메뉴 건너뛰기




Volumn 30, Issue 2, 2004, Pages 185-200

Cytoplasmic tail adaptors of Alzheimer's amyloid-β protein precursor

Author keywords

A PP(APP); Fe65; G protein; JIP; JIP1b IB1; mDab1; PID PTB; The GYENPTY motif; X11 Lin 10 Mint

Indexed keywords

ADAPTOR PROTEIN; AMYLOID PRECURSOR PROTEIN; C JUN N TERMINAL KINASE INTERACTING PROTEIN 1B; MOUSE DISABLED 1 PROTEIN; PROTEIN FE65; PROTEIN X 11; UNCLASSIFIED DRUG;

EID: 16644366941     PISSN: 08937648     EISSN: None     Source Type: Journal    
DOI: 10.1385/MN:30:2:185     Document Type: Review
Times cited : (8)

References (121)
  • 2
    • 0033103343 scopus 로고    scopus 로고
    • o heterotrimeric protein within a cell compartment specialized in signal transduction
    • o heterotrimeric protein within a cell compartment specialized in signal transduction. J. Neurosci. 19, 1717-1727.
    • (1999) J. Neurosci. , vol.19 , pp. 1717-1727
    • Brouillet, E.1    Trembleau, A.2    Galanaud, D.3
  • 3
    • 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. (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
  • 5
    • 0028596158 scopus 로고
    • An alternative to SH2 domains for binding tyrosine-phosphorylated proteins
    • Kavanaugh W. M., Williams L. T. (1994). An alternative to SH2 domains for binding tyrosine-phosphorylated proteins. Science 266, 1862-1865.
    • (1994) Science , vol.266 , pp. 1862-1865
    • Kavanaugh, W.M.1    Williams, L.T.2
  • 6
    • 0029067403 scopus 로고
    • PTB domain binding to signaling proteins through a sequence motif containing phosphotyrosine
    • Kavanaugh W. M., Turck C. W., Williams L. T. (1995). PTB domain binding to signaling proteins through a sequence motif containing phosphotyrosine. Science 268, 1177-1179.
    • (1995) Science , vol.268 , pp. 1177-1179
    • Kavanaugh, W.M.1    Turck, C.W.2    Williams, L.T.3
  • 7
    • 0029640799 scopus 로고
    • A phosphotyrosine interaction domain
    • Bork P., Margolis B. (1995). A phosphotyrosine interaction domain. Cell 80, 693-694.
    • (1995) Cell , vol.80 , pp. 693-694
    • Bork, P.1    Margolis, B.2
  • 8
    • 0025953048 scopus 로고
    • A rat brain mRNA encoding a transcriptional activator homologous to the DNA binding domain of retroviral integrases
    • Duilio A., Zambrano N., Mogavero A. R., Ammendola R., Cimino F., Russo T. (1991). A rat brain mRNA encoding a transcriptional activator homologous to the DNA binding domain of retroviral integrases. Nucl. Acids Res. 19, 5269-5274.
    • (1991) Nucl. Acids Res. , vol.19 , pp. 5269-5274
    • Duilio, A.1    Zambrano, N.2    Mogavero, A.R.3    Ammendola, R.4    Cimino, F.5    Russo, T.6
  • 9
    • 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, 30,853-30,856.
    • (1995) J. Biol. Chem. , vol.270
    • Fiore, F.1    Zambrano, N.2    Minopoli, G.3    Donini, V.4    Duilio, A.5    Russo, T.6
  • 10
    • 0029746156 scopus 로고    scopus 로고
    • Association of a novel human FE65-like protein with the cytoplasmic domain of the β-amyloid precursor protein
    • Guenette S. Y., Chen J., Jondro P. D., Tanzi R. E. (1996). Association of a novel human FE65-like protein with the cytoplasmic domain of the β-amyloid precursor protein. Proc. Natl. Acad. Sci. USA 93, 10,832-10,837.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93
    • Guenette, S.Y.1    Chen, J.2    Jondro, P.D.3    Tanzi, R.E.4
  • 11
    • 0032519711 scopus 로고    scopus 로고
    • Fe65L2: A new member of the Fe65 protein family interacting with the intracellular domain of the Alzheimer's β-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 β-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
  • 12
    • 0030894021 scopus 로고    scopus 로고
    • Interaction of the phosphotyrosine interaction/phosphotyrosine binding-related domains of Fe65 with wild-type and mutant Alzheimer's β-amyloid precursor proteins
    • Zambrano N., Buxbaum J. D., Minopoli G., et al. (1997). Interaction of the phosphotyrosine interaction/phosphotyrosine binding-related domains of Fe65 with wild-type and mutant Alzheimer's β-amyloid precursor proteins. J. Biol. Chem. 272, 6399-6405.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6399-6405
    • Zambrano, N.1    Buxbaum, J.D.2    Minopoli, G.3
  • 13
    • 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. (1998). The Fe65 adaptor protein interacts through its PID1 domain with the transcription factor CP2/LSF/LBP1. J. Biol. Chem. 273, 20,128-20,133.
    • (1998) J. Biol. Chem. , vol.273
    • Zambrano, N.1    Minopoli, G.2    De Candia, P.3    Russo, T.4
  • 14
    • 0032509346 scopus 로고    scopus 로고
    • Interaction of cytosolic adaptor proteins with neuronal apolipoprotein e receptors and the amyloid precursor protein
    • Trommsdorff M., Borg J. P., Margolis B., Herz J. (1998). Interaction of cytosolic adaptor proteins with neuronal apolipoprotein E receptors and the amyloid precursor protein. J. Biol. Chem. 273, 33,556-33,560.
    • (1998) J. Biol. Chem. , vol.273
    • Trommsdorff, M.1    Borg, J.P.2    Margolis, B.3    Herz, J.4
  • 15
    • 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., et al. (2001). 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, 8354-8361.
    • (2001) J. Neurosci. , vol.21 , pp. 8354-8361
    • Kinoshita, A.1    Whelan, C.M.2    Smith, C.J.3
  • 16
    • 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
  • 17
    • 0346435103 scopus 로고    scopus 로고
    • Generation of the β-amyloid peptide and the amyloid precursor protein C-terminal fragment γ are potentiated by FE65L1
    • Chang Y., Tesco G., Jeong W. J., et al. (2003). Generation of the β-amyloid peptide and the amyloid precursor protein C-terminal fragment γ are potentiated by FE65L1. J. Biol. Chem. 278, 51,100-51,107.
    • (2003) J. Biol. Chem. , vol.278
    • Chang, Y.1    Tesco, G.2    Jeong, W.J.3
  • 18
    • 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., et al. (1997). The WW domain of neural protein FE65 interacts with proline-rich motifs in Mena, the mammalian homolog of Drosophila enabled. J. Biol. Chem. 272, 32,869-32,877.
    • (1997) J. Biol. Chem. , vol.272
    • Ermekova, K.S.1    Zambrano, N.2    Linn, H.3
  • 19
    • 0035827587 scopus 로고    scopus 로고
    • The β-amyloid precursor protein APP is tyrosine-phosphorylated in cells expressing a constitutively active form of the Abl protoncogene
    • Zambrano N., Bruni P., Minopoli G., et al. (2001). The β-amyloid precursor protein APP is tyrosine-phosphorylated in cells expressing a constitutively active form of the Abl protoncogene. J. Biol. Chem. 276, 19,787-19,792.
    • (2001) J. Biol. Chem. , vol.276
    • Zambrano, N.1    Bruni, P.2    Minopoli, G.3
  • 20
    • 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. (2001). The Alzheimer amyloid precursor protein (APP) and FE65, an APP-binding protein, regulate cell movement. J. Cell. Biol. 153, 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
  • 21
    • 0035816661 scopus 로고    scopus 로고
    • A transcriptionally active complex of APP with Fe65 and histone acetyltransferase Tip60
    • Cao X., Sudhof T. C. (2001). A transcriptionally 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
  • 22
    • 0035794182 scopus 로고    scopus 로고
    • The β-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. (2001). The β-amyloid precursor protein functions as a cytosolic anchoring site that prevents Fe65 nuclear translocation. J. Biol. Chem. 276, 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
  • 23
    • 0142103374 scopus 로고    scopus 로고
    • The intracellular domain of the low density lipoprotein receptor-related protein modulates transactivation mediated by amyloid precursor protein and Fe65
    • Kinoshita A., Shah T., Tangredi M. M., Strickland D. K., Hyman B. T. (2003). The intracellular domain of the low density lipoprotein receptor-related protein modulates transactivation mediated by amyloid precursor protein and Fe65. J. Biol. Chem. 278, 41,182-41,188.
    • (2003) J. Biol. Chem. , vol.278
    • Kinoshita, A.1    Shah, T.2    Tangredi, M.M.3    Strickland, D.K.4    Hyman, B.T.5
  • 24
    • 0035955693 scopus 로고    scopus 로고
    • The intracellular domain of the β-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. (2001). The intracellular domain of the β-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner. J. Biol. Chem. 276, 40,288-40,292.
    • (2001) J. Biol. Chem. , vol.276
    • Kimberly, W.T.1    Zheng, J.B.2    Guenette, S.Y.3    Selkoe, D.J.4
  • 25
    • 0036677928 scopus 로고    scopus 로고
    • Direct visualization of the gamma secretase-generated carboxyl-terminal domain of the amyloid precursor protein: Association with Fe65 and translocation to the nucleus
    • Kinoshita A., Whelan C. M., Smith C. J., Berezovska O., Hyman B. T. (2002). Direct visualization of the gamma secretase-generated carboxyl-terminal domain of the amyloid precursor protein: association with Fe65 and translocation to the nucleus. J. Neurochem. 82, 839-847.
    • (2002) J. Neurochem. , vol.82 , pp. 839-847
    • Kinoshita, A.1    Whelan, C.M.2    Smith, C.J.3    Berezovska, O.4    Hyman, B.T.5
  • 26
    • 9144262348 scopus 로고    scopus 로고
    • Isoform-specific knockout of FE65 leads to impaired learning and memory
    • Wang B., Hu Q., Hearn M. G., et al. (2004). Isoform-specific knockout of FE65 leads to impaired learning and memory. J. Neurosci. Res. 75, 12-24.
    • (2004) J. Neurosci. Res. , vol.75 , pp. 12-24
    • Wang, B.1    Hu, Q.2    Hearn, M.G.3
  • 27
    • 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. (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
  • 28
    • 0033593480 scopus 로고    scopus 로고
    • Interaction of a neuron-specific protein containing PDZ domains with Alzheimer's amyloid precursor protein
    • Tomita S., Ozaki T., Taru H., et al. (1999). Interaction of a neuron-specific protein containing PDZ domains with Alzheimer's amyloid precursor protein. J. Biol. Chem. 274, 2243-2254.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2243-2254
    • Tomita, S.1    Ozaki, T.2    Taru, H.3
  • 29
    • 0033599341 scopus 로고    scopus 로고
    • X11L2, a new member of the X11 protein family, interacts with Alzheimer's β-amyloid precursor protein
    • Tanahashi H., Tabira T. (1999). X11L2, a new member of the X11 protein family, interacts with Alzheimer's β-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
  • 30
    • 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 C. H., Mandiyan V., et al. (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
  • 31
    • 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. (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
  • 32
    • 0345654356 scopus 로고    scopus 로고
    • Molecular analysis of the X11-mLin-2/CASK complex in brain
    • Borg J. P., Lopez-Figueroa M. O., de Taddeo-Borg M., et al. (1999). Molecular analysis of the X11-mLin-2/CASK complex in brain. J. Neurosci. 19, 1307-1316.
    • (1999) J. Neurosci. , vol.19 , pp. 1307-1316
    • Borg, J.P.1    Lopez-Figueroa, M.O.2    De Taddeo-Borg, M.3
  • 33
    • 0031465172 scopus 로고    scopus 로고
    • Mints, Munc18-interacting proteins in synaptic vesicle exocytosis
    • Okamoto M., Sudhof T. C. (1997). Mints, Munc18-interacting proteins in synaptic vesicle exocytosis. J. Biol. Chem. 272, 31,459-31,464.
    • (1997) J. Biol. Chem. , vol.272
    • Okamoto, M.1    Sudhof, T.C.2
  • 34
    • 0025215178 scopus 로고
    • The Caenorhabditis elegans gene lin-10 is broadly expressed while required specifically for the determination of vulval cell fates
    • Kim S. K., Horvitz H. R. (1990). The Caenorhabditis elegans gene lin-10 is broadly expressed while required specifically for the determination of vulval cell fates. Genes Dev. 4, 357-371.
    • (1990) Genes Dev. , vol.4 , pp. 357-371
    • Kim, S.K.1    Horvitz, H.R.2
  • 35
    • 0027397365 scopus 로고
    • Gene in the region of the Friedreich ataxia locus encodes a putative transmembrane protein expressed in the nervous system
    • Duclos F., Boschert U., Sirugo G., Mandel J. L., Hen R., Koenig M. (1993). Gene in the region of the Friedreich ataxia locus encodes a putative transmembrane protein expressed in the nervous system. Proc. Natl. Acad. Sci. USA 90, 109-113.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 109-113
    • Duclos, F.1    Boschert, U.2    Sirugo, G.3    Mandel, J.L.4    Hen, R.5    Koenig, M.6
  • 36
    • 0028229122 scopus 로고
    • Recombinations in individuals homozygous by descent localize the Friedreich ataxia locus in a cloned 450-kb interval
    • Rodius F., Duclos F., Wrogemann K., et al. (1994). Recombinations in individuals homozygous by descent localize the Friedreich ataxia locus in a cloned 450-kb interval. Am. J. Hum. Genet. 54, 1050-1059.
    • (1994) Am. J. Hum. Genet. , vol.54 , pp. 1050-1059
    • Rodius, F.1    Duclos, F.2    Wrogemann, K.3
  • 37
    • 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. (1996). LET-23 receptor localization by the cell junction protein LIN-7 during C. elegans vulval induction. Cell 85, 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
  • 38
    • 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. (1998). 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, 761-771.
    • (1998) Cell , vol.94 , pp. 761-771
    • Kaech, S.M.1    Whitfield, C.W.2    Kim, S.K.3
  • 39
    • 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. (1998). LIN-10 is a shared component of the polarized protein localization pathways in neurons and epithelia. Cell 94, 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
  • 40
    • 0033610842 scopus 로고    scopus 로고
    • Identification of an evolutionarily conserved heterotrimeric protein complex involved in protein targeting
    • Borg J. P., Straight S. W., Kaech S. M., et al. (1998). Identification of an evolutionarily conserved heterotrimeric protein complex involved in protein targeting. J. Biol. Chem. 273, 31,633-31,636.
    • (1998) J. Biol. Chem. , vol.273
    • Borg, J.P.1    Straight, S.W.2    Kaech, S.M.3
  • 41
    • 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. (1998). A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Cell 94, 773-782.
    • (1998) Cell , vol.94 , pp. 773-782
    • Butz, S.1    Okamoto, M.2    Sudhof, T.C.3
  • 42
    • 0032510834 scopus 로고    scopus 로고
    • The X11α protein slows cellular amyloid precursor protein processing and reduces Aβ40 and Aβ42 secretion
    • Borg J. P., Yang Y., De Taddeo-Borg M., Margolis B., Turner R. S. (1998). The X11α protein slows cellular amyloid precursor protein processing and reduces Aβ40 and Aβ42 secretion. J. Biol. Chem. 273, 14,761-14,766.
    • (1998) J. Biol. Chem. , vol.273
    • Borg, J.P.1    Yang, Y.2    De Taddeo-Borg, M.3    Margolis, B.4    Turner, R.S.5
  • 43
    • 0032575559 scopus 로고    scopus 로고
    • X11 interaction with β-amyloid precursor protein modulates its cellular stabilization and reduces amyloid β-protein secretion
    • Sastre M., Turner R. S., Levy E. (1998). X11 interaction with β-amyloid precursor protein modulates its cellular stabilization and reduces amyloid β-protein secretion. J. Biol. Chem. 273, 22,351-22,357.
    • (1998) J. Biol. Chem. , vol.273
    • Sastre, M.1    Turner, R.S.2    Levy, E.3
  • 45
    • 0034671933 scopus 로고    scopus 로고
    • Modulation of amyloid precursor protein metabolism by X11α/Mint-1. A deletion analysis of protein-protein interaction domains
    • Mueller H. T., Borg J. P., Margolis B., Turner R. S. (2000). Modulation of amyloid precursor protein metabolism by X11α/Mint-1. A deletion analysis of protein-protein interaction domains. J. Biol. Chem. 275, 39,302-39,306.
    • (2000) J. Biol. Chem. , vol.275
    • Mueller, H.T.1    Borg, J.P.2    Margolis, B.3    Turner, R.S.4
  • 46
    • 0034724689 scopus 로고    scopus 로고
    • PDZ domain-dependent suppression of NF-κB/p65-induced Aβ42 production by a neuron-specific X11-like protein
    • Tomita S., Fujita T., Kirino Y., Suzuki T. (2000). PDZ domain-dependent suppression of NF-κB/p65-induced Aβ42 production by a neuron-specific X11-like protein. J. Biol. Chem. 275, 13,056-13,060.
    • (2000) J. Biol. Chem. , vol.275
    • Tomita, S.1    Fujita, T.2    Kirino, Y.3    Suzuki, T.4
  • 47
    • 0036759068 scopus 로고    scopus 로고
    • Regulation of APP-dependent transcription complexes by Mint/X11s: Differential functions of Mint isoforms
    • Biederer T., Cao X., Sudhof T. C., Liu X. (2002). Regulation of APP-dependent transcription complexes by Mint/X11s: differential functions of Mint isoforms. J. Neurosci. 22, 7340-7351.
    • (2002) J. Neurosci. , vol.22 , pp. 7340-7351
    • Biederer, T.1    Cao, X.2    Sudhof, T.C.3    Liu, X.4
  • 48
    • 0034626631 scopus 로고    scopus 로고
    • Fe65 and X11β 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. (2000). Fe65 and X11β co-localize with and compete for binding to the amyloid precursor protein. Neuroreport 11, 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.5
  • 49
    • 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. (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
  • 50
    • 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. (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
  • 51
    • 0024338902 scopus 로고
    • Drosophila abl tyrosine kinase in embryonic CNS axons: A role in axonogenesis is revealed through dosage-sensitive interactions with disabled
    • Gertler F. B., Bennett R. L., Clark M. J., Hoffmann F. M. (1989). Drosophila abl tyrosine kinase in embryonic CNS axons: a role in axonogenesis is revealed through dosage-sensitive interactions with disabled. Cell 58, 103-113.
    • (1989) Cell , vol.58 , pp. 103-113
    • Gertler, F.B.1    Bennett, R.L.2    Clark, M.J.3    Hoffmann, F.M.4
  • 52
    • 0031035703 scopus 로고    scopus 로고
    • Mouse disabled (mDab1): A Src binding protein implicated in neuronal development
    • Howell B. W., Gertler F. B., Cooper J. A. (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    Gertler, F.B.2    Cooper, J.A.3
  • 53
    • 0030704354 scopus 로고    scopus 로고
    • Neuronal position in the developing brain is regulated by mouse disabled-1
    • Howell B. W., Hawkes R., Soriano P., Cooper J. A. (1997). Neuronal position in the developing brain is regulated by mouse disabled-1. Nature 389, 733-737.
    • (1997) Nature , vol.389 , pp. 733-737
    • Howell, B.W.1    Hawkes, R.2    Soriano, P.3    Cooper, J.A.4
  • 54
    • 0028940096 scopus 로고
    • A protein related to extracellular matrix proteins deleted in the mouse mutant reeler
    • D'Arcangelo G., Miao G. G., Chen S. C., Soares H. D., Morgan J. I., Curran T. (1995). A protein related to extracellular matrix proteins deleted in the mouse mutant reeler. Nature 374, 719-723.
    • (1995) Nature , vol.374 , pp. 719-723
    • D'Arcangelo, G.1    Miao, G.G.2    Chen, S.C.3    Soares, H.D.4    Morgan, J.I.5    Curran, T.6
  • 55
    • 0030717493 scopus 로고    scopus 로고
    • Scrambler and yotari disrupt the disabled gene and produce a reeler-like phenotype in mice
    • Sheldon M., Rice D. S., D'Arcangelo G., et al. (1997). Scrambler and yotari disrupt the disabled gene and produce a reeler-like phenotype in mice. Nature 389, 730-733.
    • (1997) Nature , vol.389 , pp. 730-733
    • Sheldon, M.1    Rice, D.S.2    D'Arcangelo, G.3
  • 56
    • 0031658384 scopus 로고    scopus 로고
    • Disabled-1 acts downstream of Reelin in a signaling pathway that controls laminar organization in the mammalian brain
    • Rice D. S., Sheldon M., D'Arcangelo G., Nakajima K., Goldowitz D., Curran T. (1998). Disabled-1 acts downstream of Reelin in a signaling pathway that controls laminar organization in the mammalian brain. Development 125, 3719-3729.
    • (1998) Development , vol.125 , pp. 3719-3729
    • Rice, D.S.1    Sheldon, M.2    D'Arcangelo, G.3    Nakajima, K.4    Goldowitz, D.5    Curran, T.6
  • 57
    • 0033003134 scopus 로고    scopus 로고
    • Reeler/Disabled-like disruption of neuronal migration in knockout mice lacking the VLDL receptor and ApoE receptor 2
    • Trommsdorff M., Gotthardt M., Hiesberger T., et al. (1999). Reeler/Disabled-like disruption of neuronal migration in knockout mice lacking the VLDL receptor and ApoE receptor 2. Cell 97, 689-701.
    • (1999) Cell , vol.97 , pp. 689-701
    • Trommsdorff, M.1    Gotthardt, M.2    Hiesberger, T.3
  • 58
    • 0033213319 scopus 로고    scopus 로고
    • Direct binding of Reelin to VLDL receptor and ApoE receptor 2 induces tyrosine phosphorylation of disabled-1 and modulates tau phosphorylation
    • Hiesberger T., Trommsdorff M., Howell B. W., et al. (1999). Direct binding of Reelin to VLDL receptor and ApoE receptor 2 induces tyrosine phosphorylation of disabled-1 and modulates tau phosphorylation. Neuron 24, 481-489.
    • (1999) Neuron , vol.24 , pp. 481-489
    • Hiesberger, T.1    Trommsdorff, M.2    Howell, B.W.3
  • 60
    • 0033544706 scopus 로고    scopus 로고
    • Proteins of the CNR family are multiple receptors for Reelin
    • Senzaki K., Ogawa M., Yagi T. (1999). Proteins of the CNR family are multiple receptors for Reelin. Cell 99, 635-647.
    • (1999) Cell , vol.99 , pp. 635-647
    • Senzaki, K.1    Ogawa, M.2    Yagi, T.3
  • 61
    • 0033624279 scopus 로고    scopus 로고
    • Reelin binds α3β1 integrin and inhibits neuronal migration
    • Dulabon L., Olson E. C., Taglienti M. G., et al. (2000). Reelin binds α3β1 integrin and inhibits neuronal migration. Neuron 27, 33-44.
    • (2000) Neuron , vol.27 , pp. 33-44
    • Dulabon, L.1    Olson, E.C.2    Taglienti, M.G.3
  • 62
    • 0034329291 scopus 로고    scopus 로고
    • Mice with combined gene knock-outs reveal essential and partially redundant functions of amyloid precursor protein family members
    • Heber S., Herms J., Gajic V., et al. (2000). Mice with combined gene knock-outs reveal essential and partially redundant functions of amyloid precursor protein family members. J. Neurosci. 20, 7951-7963.
    • (2000) J. Neurosci. , vol.20 , pp. 7951-7963
    • Heber, S.1    Herms, J.2    Gajic, V.3
  • 63
    • 0035449943 scopus 로고    scopus 로고
    • c-Jun N-terminal kinase (JNK)-interacting protein-1b/islet-brain-1 scaffolds Alzheimer's amyloid precursor protein with JNK
    • Matsuda S., Yasukawa T., Homma Y., et al. (2001). c-Jun N-terminal kinase (JNK)-interacting protein-1b/islet-brain-1 scaffolds Alzheimer's amyloid precursor protein with JNK. J. Neurosci. 21, 6597-6607.
    • (2001) J. Neurosci. , vol.21 , pp. 6597-6607
    • Matsuda, S.1    Yasukawa, T.2    Homma, Y.3
  • 64
    • 0036462590 scopus 로고    scopus 로고
    • Jun N-terminal kinase (JNK) interacting protein 1 (JIP1) binds the cytoplasmic domain of the Alzheimer's β-amyloid precursor protein (APP)
    • Scheinfeld M. H., Roncarati R., Vito P., Lopez P. A., Abdallah M., D'Adamio L. (2002). Jun N-terminal kinase (JNK) interacting protein 1 (JIP1) binds the cytoplasmic domain of the Alzheimer's β-amyloid precursor protein (APP). J. Biol. Chem. 277, 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
  • 66
    • 0033971177 scopus 로고    scopus 로고
    • Interaction of a mitogen-activated protein kinase signaling module with the neuronal protein JIP3
    • Kelkar N., Gupta S., Dickens M., Davis R. J. (2000). Interaction of a mitogen-activated protein kinase signaling module with the neuronal protein JIP3. Mol. Cell. Biol. 20, 1030-1043.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1030-1043
    • Kelkar, N.1    Gupta, S.2    Dickens, M.3    Davis, R.J.4
  • 67
    • 0033520918 scopus 로고    scopus 로고
    • Interaction of c-Jun amino-terminal kinase interacting protein-1 with p190 rhoGEF and its localization in differentiated neurons
    • Meyer D., Liu A., Margolis B. (1999). Interaction of c-Jun amino-terminal kinase interacting protein-1 with p190 rhoGEF and its localization in differentiated neurons. J. Biol. Chem. 274, 35,113-35,118.
    • (1999) J. Biol. Chem. , vol.274
    • Meyer, D.1    Liu, A.2    Margolis, B.3
  • 68
    • 0034682775 scopus 로고    scopus 로고
    • The reelin receptor ApoER2 recruits JNK-interacting proteins-1 and -2
    • Stockinger W., Brandes C., Fasching D., et al. (2000). The reelin receptor ApoER2 recruits JNK-interacting proteins-1 and -2. J. Biol. Chem. 275, 25,625-25,632.
    • (2000) J. Biol. Chem. , vol.275
    • Stockinger, W.1    Brandes, C.2    Fasching, D.3
  • 69
    • 0034682827 scopus 로고    scopus 로고
    • Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction
    • Gotthardt M., Trommsdorff M., Nevitt M. F., et al. (2000). Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction. J. Biol. Chem. 275, 25,616-25,624.
    • (2000) J. Biol. Chem. , vol.275
    • Gotthardt, M.1    Trommsdorff, M.2    Nevitt, M.F.3
  • 70
    • 0028880006 scopus 로고
    • Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis
    • Xia Z., Dickens M., Raingeaud J., Davis R. J., Greenberg M. E. (1995). Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis. Science 270, 1326-1331.
    • (1995) Science , vol.270 , pp. 1326-1331
    • Xia, Z.1    Dickens, M.2    Raingeaud, J.3    Davis, R.J.4    Greenberg, M.E.5
  • 71
    • 0033118607 scopus 로고    scopus 로고
    • The JNK1 and JNK2 protein kinases are required for regional specific apoptosis during early brain development
    • Kuan C. Y., Yang D. D., Samanta Roy D. R., Davis R. J., Rakic P., Flavell R. A. (1999). The JNK1 and JNK2 protein kinases are required for regional specific apoptosis during early brain development. Neuron 22, 667-676.
    • (1999) Neuron , vol.22 , pp. 667-676
    • Kuan, C.Y.1    Yang, D.D.2    Samanta Roy, D.R.3    Davis, R.J.4    Rakic, P.5    Flavell, R.A.6
  • 72
    • 0030780804 scopus 로고    scopus 로고
    • Absence of excitotoxicity-induced apoptosis in the hippocampus of mice lacking the Jnk3 gene
    • Yang D. D., Kuan C. Y., Whitmarsh A. J., et al. (1997). Absence of excitotoxicity-induced apoptosis in the hippocampus of mice lacking the Jnk3 gene. Nature 389, 865-870.
    • (1997) Nature , vol.389 , pp. 865-870
    • Yang, D.D.1    Kuan, C.Y.2    Whitmarsh, A.J.3
  • 73
    • 0030826412 scopus 로고    scopus 로고
    • A cytoplasmic inhibitor of the JNK signal transduction pathway
    • Dickens M., Rogers J. S., Cavanagh J., et al. (1997). A cytoplasmic inhibitor of the JNK signal transduction pathway. Science 277, 693-696.
    • (1997) Science , vol.277 , pp. 693-696
    • Dickens, M.1    Rogers, J.S.2    Cavanagh, J.3
  • 74
    • 0032508714 scopus 로고    scopus 로고
    • A mammalian scaffold complex that selectively mediates MAP kinase activation
    • Whitmarsh A. J., Cavanagh J., Tournier C., Yasuda J., Davis R. J. (1998). A mammalian scaffold complex that selectively mediates MAP kinase activation. Science 281, 1671-1674.
    • (1998) Science , vol.281 , pp. 1671-1674
    • Whitmarsh, A.J.1    Cavanagh, J.2    Tournier, C.3    Yasuda, J.4    Davis, R.J.5
  • 75
    • 0034644522 scopus 로고    scopus 로고
    • Signal transduction by the JNK group of MAP kinases
    • Davis R. J. (2000). Signal transduction by the JNK group of MAP kinases. Cell 103, 239-252.
    • (2000) Cell , vol.103 , pp. 239-252
    • Davis, R.J.1
  • 76
    • 0032422785 scopus 로고    scopus 로고
    • Structural organization of MAP-kinase signaling modules by scaffold proteins in yeast and mammals
    • Whitmarsh A. J., Davis R. J. (1998). Structural organization of MAP-kinase signaling modules by scaffold proteins in yeast and mammals. Trends Biochem. Sci. 23, 481-485.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 481-485
    • Whitmarsh, A.J.1    Davis, R.J.2
  • 77
    • 0033035827 scopus 로고    scopus 로고
    • Molecular cloning of multiple splicing variants of JIP-1 preferentially expressed in brain
    • Kim I. J., Lee K. W., Park B. Y., et al. (1999). Molecular cloning of multiple splicing variants of JIP-1 preferentially expressed in brain. J. Neurochem. 72, 1335-1343.
    • (1999) J. Neurochem. , vol.72 , pp. 1335-1343
    • Kim, I.J.1    Lee, K.W.2    Park, B.Y.3
  • 78
    • 0031915453 scopus 로고    scopus 로고
    • IB1, a JIP-1-related nuclear protein present in insulin-secreting cells
    • Bonny C., Nicod P., Waeber G. (1998). IB1, a JIP-1-related nuclear protein present in insulin-secreting cells. J. Biol. Chem. 273, 1843-1846.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1843-1846
    • Bonny, C.1    Nicod, P.2    Waeber, G.3
  • 79
    • 0033556422 scopus 로고    scopus 로고
    • Genomic organization, fine-mapping, and expression of the human islet-brain 1 (IB1)/c-Jun-amino-terminal kinase interacting protein-1 (JIP-1) gene
    • Mooser V., Maillard A., Bonny C., et al. (1999). Genomic organization, fine-mapping, and expression of the human islet-brain 1 (IB1)/c-Jun-amino- terminal kinase interacting protein-1 (JIP-1) gene. Genomics 55, 202-208.
    • (1999) Genomics , vol.55 , pp. 202-208
    • Mooser, V.1    Maillard, A.2    Bonny, C.3
  • 80
    • 0034052806 scopus 로고    scopus 로고
    • Spatial, temporal and subcellular localization of islet-brain 1 (IB1), a homologue of JIP-1, in mouse brain
    • Pellet J. B., Haefliger J. A., Staple J. K., et al. (2000). Spatial, temporal and subcellular localization of islet-brain 1 (IB1), a homologue of JIP-1, in mouse brain. Eur. J. Neurosci. 12, 621-632.
    • (2000) Eur. J. Neurosci. , vol.12 , pp. 621-632
    • Pellet, J.B.1    Haefliger, J.A.2    Staple, J.K.3
  • 81
    • 0035958938 scopus 로고    scopus 로고
    • Islet-brain1/JNK-interacting protein-1 is required for early embryogenesis in mice
    • Thompson N. A., Haefliger J. A., Senn A., et al. (2001). Islet-brain1/JNK-interacting protein-1 is required for early embryogenesis in mice. J. Biol. Chem. 276, 27,745-27,748.
    • (2001) J. Biol. Chem. , vol.276
    • Thompson, N.A.1    Haefliger, J.A.2    Senn, A.3
  • 82
    • 0035883958 scopus 로고    scopus 로고
    • Requirement of the JIP1 scaffold protein for stress-induced JNK activation
    • Whitmarsh A. J., Kuan C. Y., Kennedy N. J., et al. (2001). Requirement of the JIP1 scaffold protein for stress-induced JNK activation. Genes Dev. 15, 2421-2432.
    • (2001) Genes Dev. , vol.15 , pp. 2421-2432
    • Whitmarsh, A.J.1    Kuan, C.Y.2    Kennedy, N.J.3
  • 83
    • 0033712055 scopus 로고    scopus 로고
    • Kinesin-dependent axonal transport is mediated by the sunday driver (SYD) protein
    • Bowman A. B., Kamal A., Ritchings B. W., et al. (2000). Kinesin-dependent axonal transport is mediated by the sunday driver (SYD) protein. Cell 103, 583-594.
    • (2000) Cell , vol.103 , pp. 583-594
    • Bowman, A.B.1    Kamal, A.2    Ritchings, B.W.3
  • 84
    • 0035819072 scopus 로고    scopus 로고
    • UNC-16, a JNK-signaling scaffold protein, regulates vesicle transport in C. elegans
    • Byrd D. T., Kawasaki M., Walcoff M., Hisamoto N., Matsumoto K., Jin Y (2001). UNC-16, a JNK-signaling scaffold protein, regulates vesicle transport in C. elegans. Neuron 32, 787-800.
    • (2001) Neuron , vol.32 , pp. 787-800
    • Byrd, D.T.1    Kawasaki, M.2    Walcoff, M.3    Hisamoto, N.4    Matsumoto, K.5    Jin, Y.6
  • 85
    • 0035809914 scopus 로고    scopus 로고
    • Cargo of kinesin identified as JIP scaffolding proteins and associated signaling molecules
    • Verhey K. J., Meyer D., Deehan R., et al. (2001). Cargo of kinesin identified as JIP scaffolding proteins and associated signaling molecules. J. Cell. Biol. 152, 959-970.
    • (2001) J. Cell. Biol. , vol.152 , pp. 959-970
    • Verhey, K.J.1    Meyer, D.2    Deehan, R.3
  • 86
    • 0035829720 scopus 로고    scopus 로고
    • Disruption of axonal transport and neuronal viability by amyloid precursor protein mutations in Drosophila
    • Gunawardena S., Goldstein L. S. (2001). Disruption of axonal transport and neuronal viability by amyloid precursor protein mutations in Drosophila. Neuron 32, 389-401.
    • (2001) Neuron , vol.32 , pp. 389-401
    • Gunawardena, S.1    Goldstein, L.S.2
  • 87
    • 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., Xia C. H., Goldstein L. S. (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.5
  • 88
    • 0035818998 scopus 로고    scopus 로고
    • Kinesin-mediated axonal transport of a membrane compartment containing β-secretase and presenilin-1 requires APP
    • Kamal A., Almenar-Queralt A., LeBlanc J. F., Roberts E. A., Goldstein L. S. (2001). Kinesin-mediated axonal transport of a membrane compartment containing β-secretase and presenilin-1 requires APP. Nature 414, 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.5
  • 89
    • 0141532147 scopus 로고    scopus 로고
    • Amyloid β protein precursor (AβPP), but not AβPP-like protein 2, is bridged to the kinesin light chain by the scaffold protein JNK-interacting protein 1
    • Matsuda S., Matsuda Y., D'Adamio L. (2003). Amyloid β protein precursor (AβPP), but not AβPP-like protein 2, is bridged to the kinesin light chain by the scaffold protein JNK-interacting protein 1. J. Biol. Chem. 278, 38,601-38,606.
    • (2003) J. Biol. Chem. , vol.278
    • Matsuda, S.1    Matsuda, Y.2    D'Adamio, L.3
  • 90
    • 0034029430 scopus 로고    scopus 로고
    • A monoclonal antibody to amyloid precursor protein induces neuronal apoptosis
    • Rohn T. T., Ivins K. J., Bahr B. A., Cotman C. W., Cribbs D. H. (2000). A monoclonal antibody to amyloid precursor protein induces neuronal apoptosis. J. Neurochem. 74, 2331-2342.
    • (2000) J. Neurochem. , vol.74 , pp. 2331-2342
    • Rohn, T.T.1    Ivins, K.J.2    Bahr, B.A.3    Cotman, C.W.4    Cribbs, D.H.5
  • 91
    • 0034525215 scopus 로고    scopus 로고
    • Antibody-regulated neurotoxic function of cell surface β-amyloid precursor protein
    • Sudo H., Jiang H., Yasukawa T., et al. (2000). Antibody-regulated neurotoxic function of cell surface β-amyloid precursor protein. Mol. Cell. Neurosci. 16, 708-723.
    • (2000) Mol. Cell. Neurosci. , vol.16 , pp. 708-723
    • Sudo, H.1    Jiang, H.2    Yasukawa, T.3
  • 92
    • 0037036463 scopus 로고    scopus 로고
    • Amyloid precursor protein family-induced neuronal death is mediated by impairment of the neuroprotective calcium/calmodulin protein kinase IV-dependent signaling pathway
    • Mbebi C., See V., Mercken L., Pradier L., Muller U., Loeffler J. P. (2002). Amyloid precursor protein family-induced neuronal death is mediated by impairment of the neuroprotective calcium/calmodulin protein kinase IV-dependent signaling pathway. J. Biol. Chem. 277, 20,979-20,990.
    • (2002) J. Biol. Chem. , vol.277
    • Mbebi, C.1    See, V.2    Mercken, L.3    Pradier, L.4    Muller, U.5    Loeffler, J.P.6
  • 93
    • 0034741266 scopus 로고    scopus 로고
    • Secreted Aβ does not mediate neurotoxicity by antibody-stimulated amyloid precursor protein
    • Sudo H., Hashimoto Y., Niikura T., et al. (2001). Secreted Aβ does not mediate neurotoxicity by antibody-stimulated amyloid precursor protein. Biochem. Biophys. Res. Commun. 282, 548-556.
    • (2001) Biochem. Biophys. Res. Commun. , vol.282 , pp. 548-556
    • Sudo, H.1    Hashimoto, Y.2    Niikura, T.3
  • 94
    • 20244361899 scopus 로고    scopus 로고
    • Involvement of c-Jun N-terminal kinase in amyloid precursor protein-mediated neuronal cell death
    • Hashimoto Y., Tsuji O., Niikura T., et al. (2003). Involvement of c-Jun N-terminal kinase in amyloid precursor protein-mediated neuronal cell death. J. Neurochem. 84, 864-877.
    • (2003) J. Neurochem. , vol.84 , pp. 864-877
    • Hashimoto, Y.1    Tsuji, O.2    Niikura, T.3
  • 96
    • 0142211267 scopus 로고    scopus 로고
    • Amyloid β protein precursor is phosphorylated by JNK-1 independent of, yet facilitated by, JNK-interacting protein (JIP)-1
    • Scheinfeld M. H., Ghersi E., Davies P., D'Adamio L. (2003). Amyloid β protein precursor is phosphorylated by JNK-1 independent of, yet facilitated by, JNK-interacting protein (JIP)-1. J. Biol. Chem. 278, 42,058-42,063.
    • (2003) J. Biol. Chem. , vol.278
    • Scheinfeld, M.H.1    Ghersi, E.2    Davies, P.3    D'Adamio, L.4
  • 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. (2002). Differential roles of JIP scaffold proteins in the modulation of amyloid precursor protein metabolism. J. Biol. Chem. 277, 27,567-27,574.
    • (2002) J. Biol. Chem. , vol.277
    • Taru, H.1    Kirino, Y.2    Suzuki, T.3
  • 98
    • 0037452773 scopus 로고    scopus 로고
    • JNK-interacting protein-1 promotes transcription of Aβ protein precursor but not Aβ precursor-like proteins, mechanistically different than Fe65
    • Scheinfeld M. H., Matsuda S., D'Adamio L. (2003). JNK-interacting protein-1 promotes transcription of Aβ protein precursor but not Aβ precursor-like proteins, mechanistically different than Fe65. Proc. Natl. Acad. Sci. USA 100, 1729-1734.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 1729-1734
    • Scheinfeld, M.H.1    Matsuda, S.2    D'Adamio, L.3
  • 99
    • 0037053281 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the β-amyloid precursor protein cytoplasmic tail promotes interaction with Shc
    • Tarr P. E., Roncarati R., Pelicci G., Pelicci P. G., D'Adamio L. (2002). Tyrosine phosphorylation of the β-amyloid precursor protein cytoplasmic tail promotes interaction with Shc. J. Biol. Chem. 277, 16,798-16,804.
    • (2002) J. Biol. Chem. , vol.277
    • Tarr, P.E.1    Roncarati, R.2    Pelicci, G.3    Pelicci, P.G.4    D'Adamio, L.5
  • 100
    • 0035955712 scopus 로고    scopus 로고
    • Phosphorylation-dependent regulation of the interaction of amyloid precursor protein with Fe65 affects the production of β-amyloid
    • Ando K., Iijima K. I., Elliott J. I., Kirino Y., Suzuki T. (2001). Phosphorylation-dependent regulation of the interaction of amyloid precursor protein with Fe65 affects the production of β-amyloid. J. Biol. Chem. 276, 40,353-40,361.
    • (2001) J. Biol. Chem. , vol.276
    • Ando, K.1    Iijima, K.I.2    Elliott, J.I.3    Kirino, Y.4    Suzuki, T.5
  • 101
    • 0037049236 scopus 로고    scopus 로고
    • Expression of the Fe65 adapter protein in adult and developing mouse brain
    • Kesavapany S., Banner S. J., Lau K. F., et al. (2002). Expression of the Fe65 adapter protein in adult and developing mouse brain. Neuroscience 115, 951-960.
    • (2002) Neuroscience , vol.115 , pp. 951-960
    • Kesavapany, S.1    Banner, S.J.2    Lau, K.F.3
  • 102
    • 0033583316 scopus 로고    scopus 로고
    • Regulation of β-amyloid secretion by FE65, an amyloid protein precursor-binding protein
    • Sabo S. L., Lanier L. M., Ikin A. F., et al. (1999). Regulation of β-amyloid secretion by FE65, an amyloid protein precursor-binding protein. J. Biol. Chem. 274, 7952-7957.
    • (1999) J. Biol. Chem. , vol.274 , pp. 7952-7957
    • Sabo, S.L.1    Lanier, L.M.2    Ikin, A.F.3
  • 103
    • 0034123008 scopus 로고    scopus 로고
    • Broadly altered expression of the mRNA isoforms of FE65, a facilitator of beta amyloidogenesis, in Alzheimer cerebellum and other brain regions
    • Hu Q., Jin L. W., Starbuck M. Y., Martin G. M. (2000). Broadly altered expression of the mRNA isoforms of FE65, a facilitator of beta amyloidogenesis, in Alzheimer cerebellum and other brain regions. J. Neurosci. Res. 60, 73-86.
    • (2000) J. Neurosci. Res. , vol.60 , pp. 73-86
    • Hu, Q.1    Jin, L.W.2    Starbuck, M.Y.3    Martin, G.M.4
  • 104
    • 0035023345 scopus 로고    scopus 로고
    • FE65 in Alzheimer's disease: Neuronal distribution and association with neurofibrillary tangles
    • Delatour B., Mercken L., El Hachimi K. H., Colle M. A., Pradier L., Duyckaerts C. (2001). FE65 in Alzheimer's disease: neuronal distribution and association with neurofibrillary tangles. Am. J. Pathol. 158, 1585-1591.
    • (2001) Am. J. Pathol. , vol.158 , pp. 1585-1591
    • Delatour, B.1    Mercken, L.2    El Hachimi, K.H.3    Colle, M.A.4    Pradier, L.5    Duyckaerts, C.6
  • 105
    • 0031710443 scopus 로고    scopus 로고
    • The human FE65 gene: Genomic structure and an intronic biallelic polymorphism associated with sporadic dementia of the Alzheimer type
    • Hu Q., Kukull W. A., Bressler S. L., et al. (1998). The human FE65 gene: genomic structure and an intronic biallelic polymorphism associated with sporadic dementia of the Alzheimer type. Hum. Genet. 103, 295-303.
    • (1998) Hum. Genet. , vol.103 , pp. 295-303
    • Hu, Q.1    Kukull, W.A.2    Bressler, S.L.3
  • 106
    • 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., Cool B. H., Wang B., Hearn M. G., Martin G. M. (2002). A candidate molecular mechanism for the association of an intronic polymorphism of FE65 with resistance to very late onset dementia of the Alzheimer type. Hum. Mol. Genet. 11, 465-475.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 465-475
    • Hu, Q.1    Cool, B.H.2    Wang, B.3    Hearn, M.G.4    Martin, G.M.5
  • 107
    • 0034693448 scopus 로고    scopus 로고
    • A FE65 polymorphism associated with risk of developing sporadic late-onset alzheimer's disease but not with Aβ loading in brains
    • Lambert J. C., Mann D., Goumidi L., et al. (2000). A FE65 polymorphism associated with risk of developing sporadic late-onset alzheimer's disease but not with Aβ loading in brains. Neurosci. Lett. 293, 29-32.
    • (2000) Neurosci. Lett. , vol.293 , pp. 29-32
    • Lambert, J.C.1    Mann, D.2    Goumidi, L.3
  • 108
    • 0034672331 scopus 로고    scopus 로고
    • Evidence against association of the FE65 gene (APBB1) intron 13 polymorphism in Alzheimer's patients
    • Guenette S. Y., Bertram L., Crystal A., et al. (2000). Evidence against association of the FE65 gene (APBB1) intron 13 polymorphism in Alzheimer's patients. Neurosci. Lett. 296, 17-20.
    • (2000) Neurosci. Lett. , vol.296 , pp. 17-20
    • Guenette, S.Y.1    Bertram, L.2    Crystal, A.3
  • 109
    • 0242500800 scopus 로고    scopus 로고
    • A risk for early-onset Alzheimer's disease associated with the APBB1 gene (FE65) intron 13 polymorphism
    • Cousin E., Mannequin D., Ricard S., et al. (2003). A risk for early-onset Alzheimer's disease associated with the APBB1 gene (FE65) intron 13 polymorphism. Neurosci. Lett. 342, 5-8.
    • (2003) Neurosci. Lett. , vol.342 , pp. 5-8
    • Cousin, E.1    Mannequin, D.2    Ricard, S.3
  • 110
    • 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. (1999). 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, 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.6
  • 111
    • 0037223014 scopus 로고    scopus 로고
    • Genetic modulation of tau phosphorylation in the mouse
    • Brich J., Shie F. S., Howell B. W., et al. (2003). Genetic modulation of tau phosphorylation in the mouse. J. Neurosci. 23, 187-192.
    • (2003) J. Neurosci. , vol.23 , pp. 187-192
    • Brich, J.1    Shie, F.S.2    Howell, B.W.3
  • 112
    • 0035879075 scopus 로고    scopus 로고
    • Dishevelled regulates the metabolism of amyloid precursor protein via protein kinase C/mitogen-activated protein kinase and c-Jun terminal kinase
    • Mudher A., Chapman S., Richardson J., et al. (2001). Dishevelled regulates the metabolism of amyloid precursor protein via protein kinase C/mitogen-activated protein kinase and c-Jun terminal kinase. J. Neurosci. 21, 4987-4995.
    • (2001) J. Neurosci. , vol.21 , pp. 4987-4995
    • Mudher, A.1    Chapman, S.2    Richardson, J.3
  • 114
    • 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 E. A., Papadopoulos R., Fuller S. J., et al. (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
  • 116
    • 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 D. H., Nurcombe V., Reed G., et al. (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
  • 117
    • 0035142804 scopus 로고    scopus 로고
    • Activation and redistribution of c-Jun N-terminal kinase/stress activated protein kinase in degenerating neurons in Alzheimer's disease
    • Zhu X., Raina A. K., Rottkamp C. A., Aliev G., Perry G., Boux H., Smith M. A. (2001). Activation and redistribution of c-Jun N-terminal kinase/stress activated protein kinase in degenerating neurons in Alzheimer's disease. J. Neurochem. 76, 435-441.
    • (2001) J. Neurochem. , vol.76 , pp. 435-441
    • Zhu, X.1    Raina, A.K.2    Rottkamp, C.A.3    Aliev, G.4    Perry, G.5    Boux, H.6    Smith, M.A.7
  • 118
    • 0036580703 scopus 로고    scopus 로고
    • Activation of c-Jun N-terminal kinase and p38 in an Alzheimer's disease model is associated with amyloid deposition
    • Savage M. J., Lin Y. G., Ciallella J. R., Flood D. G., Scott R. W. (2002). Activation of c-Jun N-terminal kinase and p38 in an Alzheimer's disease model is associated with amyloid deposition. J. Neurosci. 22, 3376-3385.
    • (2002) J. Neurosci. , vol.22 , pp. 3376-3385
    • Savage, M.J.1    Lin, Y.G.2    Ciallella, J.R.3    Flood, D.G.4    Scott, R.W.5
  • 119
    • 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. (2000). Kinesin superfamily motor protein KIF17 and mLin-10 in NMDA receptor-containing vesicle transport. Science 288, 1796-1802.
    • (2000) Science , vol.288 , pp. 1796-1802
    • Setou, M.1    Nakagawa, T.2    Seog, D.H.3    Hirokawa, N.4
  • 120
    • 0034704089 scopus 로고    scopus 로고
    • Mints as adaptors. Direct binding to neurexins and recruitment of munc18
    • Biederer T., Sudhof T. C. (2000). Mints as adaptors. Direct binding to neurexins and recruitment of munc18. J. Biol. Chem. 275, 39,803-39,806.
    • (2000) J. Biol. Chem. , vol.275
    • Biederer, T.1    Sudhof, T.C.2
  • 121
    • 0032514259 scopus 로고    scopus 로고
    • Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to the basolateral membrane of epithelial cells
    • Cohen A. R., Woods D. F., Marfatia S. M., et al. (1998). Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to the basolateral membrane of epithelial cells. J. Cell. Biol. 142, 129-138.
    • (1998) J. Cell. Biol. , vol.142 , pp. 129-138
    • Cohen, A.R.1    Woods, D.F.2    Marfatia, S.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.