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Volumn 4, Issue NOVEMBER2015, 2015, Pages

APP and APLP2 interact with the synaptic release machinery and facilitate transmitter release at hippocampal synapses

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PRECURSOR PROTEIN; AMYLOID PRECURSOR PROTEIN LIKE PROTEIN 2; UNCLASSIFIED DRUG; AGENTS INTERACTING WITH TRANSMITTER, HORMONE OR DRUG RECEPTORS; APLP2 PROTEIN, MOUSE; PROTEIN BINDING;

EID: 84957900258     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.09743     Document Type: Article
Times cited : (71)

References (103)
  • 2
    • 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, Koo EH, Glass CK, Rosenfeld MG. 2002. Exchange of n-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-kappaB and beta-amyloid precursor protein. Cell 110:55-67. doi: 10.1016/S0092-8674(02)00809-7.
    • (2002) Cell , vol.110 , pp. 55-67
    • Baek, S.H.1    Ohgi, K.A.2    Rose, D.W.3    Koo, E.H.4    Glass, C.K.5    Rosenfeld, M.G.6
  • 3
    • 79952952445 scopus 로고    scopus 로고
    • The intracellular threonine of amyloid precursor protein that is essential for docking of Pin1 is dispensable for developmental function
    • Barbagallo APM, Wang Z, Zheng H, D’Adamio L, Ginsberg S. 2011a. The intracellular threonine of amyloid precursor protein that is essential for docking of Pin1 is dispensable for developmental function. PLoS ONE 6:e18006. doi: 10.1371/journal.pone.0018006.
    • (2011) Plos ONE , vol.6
    • Barbagallo, A.1    Wang, Z.2    Zheng, H.3    D’Adamio, L.4    Ginsberg, S.5
  • 4
    • 79952903577 scopus 로고    scopus 로고
    • A single tyrosine residue in the amyloid precursor protein intracellular domain is essential for developmental function
    • Barbagallo APM, Wang Z, Zheng H, D’Adamio L. 2011b. A single tyrosine residue in the amyloid precursor protein intracellular domain is essential for developmental function. Journal of Biological Chemistry 286:8717-8721. doi: 10.1074/jbc.C111.219873.
    • (2011) Journal of Biological Chemistry , vol.286 , pp. 8717-8721
    • Barbagallo, A.1    Wang, Z.2    Zheng, H.3    D’Adamio, L.4
  • 6
    • 0035816661 scopus 로고    scopus 로고
    • A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60
    • Cao X, Südhof TC. 2001. A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60. Science 293:115-120. doi: 10.1126/science.1058783.
    • (2001) Science , vol.293 , pp. 115-120
    • Cao, X.1    Südhof, T.C.2
  • 9
    • 0034839287 scopus 로고    scopus 로고
    • The amyloid precursor protein (APP)- cytoplasmic fragment generated by g-secretase is rapidly degraded but distributes partially in a nuclear fraction of neurones in culture
    • Cupers P, Orlans I, Craessaerts K, Annaert W, De Strooper B. 2001. The amyloid precursor protein (aPP)- cytoplasmic fragment generated by g-secretase is rapidly degraded but distributes partially in a nuclear fraction of neurones in culture. Journal of Neurochemistry 78:1168-1178. doi: 10.1046/j.1471-4159.2001.00516.x.
    • (2001) Journal of Neurochemistry , vol.78 , pp. 1168-1178
    • Cupers, P.1    Orlans, I.2    Craessaerts, K.3    Annaert, W.4    De Strooper, B.5
  • 10
    • 8544231403 scopus 로고    scopus 로고
    • Highly efficient small interfering RNA delivery to primary mammalian neurons induces MicroRNA-like effects before mRNA degradation
    • Davidson TJ, Harel S, Arboleda VA, Prunell GF, Shelanski ML, Greene LA, Troy CM. 2004. Highly efficient small interfering RNA delivery to primary mammalian neurons induces MicroRNA-like effects before mRNA degradation. The Journal of Neuroscience 24:10040-10046. doi: 10.1523/JNEUROSCI.3643-04.2004.
    • (2004) The Journal of Neuroscience , vol.24 , pp. 10040-10046
    • Davidson, T.J.1    Harel, S.2    Arboleda, V.A.3    Prunell, G.F.4    Shelanski, M.L.5    Greene, L.A.6    Troy, C.M.7
  • 12
    • 0037431082 scopus 로고    scopus 로고
    • Aph-1, pen-2, and nicastrin with presenilin generate an active g-secretase complex
    • De Strooper B. 2003. Aph-1, pen-2, and nicastrin with presenilin generate an active g-secretase complex. Neuron 38:9-12. doi: 10.1016/S0896-6273(03)00205-8.
    • (2003) Neuron , vol.38 , pp. 9-12
    • De Strooper, B.1
  • 13
    • 33947201115 scopus 로고    scopus 로고
    • Loss-of-function presenilin mutations in alzheimer disease. Talking point on the role of presenilin mutations in alzheimer disease
    • De Strooper B. 2007. Loss-of-function presenilin mutations in alzheimer disease. talking point on the role of presenilin mutations in alzheimer disease. EMBO Reports 8:141-146. doi: 10.1038/sj.embor.7400897.
    • (2007) EMBO Reports , vol.8 , pp. 141-146
    • De Strooper, B.1
  • 14
    • 76849086405 scopus 로고    scopus 로고
    • The secretases: Enzymes with therapeutic potential in alzheimer disease. Nature Reviews
    • De Strooper B, Vassar R, Golde T. 2010. The secretases: enzymes with therapeutic potential in alzheimer disease. Nature Reviews. Neurology 6:99-107. doi: 10.1038/nrneurol.2009.218.
    • (2010) Neurology , vol.6 , pp. 99-107
    • De Strooper, B.1    Vassar, R.2    Golde, T.3
  • 15
    • 84864432337 scopus 로고    scopus 로고
    • Alzheimer’s disease: A protective mutation
    • De Strooper B, Voet T. 2012. Alzheimer’s disease: a protective mutation. Nature 488:38-39. doi: 10.1038/488038a.
    • (2012) Nature , vol.488 , pp. 38-39
    • De Strooper, B.1    Voet, T.2
  • 16
    • 84907478709 scopus 로고    scopus 로고
    • APP is cleaved by Bace1 in pre-synaptic vesicles and establishes a pre-synaptic interactome, via its intracellular domain, with molecular complexes that regulate pre-synaptic vesicles functions
    • Del Prete D, Lombino F, Liu X, D’Adamio L. 2014. APP is cleaved by Bace1 in pre-synaptic vesicles and establishes a pre-synaptic interactome, via its intracellular domain, with molecular complexes that regulate pre-synaptic vesicles functions. PloS One 9:e108576. doi: 10.1371/journal.pone.0108576.
    • (2014) Plos One , vol.9
    • Del Prete, D.1    Lombino, F.2    Liu, X.3    D’Adamio, L.4
  • 17
    • 84856958510 scopus 로고    scopus 로고
    • Amyloid beta peptide 1-42 disturbs intracellular calcium homeostasis through activation of GluN2B-containing n-methyl-d-aspartate receptors in cortical cultures
    • Ferreira IL, Bajouco LM, Mota SI, Auberson YP, Oliveira CR, Rego AC. 2012. Amyloid beta peptide 1-42 disturbs intracellular calcium homeostasis through activation of GluN2B-containing n-methyl-d-aspartate receptors in cortical cultures. Cell Calcium 51:95-106. doi: 10.1016/j.ceca.2011.11.008.
    • (2012) Cell Calcium , vol.51 , pp. 95-106
    • Ferreira, I.L.1    Bajouco, L.M.2    Mota, S.I.3    Auberson, Y.P.4    Oliveira, C.R.5    Rego, A.C.6
  • 21
    • 52049112089 scopus 로고    scopus 로고
    • Evidence that the amyloid beta precursor protein-intracellular domain lowers the stress threshold of neurons and has a "regulated" transcriptional role
    • Giliberto L, Zhou D, Weldon R, Tamagno E, De Luca P, Tabaton M, D’Adamio L. 2008. Evidence that the amyloid beta precursor protein-intracellular domain lowers the stress threshold of neurons and has a "regulated" transcriptional role. Molecular Neurodegeneration 3:12. doi: 10.1186/1750-1326-3-12.
    • (2008) Molecular Neurodegeneration , vol.3 , pp. 12
    • Giliberto, L.1    Zhou, D.2    Weldon, R.3    Tamagno, E.4    De Luca, P.5    Tabaton, M.6    D’Adamio, L.7
  • 22
    • 77955408755 scopus 로고    scopus 로고
    • Transgenic expression of the amyloid-beta precursor protein-intracellular domain does not induce alzheimer’s disease-like traits in vivo
    • Giliberto L, d’Abramo C, Acker CM, Davies P, D’Adamio L. 2010. Transgenic expression of the amyloid-beta precursor protein-intracellular domain does not induce alzheimer’s disease-like traits in vivo. PloS One 5:e11609. doi: 10.1371/journal.pone.0011609.
    • (2010) Plos One , vol.5
    • Giliberto, L.1    D’Abramo, C.2    Acker, C.M.3    Davies, P.4    D’Adamio, L.5
  • 24
    • 67449084098 scopus 로고    scopus 로고
    • {beta}-amyloid impairs AMPA receptor trafficking and function by reducing Ca2+/calmodulin-dependent protein kinase II synaptic distribution
    • Gu Z, Liu W, Yan Z. 2009. {beta}-amyloid impairs AMPA receptor trafficking and function by reducing Ca2+/calmodulin-dependent protein kinase II synaptic distribution. The Journal of Biological Chemistry 284:10639-10649. doi: 10.1074/jbc.M806508200.
    • (2009) The Journal of Biological Chemistry , vol.284 , pp. 10639-10649
    • Gu, Z.1    Liu, W.2    Yan, Z.3
  • 25
    • 84862953172 scopus 로고    scopus 로고
    • Amyloid precursor protein revisited: Neuron- specific expression and highly stable nature of soluble derivatives
    • Guo Q, Li H, Gaddam SS, Justice NJ, Robertson CS, Zheng H. 2012. Amyloid precursor protein revisited: neuron- specific expression and highly stable nature of soluble derivatives. The Journal of Biological Chemistry 287:2437-2445. doi: 10.1074/jbc.M111.315051.
    • (2012) The Journal of Biological Chemistry , vol.287 , pp. 2437-2445
    • Guo, Q.1    Li, H.2    Gaddam, S.S.3    Justice, N.J.4    Robertson, C.S.5    Zheng, H.6
  • 28
    • 8144230876 scopus 로고    scopus 로고
    • Cortical dysplasia resembling human type 2 lissencephaly in mice lacking all three APP family members
    • Herms J, Anliker B, Heber S, Ring S, Fuhrmann M, Kretzschmar H, Sisodia S, Müller U. 2004. Cortical dysplasia resembling human type 2 lissencephaly in mice lacking all three APP family members. The EMBO Journal 23:4106-4115. doi: 10.1038/sj.emboj.7600390.
    • (2004) The EMBO Journal , vol.23 , pp. 4106-4115
    • Herms, J.1    Anliker, B.2    Heber, S.3    Ring, S.4    Fuhrmann, M.5    Kretzschmar, H.6    Sisodia, S.7    Müller, U.8
  • 30
    • 33845411954 scopus 로고    scopus 로고
    • AMPAR removal underlies Abeta-induced synaptic depression and dendritic spine loss
    • Hsieh H, Boehm J, Sato C, Iwatsubo T, Tomita T, Sisodia S, Malinow R. 2006. AMPAR removal underlies Abeta-induced synaptic depression and dendritic spine loss. Neuron 52:831-843. doi: 10.1016/j.neuron.2006.10.035.
    • (2006) Neuron , vol.52 , pp. 831-843
    • Hsieh, H.1    Boehm, J.2    Sato, C.3    Iwatsubo, T.4    Tomita, T.5    Sisodia, S.6    Malinow, R.7
  • 32
    • 33845324145 scopus 로고    scopus 로고
    • C-terminal fragments of amyloid precursor protein exert neurotoxicity by inducing glycogen synthase kinase-3beta expression
    • Kim HS, Kim EM, Lee JP, Park CH, Kim S, Seo JH, Chang KA, Yu E, Jeong SJ, Chong YH, Suh YH. 2003. C-terminal fragments of amyloid precursor protein exert neurotoxicity by inducing glycogen synthase kinase-3beta expression. FASEB Journal . 17:1951-1953. doi: 10.1096/fj.03-0106fje.
    • (2003) FASEB Journal , vol.17 , pp. 1951-1953
    • Kim, H.S.1    Kim, E.M.2    Lee, J.P.3    Park, C.H.4    Kim, S.5    Seo, J.H.6    Chang, K.A.7    Yu, E.8    Jeong, S.J.9    Chong, Y.H.10    Suh, Y.H.11
  • 33
    • 84864603831 scopus 로고    scopus 로고
    • Interactome of the amyloid precursor protein APP in brain reveals a protein network involved in synaptic vesicle turnover and a close association with synaptotagmin-1
    • Kohli BM, Pflieger D, Mueller LN, Carbonetti G, Aebersold R, Nitsch RM, Konietzko U. 2012. Interactome of the amyloid precursor protein APP in brain reveals a protein network involved in synaptic vesicle turnover and a close association with synaptotagmin-1. Journal of Proteome Research 11:4075-4090. doi: 10.1021/pr300123g.
    • (2012) Journal of Proteome Research , vol.11 , pp. 4075-4090
    • Kohli, B.M.1    Pflieger, D.2    Mueller, L.N.3    Carbonetti, G.4    Aebersold, R.5    Nitsch, R.M.6    Konietzko, U.7
  • 34
    • 84862838270 scopus 로고    scopus 로고
    • The role of APP and APLP for synaptic transmission, plasticity, and network function: Lessons from genetic mouse models
    • Korte M, Herrmann U, Zhang X, Draguhn A. 2012. The role of APP and APLP for synaptic transmission, plasticity, and network function: lessons from genetic mouse models. Experimental Brain Research 217:435-440. doi: 10.1007/s00221-011-2894-6.
    • (2012) Experimental Brain Research , vol.217 , pp. 435-440
    • Korte, M.1    Herrmann, U.2    Zhang, X.3    Draguhn, A.4
  • 36
    • 84919691959 scopus 로고    scopus 로고
    • Amyloid precursor protein knockout diminishes synaptic vesicle proteins at the presynaptic active zone in mouse brain
    • Lassek M, Weingarten J, Acker-Palmer A, Bajjalieh S, Muller U, Volknandt W. 2014. Amyloid precursor protein knockout diminishes synaptic vesicle proteins at the presynaptic active zone in mouse brain. Current Alzheimer Research 11:971-980. doi: 10.2174/1567205011666141107152458.
    • (2014) Current Alzheimer Research , vol.11 , pp. 971-980
    • Lassek, M.1    Weingarten, J.2    Acker-Palmer, A.3    Bajjalieh, S.4    Muller, U.5    Volknandt, W.6
  • 38
    • 67249087641 scopus 로고    scopus 로고
    • Soluble oligomers of amyloid beta protein facilitate hippocampal long-term depression by disrupting neuronal glutamate uptake
    • Li S, Hong S, Shepardson NE, Walsh DM, Shankar GM, Selkoe D. 2009. Soluble oligomers of amyloid beta protein facilitate hippocampal long-term depression by disrupting neuronal glutamate uptake. Neuron 62:788-801. doi: 10.1016/j.neuron.2009.05.012.
    • (2009) Neuron , vol.62 , pp. 788-801
    • Li, S.1    Hong, S.2    Shepardson, N.E.3    Walsh, D.M.4    Shankar, G.M.5    Selkoe, D.6
  • 40
    • 34748897213 scopus 로고    scopus 로고
    • Amyloid precursor protein regulates brain apolipoprotein e and cholesterol metabolism through lipoprotein receptor LRP1
    • Liu Q, Zerbinatti CV, Zhang J, Hoe HS, Wang B, Cole SL, Herz J, Muglia L, Bu G. 2007. Amyloid precursor protein regulates brain apolipoprotein e and cholesterol metabolism through lipoprotein receptor LRP1. Neuron 56:66-78. doi: 10.1016/j.neuron.2007.08.008.
    • (2007) Neuron , vol.56 , pp. 66-78
    • Liu, Q.1    Zerbinatti, C.V.2    Zhang, J.3    Hoe, H.S.4    Wang, B.5    Cole, S.L.6    Herz, J.7    Muglia, L.8    Bu, G.9
  • 43
    • 27744547991 scopus 로고    scopus 로고
    • SET protein (TAF1beta, I2PP2A) is involved in neuronal apoptosis induced by an amyloid precursor protein cytoplasmic subdomain
    • Madeira A, Pommet JM, Prochiantz A, Allinquant B. 2005. SET protein (TAF1beta, I2PP2A) is involved in neuronal apoptosis induced by an amyloid precursor protein cytoplasmic subdomain. FASEB Journal 19:1905-1907. doi: 10.1096/fj.05-3839fje.
    • (2005) FASEB Journal , vol.19 , pp. 1905-1907
    • Madeira, A.1    Pommet, J.M.2    Prochiantz, A.3    Allinquant, B.4
  • 46
    • 52049089901 scopus 로고    scopus 로고
    • BRI2 inhibits amyloid beta-peptide precursor protein processing by interfering with the docking of secretases to the substrate
    • Matsuda S, Giliberto L, Matsuda Y, McGowan EM, D’Adamio L. 2008. BRI2 inhibits amyloid beta-peptide precursor protein processing by interfering with the docking of secretases to the substrate. The Journal of Neuroscience 28:8668-8676. doi: 10.1523/JNEUROSCI.2094-08.2008.
    • (2008) The Journal of Neuroscience , vol.28 , pp. 8668-8676
    • Matsuda, S.1    Giliberto, L.2    Matsuda, Y.3    McGowan, E.M.4    D’Adamio, L.5
  • 47
    • 67650156458 scopus 로고    scopus 로고
    • BRI3 inhibits amyloid precursor protein processing in a mechanistically distinct manner from its homologue dementia gene BRI2
    • Matsuda S, Matsuda Y, D’Adamio L. 2009. BRI3 inhibits amyloid precursor protein processing in a mechanistically distinct manner from its homologue dementia gene BRI2. The Journal of Biological Chemistry 284:15815-15825. doi: 10.1074/jbc.M109.006403.
    • (2009) The Journal of Biological Chemistry , vol.284 , pp. 15815-15825
    • Matsuda, S.1    Matsuda, Y.2    D’Adamio, L.3
  • 48
    • 79960720320 scopus 로고    scopus 로고
    • Molecular mechanism and physiological functions of clathrin-mediated endocytosis
    • McMahon HT, Boucrot E. 2011. Molecular mechanism and physiological functions of clathrin-mediated endocytosis. Nature Reviews Molecular Cell Biology 12:517-533. doi: 10.1038/nrm3151.
    • (2011) Nature Reviews Molecular Cell Biology , vol.12 , pp. 517-533
    • McMahon, H.T.1    Boucrot, E.2
  • 50
    • 84886641553 scopus 로고    scopus 로고
    • Dysfunctional synapse in alzheimer’s disease - A focus on NMDA receptors
    • Mota SI, Ferreira IL, Rego AC. 2014. Dysfunctional synapse in alzheimer’s disease - a focus on NMDA receptors. Neuropharmacology 76:16-26. doi: 10.1016/j.neuropharm.2013.08.013.
    • (2014) Neuropharmacology , vol.76 , pp. 16-26
    • Mota, S.I.1    Ferreira, I.L.2    Rego, A.C.3
  • 51
    • 84880759156 scopus 로고    scopus 로고
    • Neurotoxicity of amyloid beta-protein: Synaptic and network dysfunction
    • Mucke L, Selkoe DJ. 2012. Neurotoxicity of amyloid beta-protein: synaptic and network dysfunction. Cold Spring Harbor Perspectives in Medicine 2:a006338. doi: 10.1101/cshperspect.a006338.
    • (2012) Cold Spring Harbor Perspectives in Medicine , vol.2
    • Mucke, L.1    Selkoe, D.J.2
  • 54
    • 0006325405 scopus 로고    scopus 로고
    • Alzheimer’s disease: A re-examination of the amyloid hypothesis
    • Neve RL, Robakis NK. 1998. Alzheimer’s disease: a re-examination of the amyloid hypothesis. Trends in Neurosciences 21:15-19. doi: 10.1016/S0166-2236(97)01168-5.
    • (1998) Trends in Neurosciences , vol.21 , pp. 15-19
    • Neve, R.L.1    Robakis, N.K.2
  • 55
    • 60549089207 scopus 로고    scopus 로고
    • APP binds DR6 to trigger axon pruning and neuron death via distinct caspases
    • Nikolaev A, McLaughlin T, O’Leary DD, Tessier-Lavigne M. 2009. APP binds DR6 to trigger axon pruning and neuron death via distinct caspases. Nature 457:981-989. doi: 10.1038/nature07767.
    • (2009) Nature , vol.457 , pp. 981-989
    • Nikolaev, A.1    McLaughlin, T.2    O’Leary, D.D.3    Tessier-Lavigne, M.4
  • 56
    • 78449247854 scopus 로고    scopus 로고
    • Identification of NEEP21 as a beta-amyloid precursor protein- interacting protein in vivo that modulates amyloidogenic processing in vitro
    • Norstrom EM, Zhang C, Tanzi R, Sisodia SS. 2010. Identification of NEEP21 as a beta-amyloid precursor protein- interacting protein in vivo that modulates amyloidogenic processing in vitro. The Journal of Neuroscience 30:15677-15685. doi: 10.1523/JNEUROSCI.4464-10.2010.
    • (2010) The Journal of Neuroscience , vol.30 , pp. 15677-15685
    • Norstrom, E.M.1    Zhang, C.2    Tanzi, R.3    Sisodia, S.S.4
  • 57
    • 33847727050 scopus 로고    scopus 로고
    • Ubiquitin proteasome system (UPS): What can chromatin do for you?
    • O’Connell BC, Harper JW. 2007. Ubiquitin proteasome system (uPS): what can chromatin do for you? Current Opinion in Cell Biology 19:206-214. doi: 10.1016/j.ceb.2007.02.014.
    • (2007) Current Opinion in Cell Biology , vol.19 , pp. 206-214
    • O’Connell, B.C.1    Harper, J.W.2
  • 58
    • 84879966026 scopus 로고    scopus 로고
    • From synaptic spines to nuclear signaling: Nuclear and synaptic actions of the amyloid precursor protein
    • Octave JN, Pierrot N, Ferao Santos S, Nalivaeva NN, Turner AJ. 2013. From synaptic spines to nuclear signaling: nuclear and synaptic actions of the amyloid precursor protein. Journal of Neurochemistry 126:183-190. doi: 10.1111/jnc.12239.
    • (2013) Journal of Neurochemistry , vol.126 , pp. 183-190
    • Octave, J.N.1    Pierrot, N.2    Ferao Santos, S.3    Nalivaeva, N.N.4    Turner, A.J.5
  • 59
    • 0029862137 scopus 로고    scopus 로고
    • Age-dependent neuronal and synaptic degeneration in mice transgenic for the c terminus of the amyloid precursor protein
    • Oster-Granite ML, McPhie DL, Greenan J, Neve RL. 1996. Age-dependent neuronal and synaptic degeneration in mice transgenic for the c terminus of the amyloid precursor protein. The Journal of Neuroscience 16:6732-6741.
    • (1996) The Journal of Neuroscience , vol.16 , pp. 6732-6741
    • Oster-Granite, M.L.1    McPhie, D.L.2    Greenan, J.3    Neve, R.L.4
  • 60
    • 39149117756 scopus 로고    scopus 로고
    • Amyloid beta peptides and glutamatergic synaptic dysregulation
    • Parameshwaran K, Dhanasekaran M, Suppiramaniam V. 2008. Amyloid beta peptides and glutamatergic synaptic dysregulation. Experimental Neurology 210:7-13. doi: 10.1016/j.expneurol.2007.10.008.
    • (2008) Experimental Neurology , vol.210 , pp. 7-13
    • Parameshwaran, K.1    Dhanasekaran, M.2    Suppiramaniam, V.3
  • 63
    • 0033597884 scopus 로고    scopus 로고
    • Alternative, non-secretase processing of alzheimer’s -amyloid precursor protein during apoptosis by caspase-6 and -8
    • Pellegrini L, Passer BJ, Tabaton M, Ganjei JK, D’Adamio L. 1999. Alternative, non-secretase processing of alzheimer’s -amyloid precursor protein during apoptosis by caspase-6 and -8. Journal of Biological Chemistry 274:21011-21016. doi: 10.1074/jbc.274.30.21011.
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 21011-21016
    • Pellegrini, L.1    Passer, B.J.2    Tabaton, M.3    Ganjei, J.K.4    D’Adamio, L.5
  • 66
    • 84870548539 scopus 로고    scopus 로고
    • Amyloid-beta peptide: Dr. Jekyll or mr. Hyde?
    • Puzzo D, Arancio O. 2013. Amyloid-beta peptide: dr. jekyll or mr. hyde? Journal of Alzheimer’s Disease 33:S111-120. doi: 10.3233/JAD-2012-129033.
    • (2013) Journal of Alzheimer’s Disease , vol.33
    • Puzzo, D.1    Arancio, O.2
  • 67
    • 77955089126 scopus 로고    scopus 로고
    • The functional neurophysiology of the amyloid precursor protein (APP) processing pathway
    • Randall AD, Witton J, Booth C, Hynes-Allen A, Brown JT. 2010. The functional neurophysiology of the amyloid precursor protein (aPP) processing pathway. Neuropharmacology 59:243-267. doi: 10.1016/j.neuropharm.2010.02.011.
    • (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
  • 68
    • 84898900454 scopus 로고    scopus 로고
    • Synaptic vesicle recycling: Steps and principles
    • Rizzoli SO. 2014. Synaptic vesicle recycling: steps and principles. The EMBO Journal 33:788-822. doi: 10.1002/embj.201386357.
    • (2014) The EMBO Journal , vol.33 , pp. 788-822
    • Rizzoli, S.O.1
  • 70
    • 78349278012 scopus 로고    scopus 로고
    • Clathrin-mediated endocytosis at the synaptic terminal: Bridging the gap between physiology and molecules
    • Royle SJ, Lagnado L. 2010. Clathrin-mediated endocytosis at the synaptic terminal: bridging the gap between physiology and molecules. Traffic 11:1489-1497. doi: 10.1111/j.1600-0854.2010.01104.x.
    • (2010) Traffic , vol.11 , pp. 1489-1497
    • Royle, S.J.1    Lagnado, L.2
  • 71
    • 0037114010 scopus 로고    scopus 로고
    • Processing of beta-amyloid precursor-like protein-1 and -2 by gamma-secretase regulates transcription
    • Scheinfeld MH, Ghersi E, Laky K, Fowlkes BJ, D’Adamio L. 2002. Processing of beta-amyloid precursor-like protein-1 and -2 by gamma-secretase regulates transcription. The Journal of Biological Chemistry 277:44195-44201. doi: 10.1074/jbc.M208110200.
    • (2002) The Journal of Biological Chemistry , vol.277 , pp. 44195-44201
    • Scheinfeld, M.H.1    Ghersi, E.2    Laky, K.3    Fowlkes, B.J.4    D’Adamio, L.5
  • 72
    • 0037452773 scopus 로고    scopus 로고
    • JNK-interacting protein-1 promotes transcription of a beta protein precursor but not a beta precursor-like proteins, mechanistically different than Fe65
    • Scheinfeld MH, Matsuda S, D’Adamio L. 2003. JNK-interacting protein-1 promotes transcription of a beta protein precursor but not a beta precursor-like proteins, mechanistically different than Fe65. Proceedings of the National Academy of Sciences of the United States of America 100:1729-1734. doi: 10.1073/pnas.0437908100.
    • (2003) Proceedings of the National Academy of Sciences of the United States of America , vol.100 , pp. 1729-1734
    • Scheinfeld, M.H.1    Matsuda, S.2    D’Adamio, L.3
  • 73
    • 0041355557 scopus 로고    scopus 로고
    • Notch and presenilin: Regulated intramembrane proteolysis links development and degeneration
    • Selkoe D, Kopan R. 2003. Notch and presenilin: regulated intramembrane proteolysis links development and degeneration. Annual Review of Neuroscience 26:565-597. doi: 10.1146/annurev.neuro.26.041002.131334.
    • (2003) Annual Review of Neuroscience , vol.26 , pp. 565-597
    • Selkoe, D.1    Kopan, R.2
  • 74
    • 33947314641 scopus 로고    scopus 로고
    • Natural oligomers of the alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway
    • Shankar GM, Bloodgood BL, Townsend M, Walsh DM, Selkoe DJ, Sabatini BL. 2007. Natural oligomers of the alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway. The Journal of Neuroscience 27:2866-2875. doi: 10.1523/JNEUROSCI.4970-06.2007.
    • (2007) The Journal of Neuroscience , vol.27 , pp. 2866-2875
    • Shankar, G.M.1    Bloodgood, B.L.2    Townsend, M.3    Walsh, D.M.4    Selkoe, D.J.5    Sabatini, B.L.6
  • 75
    • 0036548070 scopus 로고    scopus 로고
    • Gamma-secretase, notch, abeta and alzheimer’s disease: Where do the presenilins fit in? Nature Reviews
    • Sisodia SS, St George-Hyslop PH. 2002. Gamma-secretase, notch, abeta and alzheimer’s disease: where do the presenilins fit in? Nature Reviews. Neuroscience 3:281-290. doi: 10.1038/nrn785.
    • (2002) Neuroscience , vol.3 , pp. 281-290
    • Sisodia, S.S.1    St George-Hyslop, P.H.2
  • 76
    • 84876850027 scopus 로고    scopus 로고
    • Pathogenesis of abeta oligomers in synaptic failure
    • Sivanesan S, Tan A, Rajadas J. 2013. Pathogenesis of abeta oligomers in synaptic failure. Current Alzheimer Research 10:316-323. doi: 10.2174/1567205011310030011.
    • (2013) Current Alzheimer Research , vol.10 , pp. 316-323
    • Sivanesan, S.1    Tan, A.2    Rajadas, J.3
  • 78
    • 84863826404 scopus 로고    scopus 로고
    • The presynaptic active zone
    • Südhof TC. 2012. The presynaptic active zone. Neuron 75:11-25. doi: 10.1016/j.neuron.2012.06.012.
    • (2012) Neuron , vol.75 , pp. 11-25
    • Südhof, T.C.1
  • 79
    • 84886998869 scopus 로고    scopus 로고
    • Neurotransmitter release: The last millisecond in the life of a synaptic vesicle
    • Südhof TC. 2013. Neurotransmitter release: the last millisecond in the life of a synaptic vesicle. Neuron 80:675-690. doi: 10.1016/j.neuron.2013.10.022.
    • (2013) Neuron , vol.80 , pp. 675-690
    • Südhof, T.C.1
  • 80
    • 84874380619 scopus 로고    scopus 로고
    • Enhanced sensitivity to ethanol-induced inhibition of LTP in CA1 pyramidal neurons of socially isolated C57BL/6J mice: Role of neurosteroids
    • Talani G, Biggio G, Sanna E. 2011. Enhanced sensitivity to ethanol-induced inhibition of LTP in CA1 pyramidal neurons of socially isolated C57BL/6J mice: role of neurosteroids. Frontiers in Endocrinology 2:56. doi: 10.3389/fendo.2011.00056.
    • (2011) Frontiers in Endocrinology , vol.2 , pp. 56
    • Talani, G.1    Biggio, G.2    Sanna, E.3
  • 81
    • 84872324395 scopus 로고    scopus 로고
    • Caspase-9 mediates synaptic plasticity and memory deficits of danish dementia knock-in mice: Caspase-9 inhibition provides therapeutic protection
    • Tamayev R, Akpan N, Arancio O, Troy CM, D’Adamio L. 2012a. Caspase-9 mediates synaptic plasticity and memory deficits of danish dementia knock-in mice: caspase-9 inhibition provides therapeutic protection. Molecular Neurodegeneration 7:60. doi: 10.1186/1750-1326-7-60.
    • (2012) Molecular Neurodegeneration , vol.7 , pp. 60
    • Tamayev, R.1    Akpan, N.2    Arancio, O.3    Troy, C.M.4    D’Adamio, L.5
  • 82
    • 84862161020 scopus 로고    scopus 로고
    • Inhibition of g-secretase worsens memory deficits in a genetically congruous mouse model of danish dementia
    • Tamayev R, D’Adamio L. 2012b. Inhibition of g-secretase worsens memory deficits in a genetically congruous mouse model of danish dementia. Molecular Neurodegeneration 7:19. doi: 10.1186/1750-1326-7-19.
    • (2012) Molecular Neurodegeneration , vol.7 , pp. 19
    • Tamayev, R.1    D’Adamio, L.2
  • 83
    • 84858123000 scopus 로고    scopus 로고
    • Beta- but not gamma-secretase proteolysis of APP causes synaptic and memory deficits in a mouse model of dementia
    • Tamayev R, Matsuda S, Arancio O, D’Adamio L. 2012c. Beta- but not gamma-secretase proteolysis of APP causes synaptic and memory deficits in a mouse model of dementia. EMBO Molecular Medicine 4:171-179. doi: 10.1002/emmm.201100195.
    • (2012) EMBO Molecular Medicine , vol.4 , pp. 171-179
    • Tamayev, R.1    Matsuda, S.2    Arancio, O.3    D’Adamio, L.4
  • 85
    • 0042634362 scopus 로고    scopus 로고
    • Roles of amyloid precursor protein and its fragments in regulating neural activity, plasticity and memory
    • Turner PR, O’Connor K, Tate WP, Abraham WC. 2003. Roles of amyloid precursor protein and its fragments in regulating neural activity, plasticity and memory. Progress in Neurobiology 70:1-32. doi: 10.1016/S0301-0082(03)00089-3.
    • (2003) Progress in Neurobiology , vol.70 , pp. 1-32
    • Turner, P.R.1    O’Connor, K.2    Tate, W.P.3    Abraham, W.C.4
  • 89
    • 0033600228 scopus 로고    scopus 로고
    • A stop-codon mutation in the BRI gene associated with familial british dementia
    • Vidal R, Frangione B, Rostagno A, Mead S, Révész T, Plant G, Ghiso J. 1999. A stop-codon mutation in the BRI gene associated with familial british dementia. Nature 399:776-781. doi: 10.1038/21637.
    • (1999) Nature , vol.399 , pp. 776-781
    • Vidal, R.1    Frangione, B.2    Rostagno, A.3    Mead, S.4    Révész, T.5    Plant, G.6    Ghiso, J.7
  • 92
    • 5444275067 scopus 로고    scopus 로고
    • The APP intracellular domain forms nuclear multiprotein complexes and regulates the transcription of its own precursor
    • von Rotz RC, Kohli BM, Bosset J, Meier M, Suzuki T, Nitsch RM, Konietzko U. 2004. The APP intracellular domain forms nuclear multiprotein complexes and regulates the transcription of its own precursor. Journal of Cell Science 117:4435-4448. doi: 10.1242/jcs.01323.
    • (2004) Journal of Cell Science , vol.117 , pp. 4435-4448
    • Von Rotz, R.C.1    Kohli, B.M.2    Bosset, J.3    Meier, M.4    Suzuki, T.5    Nitsch, R.M.6    Konietzko, U.7
  • 95
    • 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, Reinhard FBM, Schuckert O, Evin G, Masters CL. 1999. Proteolytic processing of the alzheimer’s disease amyloid precursor protein within its cytoplasmic domain by caspase-like proteases. Journal of Biological Chemistry 274:5823-5829. doi: 10.1074/jbc.274.9.5823.
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 5823-5829
    • Weidemann, A.1    Paliga, K.2    Durrwang, U.3    Reinhard, F.4    Schuckert, O.5    Evin, G.6    Masters, C.L.7
  • 99
    • 84924262484 scopus 로고    scopus 로고
    • Presenilin-1 knockin mice reveal loss-of-function mechanism for familial alzheimer’s disease
    • Xia D, Watanabe H, Wu B, Lee SH, Li Y, Tsvetkov E, Bolshakov VY, Shen J, Kelleher RJ. 2015. Presenilin-1 knockin mice reveal loss-of-function mechanism for familial alzheimer’s disease. Neuron 85:967-981. doi: 10.1016/j.neuron.2015.02.010.
    • (2015) Neuron , vol.85 , pp. 967-981
    • Xia, D.1    Watanabe, H.2    Wu, B.3    Lee, S.H.4    Li, Y.5    Tsvetkov, E.6    Bolshakov, V.Y.7    Shen, J.8    Kelleher, R.J.9
  • 100
    • 67349106087 scopus 로고    scopus 로고
    • Synaptotagmin-1 functions as a Ca2+ sensor for spontaneous release
    • Xu J, Pang ZP, Shin OH, Südhof TC. 2009. Synaptotagmin-1 functions as a Ca2+ sensor for spontaneous release. Nature Neuroscience 12:759-766. doi: 10.1038/nn.2320.
    • (2009) Nature Neuroscience , vol.12 , pp. 759-766
    • Xu, J.1    Pang, Z.P.2    Shin, O.H.3    Südhof, T.C.4
  • 101
    • 20444466355 scopus 로고    scopus 로고
    • Reduced synaptic vesicle density and active zone size in mice lacking amyloid precursor protein (APP) and APP-like protein 2
    • Yang G, Gong YD, Gong K, Jiang WL, Kwon E, Wang P, Zheng H, Zhang XF, Gan WB, Zhao NM. 2005. Reduced synaptic vesicle density and active zone size in mice lacking amyloid precursor protein (aPP) and APP-like protein 2. Neuroscience Letters 384:66-71. doi: 10.1016/j.neulet.2005.04.040.
    • (2005) Neuroscience Letters , vol.384 , pp. 66-71
    • Yang, G.1    Gong, Y.D.2    Gong, K.3    Jiang, W.L.4    Kwon, E.5    Wang, P.6    Zheng, H.7    Zhang, X.F.8    Gan, W.B.9    Zhao, N.M.10
  • 103
    • 0036201201 scopus 로고    scopus 로고
    • Short-term synaptic plasticity
    • Zucker RS, Regehr WG. 2002. Short-term synaptic plasticity. Annual Review of Physiology 64:355-405. doi: 10.1146/annurev.physiol.64.092501.114547.
    • (2002) Annual Review of Physiology , vol.64 , pp. 355-405
    • Zucker, R.S.1    Regehr, W.G.2


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