    Lanier, L.M.2    Frank, R.3    Gertler, F.B.4    Cooper, J.A.5
  • 56
    • 0031710443 scopus 로고    scopus 로고
    • The human Fe65 gene: Genomic structure and intronic biallelic polymorphism associated with sporadic dementia of the Alzheimer type
    • Hu Q., Kukull W.A., Bressler S.L., Gray M.D., Cam J.A., Larson E.B., Martin G.M., Deeb S.S. The human Fe65 gene: genomic structure and intronic biallelic polymorphism associated with sporadic dementia of the Alzheimer type. Hum. Genet. 103:1998;295-303.
    • (1998) Hum. Genet. , vol.103 , pp. 295-303
    • Hu, Q.1    Kukull, W.A.2    Bressler, S.L.3    Gray, M.D.4    Cam, J.A.5    Larson, E.B.6    Martin, G.M.7    Deeb, S.S.8
  • 57
    • 0037084853 scopus 로고    scopus 로고
    • A candidate molecular mechanism for the association of an intronic polymorphism of FE65 with resistance to very late onset dementia of the Alzheimer type
    • Hu Q.B., Cool B.H., Wang B.P., Hearn M.G., Martin G.M. A candidate molecular mechanism for the association of an intronic polymorphism of FE65 with resistance to very late onset dementia of the Alzheimer type. Human Mol. Genet. 11:2002;465-475.
    • (2002) Human Mol. Genet. , vol.11 , pp. 465-475
    • Hu, Q.B.1    Cool, B.H.2    Wang, B.P.3    Hearn, M.G.4    Martin, G.M.5
  • 59
    • 0032562615 scopus 로고    scopus 로고
    • Caveolae, plasma membrane microdomains for alpha-secretase mediated processing of amyloid precursor protein
    • Ikezu T., Trapp B.D., Song K.S., Schlegel A., Lisante M.P., Okamoto T. Caveolae, plasma membrane microdomains for alpha-secretase mediated processing of amyloid precursor protein. J. Biol. Chem. 273:1998;10485-10495.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10485-10495
    • Ikezu, T.1    Trapp, B.D.2    Song, K.S.3    Schlegel, A.4    Lisante, M.P.5    Okamoto, T.6
  • 60
    • 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. A scaffold protein JIP-1b enhances amyloid precursor protein phosphorylation by JNK and its association with kinesin light chain 1. J. Biol. Chem. 278:2003;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
  • 61
    • 0028136865 scopus 로고
    • Peptides containing the RERMS sequence of amyloid beta/A4 protein-precursor bind cell-surface and promote neurite extension
    • Jin L.W., Ninomiya H., Roch J.M., Schubert D., Masliah E., Otero D.A.C., Saitoh T. Peptides containing the RERMS sequence of amyloid beta/A4 protein-precursor bind cell-surface and promote neurite extension. J. Neurosci. 14:1994;5461-5470.
    • (1994) J. Neurosci. , vol.14 , pp. 5461-5470
    • Jin, L.W.1    Ninomiya, H.2    Roch, J.M.3    Schubert, D.4    Masliah, E.5    Otero, D.A.C.6    Saitoh, T.7
  • 62
    • 0033151584 scopus 로고    scopus 로고
    • Characterization of MALS/Velis-1, -1, and -3: A family of mammalian Lin-7 homologs enriched at brain synapses in association with the postsynaptic density 95/NMDA receptor postsynaptic complex
    • Jo K., Derin R., Li M., Bredt D.S. Characterization of MALS/Velis-1, -1, and -3: a family of mammalian Lin-7 homologs enriched at brain synapses in association with the postsynaptic density 95/NMDA receptor postsynaptic complex. J. Neurosci. 19:1999;4189-4199.
    • (1999) J. Neurosci. , vol.19 , pp. 4189-4199
    • Jo, K.1    Derin, R.2    Li, M.3    Bredt, D.S.4
  • 63
    • 0024447098 scopus 로고
    • Diffuse senile plaques occur commonly in the cerebellum in Alzheimers disease
    • Joachim C.L., Morris J.H., Selkoe D.J. Diffuse senile plaques occur commonly in the cerebellum in Alzheimers disease. Am. J. Pathol. 135:1989;309-319.
    • (1989) Am. J. Pathol. , vol.135 , pp. 309-319
    • Joachim, C.L.1    Morris, J.H.2    Selkoe, D.J.3
  • 64
    • 0032544565 scopus 로고    scopus 로고
    • The LIN-2/LIN-7/LIN-10 complex mediates basolateral membrane localization of the C. elegans EGF receptor LET-23 in vulval epithelial cells
    • Kaech S.M., Whitfield C.W., Kim S.K. The LIN-2/LIN-7/LIN-10 complex mediates basolateral membrane localization of the C. elegans EGF receptor LET-23 in vulval epithelial cells. Cell. 94:1998;761-771.
    • (1998) Cell , vol.94 , pp. 761-771
    • Kaech, S.M.1    Whitfield, C.W.2    Kim, S.K.3
  • 65
    • 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 G.B., Yang Z.H., Xia C.H., Goldstein L.S.B. Axonal transport of amyloid precursor protein is mediated by direct binding to the kinesin light chain subunit of kinesin-I. Neuron. 28:2000;449-459.
    • (2000) Neuron , vol.28 , pp. 449-459
    • Kamal, A.1    Stokin, G.B.2    Yang, Z.H.3    Xia, C.H.4    Goldstein, L.S.B.5
  • 66
    • 0035818998 scopus 로고    scopus 로고
    • Kinesin-mediated axonal transport of a membrane compartment containing beta-secretase and presenilin-1 requires APP
    • Kamal A., Almenar-Queralt A., LeBlanc J.F., Roberts E.A., Goldstein L.S.B. Kinesin-mediated axonal transport of a membrane compartment containing beta-secretase and presenilin-1 requires APP. Nature. 414:2001;643-648.
    • (2001) Nature , vol.414 , pp. 643-648
    • Kamal, A.1    Almenar-Queralt, A.2    Leblanc, J.F.3    Roberts, E.A.4    Goldstein, L.S.B.5
  • 69
    • 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 W.T., Zheng J.B., Guenette S.Y., Selkoe D.J. 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. 276:2001;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
  • 70
    • 0346435147 scopus 로고    scopus 로고
    • X11alpha impairs gamma but not beta-secretase cleavage of amyloid precursor protein
    • (in press)
    • King G.D., Cherian K., Turner R.S. X11alpha impairs gamma but not beta-secretase cleavage of amyloid precursor protein. J. Neurochem. 2004;. (in press).
    • (2004) J. Neurochem.
    • King, G.D.1    Cherian, K.2    Turner, R.S.3
  • 71
    • 0037827785 scopus 로고    scopus 로고
    • X11alpha modulates secretory and endocytic trafficking and metabolism of Amyloid Precursor Protein: Mutational analysis of the YENPTY sequence
    • King G.D., Perez R.G., Steinhilb M.L., Gaut J.R., Turner R.S. X11alpha modulates secretory and endocytic trafficking and metabolism of Amyloid Precursor Protein: mutational analysis of the YENPTY sequence. Neuroscience. 120:2003;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
  • 72
    • 0035503797 scopus 로고    scopus 로고
    • Demonstration by fluorescence resonance energy transfer of two sites of interaction between the low-density lipoprotein receptor-related protein and the amyloid precursor protein: Role of the intracellular adapter protein Fe65
    • Kinoshita A., Whelan C.M., Smith C.J., Mikhailenko I., Rebeck G.W., Strickland D.K., Hyman B.T. Demonstration by fluorescence resonance energy transfer of two sites of interaction between the low-density lipoprotein receptor-related protein and the amyloid precursor protein: role of the intracellular adapter protein Fe65. J. Neurosci. 21:2001;8354-8361.
    • (2001) J. Neurosci. , vol.21 , pp. 8354-8361
    • Kinoshita, A.1    Whelan, C.M.2    Smith, C.J.3    Mikhailenko, I.4    Rebeck, G.W.5    Strickland, D.K.6    Hyman, B.T.7
  • 73
    • 0028276801 scopus 로고
    • Evidence that production and release of amyloid beta-protein involves the endocytic pathway
    • Koo E.H., Squazzo S.L. Evidence that production and release of amyloid beta-protein involves the endocytic pathway. J. Biol. Chem. 269:1994;17386- 17389.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17386-17389
    • Koo, E.H.1    Squazzo, S.L.2
  • 74
    • 0032488923 scopus 로고    scopus 로고
    • Signal-dependent trafficking of beta-amyloid precursor protein-transferrin receptor chimeras in Madin-Darby canine kidney cells
    • Lai A., Gibson A., Hopkins C.R., Trowbridge I.S. Signal-dependent trafficking of beta-amyloid precursor protein-transferrin receptor chimeras in Madin-Darby canine kidney cells. J. Biol. Chem. 273:1998;3732-3739.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3732-3739
    • Lai, A.1    Gibson, A.2    Hopkins, C.R.3    Trowbridge, I.S.4
  • 77
    • 0034626631 scopus 로고    scopus 로고
    • Fe65 and X11 beta co-localize with and compete for binding to the amyloid precursor protein
    • Lau K.F., McLoughlin D.M., Standen C.L., Irving N.G., Miller C.C.J. Fe65 and X11 beta co-localize with and compete for binding to the amyloid precursor protein. NeuroReport. 11:2000;3607-3610.
    • (2000) NeuroReport , vol.11 , pp. 3607-3610
    • Lau, K.F.1    McLoughlin, D.M.2    Standen, C.L.3    Irving, N.G.4    Miller, C.C.J.5
  • 78
    • 0027943816 scopus 로고
    • Production of Alzheimer 4-kDa beta-amyloid peptide requires the C-terminal cytosolic domain of the amyloid precursor protein
    • Leblanc A.C., Gambetti P. Production of Alzheimer 4-kDa beta-amyloid peptide requires the C-terminal cytosolic domain of the amyloid precursor protein. Biochem. Biophys. Res. Commun. 204:1994;1371-1380.
    • (1994) Biochem. Biophys. Res. Commun. , vol.204 , pp. 1371-1380
    • Leblanc, A.C.1    Gambetti, P.2
  • 79
    • 0034725615 scopus 로고    scopus 로고
    • Regulation of X11L-dependent amyloid precursor protein metabolism by XB51, a novel X11L-binding protein
    • Lee D.S., Tomita S., Kirino Y., Suzuki T. Regulation of X11L-dependent amyloid precursor protein metabolism by XB51, a novel X11L-binding protein. J. Biol. Chem. 275:2000;23134-23138.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23134-23138
    • Lee, D.S.1    Tomita, S.2    Kirino, Y.3    Suzuki, T.4
  • 80
    • 0037160063 scopus 로고    scopus 로고
    • Mammalian APH-1 interacts with Presenilin and Nicastrin and is required for intramembrane proteolysis of amyloid-beta precursor protein and Notch
    • Lee S.-F., Shah S., Li H., Yu C., Han W., Yu G. Mammalian APH-1 interacts with Presenilin and Nicastrin and is required for intramembrane proteolysis of amyloid-beta precursor protein and Notch. J. Biol. Chem. 277:2000;45013-45019.
    • (2000) J. Biol. Chem. , vol.277 , pp. 45013-45019
    • Lee, S.-F.1    Shah, S.2    Li, H.3    Yu, C.4    Han, W.5    Yu, G.6
  • 86
    • 0141532147 scopus 로고    scopus 로고
    • Amyloid beta protein precursor, but not APLP2, is bridged to the kinesin light chain by the scaffold protein JNK-interacting protein 1
    • Matsuda S., Matsuda Y., Dadamio L. Amyloid beta protein precursor, but not APLP2, is bridged to the kinesin light chain by the scaffold protein JNK-interacting protein 1. J. Biol. Chem. 278:2003;38601-38606.
    • (2003) J. Biol. Chem. , vol.278 , pp. 38601-38606
    • Matsuda, S.1    Matsuda, Y.2    Dadamio, L.3
  • 87
    • 0027478347 scopus 로고
    • Evidence for excitoprotective and intraneuronal calcium-regulating roles for secreted forms of the beta-amyloid precursor protein
    • Mattson M.P., Cheng B., Culwell A.R., Esch F.S., Lieberburg I., Rydel R.E. Evidence for excitoprotective and intraneuronal calcium-regulating roles for secreted forms of the beta-amyloid precursor protein. Neuron. 10:1993;243-254.
    • (1993) Neuron , vol.10 , pp. 243-254
    • Mattson, M.P.1    Cheng, B.2    Culwell, A.R.3    Esch, F.S.4    Lieberburg, I.5    Rydel, R.E.6
  • 88
    • 0040962408 scopus 로고    scopus 로고
    • Association of neuronal calcium channels with modular adaptor proteins
    • Maximov A., Sudhof T.C., Bezprozvanny I. Association of neuronal calcium channels with modular adaptor proteins. J. Biol. Chem. 274:1999;24453-24456.
    • (1999) J. Biol. Chem. , vol.274 , pp. 24453-24456
    • Maximov, A.1    Sudhof, T.C.2    Bezprozvanny, I.3
  • 89
    • 0030592773 scopus 로고    scopus 로고
    • The intracellular cytoplasmic domain of the Alzheimer's disease amyloid precursor protein interacts with phosphotyrosine-binding domain proteins in the yeast two-hybrid system
    • McLoughlin D.M., Miller C.C.J. The intracellular cytoplasmic domain of the Alzheimer's disease amyloid precursor protein interacts with phosphotyrosine-binding domain proteins in the yeast two-hybrid system. FEBS Lett. 397:1996;197-200.
    • (1996) FEBS Lett. , vol.397 , pp. 197-200
    • McLoughlin, D.M.1    Miller, C.C.J.2
  • 90
    • 0033006807 scopus 로고    scopus 로고
    • Mint2/X11-like colocalizes with the Alzheimer's disease amyloid precursor protein and is associated with neuritic plaques in Alzheimer's disease
    • McLoughlin D.M., Irving N.G., Brownlees J., Brion J.P., Leroy K., Miller C.C.J. Mint2/X11-like colocalizes with the Alzheimer's disease amyloid precursor protein and is associated with neuritic plaques in Alzheimer's disease. Eur. J. Neurosci. 11:1999;1988-1994.
    • (1999) Eur. J. Neurosci. , vol.11 , pp. 1988-1994
    • McLoughlin, D.M.1    Irving, N.G.2    Brownlees, J.3    Brion, J.P.4    Leroy, K.5    Miller, C.C.J.6
  • 93
    • 0035794182 scopus 로고    scopus 로고
    • The beta-amyloid precursor protein functions as a cytosolic anchoring site that prevents Fe65 nuclear translocation
    • Minopoli G., de Candia P., Bonetti A., Faraonio R., Zambrano N., Russo T. The beta-amyloid precursor protein functions as a cytosolic anchoring site that prevents Fe65 nuclear translocation. J. Biol. Chem. 276:2001;6545-6550.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6545-6550
    • Minopoli, G.1    De Candia, P.2    Bonetti, A.3    Faraonio, R.4    Zambrano, N.5    Russo, T.6
  • 95
    • 0034671933 scopus 로고    scopus 로고
    • Modulation of amyloid precursor protein metabolism by X11 alpha/Mint-1 - A deletion analysis of protein-protein interaction domains
    • Mueller H.T., Borg J.P., Margolis B., Turner R.S. Modulation of amyloid precursor protein metabolism by X11 alpha/Mint-1 - A deletion analysis of protein-protein interaction domains. J. Biol. Chem. 275:2000;39302-39306.
    • (2000) J. Biol. Chem. , vol.275 , pp. 39302-39306
    • Mueller, H.T.1    Borg, J.P.2    Margolis, B.3    Turner, R.S.4
  • 97
    • 0027447656 scopus 로고
    • Alzheimer amyloid protein-precursor complexes with brain GTP-binding protein-G(o)
    • Nishimoto I., Okamoto T., Matsuura Y., Takahashi S., Murayama Y., Ogata E. Alzheimer amyloid protein-precursor complexes with brain GTP-binding protein-G(o). Nature. 362:1993;75-79.
    • (1993) Nature , vol.362 , pp. 75-79
    • Nishimoto, I.1    Okamoto, T.2    Matsuura, Y.3    Takahashi, S.4    Murayama, Y.5    Ogata, E.6
  • 99
    • 0042357124 scopus 로고    scopus 로고
    • Autosomal recessive hypercholesterolemia protein interacts with and regulates the cell surface level of Alzheimers amyloid beta precursor protein
    • Noviello C., Vito P., Lopez P., Abdallah M., D'Adamio L. Autosomal recessive hypercholesterolemia protein interacts with and regulates the cell surface level of Alzheimers amyloid beta precursor protein. J. Biol. Chem. 278:2003;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
  • 100
    • 0031465172 scopus 로고    scopus 로고
    • Mints, Munc18-interacting proteins in synaptic vesicle exocytosis
    • Okamoto M., Sudhof T.C. Mints, Munc18-interacting proteins in synaptic vesicle exocytosis. J. Biol. Chem. 272:1997;31459-31464.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31459-31464
    • Okamoto, M.1    Sudhof, T.C.2
  • 101
    • 0031736233 scopus 로고    scopus 로고
    • Mint 3: A ubiquitous mint isoform that does not bind to munc18- 1 or -2
    • Okamoto M., Sudhof T.C. Mint 3: a ubiquitous mint isoform that does not bind to munc18- 1 or -2. Eur. J. Cell Biol. 77:1998;161-165.
    • (1998) Eur. J. Cell Biol. , vol.77 , pp. 161-165
    • Okamoto, M.1    Sudhof, T.C.2
  • 102
    • 0028935717 scopus 로고
    • Ligand-dependent G-protein coupling function of amyloid transmembrane precursor
    • Okamoto T., Takeda S., Murayama Y., Ogata E., Nishimoto I. Ligand-dependent G-protein coupling function of amyloid transmembrane precursor. J. Biol. Chem. 270:1995;4205-4208.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4205-4208
    • Okamoto, T.1    Takeda, S.2    Murayama, Y.3    Ogata, E.4    Nishimoto, I.5
  • 103
    • 0029739316 scopus 로고    scopus 로고
    • Intrinsic signaling function of APP as a novel target of three V642 mutations linked to familial Alzheimer's disease
    • Okamoto T., Takeda S., Giambarella U., Murayama Y., Matsui T., Katada T., Matsuura Y., Nishimoto I. Intrinsic signaling function of APP as a novel target of three V642 mutations linked to familial Alzheimer's disease. EMBO J. 15:1996;3769-3777.
    • (1996) EMBO J. , vol.15 , pp. 3769-3777
    • Okamoto, T.1    Takeda, S.2    Giambarella, U.3    Murayama, Y.4    Matsui, T.5    Katada, T.6    Matsuura, Y.7    Nishimoto, I.8
  • 104
    • 0033821770 scopus 로고    scopus 로고
    • Ultrastructural localization of mint1 at synapses in mouse hippocampus
    • Okamoto M., Matsuyama T., Sugita M. Ultrastructural localization of mint1 at synapses in mouse hippocampus. Eur. J. Neurosci. 12:2000;3067-3072.
    • (2000) Eur. J. Neurosci. , vol.12 , pp. 3067-3072
    • Okamoto, M.1    Matsuyama, T.2    Sugita, M.3
  • 105
    • 0035859209 scopus 로고    scopus 로고
    • Amyloid precursor protein associates independently and collaboratively with PTB and PDZ domains of mint on vesicles and at cell membrane
    • Okamoto M., Nakajima Y., Matsuyama T., Sugita M. Amyloid precursor protein associates independently and collaboratively with PTB and PDZ domains of mint on vesicles and at cell membrane. Neuroscience. 104:2001;653-665.
    • (2001) Neuroscience , vol.104 , pp. 653-665
    • Okamoto, M.1    Nakajima, Y.2    Matsuyama, T.3    Sugita, M.4
  • 106
    • 0033516554 scopus 로고    scopus 로고
    • Mutagenesis identifies new signals for beta-amyloid precursor protein endocytosis, turnover, and the generation of secreted fragments, including a beta 42
    • Perez R.G., Soriano S., Hayes J.D., Ostaszewski B., Xia W.M., Selkoe D.J., Chen X.H., Stokin G.B., Koo E.H. Mutagenesis identifies new signals for beta-amyloid precursor protein endocytosis, turnover, and the generation of secreted fragments, including A beta 42. J. Biol. Chem. 274:1999;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.M.5    Selkoe, D.J.6    Chen, X.H.7    Stokin, G.B.8    Koo, E.H.9
  • 107
    • 0034971263 scopus 로고    scopus 로고
    • Lack of replication of association findings in complex disease: An analysis of 15 polymorphisms in prior candidate genes for sporadic Alzheimer's disease
    • Prince J.A., Feuk L., Sawyer S.L., Gottfries J., Ricksten A., Nagga K., Bogdanovic N., Blennow K., Bookes A.J. Lack of replication of association findings in complex disease: an analysis of 15 polymorphisms in prior candidate genes for sporadic Alzheimer's disease. Eur. J. Hum. Genet. 9:2001;437-444.
    • (2001) Eur. J. Hum. Genet. , vol.9 , pp. 437-444
    • Prince, J.A.1    Feuk, L.2    Sawyer, S.L.3    Gottfries, J.4    Ricksten, A.5    Nagga, K.6    Bogdanovic, N.7    Blennow, K.8    Bookes, A.J.9
  • 108
    • 0032544612 scopus 로고    scopus 로고
    • LIN-10 is a shared component of the polarized protein localization pathways in neurons and epithelia
    • Rongo C., Whitfield C.W., Rodal A., Kim S.K., Kaplan J.M. LIN-10 is a shared component of the polarized protein localization pathways in neurons and epithelia. Cell. 94:1998;751-759.
    • (1998) Cell , vol.94 , pp. 751-759
    • Rongo, C.1    Whitfield, C.W.2    Rodal, A.3    Kim, S.K.4    Kaplan, J.M.5
  • 109
    • 0035118308 scopus 로고    scopus 로고
    • Identification of amino-terminally and phosphotyrosine-modified carboxy-terminal fragments of the amyloid precursor protein in Alzheimer's disease and Down's syndrome brain
    • Russo C., Salis S., Dolcini V., Venezia V., Song X.H., Teller J.K., Schettini G. Identification of amino-terminally and phosphotyrosine-modified carboxy-terminal fragments of the amyloid precursor protein in Alzheimer's disease and Down's syndrome brain. Neurobiol. Dis. 8:2001;173-180.
    • (2001) Neurobiol. Dis. , vol.8 , pp. 173-180
    • Russo, C.1    Salis, S.2    Dolcini, V.3    Venezia, V.4    Song, X.H.5    Teller, J.K.6    Schettini, G.7
  • 110
    • 0037144497 scopus 로고    scopus 로고
    • Signal transduction through tyrosine-phosphorylated C-terminal fragments of amyloid precursor protein via an enhanced interaction with Shc/Grb2 adaptor proteins in reactive astrocytes of Alzheimer's disease brain
    • Russo C., Dolcini V., Salis S., Venezia V., Zambrano N., Russo T., Schettini G. Signal transduction through tyrosine-phosphorylated C-terminal fragments of amyloid precursor protein via an enhanced interaction with Shc/ Grb2 adaptor proteins in reactive astrocytes of Alzheimer's disease brain. J. Biol. Chem. 277:2002;35282-35288.
    • (2002) J. Biol. Chem. , vol.277 , pp. 35282-35288
    • Russo, C.1    Dolcini, V.2    Salis, S.3    Venezia, V.4    Zambrano, N.5    Russo, T.6    Schettini, G.7
  • 112
    • 0035954426 scopus 로고    scopus 로고
    • The Alzheimer amyloid precursor protein (APP) and FE65, an APP-binding protein, regulate cell movement
    • Sabo S.L., Ikin A.F., Buxbaum J.D., Greengard P. The Alzheimer amyloid precursor protein (APP) and FE65, an APP-binding protein, regulate cell movement. J. Cell Biol. 153:2001;1403-1414.
    • (2001) J. Cell Biol. , vol.153 , pp. 1403-1414
    • Sabo, S.L.1    Ikin, A.F.2    Buxbaum, J.D.3    Greengard, P.4
  • 113
    • 0038722283 scopus 로고    scopus 로고
    • The amyloid precursor protein and its regulatory protein, FE65, in growth cones and synapses in vitro and in vivo
    • Sabo S., Ikin A.F., Buxbaum J.D., Greengard P. The amyloid precursor protein and its regulatory protein, FE65, in growth cones and synapses in vitro and in vivo. J. Neurosci. 23:2003;5407-5415.
    • (2003) J. Neurosci. , vol.23 , pp. 5407-5415
    • Sabo, S.1    Ikin, A.F.2    Buxbaum, J.D.3    Greengard, P.4
  • 114
    • 0034066769 scopus 로고    scopus 로고
    • Increasing neurite outgrowth capacity of beta-amyloid precursor protein proteoglycan in Alzheimer's disease
    • Salinero O., Moreno-Flores M.T., Wandosell F. Increasing neurite outgrowth capacity of beta-amyloid precursor protein proteoglycan in Alzheimer's disease. J. Neurosci. Res. 60:2000;87-97.
    • (2000) J. Neurosci. Res. , vol.60 , pp. 87-97
    • Salinero, O.1    Moreno-Flores, M.T.2    Wandosell, F.3
  • 115
    • 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 R.S., Levy E. X11 interaction with beta-amyloid precursor protein modulates its cellular stabilization and reduces amyloid beta-protein secretion. J. Biol. Chem. 273:1998;22351-22357.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22351-22357
    • Sastre, M.1    Turner, R.S.2    Levy, E.3
  • 116
    • 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 M.H., Roncarati R., Vito P., Lopez P.A., 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. 277:2002;3767-3775.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3767-3775
    • Scheinfeld, M.H.1    Roncarati, R.2    Vito, P.3    Lopez, P.A.4    Abdallah, M.5    D'Adamio, L.6
  • 117
    • 0042203565 scopus 로고    scopus 로고
    • SH2 and PTB domains in tyrosine kinase signaling
    • Schlessinger J., Lemmon M.A. SH2 and PTB domains in tyrosine kinase signaling. Science's STKE. 2003;1-11.
    • (2003) Science's STKE , pp. 1-11
    • Schlessinger, J.1    Lemmon, M.A.2
  • 118
    • 0027421474 scopus 로고
    • The expression of Amyloid-Beta Protein-Precursor protects nerve cells from beta-Amyloid and glutamate toxicity and alters their interaction with the extracellular matrix
    • Schubert D., Behl C. The expression of Amyloid-Beta Protein-Precursor protects nerve cells from beta-Amyloid and glutamate toxicity and alters their interaction with the extracellular matrix. Brain Res. 629:1993;275-282.
    • (1993) Brain Res. , vol.629 , pp. 275-282
    • Schubert, D.1    Behl, C.2
  • 119
    • 0024810385 scopus 로고
    • The regulation of amyloid-beta-protein precursor secretion and its modulatory role in cell adhesion
    • Schubert D., Jin L.W., Saitoh T., Cole G. The regulation of amyloid-beta-protein precursor secretion and its modulatory role in cell adhesion. Neuron. 3:1989;689-694.
    • (1989) Neuron , vol.3 , pp. 689-694
    • Schubert, D.1    Jin, L.W.2    Saitoh, T.3    Cole, G.4
  • 120
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe D.J. Alzheimer's disease: genes, proteins, and therapy. Physiol. Rev. 81:2001;741-766.
    • (2001) Physiol. Rev. , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 121
    • 0041355557 scopus 로고    scopus 로고
    • Notch and Presenilin: Regulated intramembrane proteolysis links development and degeneration
    • Selkoe D.J., Kopan R. Notch and Presenilin: regulated intramembrane proteolysis links development and degeneration. Annu. Rev. Neurosci. 26:2003;565-597.
    • (2003) Annu. Rev. Neurosci. , vol.26 , pp. 565-597
    • Selkoe, D.J.1    Kopan, R.2
  • 122
    • 0034625631 scopus 로고    scopus 로고
    • Kinesin superfamily motor protein KIF17 and mLin-10 in NMDA receptor-containing vesicle transport
    • Setou M., Nakagawa T., Seog D.H., Hirokawa N. Kinesin superfamily motor protein KIF17 and mLin-10 in NMDA receptor-containing vesicle transport. Science. 288:2000;1796-1802.
    • (2000) Science , vol.288 , pp. 1796-1802
    • Setou, M.1    Nakagawa, T.2    Seog, D.H.3    Hirokawa, N.4
  • 123
    • 0026691805 scopus 로고
    • Chondroitin sulfate proteoglycan form of the Alzheimers beta-amyloid precursor
    • Shioi J., Anderson J.P., Ripellino J.A., Robakis N.K. Chondroitin sulfate proteoglycan form of the Alzheimers beta-amyloid precursor. J. Biol. Chem. 267:1992;13819-13822.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13819-13822
    • Shioi, J.1    Anderson, J.P.2    Ripellino, J.A.3    Robakis, N.K.4
  • 124
    • 0027319004 scopus 로고
    • Chondroitin sulfate proteoglycan form of cellular and cell- surface Alzheimer amyloid precursor
    • Shioi J., Refolo L.M., Efthimiopoulos S., Robakis N.K. Chondroitin sulfate proteoglycan form of cellular and cell- surface Alzheimer amyloid precursor. Neurosci. Lett. 154:1993;121-124.
    • (1993) Neurosci. Lett. , vol.154 , pp. 121-124
    • Shioi, J.1    Refolo, L.M.2    Efthimiopoulos, S.3    Robakis, N.K.4
  • 125
    • 0029993728 scopus 로고    scopus 로고
    • LET-23 receptor localization by the cell junction protein LIN-7 during C. elegans vulval induction
    • Simske J.S., Kaech S.M., Harp S.A., Kim S.K. LET-23 receptor localization by the cell junction protein LIN-7 during C. elegans vulval induction. Cell. 85:1996;195-204.
    • (1996) Cell , vol.85 , pp. 195-204
    • Simske, J.S.1    Kaech, S.M.2    Harp, S.A.3    Kim, S.K.4
  • 126
    • 0037131218 scopus 로고    scopus 로고
    • PEN-2 is an integral component of the gamma-secretase complex required for the coordinated expression of presenilin and nicastrin
    • Steiner H., Winkler E., Edbauer D., Prokop S., Basset G., Yamasaki A., Kostka M., Haass C. PEN-2 is an integral component of the gamma-secretase complex required for the coordinated expression of presenilin and nicastrin. J. Biol. Chem. 277:2002;39062-39065.
    • (2002) J. Biol. Chem. , vol.277 , pp. 39062-39065
    • Steiner, H.1    Winkler, E.2    Edbauer, D.3    Prokop, S.4    Basset, G.5    Yamasaki, A.6    Kostka, M.7    Haass, C.8
  • 127
    • 0042827699 scopus 로고    scopus 로고
    • XB51 isoforms mediate Alzheimer's beta-amyloid production by X11L dependent and independent mechanisms
    • Sumioka A., Imoto S., Martins R.N., Kirino Y., Suzuki T. XB51 isoforms mediate Alzheimer's beta-amyloid production by X11L dependent and independent mechanisms. Biochem. J. 374:2003;261-268.
    • (2003) Biochem. J. , vol.374 , pp. 261-268
    • Sumioka, A.1    Imoto, S.2    Martins, R.N.3    Kirino, Y.4    Suzuki, T.5
  • 128
    • 0028295848 scopus 로고
    • Cell cycle-dependent regulation of the phosphorylation and metabolism of the Alzheimer amyloid precursor protein
    • Suzuki T., Oishi M., Marshak D.R., Czernik A.J., Nairn A.C., Greengard P. Cell cycle-dependent regulation of the phosphorylation and metabolism of the Alzheimer amyloid precursor protein. EMBO J. 13:1994;1114-1122.
    • (1994) EMBO J. , vol.13 , pp. 1114-1122
    • Suzuki, T.1    Oishi, M.2    Marshak, D.R.3    Czernik, A.J.4    Nairn, A.C.5    Greengard, P.6
  • 129
    • 0033588445 scopus 로고    scopus 로고
    • Genomic organization of the human X11L2 gene (APBA3), a third member of the X11 protein family interacting with Alzheimer's amyloid precursor protein
    • Tanahashi H., Tabira T. Genomic organization of the human X11L2 gene (APBA3), a third member of the X11 protein family interacting with Alzheimer's amyloid precursor protein. NeuroReport. 10:1999;2575-2578.
    • (1999) NeuroReport , vol.10 , pp. 2575-2578
    • Tanahashi, H.1    Tabira, T.2
  • 130
    • 0033582642 scopus 로고    scopus 로고
    • Molecular cloning of human Fe65L2 and its interaction with the Alzheimer's beta-amyloid precursor protein
    • Tanahashi H., Tabira T. Molecular cloning of human Fe65L2 and its interaction with the Alzheimer's beta-amyloid precursor protein. Neurosci. Lett. 261:1999;143-146.
    • (1999) Neurosci. Lett. , vol.261 , pp. 143-146
    • Tanahashi, H.1    Tabira, T.2
  • 131
    • 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. X11L2, a new member of the X11 protein family, interacts with Alzheimer's beta-amyloid precursor protein. Biochem. Biophys. Res. Commun. 255:1999;663-667.
    • (1999) Biochem. Biophys. Res. Commun. , vol.255 , pp. 663-667
    • Tanahashi, H.1    Tabira, T.2
  • 132
    • 0036844981 scopus 로고    scopus 로고
    • Characterization of an amyloid precursor protein (APP) binding protein, Fe65L2, and its novel isoforms lacking phosphotyrosine interaction domains
    • Tanahashi H., Tabira T. Characterization of an amyloid precursor protein (APP) binding protein, Fe65L2, and its novel isoforms lacking phosphotyrosine interaction domains. Biochem. J. 367:2002;687-695.
    • (2002) Biochem. J. , vol.367 , pp. 687-695
    • Tanahashi, H.1    Tabira, T.2
  • 133
    • 0037053281 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the beta-amyloid precursor protein cytoplasmic tail promotes interaction with Shc
    • Tarr P.E., Roncarati R., Pelicci G., Pelicci P.G., D'Adamio L. Tyrosine phosphorylation of the beta-amyloid precursor protein cytoplasmic tail promotes interaction with Shc. J. Biol. Chem. 277:2002;16798-16804.
    • (2002) J. Biol. Chem. , vol.277 , pp. 16798-16804
    • Tarr, P.E.1    Roncarati, R.2    Pelicci, G.3    Pelicci, P.G.4    D'Adamio, L.5
  • 134
    • 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. Interaction of Alzheimer's beta-amyloid precursor family proteins with scaffold proteins of the JNK signaling cascade. J. Biol. Chem. 277:2002;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
  • 135
    • 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. Differential roles of JIP scaffold proteins in the modulation of amyloid precursor protein metabolism. J. Biol. Chem. 277:2002;27567-27574.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27567-27574
    • Taru, H.1    Kirino, Y.2    Suzuki, T.3
  • 136
    • 0029060676 scopus 로고
    • Novel regulation of chondroitin sulfate glycosaminoglycan modification of amyloid precursor protein and its homolog, APLP2
    • Thinakaran G., Slunt H.H., Sisodia S.S. Novel regulation of chondroitin sulfate glycosaminoglycan modification of amyloid precursor protein and its homolog, APLP2. J. Biol. Chem. 270:1995;16522-16525.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16522-16525
    • Thinakaran, G.1    Slunt, H.H.2    Sisodia, S.S.3
  • 137
    • 0032563098 scopus 로고    scopus 로고
    • A basic amino acid in the cytoplasmic domain of Alzheimer's beta-amyloid precursor protein (APP) is essential for cleavage of APP at the alpha-site
    • Tomita S., Kirino Y., Suzuki T. A basic amino acid in the cytoplasmic domain of Alzheimer's beta-amyloid precursor protein (APP) is essential for cleavage of APP at the alpha-site. J. Biol. Chem. 273:1998;19304-19310.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19304-19310
    • Tomita, S.1    Kirino, Y.2    Suzuki, T.3
  • 138
  • 139
    • 0032509346 scopus 로고    scopus 로고
    • Interaction of cytosolic adaptor proteins with neuronal apolipoprotein e receptors and the amyloid precursor protein
    • Trommsdorff R., Borg J.P., Margolis B., Herz J. Interaction of cytosolic adaptor proteins with neuronal apolipoprotein E receptors and the amyloid precursor protein. J. Biol. Chem. 273:1998;33556-33560.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33556-33560
    • Trommsdorff, R.1    Borg, J.P.2    Margolis, B.3    Herz, J.4
  • 144
    • 0344731071 scopus 로고    scopus 로고
    • Basolateral localization of the Caenorhabditis elegans epidermal growth factor receptor in epithelial cells by the PDZ protein LIN-10
    • Whitfield C.W., Benard C., Barnes T., Hekimi S., Kim S.K. Basolateral localization of the Caenorhabditis elegans epidermal growth factor receptor in epithelial cells by the PDZ protein LIN-10. Mol. Biol. Cell. 10:1999;2087-2100.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2087-2100
    • Whitfield, C.W.1    Benard, C.2    Barnes, T.3    Hekimi, S.4    Kim, S.K.5
  • 145
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity
    • Wolfe M.S., Xia W.M., Ostaszewski B.L., Diehl T.S., Kimberly W.T., Selkoe D.J. Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity. Nature. 398:1999;513-517.
    • (1999) Nature , vol.398 , pp. 513-517
    • Wolfe, M.S.1    Xia, W.M.2    Ostaszewski, B.L.3    Diehl, T.S.4    Kimberly, W.T.5    Selkoe, D.J.6
  • 146
    • 0037416221 scopus 로고    scopus 로고
    • Structural view of a fungal toxin acting on a 14-3-3 regulatory complex
    • Wurtele M., Jelich-Ottomann C., Wittinghofer A., Oecking C. Structural view of a fungal toxin acting on a 14-3-3 regulatory complex. EMBO J. 22:2003;987-994.
    • (2003) EMBO J. , vol.22 , pp. 987-994
    • Wurtele, M.1    Jelich-Ottomann, C.2    Wittinghofer, A.3    Oecking, C.4
  • 147
    • 0031020284 scopus 로고    scopus 로고
    • Cell surface amyloid beta-protein precursor colocalizes with beta 1 integrins at substrate contact sites in neural cells
    • Yamazaki T., Koo E.H., Selkoe D.J. Cell surface amyloid beta-protein precursor colocalizes with beta 1 integrins at substrate contact sites in neural cells. J. Neurosci. 17:1997;1004-1010.
    • (1997) J. Neurosci. , vol.17 , pp. 1004-1010
    • Yamazaki, T.1    Koo, E.H.2    Selkoe, D.J.3
  • 148
    • 0035823610 scopus 로고    scopus 로고
    • BACE2 functions as an alternative alpha secretase in cells
    • Yan R., Munzner J.B., Shuck M.E., Bienkowski M.J. BACE2 functions as an alternative alpha secretase in cells. J. Biol. Chem. 276:2001;34019-34027.
    • (2001) J. Biol. Chem. , vol.276 , pp. 34019-34027
    • Yan, R.1    Munzner, J.B.2    Shuck, M.E.3    Bienkowski, M.J.4
  • 149
    • 0037138381 scopus 로고    scopus 로고
    • PTB or not PTB - That is the question
    • Yan K.S., Kuti M., Zhou M.M. PTB or not PTB - That is the question. FEBS Lett. 513:2002;67-70.
    • (2002) FEBS Lett. , vol.513 , pp. 67-70
    • Yan, K.S.1    Kuti, M.2    Zhou, M.M.3
  • 150
    • 0035827587 scopus 로고    scopus 로고
    • The beta-amyloid precursor protein APP is tyrosine- phosphorylated in cells expressing a constitutively active form of the Abl protoncogene
    • Zambrano N., Bruni P., Minopoli G., Mosca R., Molino D., Russo C., Schettini G., Sudol M., Russo T. The beta-amyloid precursor protein APP is tyrosine- phosphorylated in cells expressing a constitutively active form of the Abl protoncogene. J. Biol. Chem. 276:2001;19787-19792.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19787-19792
    • Zambrano, N.1    Bruni, P.2    Minopoli, G.3    Mosca, R.4    Molino, D.5    Russo, C.6    Schettini, G.7    Sudol, M.8    Russo, T.9
  • 151
    • 0030894021 scopus 로고    scopus 로고
    • Interaction of the phosphotyrosine interaction/phosphotyrosine binding-related domains of Fe65 with wild-type and mutant Alzheimer's beta-amyloid precursor proteins
    • Zambrano N., Buxbaum J.D., Minopoli G., Fiore F., DeCandia P., DeRenzis S., Faraonio R., Sabo S., Cheetham J., Sudol M., Russon T. Interaction of the phosphotyrosine interaction/phosphotyrosine binding-related domains of Fe65 with wild-type and mutant Alzheimer's beta-amyloid precursor proteins. J. Biol. Chem. 272:1997;6399-6405.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6399-6405
    • Zambrano, N.1    Buxbaum, J.D.2    Minopoli, G.3    Fiore, F.4    Decandia, P.5    Derenzis, S.6    Faraonio, R.7    Sabo, S.8    Cheetham, J.9    Sudol, M.10    Russon, T.11
  • 152
    • 0032493814 scopus 로고    scopus 로고
    • The Fe65 adaptor protein interacts through its PID1 domain with the transcription factor CP2/LSF/LBP1
    • Zambrano N., Minopoli G., de Candia P., Russo T. The Fe65 adaptor protein interacts through its PID1 domain with the transcription factor CP2/LSF/LBP1. J. Biol. Chem. 273:1998;20128-20133.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20128-20133
    • Zambrano, N.1    Minopoli, G.2    De Candia, P.3    Russo, T.4
  • 153
    • 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.T., Lee C.H., Mandiyan V., Borg J.P., Margolis B., Schlessinger J., Kuriyan J. Sequence-specific recognition of the internalization motif of the Alzheimer's amyloid precursor protein by the X11 PTB domain. EMBO J. 16:1997;6141-6150.
    • (1997) EMBO J. , vol.16 , pp. 6141-6150
    • Zhang, Z.T.1    Lee, C.H.2    Mandiyan, V.3    Borg, J.P.4    Margolis, B.5    Schlessinger, J.6    Kuriyan, J.7
  • 154
    • 0032410747 scopus 로고    scopus 로고
    • PAT1, a microtubule-interacting protein, recognizes the basolateral sorting signal of amyloid precursor protein
    • Zheng P.Z., Eastman J., Vande Pol S., Pimplikar S.W. PAT1, a microtubule-interacting protein, recognizes the basolateral sorting signal of amyloid precursor protein. Proc. Natl. Acad. Sci. U. S. A. 95:1998;14745-14750.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 14745-14750
    • Zheng, P.Z.1    Eastman, J.2    Vande Pol, S.3    Pimplikar, S.W.4


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