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Volumn 22, Issue 22, 2013, Pages 4646-4652

Loss of c-Jun N-terminal kinase-interacting protein-1 does not affect axonal transport of the amyloid precursor protein or Aβ production

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID A PROTEIN; AMYLOID BETA PROTEIN; C JUN N TERMINAL KINASE INTERACTING PROTEIN 1; ENHANCED GREEN FLUORESCENT PROTEIN; KINESIN 1; PROTEIN; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 84887005627     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddt313     Document Type: Article
Times cited : (16)

References (62)
  • 2
    • 33751020569 scopus 로고    scopus 로고
    • Axonal transport and neurodegenerative disease
    • Chevalier-Larsen, E. and Holzbaur, E.L. (2006) Axonal transport and neurodegenerative disease. Biochim. Biophys. Acta, 1762, 1094-1108.
    • (2006) Biochim. Biophys. Acta , vol.1762 , pp. 1094-1108
    • Chevalier-Larsen, E.1    Holzbaur, E.L.2
  • 4
    • 84875443717 scopus 로고    scopus 로고
    • Axonal transport deficits and neurodegenerative diseases
    • Millecamps, S. and Julien, J.P. (2013) Axonal transport deficits and neurodegenerative diseases. Nat. Rev. Neurosci., 14, 161-176.
    • (2013) Nat. Rev. Neurosci. , vol.14 , pp. 161-176
    • Millecamps, S.1    Julien, J.P.2
  • 5
    • 76849086405 scopus 로고    scopus 로고
    • The secretases: Enzymes with therapeutic potential in Alzheimer disease
    • De Strooper, B., Vassar, R. and Golde, T. (2010) The secretases: enzymes with therapeutic potential in Alzheimer disease. Nat. Rev. Neurol., 6, 99-107.
    • (2010) Nat. Rev. Neurol. , vol.6 , pp. 99-107
    • De Strooper, B.1    Vassar, R.2    Golde, T.3
  • 6
    • 77955089126 scopus 로고    scopus 로고
    • The functional neurophysiology of the amyloid precursor protein (APP) processing pathway
    • Randall, A.D., Witton, J., Booth, C., Hynes-Allen, A. and Brown, J.T. (2010) The functional neurophysiology of the amyloid precursor protein (APP) processing pathway. Neuropharmacology, 59, 243-267.
    • (2010) Neuropharmacology , vol.59 , pp. 243-267
    • Randall, A.D.1    Witton, J.2    Booth, C.3    Hynes-Allen, A.4    Brown, J.T.5
  • 7
    • 5344277556 scopus 로고    scopus 로고
    • Deciphering the molecular basis of memory failure in Alzheimer's disease
    • Walsh, D.M. and Selkoe, D.J. (2004) Deciphering the molecular basis of memory failure in Alzheimer's disease. Neuron, 44, 181-193.
    • (2004) Neuron , vol.44 , pp. 181-193
    • Walsh, D.M.1    Selkoe, D.J.2
  • 9
    • 84863518335 scopus 로고    scopus 로고
    • Calsyntenin-1 mediates axonal transport of the amyloid precursor protein and regulates Abeta production
    • Vagnoni, A., Perkinton, M.S., Gray, E.H., Francis, P.T., Noble, W. and Miller, C.C.J. (2012) Calsyntenin-1 mediates axonal transport of the amyloid precursor protein and regulates Abeta production. Hum. Mol. Genet., 21, 2845-2854.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 2845-2854
    • Vagnoni, A.1    Perkinton, M.S.2    Gray, E.H.3    Francis, P.T.4    Noble, W.5    Miller, C.C.J.6
  • 10
    • 84964915731 scopus 로고    scopus 로고
    • Calsyntenin-1 shelters APP from proteolytic processing during anterograde axonal transport
    • Steuble, M., Diep, T.M., Schatzle, P., Ludwig, A., Tagaya, M., Kunz, B. and Sonderegger, P. (2012) Calsyntenin-1 shelters APP from proteolytic processing during anterograde axonal transport. Biol. Open, 1, 761-774.
    • (2012) Biol. Open , vol.1 , pp. 761-774
    • Steuble, M.1    Diep, T.M.2    Schatzle, P.3    Ludwig, A.4    Tagaya, M.5    Kunz, B.6    Sonderegger, P.7
  • 11
    • 77954466407 scopus 로고    scopus 로고
    • Amyloid-beta peptide oligomers disrupt axonal transport through an NMDA receptor-dependent mechanism that is mediated by glycogen synthase kinase 3beta in primary cultured hippocampal neurons
    • Decker, H., Lo, K.Y., Unger, S.M., Ferreira, S.T. and Silverman, M.A. (2010) Amyloid-beta peptide oligomers disrupt axonal transport through an NMDA receptor-dependent mechanism that is mediated by glycogen synthase kinase 3beta in primary cultured hippocampal neurons. J. Neurosci., 30, 9166-9171.
    • (2010) J. Neurosci. , vol.30 , pp. 9166-9171
    • Decker, H.1    Lo, K.Y.2    Unger, S.M.3    Ferreira, S.T.4    Silverman, M.A.5
  • 12
    • 0141864562 scopus 로고    scopus 로고
    • Glutamate and amyloid beta-protein rapidly inhibit fast axonal transport in cultured rat hippocampal neurons by different mechanisms
    • Hiruma, H., Katakura, T., Takahashi, S., Ichikawa, T. and Kawakami, T. (2003) Glutamate and amyloid beta-protein rapidly inhibit fast axonal transport in cultured rat hippocampal neurons by different mechanisms. J. Neurosci., 23, 8967-8977.
    • (2003) J. Neurosci. , vol.23 , pp. 8967-8977
    • Hiruma, H.1    Katakura, T.2    Takahashi, S.3    Ichikawa, T.4    Kawakami, T.5
  • 13
    • 0033621641 scopus 로고    scopus 로고
    • Human amyloid-beta1-42 applied in vivo inhibits the fast axonal transport of proteins in the sciatic nerve of rat
    • Kasa, P., Papp, H., Kovacs, I., Forgon, M., Penke, B. and Yamaguchi, H. (2000) Human amyloid-beta1-42 applied in vivo inhibits the fast axonal transport of proteins in the sciatic nerve of rat. Neurosci. Lett., 278, 117-119.
    • (2000) Neurosci. Lett. , vol.278 , pp. 117-119
    • Kasa, P.1    Papp, H.2    Kovacs, I.3    Forgon, M.4    Penke, B.5    Yamaguchi, H.6
  • 15
    • 33749854516 scopus 로고    scopus 로고
    • Acute impairment of mitochondrial trafficking by beta-amyloid peptides in hippocampal neurons
    • Rui, Y., Tiwari, P., Xie, Z. and Zheng, J.Q. (2006) Acute impairment of mitochondrial trafficking by beta-amyloid peptides in hippocampal neurons. J. Neurosci., 26, 10480-10487.
    • (2006) J. Neurosci. , vol.26 , pp. 10480-10487
    • Rui, Y.1    Tiwari, P.2    Xie, Z.3    Zheng, J.Q.4
  • 16
    • 76549123596 scopus 로고    scopus 로고
    • Amyloid-beta-derived diffusible ligands cause impaired axonal transport of mitochondria in neurons
    • Wang, X., Perry, G., Smith, M.A. and Zhu, X. (2010) Amyloid-beta-derived diffusible ligands cause impaired axonal transport of mitochondria in neurons. Neurodegenerative Diseases, 7, 56-59.
    • (2010) Neurodegenerative Diseases , vol.7 , pp. 56-59
    • Wang, X.1    Perry, G.2    Smith, M.A.3    Zhu, X.4
  • 17
    • 77956587739 scopus 로고    scopus 로고
    • Abeta oligomers cause localized Ca(2+) elevation, missorting of endogenous tau into dendrites, tau phosphorylation, and destruction of microtubules and spines
    • Zempel, H., Thies, E., Mandelkow, E. and Mandelkow, E.M. (2010) Abeta oligomers cause localized Ca(2+) elevation, missorting of endogenous tau into dendrites, tau phosphorylation, and destruction of microtubules and spines. J. Neurosci., 30, 11938-11950.
    • (2010) J. Neurosci. , vol.30 , pp. 11938-11950
    • Zempel, H.1    Thies, E.2    Mandelkow, E.3    Mandelkow, E.M.4
  • 18
    • 0034075589 scopus 로고    scopus 로고
    • Axonalmembrane proteins are transported in distinct carriers: a two-color video microscopy study in cultured hippocampal neurons
    • Kaether, C., Skehel, P. and Dotti, C.G. (2000) Axonalmembrane proteins are transported in distinct carriers: a two-color video microscopy study in cultured hippocampal neurons. Mol. Biol. Cell, 11, 1213-1224.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1213-1224
    • Kaether, C.1    Skehel, P.2    Dotti, C.G.3
  • 20
    • 84861235844 scopus 로고    scopus 로고
    • Axonal transport of APP and the spatial regulation of APP cleavage and function in neuronal cells
    • Brunholz, S., Sisodia, S., Lorenzo, A., Deyts, C., Kins, S. and Morfini, G. (2011) Axonal transport of APP and the spatial regulation of APP cleavage and function in neuronal cells. Exp. Brain Res., 217, 353-364.
    • (2011) Exp. Brain Res. , vol.217 , pp. 353-364
    • Brunholz, S.1    Sisodia, S.2    Lorenzo, A.3    Deyts, C.4    Kins, S.5    Morfini, G.6
  • 21
    • 70349437416 scopus 로고    scopus 로고
    • Kinesin superfamily motor proteins and intracellular transport
    • Hirokawa, N., Noda, Y., Tanaka, Y. and Niwa, S. (2009) Kinesin superfamily motor proteins and intracellular transport. Nat. Rev. Mol. Cell Biol., 10, 682-696.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 682-696
    • Hirokawa, N.1    Noda, Y.2    Tanaka, Y.3    Niwa, S.4
  • 23
    • 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. and Goldstein, L.S.B. (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.H.3    Xia, C.H.4    Goldstein, L.S.B.5
  • 28
    • 81255138088 scopus 로고    scopus 로고
    • Akinesin-1 binding motif in vaccinia virus that is widespread throughout the human genome
    • Dodding, M.P., Mitter, R., Humphries, A.C. and Way, M. (2011) Akinesin-1 binding motif in vaccinia virus that is widespread throughout the human genome. EMBO J., 30, 4523-4538.
    • (2011) EMBO J. , vol.30 , pp. 4523-4538
    • Dodding, M.P.1    Mitter, R.2    Humphries, A.C.3    Way, M.4
  • 29
    • 79953141458 scopus 로고    scopus 로고
    • Phosphorylation of kinesin light chain-1 at serine-460 modulates binding and trafficking of calsyntenin-1
    • Vagnoni, A., Rodriguez, L., Manser, C., De Vos, K.J. and Miller, C.C.J. (2011) Phosphorylation of kinesin light chain-1 at serine-460 modulates binding and trafficking of calsyntenin-1. J. Cell Sci., 124, 1032-1042.
    • (2011) J. Cell Sci. , vol.124 , pp. 1032-1042
    • Vagnoni, A.1    Rodriguez, L.2    Manser, C.3    De Vos, K.J.4    Miller, C.C.J.5
  • 30
    • 84860921031 scopus 로고    scopus 로고
    • A small peptide sequence is sufficient for initiating Kinesin-1 activation through part of TPR region of KLC1
    • Kawano, T., Araseki, M., Araki, Y., Kinjo, M., Yamamoto, T. and Suzuki, T. (2012) A small peptide sequence is sufficient for initiating Kinesin-1 activation through part of TPR region of KLC1. Traffic, 13, 834-848.
    • (2012) Traffic , vol.13 , pp. 834-848
    • Kawano, T.1    Araseki, M.2    Araki, Y.3    Kinjo, M.4    Yamamoto, T.5    Suzuki, T.6
  • 32
    • 27944444156 scopus 로고    scopus 로고
    • Coordinated transport of phosphorylated amyloid-beta precursor protein and c-Jun NH2-terminal kinase-interacting protein-1
    • Muresan, Z. and Muresan, V. (2005) Coordinated transport of phosphorylated amyloid-beta precursor protein and c-Jun NH2-terminal kinase-interacting protein-1. J. Cell Biol., 171, 615-625.
    • (2005) J. Cell Biol. , vol.171 , pp. 615-625
    • Muresan, Z.1    Muresan, V.2
  • 33
    • 33846007738 scopus 로고    scopus 로고
    • PAT1a Modulates intracellular transport and processing of amyloid precursor protein (APP), APLP1, and APLP2
    • Kuan, Y.H., Gruebl, T., Soba, P., Eggert, S., Nesic, I., Back, S., Kirsch, J., Beyreuther, K. and Kins, S. (2006) PAT1a Modulates intracellular transport and processing of amyloid precursor protein (APP), APLP1, and APLP2. J. Biol. Chem., 281, 40114-40123.
    • (2006) J. Biol. Chem. , vol.281 , pp. 40114-40123
    • Kuan, Y.H.1    Gruebl, T.2    Soba, P.3    Eggert, S.4    Nesic, I.5    Back, S.6    Kirsch, J.7    Beyreuther, K.8    Kins, S.9
  • 34
    • 0032410747 scopus 로고    scopus 로고
    • PAT1, A microtubule-interacting protein, recognizes the basolateral sorting signal of amyloid precursor protein
    • Zheng, P., Eastman, J., Vande Pol, S. and Pimplikar, S.W. (1998) PAT1, A microtubule-interacting protein, recognizes the basolateral sorting signal of amyloid precursor protein. Proc. Natl Acad. Sci. USA, 95, 14745-12750.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 14745-12750
    • Zheng, P.1    Eastman, J.2    Vande Pol, S.3    Pimplikar, S.W.4
  • 35
    • 0141532147 scopus 로고    scopus 로고
    • Amyloid beta protein precursor (AbetaPP), but not AbetaPP like protein-2, is bridged to the kinesin light chain by the scaffold JNK-interacting protein 1
    • Matsuda, S., Matsuda, Y. and D'Adamio, L. (2003) Amyloid beta protein precursor (AbetaPP), but not AbetaPP like protein-2, is bridged to the kinesin light chain by the scaffold JNK-interacting protein 1. J. Biol. Chem., 278, 38601-38606.
    • (2003) J. Biol. Chem. , vol.278 , pp. 38601-38606
    • Matsuda, S.1    Matsuda, Y.2    D'Adamio, L.3
  • 36
    • 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. and Kitamura, N. (2003) A scaffold protein JIP-1b enhances amyloid precursor protein phosphorylation by JNK and its association with kinesin light chain 1. J. Biol. Chem., 278, 22946-22955.
    • (2003) J. Biol. Chem. , vol.278 , pp. 22946-22955
    • Inomata, H.1    Nakamura, Y.2    Hayakawa, A.3    Takata, H.4    Suzuki, T.5    Miyazawa, K.6    Kitamura, N.7
  • 38
    • 28444496758 scopus 로고    scopus 로고
    • APLIP1, A kinesin binding JIP-1/JNK scaffold protein, influences the axonal transport of both vesicles and mitochondria in Drosophila
    • Horiuchi, D., Barkus, R.V., Pilling, A.D., Gassman, A. and Saxton, W.M. (2005) APLIP1, A kinesin binding JIP-1/JNK scaffold protein, influences the axonal transport of both vesicles and mitochondria in Drosophila. Curr. Biol., 15, 2137-2141.
    • (2005) Curr. Biol. , vol.15 , pp. 2137-2141
    • Horiuchi, D.1    Barkus, R.V.2    Pilling, A.D.3    Gassman, A.4    Saxton, W.M.5
  • 39
    • 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., Ito, Y., Niikura, T., Hiraki, T., Hira, S., Ohno, S., Kita, Y., Kawasumi, M. 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    Ito, Y.4    Niikura, T.5    Hiraki, T.6    Hira, S.7    Ohno, S.8    Kita, Y.9    Kawasumi, M.10
  • 40
    • 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. and Suzuki, T. (2002) Interaction of Alzheimer's beta-amyloid precursor family proteins with scaffold proteins of the JNK signaling cascade. J. Biol. Chem., 277, 20070-20078.
    • (2002) J. Biol. Chem. , vol.277 , pp. 20070-20078
    • Taru, H.1    Iijima, K.2    Hase, M.3    Kirino, Y.4    Yagi, Y.5    Suzuki, T.6
  • 41
    • 0037178872 scopus 로고    scopus 로고
    • Differential roles of JIP scaffold proteins in the modulation of amyloid precursor protein metabolism
    • Taru, H., Kirino, Y. and Suzuki, T. (2002) Differential roles of JIP scaffold proteins in the modulation of amyloid precursor protein metabolism. J. Biol. Chem., 277, 27567-27574.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27567-27574
    • Taru, H.1    Kirino, Y.2    Suzuki, T.3
  • 42
    • 38849086625 scopus 로고    scopus 로고
    • The JIP1 scaffold protein regulates axonal development in cortical neurons
    • Dajas-Bailador, F., Jones, E.V. and Whitmarsh, A.J. (2008) The JIP1 scaffold protein regulates axonal development in cortical neurons. Curr. Biol., 18, 221-226.
    • (2008) Curr. Biol. , vol.18 , pp. 221-226
    • Dajas-Bailador, F.1    Jones, E.V.2    Whitmarsh, A.J.3
  • 47
    • 84867766569 scopus 로고    scopus 로고
    • Enhanced beta-secretase processing alters APP axonal transport and leads to axonal defects
    • Rodrigues, E.M., Weissmiller, A.M. and Goldstein, L.S. (2012) Enhanced beta-secretase processing alters APP axonal transport and leads to axonal defects. Hum. Mol. Genet., 21, 4587-4601.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 4587-4601
    • Rodrigues, E.M.1    Weissmiller, A.M.2    Goldstein, L.S.3
  • 48
    • 5444273804 scopus 로고    scopus 로고
    • MARK/PAR1 kinase is a regulator of microtubule-dependent transport in axons
    • Mandelkow, E.M., Thies, E., Trinczek, B., Biernat, J. and Mandelkow, E. (2004) MARK/PAR1 kinase is a regulator of microtubule-dependent transport in axons. J. Cell Biol., 167, 99-110.
    • (2004) J. Cell Biol. , vol.167 , pp. 99-110
    • Mandelkow, E.M.1    Thies, E.2    Trinczek, B.3    Biernat, J.4    Mandelkow, E.5
  • 49
    • 1542782550 scopus 로고    scopus 로고
    • Novel cadherin-related membrane proteins, Alcadeins, enhance the X11-like protein-mediated stabilization of amyloid beta -protein precursor metabolism
    • Araki, Y., Tomita, S., Yamaguchi, H., Miyagi, N., Sumioka, A., Kirino, Y. and Suzuki, T. (2003) Novel cadherin-related membrane proteins, Alcadeins, enhance the X11-like protein-mediated stabilization of amyloid beta -protein precursor metabolism. J. Biol. Chem., 278, 49448-49458.
    • (2003) J. Biol. Chem. , vol.278 , pp. 49448-49458
    • Araki, Y.1    Tomita, S.2    Yamaguchi, H.3    Miyagi, N.4    Sumioka, A.5    Kirino, Y.6    Suzuki, T.7
  • 50
    • 0141481046 scopus 로고    scopus 로고
    • Munc18 interacting proteins: ADP-ribosylation factor-dependent coat proteins that regulate the traffic of beta-Alzheimer's precursor protein
    • Hill,K., Li,Y.,Bennett, M.,McKay,M.,Zhu,X.,Shern, J., Torre, E.,Lah, J.J., Levey, A.I. and Kahn, R.A. (2003)Munc18 interacting proteins: ADP-ribosylation factor-dependent coat proteins that regulate the traffic of beta-Alzheimer's precursor protein. J. Biol. Chem., 278, 36032-36040.
    • (2003) J. Biol. Chem. , vol.278 , pp. 36032-36040
    • 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
    • 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. and Miller, C.C.J. (1996) 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, 197-200.
    • (1996) FEBS Lett. , vol.397 , pp. 197-200
    • McLoughlin, D.M.1    Miller, C.C.J.2
  • 52
    • 0033593480 scopus 로고    scopus 로고
    • Interaction of a neuron-specific protein containing PDZ domains withAlzheimer's amyloid precursor protein
    • Tomita, S.,Ozaki, T.,Taru,H.,Oguchi, S., Takeda, S.,Yagi, Y., Sakiyama, S., Kirino, Y. and Suzuki, T. (1999) Interaction of a neuron-specific protein containing PDZ domains withAlzheimer'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    Oguchi, S.4    Takeda, S.5    Yagi, Y.6    Sakiyama, S.7    Kirino, Y.8    Suzuki, T.9
  • 53
    • 10344227214 scopus 로고    scopus 로고
    • The neuronal adaptor protein X11beta reduces Abeta levels and amyloid plaque formation in the brains of transgenic mice
    • Lee, J.H., Lau, K.F., Perkinton, M.S., Standen, C.L., Rogelj, B., Falinska, A., McLoughlin, D.M. and Miller, C.C. (2004) The neuronal adaptor protein X11beta reduces Abeta levels and amyloid plaque formation in the brains of transgenic mice. J. Biol. Chem., 279, 49099-49104.
    • (2004) J. Biol. Chem. , vol.279 , pp. 49099-49104
    • Lee, J.H.1    Lau, K.F.2    Perkinton, M.S.3    Standen, C.L.4    Rogelj, B.5    Falinska, A.6    McLoughlin, D.M.7    Miller, C.C.8
  • 56
    • 68949105821 scopus 로고    scopus 로고
    • Phosphorylated tau interacts with c-JUN N-terminal kinase (JNK) interacting protein 1 (JIP1) in Alzheimer's disease
    • Ittner, L.M., Ke, Y.D. and Gotz, J. (2009) Phosphorylated tau interacts with c-JUN N-terminal kinase (JNK) interacting protein 1 (JIP1) in Alzheimer's disease. J. Biol. Chem., 284, 20909-20916.
    • (2009) J. Biol. Chem. , vol.284 , pp. 20909-20916
    • Ittner, L.M.1    Ke, Y.D.2    Gotz, J.3
  • 57
    • 79959453985 scopus 로고    scopus 로고
    • Alternative processing of gamma-secretase substrates in common forms of mild cognitive impairment and Alzheimer's disease: evidence for gamma-secretase dysfunction
    • Hata, S., Fujishige, S., Araki, Y., Taniguchi, M., Urakami, K., Peskind, E., Akatsu, H., Araseki, M., Yamamoto, K., Martins, R.N. et al. (2011) Alternative processing of gamma-secretase substrates in common forms of mild cognitive impairment and Alzheimer's disease: evidence for gamma-secretase dysfunction. Ann. Neurol., 69, 1026-1031.
    • (2011) Ann. Neurol. , vol.69 , pp. 1026-1031
    • Hata, S.1    Fujishige, S.2    Araki, Y.3    Taniguchi, M.4    Urakami, K.5    Peskind, E.6    Akatsu, H.7    Araseki, M.8    Yamamoto, K.9    Martins, R.N.10
  • 58
    • 84862183317 scopus 로고    scopus 로고
    • Multiple gamma-secretase product peptides are coordinately increased in concentration in the cerebrospinal fluid of a subpopulation of sporadic Alzheimer's disease subjects
    • Hata, S., Taniguchi, M., Piao, Y., Ikeuchi, T., Fagan, A.M., Holtzman, D.M., Bateman, R., Sohrabi, H.R., Martins, R.N., Gandy, S. et al. (2012) Multiple gamma-secretase product peptides are coordinately increased in concentration in the cerebrospinal fluid of a subpopulation of sporadic Alzheimer's disease subjects. Mol. Neurodegener., 7, 16.
    • (2012) Mol. Neurodegener. , vol.7 , pp. 16
    • Hata, S.1    Taniguchi, M.2    Piao, Y.3    Ikeuchi, T.4    Fagan, A.M.5    Holtzman, D.M.6    Bateman, R.7    Sohrabi, H.R.8    Martins, R.N.9    Gandy, S.10
  • 60
    • 70450197433 scopus 로고    scopus 로고
    • Amyloid precursor protein 695 assocoates with assembled NR2A- and NR2B-containingNMDAreceptors to result in the enhancement of their cell surface delivery
    • Cousins, S.L., Hoey, S.E., Stephenson, F.A. and Perkinton, M.S. (2009) Amyloid precursor protein 695 assocoates with assembled NR2A- and NR2B-containingNMDAreceptors to result in the enhancement of their cell surface delivery. J. Neurochem., 111, 1501-1513.
    • (2009) J. Neurochem. , vol.111 , pp. 1501-1513
    • Cousins, S.L.1    Hoey, S.E.2    Stephenson, F.A.3    Perkinton, M.S.4
  • 62
    • 84859246580 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis-associated mutant VAPBP56S perturbs calcium homeostasis to disrupt axonal transport of mitochondria
    • Morotz, G.M., De Vos, K.J., Vagnoni, A., Ackerley, S., Shaw, C.E. and Miller, C.C.J. (2012) Amyotrophic lateral sclerosis-associated mutant VAPBP56S perturbs calcium homeostasis to disrupt axonal transport of mitochondria. Hum. Mol. Genet., 21, 1979-1988.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 1979-1988
    • Morotz, G.M.1    De Vos, K.J.2    Vagnoni, A.3    Ackerley, S.4    Shaw, C.E.5    Miller, C.C.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.