메뉴 건너뛰기




Volumn 58, Issue 2, 2005, Pages 277-289

A pilot proteomic study of amyloid precursor interactors in Alzheimer's disease

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; AMYLOID PRECURSOR PROTEIN; BETA ACTIN; BETA TUBULIN; CHAPERONE; CRYSTALLIN; CYCLOPHILIN A; CYTOSKELETON PROTEIN; DYNAMIN; DYNEIN ADENOSINE TRIPHOSPHATASE; FODRIN; GLIAL FIBRILLARY ACIDIC PROTEIN; HEAT SHOCK PROTEIN 90; MYOSIN; NEUROFILAMENT PROTEIN; PHOSPHOGLYCERATE MUTASE; PROTEIN FE65; STRUCTURAL PROTEIN; SYNTAXIN; UBIQUITIN THIOLESTERASE; URACIL DNA GLYCOSYLTRANSFERASE;

EID: 23244456099     PISSN: 03645134     EISSN: None     Source Type: Journal    
DOI: 10.1002/ana.20554     Document Type: Article
Times cited : (61)

References (65)
  • 1
    • 85046833190 scopus 로고    scopus 로고
    • Addendum: Pathways towards and away from Alzheimer's disease
    • Mattson MP. Addendum: pathways towards and away from Alzheimer's disease. Nature 2004;431:107.
    • (2004) Nature , vol.431 , pp. 107
    • Mattson, M.P.1
  • 2
    • 33644498152 scopus 로고    scopus 로고
    • Washington, DC: U.S. Department of Health and Human Services
    • National Institute of Mental Health. Clinical trials: Alzheimer's disease and related disorders. Vol. 2005: Washington, DC: U.S. Department of Health and Human Services, 2005.
    • (2005) Clinical Trials: Alzheimer's Disease and Related Disorders , vol.2005
  • 3
    • 0040434394 scopus 로고    scopus 로고
    • Silver Spring, MD: U.S. Department of Health and Human Services, National Institutes of Health, National Institute on Aging
    • The Alzheimer's Disease Education and Referral (ADEAR) Center. National Institute on Aging progress report on Alzheimer's disease. Vol. 1998. Silver Spring, MD: U.S. Department of Health and Human Services, National Institutes of Health, National Institute on Aging, 1998.
    • (1998) National Institute on Aging Progress Report on Alzheimer's Disease , vol.1998
  • 4
    • 0037174618 scopus 로고    scopus 로고
    • Alzheimer's disease is a synaptic failure
    • Selkoe DJ. Alzheimer's disease is a synaptic failure. Science 2002;298:789-791.
    • (2002) Science , vol.298 , pp. 789-791
    • Selkoe, D.J.1
  • 5
    • 0038056193 scopus 로고    scopus 로고
    • Proteolytic processing of the amyloid-beta protein precursor of Alzheimer's disease
    • Nunan J, Small DH. Proteolytic processing of the amyloid-beta protein precursor of Alzheimer's disease. Essays Biochem 2002; 38:37-49.
    • (2002) Essays Biochem , vol.38 , pp. 37-49
    • Nunan, J.1    Small, D.H.2
  • 6
    • 0034107524 scopus 로고    scopus 로고
    • A second cytotoxic proteolytic peptide derived from amyloid beta-protein precursor
    • Lu DC, Rabizadeh S, Chandra S, et al. A second cytotoxic proteolytic peptide derived from amyloid beta-protein precursor. Nat Med 2000;6:397-404.
    • (2000) Nat Med , vol.6 , pp. 397-404
    • Lu, D.C.1    Rabizadeh, S.2    Chandra, S.3
  • 7
    • 0036064748 scopus 로고    scopus 로고
    • Caspase cleavage of members of the amyloid precursor family of proteins
    • Galvan V, Chen S, Lu D, et al. Caspase cleavage of members of the amyloid precursor family of proteins. J Neurochem 2002; 82:283-294.
    • (2002) J Neurochem , vol.82 , pp. 283-294
    • Galvan, V.1    Chen, S.2    Lu, D.3
  • 8
    • 0033597884 scopus 로고    scopus 로고
    • Alternative, non-secretase processing of Alzheimer's beta-amyloid precursor protein during apoptosis by caspase-6 and -8
    • Pellegrini L, Passer BJ, Tabaton M, et al. Alternative, non-secretase processing of Alzheimer's beta-amyloid precursor protein during apoptosis by caspase-6 and -8. J Biol Chem 1999; 274:21011-21016.
    • (1999) J Biol Chem , vol.274 , pp. 21011-21016
    • Pellegrini, L.1    Passer, B.J.2    Tabaton, M.3
  • 9
    • 0033605252 scopus 로고    scopus 로고
    • Proteolytic processing of the Alzheimer's disease amyloid precursor protein within its cytoplasmic domain by caspase-like proteases
    • Weidemann A, Paliga K, Durrwang U, et al. Proteolytic processing of the Alzheimer's disease amyloid precursor protein within its cytoplasmic domain by caspase-like proteases. J Biol Chem 1999;274:5823-5829.
    • (1999) J Biol Chem , vol.274 , pp. 5823-5829
    • Weidemann, A.1    Paliga, K.2    Durrwang, U.3
  • 10
    • 0032402095 scopus 로고    scopus 로고
    • Alzheimer amyloid protein precursor in the rat hippocampus: Transport and processing through the perforant path
    • Buxbaum JD, Thinakaran G, Koliatsos V, et al. Alzheimer amyloid protein precursor in the rat hippocampus: transport and processing through the perforant path. J Neurosci 1998;18: 9629-9637.
    • (1998) J Neurosci , vol.18 , pp. 9629-9637
    • Buxbaum, J.D.1    Thinakaran, G.2    Koliatsos, V.3
  • 11
    • 0035829720 scopus 로고    scopus 로고
    • Disruption of axonal transport and neuronal viability by amyloid precursor protein mutations in Drosophila
    • Gunawardena S, Goldstein LS. Disruption of axonal transport and neuronal viability by amyloid precursor protein mutations in Drosophila. Neuron 2001;32:389-401.
    • (2001) Neuron , vol.32 , pp. 389-401
    • Gunawardena, S.1    Goldstein, L.S.2
  • 12
    • 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 JF, et al. Kinesin-mediated axonal transport of a membrane compartment containing beta-secretase and presenilin-1 requires APP. Nature 2001;414:643-648.
    • (2001) Nature , vol.414 , pp. 643-648
    • Kamal, A.1    Almenar-Queralt, A.2    LeBlanc, J.F.3
  • 13
    • 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 SL, Ikin AF, Buxbaum JD, Greengard P. The amyloid precursor protein and its regulatory protein, FE65, in growth cones and synapses in vitro and in vivo. J Neurosci 2003;23: 5407-5415.
    • (2003) J Neurosci , vol.23 , pp. 5407-5415
    • Sabo, S.L.1    Ikin, A.F.2    Buxbaum, J.D.3    Greengard, P.4
  • 14
    • 0035954426 scopus 로고    scopus 로고
    • The Alzheimer amyloid precursor protein (APP) and FE65, an APP-binding protein, regulate cell movement
    • Sabo SL, Ikin AF, Buxbaum JD, Greengard P. The Alzheimer amyloid precursor protein (APP) and FE65, an APP-binding protein, regulate cell movement. J Cell Biol 2001;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
  • 15
    • 0344672942 scopus 로고    scopus 로고
    • APP processing and synaptic function
    • Kamenetz F, Tomita T, Hsieh H, et al. APP processing and synaptic function. Neuron 2003;37:925-937.
    • (2003) Neuron , vol.37 , pp. 925-937
    • Kamenetz, F.1    Tomita, T.2    Hsieh, H.3
  • 16
    • 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, et al. Interaction of Alzheimer's beta-amyloid precursor family proteins with scaffold proteins of the JNK signaling cascade. J Biol Chem 2002;277: 20070-20078.
    • (2002) J Biol Chem , vol.277 , pp. 20070-20078
    • Taru, H.1    Iijima, K.2    Hase, M.3
  • 17
    • 0036462590 scopus 로고    scopus 로고
    • Jun NH2-terminal kinase (JNK) interacting protein 1 (JIP1) binds the cytoplasmic domain of the Alzheimer's beta-amyloid precursor protein (APP)
    • Scheinfeld MH, Roncarati R, Vito P, et al. Jun NH2-terminal kinase (JNK) interacting protein 1 (JIP1) binds the cytoplasmic domain of the Alzheimer's beta-amyloid precursor protein (APP). J Biol Chem 2002;277:3767-3775.
    • (2002) J Biol Chem , vol.277 , pp. 3767-3775
    • Scheinfeld, M.H.1    Roncarati, R.2    Vito, P.3
  • 18
    • 0033198295 scopus 로고    scopus 로고
    • Disabled-1 binds to the cytoplasmic domain of amyloid precursor-like protein 1
    • Homayouni R, Rice DS, Sheldon M, Curran T. Disabled-1 binds to the cytoplasmic domain of amyloid precursor-like protein 1. J Neurosci 1999;19:7507-7515.
    • (1999) J Neurosci , vol.19 , pp. 7507-7515
    • Homayouni, R.1    Rice, D.S.2    Sheldon, M.3    Curran, T.4
  • 19
    • 0035449943 scopus 로고    scopus 로고
    • C-Jun N-terminal kinase (JNK)-interacting protein-1b/islet-brain-I scaffolds Alzheimer's amyloid precursor protein with JNK
    • Matsuda S, Yasukawa T, Homma Y, et al. c-Jun N-terminal kinase (JNK)-interacting protein-1b/islet-brain-I scaffolds Alzheimer's amyloid precursor protein with JNK. J Neurosci 2001; 21:6597-6607.
    • (2001) J Neurosci , vol.21 , pp. 6597-6607
    • Matsuda, S.1    Yasukawa, T.2    Homma, Y.3
  • 20
    • 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, Zamhrano N, Minopoli G, et al. 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 1995;270:30853-30856.
    • (1995) J Biol Chem , vol.270 , pp. 30853-30856
    • Fiore, F.1    Zamhrano, N.2    Minopoli, G.3
  • 21
    • 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 JD, Minopoli G, et al. 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 1997;272: 6399-6405.
    • (1997) J Biol Chem , vol.272 , pp. 6399-6405
    • Zambrano, N.1    Buxbaum, J.D.2    Minopoli, G.3
  • 22
    • 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 DM, Miller CC. 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 1996;397:197-200.
    • (1996) FEBS Lett , vol.397 , pp. 197-200
    • McLoughlin, D.M.1    Miller, C.C.2
  • 23
    • 0036759068 scopus 로고    scopus 로고
    • Regulation of APP-dependent transcription complexes by Mint/X11s: Differential functions of Mint isororms
    • Biederer T, Cao X, Sudhof TC, Liu X. Regulation of APP-dependent transcription complexes by Mint/X11s: differential functions of Mint isororms. J Neurosci 2002;22:7340-7351.
    • (2002) J Neurosci , vol.22 , pp. 7340-7351
    • Biederer, T.1    Cao, X.2    Sudhof, T.C.3    Liu, X.4
  • 24
    • 0035656206 scopus 로고    scopus 로고
    • Proteomic analysis of the brain in Alzheimer's disease: Molecular phenotype of a complex disease process
    • Schonberger SJ, Edgar PF, Kydd R, et al. Proteomic analysis of the brain in Alzheimer's disease: molecular phenotype of a complex disease process. Proteomics 2001;1:1519-1528.
    • (2001) Proteomics , vol.1 , pp. 1519-1528
    • Schonberger, S.J.1    Edgar, P.F.2    Kydd, R.3
  • 25
    • 0035663035 scopus 로고    scopus 로고
    • Analysis of the proteomic profiling of brain tissue in Alzheimer's disease
    • Tsuji T, Shimohama S. Analysis of the proteomic profiling of brain tissue in Alzheimer's disease. Dis Markers 2001;17: 247-257.
    • (2001) Dis Markers , vol.17 , pp. 247-257
    • Tsuji, T.1    Shimohama, S.2
  • 26
    • 0034805931 scopus 로고    scopus 로고
    • Deranged expression of molecular chaperones in brains of patients with Alzheimer's disease
    • Yoo BC, Kim SH, Cairns N, et al. Deranged expression of molecular chaperones in brains of patients with Alzheimer's disease. Biochem Biophys Res Commun 2001;280:249-258.
    • (2001) Biochem Biophys Res Commun , vol.280 , pp. 249-258
    • Yoo, B.C.1    Kim, S.H.2    Cairns, N.3
  • 27
    • 0037101889 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part 1: Creatine kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1
    • Castegna A, Aksenov M, Aksenova M, et al. Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part 1: creatine kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1. Free Radic Biol Med 2002;33:562-571.
    • (2002) Free Radic Biol Med , vol.33 , pp. 562-571
    • Castegna, A.1    Aksenov, M.2    Aksenova, M.3
  • 28
    • 0026500019 scopus 로고
    • Amyloid beta-protein precursor deposition in rat hippocampus lesioned by ibotenic acid injection
    • Nakamura Y, Takeda M, Niigawa H, et al. Amyloid beta-protein precursor deposition in rat hippocampus lesioned by ibotenic acid injection. Neurosci Lett 1992;136:95-98.
    • (1992) Neurosci Lett , vol.136 , pp. 95-98
    • Nakamura, Y.1    Takeda, M.2    Niigawa, H.3
  • 29
    • 0027212769 scopus 로고
    • Identification and transport of full-length amyloid precursor proteins in rat peripheral nervous system
    • Sisodia SS, Koo EH, Hoffman PN, et al. Identification and transport of full-length amyloid precursor proteins in rat peripheral nervous system. J Neurosci 1993;13:3136-3142.
    • (1993) J Neurosci , vol.13 , pp. 3136-3142
    • Sisodia, S.S.1    Koo, E.H.2    Hoffman, P.N.3
  • 30
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins DN, Pappin DJ, Creasy DM, Cottrell JS. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999;20: 3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 31
    • 0037067655 scopus 로고    scopus 로고
    • Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-kappaB and beta-amyloid precursor protein
    • Baek SH, Ohgi KA, Rose DW, et al. Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-kappaB and beta-amyloid precursor protein. Cell 2002; 110:55-67.
    • (2002) Cell , vol.110 , pp. 55-67
    • Baek, S.H.1    Ohgi, K.A.2    Rose, D.W.3
  • 32
    • 0035816661 scopus 로고    scopus 로고
    • A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60
    • Cao X, Sudhof TC. A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60. Science 2001;293:115-120.
    • (2001) Science , vol.293 , pp. 115-120
    • Cao, X.1    Sudhof, T.C.2
  • 33
    • 0035955693 scopus 로고    scopus 로고
    • The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner
    • Kimberly WT, Zheng JB, Guenette SY, Selkoe DJ. 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 2001;276:40288-40292.
    • (2001) J Biol Chem , vol.276 , pp. 40288-40292
    • Kimberly, W.T.1    Zheng, J.B.2    Guenette, S.Y.3    Selkoe, D.J.4
  • 34
    • 4844230325 scopus 로고    scopus 로고
    • 14-3-3 Proteins and zeta isoform containing neurofibrillary tangles in patients with Alzheimer's disease
    • Umahara T, Uchihara T, Tsuchiya K, et al. 14-3-3 proteins and zeta isoform containing neurofibrillary tangles in patients with Alzheimer's disease. Acta Neuropathol (Berl) 2004;108: 279-286.
    • (2004) Acta Neuropathol (Berl) , vol.108 , pp. 279-286
    • Umahara, T.1    Uchihara, T.2    Tsuchiya, K.3
  • 35
    • 1242337344 scopus 로고    scopus 로고
    • Zeta 14-3-3 protein favours the formation of human tau fibrillar polymers
    • Hernandez F, Cuadros R, Avila J. Zeta 14-3-3 protein favours the formation of human tau fibrillar polymers. Neurosci Lett 2004;357:143-146.
    • (2004) Neurosci Lett , vol.357 , pp. 143-146
    • Hernandez, F.1    Cuadros, R.2    Avila, J.3
  • 36
    • 0034682667 scopus 로고    scopus 로고
    • 14-3-3Zeta is an effector of tau protein phosphorylation
    • Hashiguchi M, Sobue K, Paudel HK. 14-3-3zeta is an effector of tau protein phosphorylation. J Biol Chem 2000;275: 25247-25254.
    • (2000) J Biol Chem , vol.275 , pp. 25247-25254
    • Hashiguchi, M.1    Sobue, K.2    Paudel, H.K.3
  • 37
    • 0036638443 scopus 로고    scopus 로고
    • Apolipoprotein e and other cerebrospinal fluid proteins differentiate ante mortem variant Creutzfeldt-Jakob disease from ante mortem sporadic Creutzfeldt-Jakob disease
    • Choe LH, Green A, Knight RS, et al. Apolipoprotein E and other cerebrospinal fluid proteins differentiate ante mortem variant Creutzfeldt-Jakob disease from ante mortem sporadic Creutzfeldt-Jakob disease. Electrophoresis 2002;23:2242-2246.
    • (2002) Electrophoresis , vol.23 , pp. 2242-2246
    • Choe, L.H.1    Green, A.2    Knight, R.S.3
  • 38
    • 0033584258 scopus 로고    scopus 로고
    • The molecular chaperone alphaB-crystallin enhances amyloid beta neurotoxicity
    • Stege GJ, Renkawek K, Overkamp PS, et al. The molecular chaperone alphaB-crystallin enhances amyloid beta neurotoxicity. Biochem Biophys Res Commun 1999;262:152-156.
    • (1999) Biochem Biophys Res Commun , vol.262 , pp. 152-156
    • Stege, G.J.1    Renkawek, K.2    Overkamp, P.S.3
  • 39
    • 0034602513 scopus 로고    scopus 로고
    • Interaction between beta-amyloid and lens alphaB-crystallin
    • Liang JJ. Interaction between beta-amyloid and lens alphaB-crystallin. FEBS Lett 2000;484:98-101.
    • (2000) FEBS Lett , vol.484 , pp. 98-101
    • Liang, J.J.1
  • 40
    • 0037047163 scopus 로고    scopus 로고
    • Interaction of intracellular beta amyloid peptide with chaperone proteins
    • Fonte V, Kapulkin V, Taft A, et al. Interaction of intracellular beta amyloid peptide with chaperone proteins. Proc Natl Acad Sci U S A 2002;99:9439-9444.
    • (2002) Proc Natl Acad Sci U S a , vol.99 , pp. 9439-9444
    • Fonte, V.1    Kapulkin, V.2    Taft, A.3
  • 41
    • 0037405291 scopus 로고    scopus 로고
    • Gene expression analysis in a transgenic Caenorhabditis elegans Alzheimer's disease model
    • Link CD, Taft A, Kapulkin V, et al. Gene expression analysis in a transgenic Caenorhabditis elegans Alzheimer's disease model. Neurobiol Aging 2003;24:397-413.
    • (2003) Neurobiol Aging , vol.24 , pp. 397-413
    • Link, C.D.1    Taft, A.2    Kapulkin, V.3
  • 42
    • 13044287361 scopus 로고    scopus 로고
    • Plaque-independent disruption of neural circuits in Alzheimer's disease mouse models
    • Hsia AY, Masliah E, McConlogue L, et al. Plaque-independent disruption of neural circuits in Alzheimer's disease mouse models. Proc Natl Acad Sci U S A 1999;96:3228-3233.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 3228-3233
    • Hsia, A.Y.1    Masliah, E.2    McConlogue, L.3
  • 43
    • 0034213718 scopus 로고    scopus 로고
    • High-level neuronal expression of abeta 1-42 in wild-type human amyloid protein precursor transgenic mice: Synaptotoxicity without plaque formation
    • Mucke L, Masliah E, Yu GQ, et al. High-level neuronal expression of abeta 1-42 in wild-type human amyloid protein precursor transgenic mice: synaptotoxicity without plaque formation. J Neurosci 2000;20:4050-4058.
    • (2000) J Neurosci , vol.20 , pp. 4050-4058
    • Mucke, L.1    Masliah, E.2    Yu, G.Q.3
  • 44
    • 2942642590 scopus 로고    scopus 로고
    • Automatic and quantitative measurement of protein-protein colocalization in live cells
    • Costes SV, Daelemans D, Cho EH, et al. Automatic and quantitative measurement of protein-protein colocalization in live cells. Biophys J 2004;86:3993-4003.
    • (2004) Biophys J , vol.86 , pp. 3993-4003
    • Costes, S.V.1    Daelemans, D.2    Cho, E.H.3
  • 45
    • 0345803941 scopus 로고    scopus 로고
    • Inhibition of receptor-mediated endocytosis demonstrates generation of amyloid beta-protein at the cell surface
    • Chyung JH, Selkoe DJ. Inhibition of receptor-mediated endocytosis demonstrates generation of amyloid beta-protein at the cell surface. J Biol Chem 2003;278:51035-51043.
    • (2003) J Biol Chem , vol.278 , pp. 51035-51043
    • Chyung, J.H.1    Selkoe, D.J.2
  • 46
    • 0037421206 scopus 로고    scopus 로고
    • Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts
    • Ehehalt R, Keller P, Haass C, et al. Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts. J Cell Biol 2003;160:113-123.
    • (2003) J Cell Biol , vol.160 , pp. 113-123
    • Ehehalt, R.1    Keller, P.2    Haass, C.3
  • 47
    • 0033571721 scopus 로고    scopus 로고
    • Amyloid precursor protein, although partially detergent-insoluble in mouse cerebral cortex, behaves as an atypical lipid raft protein
    • Parkin ET, Turner AJ, Hooper NM. Amyloid precursor protein, although partially detergent-insoluble in mouse cerebral cortex, behaves as an atypical lipid raft protein. Biochem J 1999;344(pt 1):23-30.
    • (1999) Biochem J , vol.344 , Issue.PART 1 , pp. 23-30
    • Parkin, E.T.1    Turner, A.J.2    Hooper, N.M.3
  • 48
    • 0036674082 scopus 로고    scopus 로고
    • Lipid rafts play an important role in a beta biogenesis by regulating the beta-secretase pathway
    • Tun H, Marlow L, Pinnix I, et al. Lipid rafts play an important role in A beta biogenesis by regulating the beta-secretase pathway. J Mol Neurosci 2002;19:31-35.
    • (2002) J Mol Neurosci , vol.19 , pp. 31-35
    • Tun, H.1    Marlow, L.2    Pinnix, I.3
  • 49
    • 0842269066 scopus 로고    scopus 로고
    • Myosin-dependent transport in neurons
    • Bridgman PC. Myosin-dependent transport in neurons. J Neurobiol 2004;58:164-174.
    • (2004) J Neurobiol , vol.58 , pp. 164-174
    • Bridgman, P.C.1
  • 50
    • 0035510709 scopus 로고    scopus 로고
    • Kinesin, dynein and neurofilament transport
    • Shea TB, Flanagan LA. Kinesin, dynein and neurofilament transport. Trends Neurosci 2001;24:644-648.
    • (2001) Trends Neurosci , vol.24 , pp. 644-648
    • Shea, T.B.1    Flanagan, L.A.2
  • 51
    • 0037178838 scopus 로고    scopus 로고
    • Synergistic effects of Munc18a and X11 proteins on amyloid precursor protein metabolism
    • Ho CS, Marinescu V, Steinhilb ML, et al. Synergistic effects of Munc18a and X11 proteins on amyloid precursor protein metabolism. J Biol Chem 2002;277:27021-27028.
    • (2002) J Biol Chem , vol.277 , pp. 27021-27028
    • Ho, C.S.1    Marinescu, V.2    Steinhilb, M.L.3
  • 52
    • 0034086882 scopus 로고    scopus 로고
    • Release of kinesin from vesicles by hsc70 and regulation of fast axonal transport
    • Tsai MY, Morfini G, Szebenyi G, Brady ST. Release of kinesin from vesicles by hsc70 and regulation of fast axonal transport. Mol Biol Cell 2000;11:2161-2173.
    • (2000) Mol Biol Cell , vol.11 , pp. 2161-2173
    • Tsai, M.Y.1    Morfini, G.2    Szebenyi, G.3    Brady, S.T.4
  • 53
    • 0037195182 scopus 로고    scopus 로고
    • Impaired recycling of synaptic vesicles after acute perturbation of the presynaptic actin cytoskeleton
    • Shupliakov O, Bloom O, Gustafsson JS, et al. Impaired recycling of synaptic vesicles after acute perturbation of the presynaptic actin cytoskeleton. Proc Natl Acad Sci U S A 2002;99: 14476-14481.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 14476-14481
    • Shupliakov, O.1    Bloom, O.2    Gustafsson, J.S.3
  • 54
    • 0034650872 scopus 로고    scopus 로고
    • 14-3-3 Isotypes facilitate coupling of protein kinase C-zeta to Raf-1: Negative regulation by 14-3-3 phosphorylation
    • Van Der Hoeven PC, Van Der Wal JC, Ruurs P, et al. 14-3-3 isotypes facilitate coupling of protein kinase C-zeta to Raf-1: negative regulation by 14-3-3 phosphorylation. Biochem J 2000;345(pt 2):297-306.
    • (2000) Biochem J , vol.345 , Issue.PART 2 , pp. 297-306
    • Van Der Hoeven, P.C.1    Van Der Wal, J.C.2    Ruurs, P.3
  • 55
    • 0032585827 scopus 로고    scopus 로고
    • Increased levels of 14-3-3 gamma and epsilon proteins in brain of patients with Alzheimer's disease and Down syndrome
    • Fountoulakis M, Cairns N, Lubec G. Increased levels of 14-3-3 gamma and epsilon proteins in brain of patients with Alzheimer's disease and Down syndrome. J Neural Transm Suppl 1999;57:323-335.
    • (1999) J Neural Transm Suppl , vol.57 , pp. 323-335
    • Fountoulakis, M.1    Cairns, N.2    Lubec, G.3
  • 56
    • 0036532117 scopus 로고    scopus 로고
    • Ion transport proteins anchor and regulate the cytoskeleton
    • Denker SP, Barber DL. Ion transport proteins anchor and regulate the cytoskeleton. Curr Opin Cell Biol 2002;14:214-220.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 214-220
    • Denker, S.P.1    Barber, D.L.2
  • 57
    • 0036007118 scopus 로고    scopus 로고
    • Drosophila nicastrin is essential for the intramembranous cleavage of notch
    • Lopez-Schier H, St Johnston D. Drosophila nicastrin is essential for the intramembranous cleavage of notch. Dev Cell 2002;2: 79-89.
    • (2002) Dev Cell , vol.2 , pp. 79-89
    • Lopez-Schier, H.1    St. Johnston, D.2
  • 58
    • 0034982557 scopus 로고    scopus 로고
    • Calreticulin functions as a molecular chaperone for the beta-amyloid precursor protein
    • Johnson RJ, Xiao G, Shanmugaratnam J, Fine RE. Calreticulin functions as a molecular chaperone for the beta-amyloid precursor protein. Neurobiol Aging 2001;22:387-395.
    • (2001) Neurobiol Aging , vol.22 , pp. 387-395
    • Johnson, R.J.1    Xiao, G.2    Shanmugaratnam, J.3    Fine, R.E.4
  • 59
    • 0032475957 scopus 로고    scopus 로고
    • The chaperone BiP/GRP78 binds to amyloid precursor protein and decreases Abeta40 and Abeta42 secretion
    • Yang Y, Turner RS, Gaut JR. The chaperone BiP/GRP78 binds to amyloid precursor protein and decreases Abeta40 and Abeta42 secretion. J Biol Chem 1998;273:25552-25555.
    • (1998) J Biol Chem , vol.273 , pp. 25552-25555
    • Yang, Y.1    Turner, R.S.2    Gaut, J.R.3
  • 60
    • 0025167955 scopus 로고
    • Cardiac alpha-crystallin. III. Involvement during heart ischemia
    • Chiesi M, Longoni S, Limbruno U. Cardiac alpha-crystallin. III. Involvement during heart ischemia. Mol Cell Biochem 1990;97:129-136.
    • (1990) Mol Cell Biochem , vol.97 , pp. 129-136
    • Chiesi, M.1    Longoni, S.2    Limbruno, U.3
  • 61
    • 0035823499 scopus 로고    scopus 로고
    • The molecular chaperone, alpha-crystallin, inhibits amyloid formation by apolipoprotein C-II
    • Hatters DM, Lindner RA, Carver JA, Howlett GJ. The molecular chaperone, alpha-crystallin, inhibits amyloid formation by apolipoprotein C-II. J Biol Chem 2001;276:33755-33761.
    • (2001) J Biol Chem , vol.276 , pp. 33755-33761
    • Hatters, D.M.1    Lindner, R.A.2    Carver, J.A.3    Howlett, G.J.4
  • 62
    • 0036239489 scopus 로고    scopus 로고
    • Inhibition of proteasomes induces accumulation, phosphorylation, and recruitment of HSP27 and alphaB-crystallin to aggresomes
    • Ito H, Kamei K, Iwamoto I, et al. Inhibition of proteasomes induces accumulation, phosphorylation, and recruitment of HSP27 and alphaB-crystallin to aggresomes. J Biochem (Tokyo) 2002;131:593-603.
    • (2002) J Biochem (Tokyo) , vol.131 , pp. 593-603
    • Ito, H.1    Kamei, K.2    Iwamoto, I.3
  • 63
    • 0033608219 scopus 로고    scopus 로고
    • Proteasome inhibitors induce the association of Alzheimer's amyloid precursor protein with Hsc7.3
    • Kouchi Z, Sorimachi H, Suzuki K, Ishiura S. Proteasome inhibitors induce the association of Alzheimer's amyloid precursor protein with Hsc7.3. Biochem Biophys Res Commun 1999;254: 804-810.
    • (1999) Biochem Biophys Res Commun , vol.254 , pp. 804-810
    • Kouchi, Z.1    Sorimachi, H.2    Suzuki, K.3    Ishiura, S.4
  • 64
    • 0141638441 scopus 로고    scopus 로고
    • Essential role of E2-25K/ Hip-2 in mediating amyloid-beta neurotoxicity
    • Song S, Kim SY, Hong YM, et al. Essential role of E2-25K/ Hip-2 in mediating amyloid-beta neurotoxicity. Mol Cell 2003; 12:553-563.
    • (2003) Mol Cell , vol.12 , pp. 553-563
    • Song, S.1    Kim, S.Y.2    Hong, Y.M.3
  • 65
    • 0036606540 scopus 로고    scopus 로고
    • ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats
    • Nishitoh H, Matsuzawa A, Tobiume K, et al. ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev 2002;16:1345-1355.
    • (2002) Genes Dev , vol.16 , pp. 1345-1355
    • Nishitoh, H.1    Matsuzawa, A.2    Tobiume, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.