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Volumn 69, Issue 1, 2011, Pages 22-32

Deconstruction for Reconstruction: The Role of Proteolysis in Neural Plasticity and Disease

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; AMPA RECEPTOR; AMYLOID BETA PROTEIN; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; CYCLIC AMP DEPENDENT PROTEIN KINASE; PARKIN; POLYUBIQUITIN; PROTEASOME; RING FINGER PROTEIN; TAU PROTEIN; UBIQUITIN; UBIQUITIN PROTEIN LIGASE; UBIQUITIN PROTEIN LIGASE E3;

EID: 78650962524     PISSN: 08966273     EISSN: 10974199     Source Type: Journal    
DOI: 10.1016/j.neuron.2010.11.006     Document Type: Review
Times cited : (234)

References (141)
  • 1
    • 33646461282 scopus 로고    scopus 로고
    • Beta-amyloid accumulation impairs multivesicular body sorting by inhibiting the ubiquitin-proteasome system
    • Almeida C.G., Takahashi R.H., Gouras G.K. Beta-amyloid accumulation impairs multivesicular body sorting by inhibiting the ubiquitin-proteasome system. J. Neurosci. 2006, 26:4277-4288.
    • (2006) J. Neurosci. , vol.26 , pp. 4277-4288
    • Almeida, C.G.1    Takahashi, R.H.2    Gouras, G.K.3
  • 2
    • 57649165427 scopus 로고    scopus 로고
    • Regulation of postsynaptic RapGAP SPAR by Polo-like kinase 2 and the SCFbeta-TRCP ubiquitin ligase in hippocampal neurons
    • Ang X.L., Seeburg D.P., Sheng M., Harper J.W. Regulation of postsynaptic RapGAP SPAR by Polo-like kinase 2 and the SCFbeta-TRCP ubiquitin ligase in hippocampal neurons. J. Biol. Chem. 2008, 283:29424-29432.
    • (2008) J. Biol. Chem. , vol.283 , pp. 29424-29432
    • Ang, X.L.1    Seeburg, D.P.2    Sheng, M.3    Harper, J.W.4
  • 3
    • 45149125084 scopus 로고    scopus 로고
    • Protein degradation, as with protein synthesis, is required during not only long-term spatial memory consolidation but also reconsolidation
    • Artinian J., McGauran A.M., De Jaeger X., Mouledous L., Frances B., Roullet P. Protein degradation, as with protein synthesis, is required during not only long-term spatial memory consolidation but also reconsolidation. Eur. J. Neurosci. 2008, 27:3009-3019.
    • (2008) Eur. J. Neurosci. , vol.27 , pp. 3009-3019
    • Artinian, J.1    McGauran, A.M.2    De Jaeger, X.3    Mouledous, L.4    Frances, B.5    Roullet, P.6
  • 4
    • 30344449514 scopus 로고    scopus 로고
    • Synaptic protein synthesis associated with memory is regulated by the RISC pathway in Drosophila
    • Ashraf S.I., McLoon A.L., Sclarsic S.M., Kunes S. Synaptic protein synthesis associated with memory is regulated by the RISC pathway in Drosophila. Cell 2006, 124:191-205.
    • (2006) Cell , vol.124 , pp. 191-205
    • Ashraf, S.I.1    McLoon, A.L.2    Sclarsic, S.M.3    Kunes, S.4
  • 5
    • 72149086111 scopus 로고    scopus 로고
    • A coordinated local translational control point at the synapse involving relief from silencing and MOV10 degradation
    • Banerjee S., Neveu P., Kosik K.S. A coordinated local translational control point at the synapse involving relief from silencing and MOV10 degradation. Neuron 2009, 64:871-884.
    • (2009) Neuron , vol.64 , pp. 871-884
    • Banerjee, S.1    Neveu, P.2    Kosik, K.S.3
  • 6
    • 51149121890 scopus 로고    scopus 로고
    • Depletion of 26S proteasomes in mouse brain neurons causes neurodegeneration and Lewy-like inclusions resembling human pale bodies
    • Bedford L., Hay D., Devoy A., Paine S., Powe D.G., Seth R., Gray T., Topham I., Fone K., Rezvani N., et al. Depletion of 26S proteasomes in mouse brain neurons causes neurodegeneration and Lewy-like inclusions resembling human pale bodies. J. Neurosci. 2008, 28:8189-8198.
    • (2008) J. Neurosci. , vol.28 , pp. 8189-8198
    • Bedford, L.1    Hay, D.2    Devoy, A.3    Paine, S.4    Powe, D.G.5    Seth, R.6    Gray, T.7    Topham, I.8    Fone, K.9    Rezvani, N.10
  • 7
    • 5344250985 scopus 로고    scopus 로고
    • A proteasome-sensitive connection between PSD-95 and GluR1 endocytosis
    • Bingol B., Schuman E.M. A proteasome-sensitive connection between PSD-95 and GluR1 endocytosis. Neuropharmacology 2004, 47:755-763.
    • (2004) Neuropharmacology , vol.47 , pp. 755-763
    • Bingol, B.1    Schuman, E.M.2
  • 8
    • 25844512787 scopus 로고    scopus 로고
    • Synaptic protein degradation by the ubiquitin proteasome system
    • Bingol B., Schuman E.M. Synaptic protein degradation by the ubiquitin proteasome system. Curr. Opin. Neurobiol. 2005, 15:536-541.
    • (2005) Curr. Opin. Neurobiol. , vol.15 , pp. 536-541
    • Bingol, B.1    Schuman, E.M.2
  • 9
    • 33745593049 scopus 로고    scopus 로고
    • Activity-dependent dynamics and sequestration of proteasomes in dendritic spines
    • Bingol B., Schuman E.M. Activity-dependent dynamics and sequestration of proteasomes in dendritic spines. Nature 2006, 441:1144-1148.
    • (2006) Nature , vol.441 , pp. 1144-1148
    • Bingol, B.1    Schuman, E.M.2
  • 10
    • 76749131595 scopus 로고    scopus 로고
    • Autophosphorylated CaMKIIalpha acts as a scaffold to recruit proteasomes to dendritic spines
    • Bingol B., Wang C.F., Arnott D., Cheng D., Peng J., Sheng M. Autophosphorylated CaMKIIalpha acts as a scaffold to recruit proteasomes to dendritic spines. Cell 2010, 140:567-578.
    • (2010) Cell , vol.140 , pp. 567-578
    • Bingol, B.1    Wang, C.F.2    Arnott, D.3    Cheng, D.4    Peng, J.5    Sheng, M.6
  • 11
    • 35348958381 scopus 로고    scopus 로고
    • The requirement for Phr1 in CNS axon tract formation reveals the corticostriatal boundary as a choice point for cortical axons
    • Bloom A.J., Miller B.R., Sanes J.R., DiAntonio A. The requirement for Phr1 in CNS axon tract formation reveals the corticostriatal boundary as a choice point for cortical axons. Genes Dev. 2007, 21:2593-2606.
    • (2007) Genes Dev. , vol.21 , pp. 2593-2606
    • Bloom, A.J.1    Miller, B.R.2    Sanes, J.R.3    DiAntonio, A.4
  • 12
    • 49049096562 scopus 로고    scopus 로고
    • Autophagy induction and autophagosome clearance in neurons: Relationship to autophagic pathology in Alzheimer's disease
    • Boland B., Kumar A., Lee S., Platt F.M., Wegiel J., Yu W.H., Nixon R.A. Autophagy induction and autophagosome clearance in neurons: Relationship to autophagic pathology in Alzheimer's disease. J. Neurosci. 2008, 28:6926-6937.
    • (2008) J. Neurosci. , vol.28 , pp. 6926-6937
    • Boland, B.1    Kumar, A.2    Lee, S.3    Platt, F.M.4    Wegiel, J.5    Yu, W.H.6    Nixon, R.A.7
  • 13
    • 43449117577 scopus 로고    scopus 로고
    • Balancing structure and function at hippocampal dendritic spines
    • Bourne J.N., Harris K.M. Balancing structure and function at hippocampal dendritic spines. Annu. Rev. Neurosci. 2008, 31:47-67.
    • (2008) Annu. Rev. Neurosci. , vol.31 , pp. 47-67
    • Bourne, J.N.1    Harris, K.M.2
  • 14
    • 34447552405 scopus 로고    scopus 로고
    • In vivo roles for matrix metalloproteinase-9 in mature hippocampal synaptic physiology and plasticity
    • Bozdagi O., Nagy V., Kwei K.T., Huntley G.W. In vivo roles for matrix metalloproteinase-9 in mature hippocampal synaptic physiology and plasticity. J. Neurophysiol. 2007, 98:334-344.
    • (2007) J. Neurophysiol. , vol.98 , pp. 334-344
    • Bozdagi, O.1    Nagy, V.2    Kwei, K.T.3    Huntley, G.W.4
  • 15
    • 0037014445 scopus 로고    scopus 로고
    • Ubiquitin and AP180 regulate the abundance of GLR-1 glutamate receptors at postsynaptic elements in C. elegans
    • Burbea M., Dreier L., Dittman J.S., Grunwald M.E., Kaplan J.M. Ubiquitin and AP180 regulate the abundance of GLR-1 glutamate receptors at postsynaptic elements in C. elegans. Neuron 2002, 35:107-120.
    • (2002) Neuron , vol.35 , pp. 107-120
    • Burbea, M.1    Dreier, L.2    Dittman, J.S.3    Grunwald, M.E.4    Kaplan, J.M.5
  • 16
    • 0035900794 scopus 로고    scopus 로고
    • Ubiquitination precedes internalization and proteolytic cleavage of plasma membrane-bound glycine receptors
    • Büttner C., Sadtler S., Leyendecker A., Laube B., Griffon N., Betz H., Schmalzing G. Ubiquitination precedes internalization and proteolytic cleavage of plasma membrane-bound glycine receptors. J. Biol. Chem. 2001, 276:42978-42985.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42978-42985
    • Büttner, C.1    Sadtler, S.2    Leyendecker, A.3    Laube, B.4    Griffon, N.5    Betz, H.6    Schmalzing, G.7
  • 17
    • 77955790177 scopus 로고    scopus 로고
    • Protein homeostasis and synaptic plasticity
    • Cajigas I.J., Will T., Schuman E.M. Protein homeostasis and synaptic plasticity. EMBO J. 2010, 29:2746-2752.
    • (2010) EMBO J. , vol.29 , pp. 2746-2752
    • Cajigas, I.J.1    Will, T.2    Schuman, E.M.3
  • 18
    • 0035924590 scopus 로고    scopus 로고
    • Chemotropic responses of retinal growth cones mediated by rapid local protein synthesis and degradation
    • Campbell D.S., Holt C.E. Chemotropic responses of retinal growth cones mediated by rapid local protein synthesis and degradation. Neuron 2001, 32:1013-1026.
    • (2001) Neuron , vol.32 , pp. 1013-1026
    • Campbell, D.S.1    Holt, C.E.2
  • 21
    • 69749110327 scopus 로고    scopus 로고
    • The proteasome-associated deubiquitinating enzyme Usp14 is essential for the maintenance of synaptic ubiquitin levels and the development of neuromuscular junctions
    • Chen P.C., Qin L.N., Li X.M., Walters B.J., Wilson J.A., Mei L., Wilson S.M. The proteasome-associated deubiquitinating enzyme Usp14 is essential for the maintenance of synaptic ubiquitin levels and the development of neuromuscular junctions. J. Neurosci. 2009, 29:10909-10919.
    • (2009) J. Neurosci. , vol.29 , pp. 10909-10919
    • Chen, P.C.1    Qin, L.N.2    Li, X.M.3    Walters, B.J.4    Wilson, J.A.5    Mei, L.6    Wilson, S.M.7
  • 22
    • 0037144498 scopus 로고    scopus 로고
    • Staring, a novel E3 ubiquitin-protein ligase that targets syntaxin 1 for degradation
    • Chin L.S., Vavalle J.P., Li L. Staring, a novel E3 ubiquitin-protein ligase that targets syntaxin 1 for degradation. J. Biol. Chem. 2002, 277:35071-35079.
    • (2002) J. Biol. Chem. , vol.277 , pp. 35071-35079
    • Chin, L.S.1    Vavalle, J.P.2    Li, L.3
  • 23
    • 0034004683 scopus 로고    scopus 로고
    • Ubiquitin immunochemistry as a diagnostic aid for community pathologists evaluating patients who have dementia
    • Chu C.T., Caruso J.L., Cummings T.J., Ervin J., Rosenberg C., Hulette C.M. Ubiquitin immunochemistry as a diagnostic aid for community pathologists evaluating patients who have dementia. Mod. Pathol. 2000, 13:420-426.
    • (2000) Mod. Pathol. , vol.13 , pp. 420-426
    • Chu, C.T.1    Caruso, J.L.2    Cummings, T.J.3    Ervin, J.4    Rosenberg, C.5    Hulette, C.M.6
  • 24
    • 33745879143 scopus 로고    scopus 로고
    • Intracellular protein degradation: From a vague idea thru the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting
    • Ciechanover A. Intracellular protein degradation: From a vague idea thru the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting. Exp. Biol. Med. 2006, 231:1197-1211.
    • (2006) Exp. Biol. Med. , vol.231 , pp. 1197-1211
    • Ciechanover, A.1
  • 27
    • 33745497728 scopus 로고    scopus 로고
    • Highwire restrains synaptic growth by attenuating a MAP kinase signal
    • Collins C.A., Wairkar Y.P., Johnson S.L., DiAntonio A. Highwire restrains synaptic growth by attenuating a MAP kinase signal. Neuron 2006, 51:57-69.
    • (2006) Neuron , vol.51 , pp. 57-69
    • Collins, C.A.1    Wairkar, Y.P.2    Johnson, S.L.3    DiAntonio, A.4
  • 28
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy
    • Cuervo A.M., Stefanis L., Fredenburg R., Lansbury P.T., Sulzer D. Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. Science 2004, 305:1292-1295.
    • (2004) Science , vol.305 , pp. 1292-1295
    • Cuervo, A.M.1    Stefanis, L.2    Fredenburg, R.3    Lansbury, P.T.4    Sulzer, D.5
  • 29
    • 0141741347 scopus 로고    scopus 로고
    • Parkinson's disease: Mechanisms and models
    • Dauer W., Przedborski S. Parkinson's disease: Mechanisms and models. Neuron 2003, 39:889-909.
    • (2003) Neuron , vol.39 , pp. 889-909
    • Dauer, W.1    Przedborski, S.2
  • 31
    • 33745959291 scopus 로고    scopus 로고
    • Deletion of the ubiquitin ligase CHIP leads to the accumulation, but not the aggregation, of both endogenous phospho- and caspase-3-cleaved tau species
    • Dickey C.A., Yue M., Lin W.L., Dickson D.W., Dunmore J.H., Lee W.C., Zehr C., West G., Cao S., Clark A.M., et al. Deletion of the ubiquitin ligase CHIP leads to the accumulation, but not the aggregation, of both endogenous phospho- and caspase-3-cleaved tau species. J. Neurosci. 2006, 26:6985-6996.
    • (2006) J. Neurosci. , vol.26 , pp. 6985-6996
    • Dickey, C.A.1    Yue, M.2    Lin, W.L.3    Dickson, D.W.4    Dunmore, J.H.5    Lee, W.C.6    Zehr, C.7    West, G.8    Cao, S.9    Clark, A.M.10
  • 32
    • 34548044548 scopus 로고    scopus 로고
    • Spatial regulation of an E3 ubiquitin ligase directs selective synapse elimination
    • Ding M., Chao D., Wang G., Shen K. Spatial regulation of an E3 ubiquitin ligase directs selective synapse elimination. Science 2007, 317:947-951.
    • (2007) Science , vol.317 , pp. 947-951
    • Ding, M.1    Chao, D.2    Wang, G.3    Shen, K.4
  • 33
    • 77954526026 scopus 로고    scopus 로고
    • Remodeling of extracellular matrix and epileptogenesis
    • Dityatev A. Remodeling of extracellular matrix and epileptogenesis. Epilepsia 2010, 51(Suppl 3):61-65.
    • (2010) Epilepsia , vol.51 , Issue.SUPPL 3 , pp. 61-65
    • Dityatev, A.1
  • 34
    • 70350389831 scopus 로고    scopus 로고
    • Regulation of the proteasome by neuronal activity and calcium/calmodulin-dependent protein kinase II
    • Djakovic S.N., Schwarz L.A., Barylko B., DeMartino G.N., Patrick G.N. Regulation of the proteasome by neuronal activity and calcium/calmodulin-dependent protein kinase II. J. Biol. Chem. 2009, 284:26655-26665.
    • (2009) J. Biol. Chem. , vol.284 , pp. 26655-26665
    • Djakovic, S.N.1    Schwarz, L.A.2    Barylko, B.3    DeMartino, G.N.4    Patrick, G.N.5
  • 35
    • 43049090872 scopus 로고    scopus 로고
    • Proteasome inhibition enhances the induction and impairs the maintenance of late-phase long-term potentiation
    • Dong C., Upadhya S.C., Ding L., Smith T.K., Hegde A.N. Proteasome inhibition enhances the induction and impairs the maintenance of late-phase long-term potentiation. Learn. Mem. 2008, 15:335-347.
    • (2008) Learn. Mem. , vol.15 , pp. 335-347
    • Dong, C.1    Upadhya, S.C.2    Ding, L.3    Smith, T.K.4    Hegde, A.N.5
  • 37
    • 0033639083 scopus 로고    scopus 로고
    • Reinsertion or degradation of AMPA receptors determined by activity-dependent endocytic sorting
    • Ehlers M.D. Reinsertion or degradation of AMPA receptors determined by activity-dependent endocytic sorting. Neuron 2000, 28:511-525.
    • (2000) Neuron , vol.28 , pp. 511-525
    • Ehlers, M.D.1
  • 38
    • 0037374587 scopus 로고    scopus 로고
    • Activity level controls postsynaptic composition and signaling via the ubiquitin-proteasome system
    • Ehlers M.D. Activity level controls postsynaptic composition and signaling via the ubiquitin-proteasome system. Nat. Neurosci. 2003, 6:231-242.
    • (2003) Nat. Neurosci. , vol.6 , pp. 231-242
    • Ehlers, M.D.1
  • 40
    • 33749620749 scopus 로고    scopus 로고
    • A balance of protein synthesis and proteasome-dependent degradation determines the maintenance of LTP
    • Fonseca R., Vabulas R.M., Hartl F.U., Bonhoeffer T., Nägerl U.V. A balance of protein synthesis and proteasome-dependent degradation determines the maintenance of LTP. Neuron 2006, 52:239-245.
    • (2006) Neuron , vol.52 , pp. 239-245
    • Fonseca, R.1    Vabulas, R.M.2    Hartl, F.U.3    Bonhoeffer, T.4    Nägerl, U.V.5
  • 42
    • 20444384416 scopus 로고    scopus 로고
    • Proteasome plasticity
    • Glickman M.H., Raveh D. Proteasome plasticity. FEBS Lett. 2005, 579:3214-3223.
    • (2005) FEBS Lett. , vol.579 , pp. 3214-3223
    • Glickman, M.H.1    Raveh, D.2
  • 45
    • 33846863144 scopus 로고    scopus 로고
    • Glutamate stimulates glutamate receptor interacting protein 1 degradation by ubiquitin-proteasome system to regulate surface expression of GluR2
    • Guo L., Wang Y. Glutamate stimulates glutamate receptor interacting protein 1 degradation by ubiquitin-proteasome system to regulate surface expression of GluR2. Neuroscience 2007, 145:100-109.
    • (2007) Neuroscience , vol.145 , pp. 100-109
    • Guo, L.1    Wang, Y.2
  • 47
    • 4143112402 scopus 로고    scopus 로고
    • Ubiquitin-proteasome-mediated local protein degradation and synaptic plasticity
    • Hegde A.N. Ubiquitin-proteasome-mediated local protein degradation and synaptic plasticity. Prog. Neurobiol. 2004, 73:311-357.
    • (2004) Prog. Neurobiol. , vol.73 , pp. 311-357
    • Hegde, A.N.1
  • 48
    • 77954416653 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway and synaptic plasticity
    • Hegde A.N. The ubiquitin-proteasome pathway and synaptic plasticity. Learn. Mem. 2010, 17:314-327.
    • (2010) Learn. Mem. , vol.17 , pp. 314-327
    • Hegde, A.N.1
  • 49
    • 0027304239 scopus 로고
    • Regulatory subunits of cAMP-dependent protein kinases are degraded after conjugation to ubiquitin: A molecular mechanism underlying long-term synaptic plasticity
    • Hegde A.N., Goldberg A.L., Schwartz J.H. Regulatory subunits of cAMP-dependent protein kinases are degraded after conjugation to ubiquitin: A molecular mechanism underlying long-term synaptic plasticity. Proc. Natl. Acad. Sci. USA 1993, 90:7436-7440.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7436-7440
    • Hegde, A.N.1    Goldberg, A.L.2    Schwartz, J.H.3
  • 51
    • 66249098873 scopus 로고    scopus 로고
    • PHR regulates growth cone pausing at intermediate targets through microtubule disassembly
    • Hendricks M., Jesuthasan S. PHR regulates growth cone pausing at intermediate targets through microtubule disassembly. J. Neurosci. 2009, 29:6593-6598.
    • (2009) J. Neurosci. , vol.29 , pp. 6593-6598
    • Hendricks, M.1    Jesuthasan, S.2
  • 52
    • 34047107208 scopus 로고    scopus 로고
    • Liprinalpha1 degradation by calcium/calmodulin-dependent protein kinase II regulates LAR receptor tyrosine phosphatase distribution and dendrite development
    • Hoogenraad C.C., Feliu-Mojer M.I., Spangler S.A., Milstein A.D., Dunah A.W., Hung A.Y., Sheng M. Liprinalpha1 degradation by calcium/calmodulin-dependent protein kinase II regulates LAR receptor tyrosine phosphatase distribution and dendrite development. Dev. Cell 2007, 12:587-602.
    • (2007) Dev. Cell , vol.12 , pp. 587-602
    • Hoogenraad, C.C.1    Feliu-Mojer, M.I.2    Spangler, S.A.3    Milstein, A.D.4    Dunah, A.W.5    Hung, A.Y.6    Sheng, M.7
  • 53
    • 33746866693 scopus 로고    scopus 로고
    • Dynamic translational and proteasomal regulation of fragile X mental retardation protein controls mGluR-dependent long-term depression
    • Hou L., Antion M.D., Hu D., Spencer C.M., Paylor R., Klann E. Dynamic translational and proteasomal regulation of fragile X mental retardation protein controls mGluR-dependent long-term depression. Neuron 2006, 51:441-454.
    • (2006) Neuron , vol.51 , pp. 441-454
    • Hou, L.1    Antion, M.D.2    Hu, D.3    Spencer, C.M.4    Paylor, R.5    Klann, E.6
  • 54
    • 78149460672 scopus 로고    scopus 로고
    • Degradation of postsynaptic scaffold GKAP and regulation of dendritic spine morphology by the TRIM3 ubiquitin ligase in rat hippocampal neurons
    • Hung A.Y., Sung C.C., Brito I.L., Sheng M. Degradation of postsynaptic scaffold GKAP and regulation of dendritic spine morphology by the TRIM3 ubiquitin ligase in rat hippocampal neurons. PLoS ONE 2010, 5:e9842.
    • (2010) PLoS ONE , vol.5
    • Hung, A.Y.1    Sung, C.C.2    Brito, I.L.3    Sheng, M.4
  • 55
    • 36749010218 scopus 로고    scopus 로고
    • The age of crosstalk: Phosphorylation, ubiquitination, and beyond
    • Hunter T. The age of crosstalk: Phosphorylation, ubiquitination, and beyond. Mol. Cell 2007, 28:730-738.
    • (2007) Mol. Cell , vol.28 , pp. 730-738
    • Hunter, T.1
  • 57
    • 76149085199 scopus 로고    scopus 로고
    • A role for the ubiquitin-proteasome system in activity-dependent presynaptic silencing
    • Jiang X., Litkowski P.E., Taylor A.A., Lin Y., Snider B.J., Moulder K.L. A role for the ubiquitin-proteasome system in activity-dependent presynaptic silencing. J. Neurosci. 2010, 30:1798-1809.
    • (2010) J. Neurosci. , vol.30 , pp. 1798-1809
    • Jiang, X.1    Litkowski, P.E.2    Taylor, A.A.3    Lin, Y.4    Snider, B.J.5    Moulder, K.L.6
  • 58
    • 0032192481 scopus 로고    scopus 로고
    • Mutation of the Angelman ubiquitin ligase in mice causes increased cytoplasmic p53 and deficits of contextual learning and long-term potentiation
    • Jiang Y.H., Armstrong D., Albrecht U., Atkins C.M., Noebels J.L., Eichele G., Sweatt J.D., Beaudet A.L. Mutation of the Angelman ubiquitin ligase in mice causes increased cytoplasmic p53 and deficits of contextual learning and long-term potentiation. Neuron 1998, 21:799-811.
    • (1998) Neuron , vol.21 , pp. 799-811
    • Jiang, Y.H.1    Armstrong, D.2    Albrecht, U.3    Atkins, C.M.4    Noebels, J.L.5    Eichele, G.6    Sweatt, J.D.7    Beaudet, A.L.8
  • 59
    • 33646918035 scopus 로고    scopus 로고
    • Involvement of protein synthesis and degradation in long-term potentiation of Schaffer collateral CA1 synapses
    • Karpova A., Mikhaylova M., Thomas U., Knöpfel T., Behnisch T. Involvement of protein synthesis and degradation in long-term potentiation of Schaffer collateral CA1 synapses. J. Neurosci. 2006, 26:4949-4955.
    • (2006) J. Neurosci. , vol.26 , pp. 4949-4955
    • Karpova, A.1    Mikhaylova, M.2    Thomas, U.3    Knöpfel, T.4    Behnisch, T.5
  • 60
    • 17244381176 scopus 로고    scopus 로고
    • Activity-dependent NMDA receptor degradation mediated by retrotranslocation and ubiquitination
    • Kato A., Rouach N., Nicoll R.A., Bredt D.S. Activity-dependent NMDA receptor degradation mediated by retrotranslocation and ubiquitination. Proc. Natl. Acad. Sci. USA 2005, 102:5600-5605.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 5600-5605
    • Kato, A.1    Rouach, N.2    Nicoll, R.A.3    Bredt, D.S.4
  • 62
    • 77950371695 scopus 로고    scopus 로고
    • PINK1 is recruited to mitochondria with parkin and associates with LC3 in mitophagy
    • Kawajiri S., Saiki S., Sato S., Sato F., Hatano T., Eguchi H., Hattori N. PINK1 is recruited to mitochondria with parkin and associates with LC3 in mitophagy. FEBS Lett. 2010, 584:1073-1079.
    • (2010) FEBS Lett. , vol.584 , pp. 1073-1079
    • Kawajiri, S.1    Saiki, S.2    Sato, S.3    Sato, F.4    Hatano, T.5    Eguchi, H.6    Hattori, N.7
  • 63
    • 0037381710 scopus 로고    scopus 로고
    • Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease
    • Keck S., Nitsch R., Grune T., Ullrich O. Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease. J. Neurochem. 2003, 85:115-122.
    • (2003) J. Neurochem. , vol.85 , pp. 115-122
    • Keck, S.1    Nitsch, R.2    Grune, T.3    Ullrich, O.4
  • 64
    • 0034131044 scopus 로고    scopus 로고
    • Impaired proteasome function in Alzheimer's disease
    • Keller J.N., Hanni K.B., Markesbery W.R. Impaired proteasome function in Alzheimer's disease. J. Neurochem. 2000, 75:436-439.
    • (2000) J. Neurochem. , vol.75 , pp. 436-439
    • Keller, J.N.1    Hanni, K.B.2    Markesbery, W.R.3
  • 65
    • 0031012849 scopus 로고    scopus 로고
    • UBE3A/E6-AP mutations cause Angelman syndrome
    • Kishino T., Lalande M., Wagstaff J. UBE3A/E6-AP mutations cause Angelman syndrome. Nat. Genet. 1997, 15:70-73.
    • (1997) Nat. Genet. , vol.15 , pp. 70-73
    • Kishino, T.1    Lalande, M.2    Wagstaff, J.3
  • 67
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains: Structure and function of the deubiquitinases
    • Komander D., Clague M.J., Urbé S. Breaking the chains: Structure and function of the deubiquitinases. Nat. Rev. Mol. Cell Biol. 2009, 10:550-563.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 550-563
    • Komander, D.1    Clague, M.J.2    Urbé, S.3
  • 70
    • 1142274208 scopus 로고    scopus 로고
    • Cdh1-APC controls axonal growth and patterning in the mammalian brain
    • Konishi Y., Stegmüller J., Matsuda T., Bonni S., Bonni A. Cdh1-APC controls axonal growth and patterning in the mammalian brain. Science 2004, 303:1026-1030.
    • (2004) Science , vol.303 , pp. 1026-1030
    • Konishi, Y.1    Stegmüller, J.2    Matsuda, T.3    Bonni, S.4    Bonni, A.5
  • 71
    • 27244440860 scopus 로고    scopus 로고
    • Dendrite-specific remodeling of Drosophila sensory neurons requires matrix metalloproteases, ubiquitin-proteasome, and ecdysone signaling
    • Kuo C.T., Jan L.Y., Jan Y.N. Dendrite-specific remodeling of Drosophila sensory neurons requires matrix metalloproteases, ubiquitin-proteasome, and ecdysone signaling. Proc. Natl. Acad. Sci. USA 2005, 102:15230-15235.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15230-15235
    • Kuo, C.T.1    Jan, L.Y.2    Jan, Y.N.3
  • 72
    • 33746363831 scopus 로고    scopus 로고
    • Identification of E2/E3 ubiquitinating enzymes and caspase activity regulating Drosophila sensory neuron dendrite pruning
    • Kuo C.T., Zhu S., Younger S., Jan L.Y., Jan Y.N. Identification of E2/E3 ubiquitinating enzymes and caspase activity regulating Drosophila sensory neuron dendrite pruning. Neuron 2006, 51:283-290.
    • (2006) Neuron , vol.51 , pp. 283-290
    • Kuo, C.T.1    Zhu, S.2    Younger, S.3    Jan, L.Y.4    Jan, Y.N.5
  • 75
    • 77952326081 scopus 로고    scopus 로고
    • Disease-causing mutations in parkin impair mitochondrial ubiquitination, aggregation, and HDAC6-dependent mitophagy
    • Lee J.Y., Nagano Y., Taylor J.P., Lim K.L., Yao T.P. Disease-causing mutations in parkin impair mitochondrial ubiquitination, aggregation, and HDAC6-dependent mitophagy. J. Cell Biol. 2010, 189:671-679.
    • (2010) J. Cell Biol. , vol.189 , pp. 671-679
    • Lee, J.Y.1    Nagano, Y.2    Taylor, J.P.3    Lim, K.L.4    Yao, T.P.5
  • 77
    • 3242656596 scopus 로고    scopus 로고
    • Subunit rules governing the sorting of internalized AMPA receptors in hippocampal neurons
    • Lee S.H., Simonetta A., Sheng M. Subunit rules governing the sorting of internalized AMPA receptors in hippocampal neurons. Neuron 2004, 43:221-236.
    • (2004) Neuron , vol.43 , pp. 221-236
    • Lee, S.H.1    Simonetta, A.2    Sheng, M.3
  • 78
    • 36048943648 scopus 로고    scopus 로고
    • The ubiquitin ligase Phr1 regulates axon outgrowth through modulation of microtubule dynamics
    • Lewcock J.W., Genoud N., Lettieri K., Pfaff S.L. The ubiquitin ligase Phr1 regulates axon outgrowth through modulation of microtubule dynamics. Neuron 2007, 56:604-620.
    • (2007) Neuron , vol.56 , pp. 604-620
    • Lewcock, J.W.1    Genoud, N.2    Lettieri, K.3    Pfaff, S.L.4
  • 79
    • 77953271477 scopus 로고    scopus 로고
    • Caspase-3 activation via mitochondria is required for long-term depression and AMPA receptor internalization
    • Li Z., Jo J., Jia J.M., Lo S.C., Whitcomb D.J., Jiao S., Cho K., Sheng M. Caspase-3 activation via mitochondria is required for long-term depression and AMPA receptor internalization. Cell 2010, 141:859-871.
    • (2010) Cell , vol.141 , pp. 859-871
    • Li, Z.1    Jo, J.2    Jia, J.M.3    Lo, S.C.4    Whitcomb, D.J.5    Jiao, S.6    Cho, K.7    Sheng, M.8
  • 81
    • 58449101589 scopus 로고    scopus 로고
    • Abeta42-induced neurodegeneration via an age-dependent autophagic-lysosomal injury in Drosophila
    • Ling D., Song H.J., Garza D., Neufeld T.P., Salvaterra P.M. Abeta42-induced neurodegeneration via an age-dependent autophagic-lysosomal injury in Drosophila. PLoS ONE 2009, 4:e4201.
    • (2009) PLoS ONE , vol.4
    • Ling, D.1    Song, H.J.2    Garza, D.3    Neufeld, T.P.4    Salvaterra, P.M.5
  • 84
    • 77951181836 scopus 로고    scopus 로고
    • PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy
    • Matsuda N., Sato S., Shiba K., Okatsu K., Saisho K., Gautier C.A., Sou Y.S., Saiki S., Kawajiri S., Sato F., et al. PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy. J. Cell Biol. 2010, 189:211-221.
    • (2010) J. Cell Biol. , vol.189 , pp. 211-221
    • Matsuda, N.1    Sato, S.2    Shiba, K.3    Okatsu, K.4    Saisho, K.5    Gautier, C.A.6    Sou, Y.S.7    Saiki, S.8    Kawajiri, S.9    Sato, F.10
  • 86
    • 33645103421 scopus 로고    scopus 로고
    • Effects of extracellular matrix-degrading proteases matrix metalloproteinases 3 and 9 on spatial learning and synaptic plasticity
    • Meighan S.E., Meighan P.C., Choudhury P., Davis C.J., Olson M.L., Zornes P.A., Wright J.W., Harding J.W. Effects of extracellular matrix-degrading proteases matrix metalloproteinases 3 and 9 on spatial learning and synaptic plasticity. J. Neurochem. 2006, 96:1227-1241.
    • (2006) J. Neurochem. , vol.96 , pp. 1227-1241
    • Meighan, S.E.1    Meighan, P.C.2    Choudhury, P.3    Davis, C.J.4    Olson, M.L.5    Zornes, P.A.6    Wright, J.W.7    Harding, J.W.8
  • 89
    • 0027185303 scopus 로고
    • The Drosophila bendless gene encodes a neural protein related to ubiquitin-conjugating enzymes
    • Muralidhar M.G., Thomas J.B. The Drosophila bendless gene encodes a neural protein related to ubiquitin-conjugating enzymes. Neuron 1993, 11:253-266.
    • (1993) Neuron , vol.11 , pp. 253-266
    • Muralidhar, M.G.1    Thomas, J.B.2
  • 91
    • 77749341438 scopus 로고    scopus 로고
    • Ubiquitin ligase complexes: From substrate selectivity to conjugational specificity
    • Nagy V., Dikic I. Ubiquitin ligase complexes: From substrate selectivity to conjugational specificity. Biol. Chem. 2010, 391:163-169.
    • (2010) Biol. Chem. , vol.391 , pp. 163-169
    • Nagy, V.1    Dikic, I.2
  • 92
    • 13544262428 scopus 로고    scopus 로고
    • Regulation of a DLK-1 and p38 MAP kinase pathway by the ubiquitin ligase RPM-1 is required for presynaptic development
    • Nakata K., Abrams B., Grill B., Goncharov A., Huang X., Chisholm A.D., Jin Y. Regulation of a DLK-1 and p38 MAP kinase pathway by the ubiquitin ligase RPM-1 is required for presynaptic development. Cell 2005, 120:407-420.
    • (2005) Cell , vol.120 , pp. 407-420
    • Nakata, K.1    Abrams, B.2    Grill, B.3    Goncharov, A.4    Huang, X.5    Chisholm, A.D.6    Jin, Y.7
  • 93
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • Narendra D., Tanaka A., Suen D.F., Youle R.J. Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J. Cell Biol. 2008, 183:795-803.
    • (2008) J. Cell Biol. , vol.183 , pp. 795-803
    • Narendra, D.1    Tanaka, A.2    Suen, D.F.3    Youle, R.J.4
  • 95
    • 60549089207 scopus 로고    scopus 로고
    • APP binds DR6 to trigger axon pruning and neuron death via distinct caspases
    • Nikolaev A., McLaughlin T., O'Leary D.D., Tessier-Lavigne M. APP binds DR6 to trigger axon pruning and neuron death via distinct caspases. Nature 2009, 457:981-989.
    • (2009) Nature , vol.457 , pp. 981-989
    • Nikolaev, A.1    McLaughlin, T.2    O'Leary, D.D.3    Tessier-Lavigne, M.4
  • 96
    • 0344443828 scopus 로고    scopus 로고
    • Targeted protein degradation and synapse remodeling by an inducible protein kinase
    • Pak D.T., Sheng M. Targeted protein degradation and synapse remodeling by an inducible protein kinase. Science 2003, 302:1368-1373.
    • (2003) Science , vol.302 , pp. 1368-1373
    • Pak, D.T.1    Sheng, M.2
  • 97
    • 51549086469 scopus 로고    scopus 로고
    • Neuroprotection of rapamycin in lactacystin-induced neurodegeneration via autophagy enhancement
    • Pan T., Kondo S., Zhu W., Xie W., Jankovic J., Le W. Neuroprotection of rapamycin in lactacystin-induced neurodegeneration via autophagy enhancement. Neurobiol. Dis. 2008, 32:16-25.
    • (2008) Neurobiol. Dis. , vol.32 , pp. 16-25
    • Pan, T.1    Kondo, S.2    Zhu, W.3    Xie, W.4    Jankovic, J.5    Le, W.6
  • 99
    • 0344663966 scopus 로고    scopus 로고
    • Ubiquitin-mediated proteasome activity is required for agonist-induced endocytosis of GluRs
    • Patrick G.N., Bingol B., Weld H.A., Schuman E.M. Ubiquitin-mediated proteasome activity is required for agonist-induced endocytosis of GluRs. Curr. Biol. 2003, 13:2073-2081.
    • (2003) Curr. Biol. , vol.13 , pp. 2073-2081
    • Patrick, G.N.1    Bingol, B.2    Weld, H.A.3    Schuman, E.M.4
  • 102
    • 77749323170 scopus 로고    scopus 로고
    • Ubiquitination acutely regulates presynaptic neurotransmitter release in mammalian neurons
    • Rinetti G.V., Schweizer F.E. Ubiquitination acutely regulates presynaptic neurotransmitter release in mammalian neurons. J. Neurosci. 2010, 30:3157-3166.
    • (2010) J. Neurosci. , vol.30 , pp. 3157-3166
    • Rinetti, G.V.1    Schweizer, F.E.2
  • 103
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross C.A., Poirier M.A. Protein aggregation and neurodegenerative disease. Nat. Med. 2004, 10(Suppl):S10-S17.
    • (2004) Nat. Med. , vol.10 , Issue.SUPPL
    • Ross, C.A.1    Poirier, M.A.2
  • 104
    • 32544432831 scopus 로고    scopus 로고
    • Presynaptic terminals independently regulate synaptic clustering and autophagy of GABAA receptors in Caenorhabditis elegans
    • Rowland A.M., Richmond J.E., Olsen J.G., Hall D.H., Bamber B.A. Presynaptic terminals independently regulate synaptic clustering and autophagy of GABAA receptors in Caenorhabditis elegans. J. Neurosci. 2006, 26:1711-1720.
    • (2006) J. Neurosci. , vol.26 , pp. 1711-1720
    • Rowland, A.M.1    Richmond, J.E.2    Olsen, J.G.3    Hall, D.H.4    Bamber, B.A.5
  • 106
    • 36849047854 scopus 로고    scopus 로고
    • Activity-dependent ubiquitination of GABA(A) receptors regulates their accumulation at synaptic sites
    • Saliba R.S., Michels G., Jacob T.C., Pangalos M.N., Moss S.J. Activity-dependent ubiquitination of GABA(A) receptors regulates their accumulation at synaptic sites. J. Neurosci. 2007, 27:13341-13351.
    • (2007) J. Neurosci. , vol.27 , pp. 13341-13351
    • Saliba, R.S.1    Michels, G.2    Jacob, T.C.3    Pangalos, M.N.4    Moss, S.J.5
  • 107
    • 0033696920 scopus 로고    scopus 로고
    • Rpm-1, a conserved neuronal gene that regulates targeting and synaptogenesis in C. elegans
    • Schaefer A.M., Hadwiger G.D., Nonet M.L. rpm-1, a conserved neuronal gene that regulates targeting and synaptogenesis in C. elegans. Neuron 2000, 26:345-356.
    • (2000) Neuron , vol.26 , pp. 345-356
    • Schaefer, A.M.1    Hadwiger, G.D.2    Nonet, M.L.3
  • 108
    • 43649097642 scopus 로고    scopus 로고
    • Critical role of CDK5 and Polo-like kinase 2 in homeostatic synaptic plasticity during elevated activity
    • Seeburg D.P., Feliu-Mojer M., Gaiottino J., Pak D.T., Sheng M. Critical role of CDK5 and Polo-like kinase 2 in homeostatic synaptic plasticity during elevated activity. Neuron 2008, 58:571-583.
    • (2008) Neuron , vol.58 , pp. 571-583
    • Seeburg, D.P.1    Feliu-Mojer, M.2    Gaiottino, J.3    Pak, D.T.4    Sheng, M.5
  • 110
    • 70449727080 scopus 로고    scopus 로고
    • Autophagy promotes synapse development in Drosophila
    • Shen W., Ganetzky B. Autophagy promotes synapse development in Drosophila. J. Cell Biol. 2009, 187:71-79.
    • (2009) J. Cell Biol. , vol.187 , pp. 71-79
    • Shen, W.1    Ganetzky, B.2
  • 111
    • 0034044563 scopus 로고    scopus 로고
    • The Shank family of scaffold proteins
    • Sheng M., Kim E. The Shank family of scaffold proteins. J. Cell Sci. 2000, 113:1851-1856.
    • (2000) J. Cell Sci. , vol.113 , pp. 1851-1856
    • Sheng, M.1    Kim, E.2
  • 112
    • 1042266624 scopus 로고    scopus 로고
    • CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival
    • Shimura H., Schwartz D., Gygi S.P., Kosik K.S. CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival. J. Biol. Chem. 2004, 279:4869-4876.
    • (2004) J. Biol. Chem. , vol.279 , pp. 4869-4876
    • Shimura, H.1    Schwartz, D.2    Gygi, S.P.3    Kosik, K.S.4
  • 114
    • 0038413759 scopus 로고    scopus 로고
    • Aggregated and monomeric alpha-synuclein bind to the S6' proteasomal protein and inhibit proteasomal function
    • Snyder H., Mensah K., Theisler C., Lee J., Matouschek A., Wolozin B. Aggregated and monomeric alpha-synuclein bind to the S6' proteasomal protein and inhibit proteasomal function. J. Biol. Chem. 2003, 278:11753-11759.
    • (2003) J. Biol. Chem. , vol.278 , pp. 11753-11759
    • Snyder, H.1    Mensah, K.2    Theisler, C.3    Lee, J.4    Matouschek, A.5    Wolozin, B.6
  • 115
    • 0037422010 scopus 로고    scopus 로고
    • Parkin is a component of an SCF-like ubiquitin ligase complex and protects postmitotic neurons from kainate excitotoxicity
    • Staropoli J.F., McDermott C., Martinat C., Schulman B., Demireva E., Abeliovich A. Parkin is a component of an SCF-like ubiquitin ligase complex and protects postmitotic neurons from kainate excitotoxicity. Neuron 2003, 37:735-749.
    • (2003) Neuron , vol.37 , pp. 735-749
    • Staropoli, J.F.1    McDermott, C.2    Martinat, C.3    Schulman, B.4    Demireva, E.5    Abeliovich, A.6
  • 116
    • 33749077101 scopus 로고    scopus 로고
    • Dendritic protein synthesis, synaptic plasticity, and memory
    • Sutton M.A., Schuman E.M. Dendritic protein synthesis, synaptic plasticity, and memory. Cell 2006, 127:49-58.
    • (2006) Cell , vol.127 , pp. 49-58
    • Sutton, M.A.1    Schuman, E.M.2
  • 117
    • 77953467032 scopus 로고    scopus 로고
    • Characterization of the Brain 26S Proteasome and its Interacting Proteins
    • Tai H.C., Besche H., Goldberg A.L., Schuman E.M. Characterization of the Brain 26S Proteasome and its Interacting Proteins. Front Mol Neurosci 2010, 3:12.
    • (2010) Front Mol Neurosci , vol.3 , pp. 12
    • Tai, H.C.1    Besche, H.2    Goldberg, A.L.3    Schuman, E.M.4
  • 118
    • 54249158324 scopus 로고    scopus 로고
    • Ubiquitin, the proteasome and protein degradation in neuronal function and dysfunction
    • Tai H.C., Schuman E.M. Ubiquitin, the proteasome and protein degradation in neuronal function and dysfunction. Nat. Rev. Neurosci. 2008, 9:826-838.
    • (2008) Nat. Rev. Neurosci. , vol.9 , pp. 826-838
    • Tai, H.C.1    Schuman, E.M.2
  • 120
    • 78049231804 scopus 로고    scopus 로고
    • A small-molecule scaffold induces autophagy in primary neurons and protects against toxicity in a Huntington disease model
    • Tsvetkov A.S., Miller J., Arrasate M., Wong J.S., Pleiss M.A., Finkbeiner S. A small-molecule scaffold induces autophagy in primary neurons and protects against toxicity in a Huntington disease model. Proc. Natl. Acad. Sci. USA 2010, 107:16982-16987.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 16982-16987
    • Tsvetkov, A.S.1    Miller, J.2    Arrasate, M.3    Wong, J.S.4    Pleiss, M.A.5    Finkbeiner, S.6
  • 124
    • 3142523288 scopus 로고    scopus 로고
    • Genetic clues to the pathogenesis of Parkinson's disease
    • Vila M., Przedborski S. Genetic clues to the pathogenesis of Parkinson's disease. Nat. Med. 2004, 10(Suppl):S58-S62.
    • (2004) Nat. Med. , vol.10 , Issue.SUPPL
    • Vila, M.1    Przedborski, S.2
  • 125
    • 77955347088 scopus 로고    scopus 로고
    • PINK1 points Parkin to mitochondria
    • Vives-Bauza C., Przedborski S. PINK1 points Parkin to mitochondria. Autophagy 2010, 6:674-675.
    • (2010) Autophagy , vol.6 , pp. 674-675
    • Vives-Bauza, C.1    Przedborski, S.2
  • 126
    • 53049098471 scopus 로고    scopus 로고
    • Wild type alpha-synuclein is degraded by chaperone-mediated autophagy and macroautophagy in neuronal cells
    • Vogiatzi T., Xilouri M., Vekrellis K., Stefanis L. Wild type alpha-synuclein is degraded by chaperone-mediated autophagy and macroautophagy in neuronal cells. J. Biol. Chem. 2008, 283:23542-23556.
    • (2008) J. Biol. Chem. , vol.283 , pp. 23542-23556
    • Vogiatzi, T.1    Xilouri, M.2    Vekrellis, K.3    Stefanis, L.4
  • 128
    • 58049191338 scopus 로고    scopus 로고
    • Extracellular proteolysis by matrix metalloproteinase-9 drives dendritic spine enlargement and long-term potentiation coordinately
    • Wang X.B., Bozdagi O., Nikitczuk J.S., Zhai Z.W., Zhou Q., Huntley G.W. Extracellular proteolysis by matrix metalloproteinase-9 drives dendritic spine enlargement and long-term potentiation coordinately. Proc. Natl. Acad. Sci. USA 2008, 105:19520-19525.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 19520-19525
    • Wang, X.B.1    Bozdagi, O.2    Nikitczuk, J.S.3    Zhai, Z.W.4    Zhou, Q.5    Huntley, G.W.6
  • 129
    • 0038198738 scopus 로고    scopus 로고
    • Axon pruning during Drosophila metamorphosis: Evidence for local degeneration and requirement of the ubiquitin-proteasome system
    • Watts R.J., Hoopfer E.D., Luo L. Axon pruning during Drosophila metamorphosis: Evidence for local degeneration and requirement of the ubiquitin-proteasome system. Neuron 2003, 38:871-885.
    • (2003) Neuron , vol.38 , pp. 871-885
    • Watts, R.J.1    Hoopfer, E.D.2    Luo, L.3
  • 131
    • 0037155924 scopus 로고    scopus 로고
    • Regulation of synaptophysin degradation by mammalian homologues of seven in absentia
    • Wheeler T.C., Chin L.S., Li Y., Roudabush F.L., Li L. Regulation of synaptophysin degradation by mammalian homologues of seven in absentia. J. Biol. Chem. 2002, 277:10273-10282.
    • (2002) J. Biol. Chem. , vol.277 , pp. 10273-10282
    • Wheeler, T.C.1    Chin, L.S.2    Li, Y.3    Roudabush, F.L.4    Li, L.5
  • 132
    • 33750959090 scopus 로고    scopus 로고
    • Proteasome inhibition triggers activity-dependent increase in the size of the recycling vesicle pool in cultured hippocampal neurons
    • Willeumier K., Pulst S.M., Schweizer F.E. Proteasome inhibition triggers activity-dependent increase in the size of the recycling vesicle pool in cultured hippocampal neurons. J. Neurosci. 2006, 26:11333-11341.
    • (2006) J. Neurosci. , vol.26 , pp. 11333-11341
    • Willeumier, K.1    Pulst, S.M.2    Schweizer, F.E.3
  • 135
    • 77954116814 scopus 로고    scopus 로고
    • Autophagy gone awry in neurodegenerative diseases
    • Wong E., Cuervo A.M. Autophagy gone awry in neurodegenerative diseases. Nat. Neurosci. 2010, 13:805-811.
    • (2010) Nat. Neurosci. , vol.13 , pp. 805-811
    • Wong, E.1    Cuervo, A.M.2
  • 136
    • 33747870115 scopus 로고    scopus 로고
    • Calpain and synaptic function
    • Wu H.Y., Lynch D.R. Calpain and synaptic function. Mol. Neurobiol. 2006, 33:215-236.
    • (2006) Mol. Neurobiol. , vol.33 , pp. 215-236
    • Wu, H.Y.1    Lynch, D.R.2
  • 138
    • 33847410541 scopus 로고    scopus 로고
    • Emerging roles for ubiquitin and protein degradation in neuronal function
    • Yi J.J., Ehlers M.D. Emerging roles for ubiquitin and protein degradation in neuronal function. Pharmacol. Rev. 2007, 59:14-39.
    • (2007) Pharmacol. Rev. , vol.59 , pp. 14-39
    • Yi, J.J.1    Ehlers, M.D.2
  • 140
    • 0037851010 scopus 로고    scopus 로고
    • The ubiquitin proteasome system functions as an inhibitory constraint on synaptic strengthening
    • Zhao Y., Hegde A.N., Martin K.C. The ubiquitin proteasome system functions as an inhibitory constraint on synaptic strengthening. Curr. Biol. 2003, 13:887-898.
    • (2003) Curr. Biol. , vol.13 , pp. 887-898
    • Zhao, Y.1    Hegde, A.N.2    Martin, K.C.3
  • 141
    • 0033710880 scopus 로고    scopus 로고
    • Regulation of presynaptic terminal organization by C. elegans RPM-1, a putative guanine nucleotide exchanger with a RING-H2 finger domain
    • Zhen M., Huang X., Bamber B., Jin Y. Regulation of presynaptic terminal organization by C. elegans RPM-1, a putative guanine nucleotide exchanger with a RING-H2 finger domain. Neuron 2000, 26:331-343.
    • (2000) Neuron , vol.26 , pp. 331-343
    • Zhen, M.1    Huang, X.2    Bamber, B.3    Jin, Y.4


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