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Volumn 6, Issue , 2015, Pages

Aβ-dependent reduction of NCAM2-mediated synaptic adhesion contributes to synapse loss in Alzheimer's disease

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; NERVE CELL ADHESION MOLECULE; NEURAL CELL ADHESION MOLECULE 2; UNCLASSIFIED DRUG; AMPA RECEPTOR; AMYLOID PRECURSOR PROTEIN; GLUTAMATE RECEPTOR IONOTROPIC, AMPA 1; NCAM2 PROTEIN, HUMAN; NCAM2 PROTEIN, MOUSE; NERVE CELL ADHESION MOLECULE L1;

EID: 84948689255     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms9836     Document Type: Article
Times cited : (69)

References (51)
  • 1
    • 0037175399 scopus 로고    scopus 로고
    • Neural cell adhesion molecule promotes accumulation of TGN organelles at sites of neuron-to-neuron contacts
    • Sytnyk, V. et al. Neural cell adhesion molecule promotes accumulation of TGN organelles at sites of neuron-to-neuron contacts. J. Cell Biol. 159, 649-661 (2002).
    • (2002) J. Cell Biol. , vol.159 , pp. 649-661
    • Sytnyk, V.1
  • 2
    • 77951162263 scopus 로고    scopus 로고
    • The architecture of an excitatory synapse
    • Chua, J. J., Kindler, S., Boyken, J. & Jahn, R. The architecture of an excitatory synapse. J. Cell Sci. 123, 819-823 (2010).
    • (2010) J. Cell Sci. , vol.123 , pp. 819-823
    • Chua, J.J.1    Kindler, S.2    Boyken, J.3    Jahn, R.4
  • 3
    • 84863454160 scopus 로고    scopus 로고
    • Synapse adhesion: A dynamic equilibrium conferring stability and flexibility
    • Benson, D. L. & Huntley, G. W. Synapse adhesion: a dynamic equilibrium conferring stability and flexibility. Curr. Opin. Neurobiol. 22, 397-404 (2012).
    • (2012) Curr. Opin. Neurobiol. , vol.22 , pp. 397-404
    • Benson, D.L.1    Huntley, G.W.2
  • 4
    • 7044254722 scopus 로고    scopus 로고
    • Polysialylated neural cell adhesion molecule promotes remodeling and formation of hippocampal synapses
    • Dityatev, A. et al. Polysialylated neural cell adhesion molecule promotes remodeling and formation of hippocampal synapses. J. Neurosci. 24, 9372-9382 (2004).
    • (2004) J. Neurosci. , vol.24 , pp. 9372-9382
    • Dityatev, A.1
  • 5
    • 33744535466 scopus 로고    scopus 로고
    • Cell adhesion molecules at the synapse
    • Gerrow, K. & El-Husseini, A. Cell adhesion molecules at the synapse. Front. Biosci. 11, 2400-2419 (2006).
    • (2006) Front. Biosci. , vol.11 , pp. 2400-2419
    • Gerrow, K.1    El-Husseini, A.2
  • 6
    • 33749037455 scopus 로고    scopus 로고
    • NCAM promotes assembly and activity-dependent remodeling of the postsynaptic signaling complex
    • Sytnyk, V., Leshchyns'ka, I., Nikonenko, A. G. & Schachner, M. NCAM promotes assembly and activity-dependent remodeling of the postsynaptic signaling complex. J. Cell Biol. 174, 1071-1085 (2006).
    • (2006) J. Cell Biol. , vol.174 , pp. 1071-1085
    • Sytnyk, V.1    Leshchyns'Ka, I.2    Nikonenko, A.G.3    Schachner, M.4
  • 7
    • 80052754261 scopus 로고    scopus 로고
    • NCAM/spectrin complex disassembly results in PSD perforation and postsynaptic endocytic zone formation
    • Puchkov, D., Leshchyns'ka, I., Nikonenko, A. G., Schachner, M. & Sytnyk, V. NCAM/spectrin complex disassembly results in PSD perforation and postsynaptic endocytic zone formation. Cereb. Cortex 21, 2217-2232 (2011).
    • (2011) Cereb. Cortex , vol.21 , pp. 2217-2232
    • Puchkov, D.1    Leshchyns'Ka, I.2    Nikonenko, A.G.3    Schachner, M.4    Sytnyk, V.5
  • 8
    • 33847119026 scopus 로고    scopus 로고
    • Cell adhesion molecules: Signalling functions at the synapse
    • Dalva, M. B., McClelland, A. C. & Kayser, M. S. Cell adhesion molecules: signalling functions at the synapse. Nat. Rev. Neurosci. 8, 206-220 (2007).
    • (2007) Nat. Rev. Neurosci. , vol.8 , pp. 206-220
    • Dalva, M.B.1    McClelland, A.C.2    Kayser, M.S.3
  • 9
    • 70449704590 scopus 로고    scopus 로고
    • Modulation of synaptic transmission and plasticity by cell adhesion and repulsion molecules
    • Dityatev, A., Bukalo, O. & Schachner, M. Modulation of synaptic transmission and plasticity by cell adhesion and repulsion molecules. Neuron Glia Biol. 4, 197-209 (2008).
    • (2008) Neuron Glia Biol. , vol.4 , pp. 197-209
    • Dityatev, A.1    Bukalo, O.2    Schachner, M.3
  • 10
    • 54049091941 scopus 로고    scopus 로고
    • Neuroligins and neurexins link synaptic function to cognitive disease
    • Sudhof, T. C. Neuroligins and neurexins link synaptic function to cognitive disease. Nature 455, 903-911 (2008).
    • (2008) Nature , vol.455 , pp. 903-911
    • Sudhof, T.C.1
  • 11
    • 0345276568 scopus 로고    scopus 로고
    • Synaptic pathology in Alzheimer's disease: A review of ultrastructural studies
    • Scheff, S. W. & Price, D. A. Synaptic pathology in Alzheimer's disease: a review of ultrastructural studies. Neurobiol. Aging 24, 1029-1046 (2003).
    • (2003) Neurobiol. Aging , vol.24 , pp. 1029-1046
    • Scheff, S.W.1    Price, D.A.2
  • 12
    • 85027929889 scopus 로고    scopus 로고
    • Abeta oligomer-induced synapse degeneration in Alzheimer's disease
    • Wilcox, K. C., Lacor, P. N., Pitt, J. & Klein, W. L. Abeta oligomer-induced synapse degeneration in Alzheimer's disease. Cell. Mol. Neurobiol. 31, 939-948 (2011).
    • (2011) Cell. Mol. Neurobiol. , vol.31 , pp. 939-948
    • Wilcox, K.C.1    Lacor, P.N.2    Pitt, J.3    Klein, W.L.4
  • 13
    • 33846633336 scopus 로고    scopus 로고
    • Abeta oligomer-induced aberrations in synapse composition, shape, and density provide a molecular basis for loss of connectivity in Alzheimer's disease
    • Lacor, P. N. et al. Abeta oligomer-induced aberrations in synapse composition, shape, and density provide a molecular basis for loss of connectivity in Alzheimer's disease. J. Neurosci. 27, 796-807 (2007).
    • (2007) J. Neurosci. , vol.27 , pp. 796-807
    • Lacor, P.N.1
  • 14
    • 77954358003 scopus 로고    scopus 로고
    • Progressive accumulation of amyloid-beta oligomers in Alzheimer's disease and in amyloid precursor protein transgenic mice is accompanied by selective alterations in synaptic scaffold proteins
    • Pham, E. et al. Progressive accumulation of amyloid-beta oligomers in Alzheimer's disease and in amyloid precursor protein transgenic mice is accompanied by selective alterations in synaptic scaffold proteins. FEBS J. 277, 3051-3067 (2010).
    • (2010) FEBS J. , vol.277 , pp. 3051-3067
    • Pham, E.1
  • 15
    • 0030746609 scopus 로고    scopus 로고
    • OCAM: A new member of the neural cell adhesion molecule family related to zone-to-zone projection of olfactory and vomeronasal axons
    • Yoshihara, Y. et al. OCAM: a new member of the neural cell adhesion molecule family related to zone-to-zone projection of olfactory and vomeronasal axons. J. Neurosci. 17, 5830-5842 (1997).
    • (1997) J. Neurosci. , vol.17 , pp. 5830-5842
    • Yoshihara, Y.1
  • 16
    • 79551696709 scopus 로고    scopus 로고
    • Structural model and trans-interaction of the entire ectodomain of the olfactory cell adhesion molecule
    • Kulahin, N. et al. Structural model and trans-interaction of the entire ectodomain of the olfactory cell adhesion molecule. Structure 19, 203-211 (2011).
    • (2011) Structure , vol.19 , pp. 203-211
    • Kulahin, N.1
  • 17
    • 0031193390 scopus 로고    scopus 로고
    • Cloning of a novel human neural cell adhesion molecule gene (NCAM2) that maps to chromosome region 21q21 and is potentially involved in Down syndrome
    • Paoloni-Giacobino, A., Chen, H. & Antonarakis, S. E. Cloning of a novel human neural cell adhesion molecule gene (NCAM2) that maps to chromosome region 21q21 and is potentially involved in Down syndrome. Genomics 43, 43-51 (1997).
    • (1997) Genomics , vol.43 , pp. 43-51
    • Paoloni-Giacobino, A.1    Chen, H.2    Antonarakis, S.E.3
  • 18
    • 33744986689 scopus 로고    scopus 로고
    • Disrupted compartmental organization of axons and dendrites within olfactory glomeruli of mice deficient in the olfactory cell adhesion molecule, OCAM
    • Walz, A., Mombaerts, P., Greer, C. A. & Treloar, H. B. Disrupted compartmental organization of axons and dendrites within olfactory glomeruli of mice deficient in the olfactory cell adhesion molecule, OCAM. Mol. Cell. Neurosci. 32, 1-14 (2006).
    • (2006) Mol. Cell. Neurosci. , vol.32 , pp. 1-14
    • Walz, A.1    Mombaerts, P.2    Greer, C.A.3    Treloar, H.B.4
  • 19
    • 84921894913 scopus 로고    scopus 로고
    • Neural cell adhesion molecule 2 promotes the formation of filopodia and neurite branching by inducing submembrane increases in Ca2 levels
    • Sheng, L., Leshchyns'ka, I. & Sytnyk, V. Neural cell adhesion molecule 2 promotes the formation of filopodia and neurite branching by inducing submembrane increases in Ca2 levels. J. Neurosci. 35, 1739-1752 (2015).
    • (2015) J. Neurosci. , vol.35 , pp. 1739-1752
    • Sheng, L.1    Leshchyns'Ka, I.2    Sytnyk, V.3
  • 20
    • 33846533244 scopus 로고    scopus 로고
    • The DYRK1A gene, encoded in chromosome 21 Down syndrome critical region, bridges between beta-amyloid production and tau phosphorylation in Alzheimer disease
    • Kimura, R. et al. The DYRK1A gene, encoded in chromosome 21 Down syndrome critical region, bridges between beta-amyloid production and tau phosphorylation in Alzheimer disease. Hum. Mol. Genet. 16, 15-23 (2007).
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 15-23
    • Kimura, R.1
  • 21
    • 77957597251 scopus 로고    scopus 로고
    • Genome-wide association reveals genetic effects on human Abeta42 and tau protein levels in cerebrospinal fluids: A case control study
    • Han, M. R., Schellenberg, G. D. & Wang, L. S. Genome-wide association reveals genetic effects on human Abeta42 and tau protein levels in cerebrospinal fluids: a case control study. BMC Neurol. 10, 90 (2010).
    • (2010) BMC Neurol. , vol.10 , pp. 90
    • Han, M.R.1    Schellenberg, G.D.2    Wang, L.S.3
  • 22
    • 84922768905 scopus 로고    scopus 로고
    • IgLON cell adhesion molecules are shed from the cell surface of cortical neurons to promote neuronal growth
    • Sanz, R., Ferraro, G. B. & Fournier, A. E. IgLON cell adhesion molecules are shed from the cell surface of cortical neurons to promote neuronal growth. J. Biol. Chem. 290, 4330-4342 (2015).
    • (2015) J. Biol. Chem. , vol.290 , pp. 4330-4342
    • Sanz, R.1    Ferraro, G.B.2    Fournier, A.E.3
  • 23
    • 0037422540 scopus 로고    scopus 로고
    • Amyloid beta-protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways
    • Bitan, G. et al. Amyloid beta-protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways. Proc. Natl Acad. Sci. USA 100, 330-335 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 330-335
    • Bitan, G.1
  • 24
    • 77951975748 scopus 로고    scopus 로고
    • Structural conversion of neurotoxic amyloid-beta(1-42) oligomers to fibrils
    • Ahmed, M. et al. Structural conversion of neurotoxic amyloid-beta(1-42) oligomers to fibrils. Nat. Struct. Mol. Biol. 17, 561-567 (2010).
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 561-567
    • Ahmed, M.1
  • 25
    • 84872142073 scopus 로고    scopus 로고
    • Neuron loss in the 5XFAD mouse model of Alzheimer's disease correlates with intraneuronal Abeta42 accumulation and Caspase-3 activation
    • Eimer, W. A. & Vassar, R. Neuron loss in the 5XFAD mouse model of Alzheimer's disease correlates with intraneuronal Abeta42 accumulation and Caspase-3 activation. Mol. Neurodegener. 8, 2 (2013).
    • (2013) Mol. Neurodegener. , vol.8 , pp. 2
    • Eimer, W.A.1    Vassar, R.2
  • 26
    • 33845445238 scopus 로고    scopus 로고
    • The adhesion molecule CHL1 regulates uncoating of clathrin-coated synaptic vesicles
    • Leshchyns'ka, I. et al. The adhesion molecule CHL1 regulates uncoating of clathrin-coated synaptic vesicles. Neuron 52, 1011-1025 (2006).
    • (2006) Neuron , vol.52 , pp. 1011-1025
    • Leshchyns'Ka, I.1
  • 27
    • 77957765862 scopus 로고    scopus 로고
    • CHL1 is a selective organizer of the presynaptic machinery chaperoning the SNARE complex
    • Andreyeva, A. et al. CHL1 is a selective organizer of the presynaptic machinery chaperoning the SNARE complex. PLoS ONE 5, e12018 (2010).
    • (2010) PLoS ONE , vol.5 , pp. e12018
    • Andreyeva, A.1
  • 28
    • 0011444914 scopus 로고    scopus 로고
    • Two amyloid precursor protein transgenic mouse models with Alzheimer disease-like pathology
    • Sturchler-Pierrat, C. et al. Two amyloid precursor protein transgenic mouse models with Alzheimer disease-like pathology. Proc. Natl Acad. Sci. USA 94, 13287-13292 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 13287-13292
    • Sturchler-Pierrat, C.1
  • 29
    • 0025987048 scopus 로고
    • Physical basis of cognitive alterations in Alzheimer's disease: Synapse loss is the major correlate of cognitive impairment
    • Terry, R. D. et al. Physical basis of cognitive alterations in Alzheimer's disease: synapse loss is the major correlate of cognitive impairment. Ann. Neurol. 30, 572-580 (1991).
    • (1991) Ann. Neurol. , vol.30 , pp. 572-580
    • Terry, R.D.1
  • 30
    • 0028235419 scopus 로고
    • Synaptic and neuritic alterations during the progression of Alzheimer's disease
    • Masliah, E. et al. Synaptic and neuritic alterations during the progression of Alzheimer's disease. Neurosci. Lett. 174, 67-72 (1994).
    • (1994) Neurosci. Lett. , vol.174 , pp. 67-72
    • Masliah, E.1
  • 31
    • 0025970091 scopus 로고
    • Immunoelectron microscopic study of synaptic pathology in Alzheimer's disease
    • Masliah, E., Hansen, L., Albright, T., Mallory, M. & Terry, R. D. Immunoelectron microscopic study of synaptic pathology in Alzheimer's disease. Acta Neuropathol. 81, 428-433 (1991).
    • (1991) Acta Neuropathol. , vol.81 , pp. 428-433
    • Masliah, E.1    Hansen, L.2    Albright, T.3    Mallory, M.4    Terry, R.D.5
  • 32
    • 0037174618 scopus 로고    scopus 로고
    • Alzheimer's disease is a synaptic failure
    • Selkoe, D. J. Alzheimer's disease is a synaptic failure. Science 298, 789-791 (2002).
    • (2002) Science , vol.298 , pp. 789-791
    • Selkoe, D.J.1
  • 33
    • 0035830408 scopus 로고    scopus 로고
    • Altered expression of synaptic proteins occurs early during progression of Alzheimer's disease
    • Masliah, E. et al. Altered expression of synaptic proteins occurs early during progression of Alzheimer's disease. Neurology 56, 127-129 (2001).
    • (2001) Neurology , vol.56 , pp. 127-129
    • Masliah, E.1
  • 34
    • 23044468691 scopus 로고    scopus 로고
    • The synaptic Abeta hypothesis of Alzheimer disease
    • Tanzi, R. E. The synaptic Abeta hypothesis of Alzheimer disease. Nat. Neurosci. 8, 977-979 (2005).
    • (2005) Nat. Neurosci. , vol.8 , pp. 977-979
    • Tanzi, R.E.1
  • 36
    • 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. 15, 1227-1235 (2012).
    • (2012) Nat. Neurosci. , vol.15 , pp. 1227-1235
    • Um, J.W.1
  • 37
    • 84878156206 scopus 로고    scopus 로고
    • Adhesion molecule L1 binds to amyloid beta and reduces Alzheimer's disease pathology in mice
    • Djogo, N. et al. Adhesion molecule L1 binds to amyloid beta and reduces Alzheimer's disease pathology in mice. Neurobiol. Dis. 56, 104-115 (2013).
    • (2013) Neurobiol. Dis. , vol.56 , pp. 104-115
    • Djogo, N.1
  • 38
    • 84863342447 scopus 로고    scopus 로고
    • Selective interaction of amyloid precursor protein with different isoforms of neural cell adhesion molecule
    • Chen, K. P. & Dou, F. Selective interaction of amyloid precursor protein with different isoforms of neural cell adhesion molecule. J. Mol. Neurosci. 46, 203-209 (2012).
    • (2012) J. Mol. Neurosci. , vol.46 , pp. 203-209
    • Chen, K.P.1    Dou, F.2
  • 39
    • 40249114896 scopus 로고    scopus 로고
    • A TAG1-APP signalling pathway through Fe65 negatively modulates neurogenesis
    • Ma, Q. H. et al. A TAG1-APP signalling pathway through Fe65 negatively modulates neurogenesis. Nat. Cell Biol. 10, 283-294 (2008).
    • (2008) Nat. Cell Biol. , vol.10 , pp. 283-294
    • Ma, Q.H.1
  • 40
    • 18544376071 scopus 로고    scopus 로고
    • Prion protein recruits its neuronal receptor NCAM to lipid rafts to activate p59fyn and to enhance neurite outgrowth
    • Santuccione, A., Sytnyk, V., Leshchyns'ka, I. & Schachner, M. Prion protein recruits its neuronal receptor NCAM to lipid rafts to activate p59fyn and to enhance neurite outgrowth. J. Cell Biol. 169, 341-354 (2005).
    • (2005) J. Cell Biol. , vol.169 , pp. 341-354
    • Santuccione, A.1    Sytnyk, V.2    Leshchyns'Ka, I.3    Schachner, M.4
  • 41
    • 0025139119 scopus 로고
    • Functional cooperation between the neural adhesion molecules L1 and N-CAM is carbohydrate dependent
    • Kadmon, G., Kowitz, A., Altevogt, P. & Schachner, M. Functional cooperation between the neural adhesion molecules L1 and N-CAM is carbohydrate dependent. J. Cell Biol. 110, 209-218 (1990).
    • (1990) J. Cell Biol. , vol.110 , pp. 209-218
    • Kadmon, G.1    Kowitz, A.2    Altevogt, P.3    Schachner, M.4
  • 42
    • 33846909739 scopus 로고    scopus 로고
    • Amyloid beta inhibits ectodomain shedding of N-cadherin via down-regulation of cell-surface NMDA receptor
    • Uemura, K. et al. Amyloid beta inhibits ectodomain shedding of N-cadherin via down-regulation of cell-surface NMDA receptor. Neuroscience 145, 5-10 (2007).
    • (2007) Neuroscience , vol.145 , pp. 5-10
    • Uemura, K.1
  • 43
    • 79954420180 scopus 로고    scopus 로고
    • Amyloid-beta oligomers increase the localization of prion protein at the cell surface
    • Caetano, F. A. et al. Amyloid-beta oligomers increase the localization of prion protein at the cell surface. J. Neurochem. 117, 538-553 (2011).
    • (2011) J. Neurochem. , vol.117 , pp. 538-553
    • Caetano, F.A.1
  • 44
    • 84872076906 scopus 로고    scopus 로고
    • The neural cell adhesion molecule (NCAM) associates with and signals through p21-activated kinase 1 (Pak1)
    • Li, S., Leshchyns'ka, I., Chernyshova, Y., Schachner, M. & Sytnyk, V. The neural cell adhesion molecule (NCAM) associates with and signals through p21-activated kinase 1 (Pak1). J. Neurosci. 33, 790-803 (2013).
    • (2013) J. Neurosci. , vol.33 , pp. 790-803
    • Li, S.1    Leshchyns'Ka, I.2    Chernyshova, Y.3    Schachner, M.4    Sytnyk, V.5
  • 45
    • 84857030932 scopus 로고    scopus 로고
    • National Institute on Aging-Alzheimer's Association guidelines for the neuropathologic assessment of Alzheimer's disease: A practical approach
    • Montine, T. J. et al. National Institute on Aging-Alzheimer's Association guidelines for the neuropathologic assessment of Alzheimer's disease: a practical approach. Acta Neuropathol. 123, 1-11 (2012).
    • (2012) Acta Neuropathol. , vol.123 , pp. 1-11
    • Montine, T.J.1
  • 46
    • 84885440959 scopus 로고    scopus 로고
    • The neural cell adhesion molecule promotes maturation of the presynaptic endocytotic machinery by switching synaptic vesicle recycling from adaptor protein 3 (AP-3)-to AP-2-dependent mechanisms
    • Shetty, A. et al. The neural cell adhesion molecule promotes maturation of the presynaptic endocytotic machinery by switching synaptic vesicle recycling from adaptor protein 3 (AP-3)-to AP-2-dependent mechanisms. J. Neurosci. 33, 16828-16845 (2013).
    • (2013) J. Neurosci. , vol.33 , pp. 16828-16845
    • Shetty, A.1
  • 47
    • 0034740197 scopus 로고    scopus 로고
    • Vaccination with soluble Abeta oligomers generates toxicity-neutralizing antibodies
    • Lambert, M. P. et al. Vaccination with soluble Abeta oligomers generates toxicity-neutralizing antibodies. J. Neurochem. 79, 595-605 (2001).
    • (2001) J. Neurochem. , vol.79 , pp. 595-605
    • Lambert, M.P.1
  • 48
    • 0035993237 scopus 로고    scopus 로고
    • Abeta toxicity in Alzheimer's disease: Globular oligomers (ADDLs) as new vaccine and drug targets
    • Klein, W. L. Abeta toxicity in Alzheimer's disease: globular oligomers (ADDLs) as new vaccine and drug targets. Neurochem. Int. 41, 345-352 (2002).
    • (2002) Neurochem. Int. , vol.41 , pp. 345-352
    • Klein, W.L.1
  • 49
    • 77955322042 scopus 로고    scopus 로고
    • Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer's disease mouse models
    • Ittner, L. M. et al. Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer's disease mouse models. Cell 142, 387-397 (2010).
    • (2010) Cell , vol.142 , pp. 387-397
    • Ittner, L.M.1
  • 50
    • 84871790544 scopus 로고    scopus 로고
    • Lipid raft-dependent endocytosis of close homolog of adhesion molecule L1 (CHL1) promotes neuritogenesis
    • Tian, N. et al. Lipid raft-dependent endocytosis of close homolog of adhesion molecule L1 (CHL1) promotes neuritogenesis. J. Biol. Chem. 287, 44447-44463 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 44447-44463
    • Tian, N.1
  • 51
    • 0026727853 scopus 로고
    • Clathrin-coated vesicles in nervous tissue are involved primarily in synaptic vesicle recycling
    • Maycox, P. R., Link, E., Reetz, A., Morris, S. A. & Jahn, R. Clathrin-coated vesicles in nervous tissue are involved primarily in synaptic vesicle recycling. J. Cell Biol. 118, 1379-1388 (1992).
    • (1992) J. Cell Biol. , vol.118 , pp. 1379-1388
    • Maycox, P.R.1    Link, E.2    Reetz, A.3    Morris, S.A.4    Jahn, R.5


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