메뉴 건너뛰기




Volumn 55, Issue , 2013, Pages 129-139

Deleterious effects of soluble amyloid-β oligomers on multiple steps of synaptic vesicle trafficking

Author keywords

Alzheimer's disease; Cyclin dependent kinase 5 (CDK5); Phosphatidylinositol 4,5 bisphosphate (PtdIns(4,5)P2); Soluble A oligomers; Synaptic vesicle trafficking

Indexed keywords

AMYLOID BETA OLIGOMER; AMYLOID BETA PROTEIN; CALPAIN; CYCLIN DEPENDENT KINASE 5; PHOSPHATIDYLINOSITOL 4 PHOSPHATE 5 KINASE TYPE 1 GAMMA; PHOSPHATIDYLINOSITOL 4 PHOSPHATE KINASE; UNCLASSIFIED DRUG;

EID: 84877625957     PISSN: 09699961     EISSN: 1095953X     Source Type: Journal    
DOI: 10.1016/j.nbd.2013.03.004     Document Type: Article
Times cited : (49)

References (66)
  • 1
    • 70549106846 scopus 로고    scopus 로고
    • Amyloid-beta as a positive endogenous regulator of release probability at hippocampal synapses
    • Abramov E., et al. Amyloid-beta as a positive endogenous regulator of release probability at hippocampal synapses. Nat. Neurosci. 2009, 12:1567-1576.
    • (2009) Nat. Neurosci. , vol.12 , pp. 1567-1576
    • Abramov, E.1
  • 2
    • 33644954146 scopus 로고    scopus 로고
    • Amino acid sequence motifs and mechanistic features of the membrane translocation of alpha-synuclein
    • Ahn K.J., et al. Amino acid sequence motifs and mechanistic features of the membrane translocation of alpha-synuclein. J. Neurochem. 2006, 97:265-279.
    • (2006) J. Neurochem. , vol.97 , pp. 265-279
    • Ahn, K.J.1
  • 3
    • 38049180885 scopus 로고    scopus 로고
    • Single-vesicle imaging reveals that synaptic vesicle exocytosis and endocytosis are coupled by a single stochastic mode
    • Balaji J., Ryan T.A. Single-vesicle imaging reveals that synaptic vesicle exocytosis and endocytosis are coupled by a single stochastic mode. Proc. Natl. Acad. Sci. U. S. A. 2007, 104:20576-20581.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 20576-20581
    • Balaji, J.1    Ryan, T.A.2
  • 4
    • 42649090113 scopus 로고    scopus 로고
    • Oligomeric amyloid-beta peptide disrupts phosphatidylinositol-4,5-bisphosphate metabolism
    • Berman D.E., et al. Oligomeric amyloid-beta peptide disrupts phosphatidylinositol-4,5-bisphosphate metabolism. Nat. Neurosci. 2008, 11:547-554.
    • (2008) Nat. Neurosci. , vol.11 , pp. 547-554
    • Berman, D.E.1
  • 5
    • 14644442872 scopus 로고    scopus 로고
    • Intraneuronal Abeta causes the onset of early Alzheimer's disease-related cognitive deficits in transgenic mice
    • Billings L.M., et al. Intraneuronal Abeta causes the onset of early Alzheimer's disease-related cognitive deficits in transgenic mice. Neuron 2005, 45:675-688.
    • (2005) Neuron , vol.45 , pp. 675-688
    • Billings, L.M.1
  • 6
    • 34548860902 scopus 로고    scopus 로고
    • Studying vesicle cycling in presynaptic terminals using the genetically encoded probe synaptopHluorin
    • Burrone J., et al. Studying vesicle cycling in presynaptic terminals using the genetically encoded probe synaptopHluorin. Nat. Protoc. 2006, 1:2970-2978.
    • (2006) Nat. Protoc. , vol.1 , pp. 2970-2978
    • Burrone, J.1
  • 7
    • 34249696007 scopus 로고    scopus 로고
    • Rapid, concurrent alterations in pre- and postsynaptic structure induced by naturally-secreted amyloid-beta protein
    • Calabrese B., et al. Rapid, concurrent alterations in pre- and postsynaptic structure induced by naturally-secreted amyloid-beta protein. Mol. Cell. Neurosci. 2007, 35:183-193.
    • (2007) Mol. Cell. Neurosci. , vol.35 , pp. 183-193
    • Calabrese, B.1
  • 8
    • 34147112878 scopus 로고    scopus 로고
    • Beta-amyloid causes downregulation of calcineurin in neurons through induction of oxidative stress
    • Celsi F., et al. Beta-amyloid causes downregulation of calcineurin in neurons through induction of oxidative stress. Neurobiol. Dis. 2007, 26:342-352.
    • (2007) Neurobiol. Dis. , vol.26 , pp. 342-352
    • Celsi, F.1
  • 9
    • 0034934782 scopus 로고    scopus 로고
    • Glutamate regulates actin-based motility in axonal filopodia
    • Chang S., De Camilli P. Glutamate regulates actin-based motility in axonal filopodia. Nat. Neurosci. 2001, 4:787-793.
    • (2001) Nat. Neurosci. , vol.4 , pp. 787-793
    • Chang, S.1    De Camilli, P.2
  • 10
    • 2442711560 scopus 로고    scopus 로고
    • Fyn kinase modulates synaptotoxicity, but not aberrant sprouting, in human amyloid precursor protein transgenic mice
    • Chin J., et al. Fyn kinase modulates synaptotoxicity, but not aberrant sprouting, in human amyloid precursor protein transgenic mice. J. Neurosci. 2004, 24:4692-4697.
    • (2004) J. Neurosci. , vol.24 , pp. 4692-4697
    • Chin, J.1
  • 11
    • 16644379264 scopus 로고    scopus 로고
    • Natural oligomers of the amyloid-beta protein specifically disrupt cognitive function
    • Cleary J.P., et al. Natural oligomers of the amyloid-beta protein specifically disrupt cognitive function. Nat. Neurosci. 2005, 8:79-84.
    • (2005) Nat. Neurosci. , vol.8 , pp. 79-84
    • Cleary, J.P.1
  • 12
    • 33749826587 scopus 로고    scopus 로고
    • P25/cyclin-dependent kinase 5 induces production and intraneuronal accumulation of amyloid beta in vivo
    • Cruz J.C., et al. p25/cyclin-dependent kinase 5 induces production and intraneuronal accumulation of amyloid beta in vivo. J. Neurosci. 2006, 26:10536-10541.
    • (2006) J. Neurosci. , vol.26 , pp. 10536-10541
    • Cruz, J.C.1
  • 13
    • 0037200117 scopus 로고    scopus 로고
    • Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability
    • Dahlgren K.N., et al. Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability. J. Biol. Chem. 2002, 277:32046-32053.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32046-32053
    • Dahlgren, K.N.1
  • 14
    • 77049173124 scopus 로고
    • Quantal components of the end-plate potential
    • Del Castillo J., Katz B. Quantal components of the end-plate potential. J. Physiol. 1954, 124:560-573.
    • (1954) J. Physiol. , vol.124 , pp. 560-573
    • Del Castillo, J.1    Katz, B.2
  • 15
    • 20444496481 scopus 로고    scopus 로고
    • Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers
    • Demuro A., et al. Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. J. Biol. Chem. 2005, 280:17294-17300.
    • (2005) J. Biol. Chem. , vol.280 , pp. 17294-17300
    • Demuro, A.1
  • 16
    • 4644262299 scopus 로고    scopus 로고
    • Impaired PtdIns(4,5)P2 synthesis in nerve terminals produces defects in synaptic vesicle trafficking
    • Di Paolo G., et al. Impaired PtdIns(4,5)P2 synthesis in nerve terminals produces defects in synaptic vesicle trafficking. Nature 2004, 431:415-422.
    • (2004) Nature , vol.431 , pp. 415-422
    • Di Paolo, G.1
  • 17
    • 70350218812 scopus 로고    scopus 로고
    • Molecular circuitry of endocytosis at nerve terminals
    • Dittman J., Ryan T.A. Molecular circuitry of endocytosis at nerve terminals. Annu. Rev. Cell Dev. Biol. 2009, 25:133-160.
    • (2009) Annu. Rev. Cell Dev. Biol. , vol.25 , pp. 133-160
    • Dittman, J.1    Ryan, T.A.2
  • 18
    • 0036240395 scopus 로고    scopus 로고
    • Immunization reverses memory deficits without reducing brain Abeta burden in Alzheimer's disease model
    • Dodart J.C., et al. Immunization reverses memory deficits without reducing brain Abeta burden in Alzheimer's disease model. Nat. Neurosci. 2002, 5:452-457.
    • (2002) Nat. Neurosci. , vol.5 , pp. 452-457
    • Dodart, J.C.1
  • 19
    • 57649205381 scopus 로고    scopus 로고
    • The role of endocytosis in regulating the strength of hippocampal synapses
    • Granseth B., Lagnado L. The role of endocytosis in regulating the strength of hippocampal synapses. J. Physiol. 2008, 586:5969-5982.
    • (2008) J. Physiol. , vol.586 , pp. 5969-5982
    • Granseth, B.1    Lagnado, L.2
  • 20
    • 33748576937 scopus 로고    scopus 로고
    • Clathrin-mediated endocytosis is the dominant mechanism of vesicle retrieval at hippocampal synapses
    • Granseth B., et al. Clathrin-mediated endocytosis is the dominant mechanism of vesicle retrieval at hippocampal synapses. Neuron 2006, 51:773-786.
    • (2006) Neuron , vol.51 , pp. 773-786
    • Granseth, B.1
  • 21
    • 47749095383 scopus 로고    scopus 로고
    • Linking calcium to Abeta and Alzheimer's disease
    • Green K.N., LaFerla F.M. Linking calcium to Abeta and Alzheimer's disease. Neuron 2008, 59:190-194.
    • (2008) Neuron , vol.59 , pp. 190-194
    • Green, K.N.1    LaFerla, F.M.2
  • 22
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide
    • Haass C., Selkoe D.J. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nat. Rev. Mol. Cell Biol. 2007, 8:101-112.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 23
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics
    • Hardy J., Selkoe D.J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 2002, 297:353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 24
    • 33845411954 scopus 로고    scopus 로고
    • AMPAR removal underlies Abeta-induced synaptic depression and dendritic spine loss
    • Hsieh H., et al. AMPAR removal underlies Abeta-induced synaptic depression and dendritic spine loss. Neuron 2006, 52:831-843.
    • (2006) Neuron , vol.52 , pp. 831-843
    • Hsieh, H.1
  • 25
    • 28444452974 scopus 로고    scopus 로고
    • Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins
    • Itoh T., et al. Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins. Dev. Cell 2005, 9:791-804.
    • (2005) Dev. Cell , vol.9 , pp. 791-804
    • Itoh, T.1
  • 26
    • 34249935856 scopus 로고    scopus 로고
    • Beta-amyloid disrupted synaptic vesicle endocytosis in cultured hippocampal neurons
    • Kelly B.L., Ferreira A. Beta-amyloid disrupted synaptic vesicle endocytosis in cultured hippocampal neurons. Neuroscience 2007, 147:60-70.
    • (2007) Neuroscience , vol.147 , pp. 60-70
    • Kelly, B.L.1    Ferreira, A.2
  • 27
    • 77956314453 scopus 로고    scopus 로고
    • CDK5 serves as a major control point in neurotransmitter release
    • Kim S.H., Ryan T.A. CDK5 serves as a major control point in neurotransmitter release. Neuron 2010, 67:797-809.
    • (2010) Neuron , vol.67 , pp. 797-809
    • Kim, S.H.1    Ryan, T.A.2
  • 28
    • 0037168590 scopus 로고    scopus 로고
    • Delayed reentry of recycling vesicles into the fusion-competent synaptic vesicle pool in synaptojanin 1 knockout mice
    • Kim W.T., et al. Delayed reentry of recycling vesicles into the fusion-competent synaptic vesicle pool in synaptojanin 1 knockout mice. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:17143-17148.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 17143-17148
    • Kim, W.T.1
  • 29
    • 33845651694 scopus 로고    scopus 로고
    • Regulation of transferrin recycling kinetics by PtdIns[4,5]P2 availability
    • Kim S., et al. Regulation of transferrin recycling kinetics by PtdIns[4,5]P2 availability. FASEB J. 2006, 20:2399-2401.
    • (2006) FASEB J. , vol.20 , pp. 2399-2401
    • Kim, S.1
  • 30
    • 21044453723 scopus 로고    scopus 로고
    • Amyloid beta protein immunotherapy neutralizes Abeta oligomers that disrupt synaptic plasticity in vivo
    • Klyubin I., et al. Amyloid beta protein immunotherapy neutralizes Abeta oligomers that disrupt synaptic plasticity in vivo. Nat. Med. 2005, 11:556-561.
    • (2005) Nat. Med. , vol.11 , pp. 556-561
    • Klyubin, I.1
  • 31
    • 0036703483 scopus 로고    scopus 로고
    • Reversible memory loss in a mouse transgenic model of Alzheimer's disease
    • Kotilinek L.A., et al. Reversible memory loss in a mouse transgenic model of Alzheimer's disease. J. Neurosci. 2002, 22:6331-6335.
    • (2002) J. Neurosci. , vol.22 , pp. 6331-6335
    • Kotilinek, L.A.1
  • 32
    • 11544279355 scopus 로고    scopus 로고
    • Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins
    • Lambert M.P., et al. Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins. Proc. Natl. Acad. Sci. U. S. A. 1998, 95:6448-6453.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 6448-6453
    • Lambert, M.P.1
  • 33
    • 61349201380 scopus 로고    scopus 로고
    • Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers
    • Lauren J., et al. Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers. Nature 2009, 457:1128-1132.
    • (2009) Nature , vol.457 , pp. 1128-1132
    • Lauren, J.1
  • 34
    • 0034682414 scopus 로고    scopus 로고
    • Neurotoxicity induces cleavage of p35 to p25 by calpain
    • Lee M.S., et al. Neurotoxicity induces cleavage of p35 to p25 by calpain. Nature 2000, 405:360-364.
    • (2000) Nature , vol.405 , pp. 360-364
    • Lee, M.S.1
  • 35
    • 0034940160 scopus 로고    scopus 로고
    • Neurodegenerative tauopathies
    • Lee V.M., et al. Neurodegenerative tauopathies. Annu. Rev. Neurosci. 2001, 24:1121-1159.
    • (2001) Annu. Rev. Neurosci. , vol.24 , pp. 1121-1159
    • Lee, V.M.1
  • 36
    • 33750208648 scopus 로고    scopus 로고
    • SPIN90/WISH interacts with PSD-95 and regulates dendritic spinogenesis via an N-WASP-independent mechanism
    • Lee S., et al. SPIN90/WISH interacts with PSD-95 and regulates dendritic spinogenesis via an N-WASP-independent mechanism. EMBO J. 2006, 25:4983-4995.
    • (2006) EMBO J. , vol.25 , pp. 4983-4995
    • Lee, S.1
  • 37
    • 44749083979 scopus 로고    scopus 로고
    • Assembly-dependent endocytosis and clearance of extracellular alpha-synuclein
    • Lee H.J., et al. Assembly-dependent endocytosis and clearance of extracellular alpha-synuclein. Int. J. Biochem. Cell Biol. 2008, 40:1835-1849.
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 1835-1849
    • Lee, H.J.1
  • 38
    • 0032590054 scopus 로고    scopus 로고
    • Soluble pool of Abeta amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease
    • McLean C.A., et al. Soluble pool of Abeta amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease. Ann. Neurol. 1999, 46:860-866.
    • (1999) Ann. Neurol. , vol.46 , pp. 860-866
    • McLean, C.A.1
  • 39
    • 0032500053 scopus 로고    scopus 로고
    • Visualizing secretion and synaptic transmission with pH-sensitive green fluorescent proteins
    • Miesenbock G., et al. Visualizing secretion and synaptic transmission with pH-sensitive green fluorescent proteins. Nature 1998, 394:192-195.
    • (1998) Nature , vol.394 , pp. 192-195
    • Miesenbock, G.1
  • 40
    • 65249174019 scopus 로고    scopus 로고
    • Synaptic transmission block by presynaptic injection of oligomeric amyloid beta
    • Moreno H., et al. Synaptic transmission block by presynaptic injection of oligomeric amyloid beta. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:5901-5906.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 5901-5906
    • Moreno, H.1
  • 41
    • 0042858417 scopus 로고    scopus 로고
    • Cell biology of the presynaptic terminal
    • Murthy V.N., De Camilli P. Cell biology of the presynaptic terminal. Annu. Rev. Neurosci. 2003, 26:701-728.
    • (2003) Annu. Rev. Neurosci. , vol.26 , pp. 701-728
    • Murthy, V.N.1    De Camilli, P.2
  • 42
    • 0033361973 scopus 로고    scopus 로고
    • Reversal of synaptic vesicle docking at central synapses
    • Murthy V.N., Stevens C.F. Reversal of synaptic vesicle docking at central synapses. Nat. Neurosci. 1999, 2:503-507.
    • (1999) Nat. Neurosci. , vol.2 , pp. 503-507
    • Murthy, V.N.1    Stevens, C.F.2
  • 43
    • 38549141544 scopus 로고    scopus 로고
    • Amyloid beta oligomers (A beta(1-42) globulomer) suppress spontaneous synaptic activity by inhibition of P/Q-type calcium currents
    • Nimmrich V., et al. Amyloid beta oligomers (A beta(1-42) globulomer) suppress spontaneous synaptic activity by inhibition of P/Q-type calcium currents. J. Neurosci. 2008, 28:788-797.
    • (2008) J. Neurosci. , vol.28 , pp. 788-797
    • Nimmrich, V.1
  • 44
    • 78650064098 scopus 로고    scopus 로고
    • Phospholipase d2 ablation ameliorates Alzheimer's disease-linked synaptic dysfunction and cognitive deficits
    • Oliveira T.G., et al. Phospholipase d2 ablation ameliorates Alzheimer's disease-linked synaptic dysfunction and cognitive deficits. J. Neurosci. 2010, 30:16419-16428.
    • (2010) J. Neurosci. , vol.30 , pp. 16419-16428
    • Oliveira, T.G.1
  • 45
    • 77954132249 scopus 로고    scopus 로고
    • Amyloid-beta-induced neuronal dysfunction in Alzheimer's disease: from synapses toward neural networks
    • Palop J.J., Mucke L. Amyloid-beta-induced neuronal dysfunction in Alzheimer's disease: from synapses toward neural networks. Nat. Neurosci. 2010, 13:812-818.
    • (2010) Nat. Neurosci. , vol.13 , pp. 812-818
    • Palop, J.J.1    Mucke, L.2
  • 46
    • 0033540060 scopus 로고    scopus 로고
    • Conversion of p35 to p25 deregulates Cdk5 activity and promotes neurodegeneration
    • Patrick G.N., et al. Conversion of p35 to p25 deregulates Cdk5 activity and promotes neurodegeneration. Nature 1999, 402:615-622.
    • (1999) Nature , vol.402 , pp. 615-622
    • Patrick, G.N.1
  • 47
    • 0742288598 scopus 로고    scopus 로고
    • The dynamin superfamily: universal membrane tubulation and fission molecules?
    • Praefcke G.J., McMahon H.T. The dynamin superfamily: universal membrane tubulation and fission molecules?. Nat. Rev. Mol. Cell Biol. 2004, 5:133-147.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 133-147
    • Praefcke, G.J.1    McMahon, H.T.2
  • 48
    • 58149385218 scopus 로고    scopus 로고
    • Picomolar amyloid-beta positively modulates synaptic plasticity and memory in hippocampus
    • Puzzo D., et al. Picomolar amyloid-beta positively modulates synaptic plasticity and memory in hippocampus. J. Neurosci. 2008, 28:14537-14545.
    • (2008) J. Neurosci. , vol.28 , pp. 14537-14545
    • Puzzo, D.1
  • 49
    • 80052150240 scopus 로고    scopus 로고
    • S-Nitrosylation activates Cdk5 and contributes to synaptic spine loss induced by beta-amyloid peptide
    • Qu J., et al. S-Nitrosylation activates Cdk5 and contributes to synaptic spine loss induced by beta-amyloid peptide. Proc. Natl. Acad. Sci. U. S. A. 2011, 108:14330-14335.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 14330-14335
    • Qu, J.1
  • 50
    • 33745026786 scopus 로고    scopus 로고
    • GTP-dependent twisting of dynamin implicates constriction and tension in membrane fission
    • Roux A., et al. GTP-dependent twisting of dynamin implicates constriction and tension in membrane fission. Nature 2006, 441:528-531.
    • (2006) Nature , vol.441 , pp. 528-531
    • Roux, A.1
  • 51
    • 0029062202 scopus 로고
    • Vesicle pool mobilization during action potential firing at hippocampal synapses
    • Ryan T.A., Smith S.J. Vesicle pool mobilization during action potential firing at hippocampal synapses. Neuron 1995, 14:983-989.
    • (1995) Neuron , vol.14 , pp. 983-989
    • Ryan, T.A.1    Smith, S.J.2
  • 52
    • 0033786834 scopus 로고    scopus 로고
    • Real-time measurements of vesicle-SNARE recycling in synapses of the central nervous system
    • Sankaranarayanan S., Ryan T.A. Real-time measurements of vesicle-SNARE recycling in synapses of the central nervous system. Nat. Cell Biol. 2000, 2:197-204.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 197-204
    • Sankaranarayanan, S.1    Ryan, T.A.2
  • 53
    • 0035146137 scopus 로고    scopus 로고
    • Calcium accelerates endocytosis of vSNAREs at hippocampal synapses
    • Sankaranarayanan S., Ryan T.A. Calcium accelerates endocytosis of vSNAREs at hippocampal synapses. Nat. Neurosci. 2001, 4:129-136.
    • (2001) Nat. Neurosci. , vol.4 , pp. 129-136
    • Sankaranarayanan, S.1    Ryan, T.A.2
  • 54
    • 0033803597 scopus 로고    scopus 로고
    • The use of pHluorins for optical measurements of presynaptic activity
    • Sankaranarayanan S., et al. The use of pHluorins for optical measurements of presynaptic activity. Biophys. J. 2000, 79:2199-2208.
    • (2000) Biophys. J. , vol.79 , pp. 2199-2208
    • Sankaranarayanan, S.1
  • 55
    • 0035095914 scopus 로고    scopus 로고
    • Morphological correlates of functionally defined synaptic vesicle populations
    • Schikorski T., Stevens C.F. Morphological correlates of functionally defined synaptic vesicle populations. Nat. Neurosci. 2001, 4:391-395.
    • (2001) Nat. Neurosci. , vol.4 , pp. 391-395
    • Schikorski, T.1    Stevens, C.F.2
  • 56
    • 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 G.M., et al. Natural oligomers of the Alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway. J. Neurosci. 2007, 27:2866-2875.
    • (2007) J. Neurosci. , vol.27 , pp. 2866-2875
    • Shankar, G.M.1
  • 57
    • 35348988598 scopus 로고    scopus 로고
    • Sorting nexin 9 interacts with dynamin 1 and N-WASP and coordinates synaptic vesicle endocytosis
    • Shin N., et al. Sorting nexin 9 interacts with dynamin 1 and N-WASP and coordinates synaptic vesicle endocytosis. J. Biol. Chem. 2007, 282:28939-28950.
    • (2007) J. Biol. Chem. , vol.282 , pp. 28939-28950
    • Shin, N.1
  • 58
    • 23044445669 scopus 로고    scopus 로고
    • Regulation of NMDA receptor trafficking by amyloid-beta
    • Snyder E.M., et al. Regulation of NMDA receptor trafficking by amyloid-beta. Nat. Neurosci. 2005, 8:1051-1058.
    • (2005) Nat. Neurosci. , vol.8 , pp. 1051-1058
    • Snyder, E.M.1
  • 59
    • 0035446006 scopus 로고    scopus 로고
    • Clathrin-mediated endocytosis: membrane factors pull the trigger
    • Takei K., Haucke V. Clathrin-mediated endocytosis: membrane factors pull the trigger. Trends Cell Biol. 2001, 11:385-391.
    • (2001) Trends Cell Biol. , vol.11 , pp. 385-391
    • Takei, K.1    Haucke, V.2
  • 60
    • 0033130119 scopus 로고    scopus 로고
    • Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis
    • Takei K., et al. Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis. Nat. Cell Biol. 1999, 1:33-39.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 33-39
    • Takei, K.1
  • 61
    • 84866065959 scopus 로고    scopus 로고
    • Alzheimer amyloid-beta oligomer bound to postsynaptic prion protein activates Fyn to impair neurons
    • Um J.W., et al. Alzheimer amyloid-beta oligomer bound to postsynaptic prion protein activates Fyn to impair neurons. Nat. Neurosci. 2012, 15:1227-1235.
    • (2012) Nat. Neurosci. , vol.15 , pp. 1227-1235
    • Um, J.W.1
  • 62
    • 33745494172 scopus 로고    scopus 로고
    • Distinct endocytic pathways control the rate and extent of synaptic vesicle protein recycling
    • Voglmaier S.M., et al. Distinct endocytic pathways control the rate and extent of synaptic vesicle protein recycling. Neuron 2006, 51:71-84.
    • (2006) Neuron , vol.51 , pp. 71-84
    • Voglmaier, S.M.1
  • 63
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh D.M., et al. Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 2002, 416:535-539.
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1
  • 64
    • 0036669881 scopus 로고    scopus 로고
    • Amyloid-beta oligomers: their production, toxicity and therapeutic inhibition
    • Walsh D.M., et al. Amyloid-beta oligomers: their production, toxicity and therapeutic inhibition. Biochem. Soc. Trans. 2002, 30:552-557.
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 552-557
    • Walsh, D.M.1
  • 65
    • 0034740730 scopus 로고    scopus 로고
    • PIP kinase Igamma is the major PI(4,5)P(2) synthesizing enzyme at the synapse
    • Wenk M.R., et al. PIP kinase Igamma is the major PI(4,5)P(2) synthesizing enzyme at the synapse. Neuron 2001, 32:79-88.
    • (2001) Neuron , vol.32 , pp. 79-88
    • Wenk, M.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.