메뉴 건너뛰기




Volumn 4, Issue 10, 2009, Pages

COP9 Limits Dendritic Branching via Cullin3-Dependent Degradation of the Actin-Crosslinking BTB-Domain Protein Kelch

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; COP9 SIGNALOSOME; CULLIN; DROSOPHILA PROTEIN; GFT PROTEIN, DROSOPHILA; KEL PROTEIN, DROSOPHILA; MULTIPROTEIN COMPLEX; PEPTIDE HYDROLASE;

EID: 77949322235     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0007598     Document Type: Article
Times cited : (24)

References (63)
  • 1
    • 0029998871 scopus 로고    scopus 로고
    • The dynamics of dendritic structure in developing hippocampal slices
    • Dailey ME, Smith SJ, (1996) The dynamics of dendritic structure in developing hippocampal slices. J Neurosci 16: 2983-2994.
    • (1996) J Neurosci , vol.16 , pp. 2983-2994
    • Dailey, M.E.1    Smith, S.J.2
  • 2
    • 0036441201 scopus 로고    scopus 로고
    • Actin cytoskeleton regulation in neuronal morphogenesis and structural plasticity
    • Luo L, (2002) Actin cytoskeleton regulation in neuronal morphogenesis and structural plasticity. Annu Rev Cell Dev Biol 18: 601-635.
    • (2002) Annu Rev Cell Dev Biol , vol.18 , pp. 601-635
    • Luo, L.1
  • 3
    • 33646227185 scopus 로고    scopus 로고
    • Dendritic pathology in mental retardation: from molecular genetics to neurobiology
    • Dierssen M, Ramakers GJ, (2006) Dendritic pathology in mental retardation: from molecular genetics to neurobiology. Genes Brain Behav 5 (Suppl 2): 48-60.
    • (2006) Genes Brain Behav , vol.5 , Issue.SUPPL. 2 , pp. 48-60
    • Dierssen, M.1    Ramakers, G.J.2
  • 4
    • 47649093892 scopus 로고    scopus 로고
    • Dendritic spine dynamics-a key role for kalirin-7
    • Penzes P, Jones KA, (2008) Dendritic spine dynamics-a key role for kalirin-7. Trends Neurosci 31: 419-427.
    • (2008) Trends Neurosci , vol.31 , pp. 419-427
    • Penzes, P.1    Jones, K.A.2
  • 5
    • 17844372504 scopus 로고    scopus 로고
    • From mRNP trafficking to spine dysmorphogenesis: the roots of fragile X syndrome
    • Bagni C, Greenough WT, (2005) From mRNP trafficking to spine dysmorphogenesis: the roots of fragile X syndrome. Nat Rev Neurosci 6: 376-387.
    • (2005) Nat Rev Neurosci , vol.6 , pp. 376-387
    • Bagni, C.1    Greenough, W.T.2
  • 6
    • 27944508782 scopus 로고    scopus 로고
    • The neuropathology of autism: a review
    • Pickett J, London E, (2005) The neuropathology of autism: a review. J Neuropathol Exp Neurol 64: 925-935.
    • (2005) J Neuropathol Exp Neurol , vol.64 , pp. 925-935
    • Pickett, J.1    London, E.2
  • 7
    • 33746314832 scopus 로고    scopus 로고
    • Searching for ways out of the autism maze: genetic, epigenetic and environmental clues
    • Persico AM, Bourgeron T, (2006) Searching for ways out of the autism maze: genetic, epigenetic and environmental clues. Trends Neurosci 29: 349-358.
    • (2006) Trends Neurosci , vol.29 , pp. 349-358
    • Persico, A.M.1    Bourgeron, T.2
  • 8
    • 33749590330 scopus 로고    scopus 로고
    • Brain-specific phosphorylation of MeCP2 regulates activity-dependent Bdnf transcription, dendritic growth, and spine maturation
    • Zhou Z, Hong EJ, Cohen S, Zhao WN, Ho HY, et al.(2006) Brain-specific phosphorylation of MeCP2 regulates activity-dependent Bdnf transcription, dendritic growth, and spine maturation. Neuron 52: 255-269.
    • (2006) Neuron , vol.52 , pp. 255-269
    • Zhou, Z.1    Hong, E.J.2    Cohen, S.3    Zhao, W.N.4    Ho, H.Y.5
  • 9
    • 0347722470 scopus 로고    scopus 로고
    • Altered cortical glutamate neurotransmission in schizophrenia: evidence from morphological studies of pyramidal neurons
    • Lewis DA, Glantz LA, Pierri JN, Sweet RA, (2003) Altered cortical glutamate neurotransmission in schizophrenia: evidence from morphological studies of pyramidal neurons. Ann N Y Acad Sci 1003: 102-112.
    • (2003) Ann N Y Acad Sci , vol.1003 , pp. 102-112
    • Lewis, D.A.1    Glantz, L.A.2    Pierri, J.N.3    Sweet, R.A.4
  • 10
    • 4544359112 scopus 로고    scopus 로고
    • Structural plasticity associated with exposure to drugs of abuse
    • Robinson TE, Kolb B, (2004) Structural plasticity associated with exposure to drugs of abuse. Neuropharmacology 47 (Suppl 1): 33-46.
    • (2004) Neuropharmacology , vol.47 , Issue.SUPPL. 1 , pp. 33-46
    • Robinson, T.E.1    Kolb, B.2
  • 11
    • 50349083093 scopus 로고    scopus 로고
    • Dendritic spine loss and synaptic alterations in Alzheimer's disease
    • Knobloch M, Mansuy IM, (2008) Dendritic spine loss and synaptic alterations in Alzheimer's disease. Mol Neurobiol 37: 73-82.
    • (2008) Mol Neurobiol , vol.37 , pp. 73-82
    • Knobloch, M.1    Mansuy, I.M.2
  • 12
    • 2942620844 scopus 로고    scopus 로고
    • Dendritic spine pathology and deficits in experience-dependent dendritic plasticity in R6/1 Huntington's disease transgenic mice
    • Spires TL, Grote HE, Garry S, Cordery PM, Van Dellen A, et al.(2004) Dendritic spine pathology and deficits in experience-dependent dendritic plasticity in R6/1 Huntington's disease transgenic mice. Eur J Neurosci 19: 2799-2807.
    • (2004) Eur J Neurosci , vol.19 , pp. 2799-2807
    • Spires, T.L.1    Grote, H.E.2    Garry, S.3    Cordery, P.M.4    Van Dellen, A.5
  • 13
    • 31544465246 scopus 로고    scopus 로고
    • Selective elimination of glutamatergic synapses on striatopallidal neurons in Parkinson disease models
    • Day M, Wang Z, Ding J, An X, Ingham CA, et al.(2006) Selective elimination of glutamatergic synapses on striatopallidal neurons in Parkinson disease models. Nat Neurosci 9: 251-259.
    • (2006) Nat Neurosci , vol.9 , pp. 251-259
    • Day, M.1    Wang, Z.2    Ding, J.3    An, X.4    Ingham, C.A.5
  • 14
    • 0033797735 scopus 로고    scopus 로고
    • Dendritic anomalies in disorders associated with mental retardation
    • Kaufmann WE, Moser HW, (2000) Dendritic anomalies in disorders associated with mental retardation. Cereb Cortex 10: 981-991.
    • (2000) Cereb Cortex , vol.10 , pp. 981-991
    • Kaufmann, W.E.1    Moser, H.W.2
  • 16
    • 32344435520 scopus 로고    scopus 로고
    • Molecular mechanisms of dendritic spine morphogenesis
    • Tada T, Sheng M, (2006) Molecular mechanisms of dendritic spine morphogenesis. Curr Opin Neurobiol 16: 95-101.
    • (2006) Curr Opin Neurobiol , vol.16 , pp. 95-101
    • Tada, T.1    Sheng, M.2
  • 17
    • 42349091996 scopus 로고    scopus 로고
    • Actin in action: the interplay between the actin cytoskeleton and synaptic efficacy
    • Cingolani LA, Goda Y, (2008) Actin in action: the interplay between the actin cytoskeleton and synaptic efficacy. Nat Rev Neurosci 9: 344-356.
    • (2008) Nat Rev Neurosci , vol.9 , pp. 344-356
    • Cingolani, L.A.1    Goda, Y.2
  • 18
    • 13844250636 scopus 로고    scopus 로고
    • Growth of dendritic spines: a continuing story
    • Matus A, (2005) Growth of dendritic spines: a continuing story. Curr Opin Neurobiol 15: 67-72.
    • (2005) Curr Opin Neurobiol , vol.15 , pp. 67-72
    • Matus, A.1
  • 20
    • 4143112402 scopus 로고    scopus 로고
    • Ubiquitin-proteasome-mediated local protein degradation and synaptic plasticity
    • Hegde AN, (2004) Ubiquitin-proteasome-mediated local protein degradation and synaptic plasticity. Prog Neurobiol 73: 311-357.
    • (2004) Prog Neurobiol , vol.73 , pp. 311-357
    • Hegde, A.N.1
  • 21
    • 54249158324 scopus 로고    scopus 로고
    • Ubiquitin, the proteasome and protein degradation in neuronal function and dysfunction
    • Tai HC, Schuman EM, (2008) Ubiquitin, the proteasome and protein degradation in neuronal function and dysfunction. Nat Rev Neurosci 9: 826-838.
    • (2008) Nat Rev Neurosci , vol.9 , pp. 826-838
    • Tai, H.C.1    Schuman, E.M.2
  • 22
    • 33847410541 scopus 로고    scopus 로고
    • Emerging roles for ubiquitin and protein degradation in neuronal function
    • Yi JJ, Ehlers MD, (2007) Emerging roles for ubiquitin and protein degradation in neuronal function. Pharmacol Rev 59: 14-39.
    • (2007) Pharmacol Rev , vol.59 , pp. 14-39
    • Yi, J.J.1    Ehlers, M.D.2
  • 24
    • 11244351579 scopus 로고    scopus 로고
    • Function and regulation of cullin-RING ubiquitin ligases
    • Petroski MD, Deshaies RJ, (2005) Function and regulation of cullin-RING ubiquitin ligases. Nat Rev Mol Cell Biol 6: 9-20.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 9-20
    • Petroski, M.D.1    Deshaies, R.J.2
  • 25
    • 0141426637 scopus 로고    scopus 로고
    • COP9 signalosome: a multifunctional regulator of SCF and other cullin-based ubiquitin ligases
    • Cope GA, Deshaies RJ, (2003) COP9 signalosome: a multifunctional regulator of SCF and other cullin-based ubiquitin ligases. Cell 114: 663-671.
    • (2003) Cell , vol.114 , pp. 663-671
    • Cope, G.A.1    Deshaies, R.J.2
  • 26
    • 9644272422 scopus 로고    scopus 로고
    • The COP9 signalosome (CSN): an evolutionary conserved proteolysis regulator in eukaryotic development
    • Schwechheimer C, (2004) The COP9 signalosome (CSN): an evolutionary conserved proteolysis regulator in eukaryotic development. Biochim Biophys Acta 1695: 45-54.
    • (2004) Biochim Biophys Acta , vol.1695 , pp. 45-54
    • Schwechheimer, C.1
  • 27
    • 0345099331 scopus 로고    scopus 로고
    • The COP9 signalosome: an assembly and maintenance platform for cullin ubiquitin ligases?
    • Wolf DA, Zhou C, Wee S, (2003) The COP9 signalosome: an assembly and maintenance platform for cullin ubiquitin ligases? Nat Cell Biol 5: 1029-1033.
    • (2003) Nat Cell Biol , vol.5 , pp. 1029-1033
    • Wolf, D.A.1    Zhou, C.2    Wee, S.3
  • 28
    • 0038329328 scopus 로고    scopus 로고
    • The COP9 signalosome promotes degradation of Cyclin E during early Drosophila oogenesis
    • Doronkin S, Djagaeva I, Beckendorf SK, (2003) The COP9 signalosome promotes degradation of Cyclin E during early Drosophila oogenesis. Dev Cell 4: 699-710.
    • (2003) Dev Cell , vol.4 , pp. 699-710
    • Doronkin, S.1    Djagaeva, I.2    Beckendorf, S.K.3
  • 29
    • 0035906430 scopus 로고    scopus 로고
    • Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome
    • Lyapina S, Cope G, Shevchenko A, Serino G, Tsuge T, et al.(2001) Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome. Science 292: 1382-1385.
    • (2001) Science , vol.292 , pp. 1382-1385
    • Lyapina, S.1    Cope, G.2    Shevchenko, A.3    Serino, G.4    Tsuge, T.5
  • 30
    • 0037131242 scopus 로고    scopus 로고
    • Role of predicted metalloprotease motif of Jab1/Csn5 in cleavage of Nedd8 from Cul1
    • Cope GA, Suh GS, Aravind L, Schwarz SE, Zipursky SL, et al.(2002) Role of predicted metalloprotease motif of Jab1/Csn5 in cleavage of Nedd8 from Cul1. Science 298: 608-611.
    • (2002) Science , vol.298 , pp. 608-611
    • Cope, G.A.1    Suh, G.S.2    Aravind, L.3    Schwarz, S.E.4    Zipursky, S.L.5
  • 31
    • 3042727952 scopus 로고    scopus 로고
    • The fission yeast COP9/signalosome is involved in cullin modification by ubiquitin-related Ned8p
    • Zhou C, Seibert V, Geyer R, Rhee E, Lyapina S, et al.(2001) The fission yeast COP9/signalosome is involved in cullin modification by ubiquitin-related Ned8p. BMC Biochem 2: 7.
    • (2001) BMC Biochem , vol.2 , pp. 7
    • Zhou, C.1    Seibert, V.2    Geyer, R.3    Rhee, E.4    Lyapina, S.5
  • 32
    • 0033118309 scopus 로고    scopus 로고
    • Subunit 3 of the COP9 signal transduction complex is conserved from plants to humans and maps within the smith-magenis syndrome critical region in 17p11.2
    • Potocki L, Chen KS, Lupski JR, (1999) Subunit 3 of the COP9 signal transduction complex is conserved from plants to humans and maps within the smith-magenis syndrome critical region in 17p11.2. Genomics 57: 180-182.
    • (1999) Genomics , vol.57 , pp. 180-182
    • Potocki, L.1    Chen, K.S.2    Lupski, J.R.3
  • 33
    • 0034042539 scopus 로고    scopus 로고
    • Circadian rhythm abnormalities of melatonin in Smith-Magenis syndrome
    • Potocki L, Glaze D, Tan DX, Park SS, Kashork CD, et al.(2000) Circadian rhythm abnormalities of melatonin in Smith-Magenis syndrome. J Med Genet 37: 428-433.
    • (2000) J Med Genet , vol.37 , pp. 428-433
    • Potocki, L.1    Glaze, D.2    Tan, D.X.3    Park, S.S.4    Kashork, C.D.5
  • 34
    • 0032732145 scopus 로고    scopus 로고
    • Hemizygosity for the COP9 signalosome subunit gene, SGN3, in the Smith-Magenis syndrome
    • Elsea SH, Mykytyn K, Ferrell K, Coulter KL, Das P, et al.(1999) Hemizygosity for the COP9 signalosome subunit gene, SGN3, in the Smith-Magenis syndrome. Am J Med Genet 87: 342-348.
    • (1999) Am J Med Genet , vol.87 , pp. 342-348
    • Elsea, S.H.1    Mykytyn, K.2    Ferrell, K.3    Coulter, K.L.4    Das, P.5
  • 35
    • 0141669190 scopus 로고    scopus 로고
    • COP9 signalosome subunit 3 is essential for maintenance of cell proliferation in the mouse embryonic epiblast
    • Yan J, Walz K, Nakamura H, Carattini-Rivera S, Zhao Q, et al.(2003) COP9 signalosome subunit 3 is essential for maintenance of cell proliferation in the mouse embryonic epiblast. Mol Cell Biol 23: 6798-6808.
    • (2003) Mol Cell Biol , vol.23 , pp. 6798-6808
    • Yan, J.1    Walz, K.2    Nakamura, H.3    Carattini-Rivera, S.4    Zhao, Q.5
  • 36
    • 0036148535 scopus 로고    scopus 로고
    • Aberrant expression of signaling-related proteins 14-3-3 gamma and RACK1 in fetal Down syndrome brain (trisomy 21)
    • Peyrl A, Weitzdoerfer R, Gulesserian T, Fountoulakis M, Lubec G, (2002) Aberrant expression of signaling-related proteins 14-3-3 gamma and RACK1 in fetal Down syndrome brain (trisomy 21). Electrophoresis 23: 152-157.
    • (2002) Electrophoresis , vol.23 , pp. 152-157
    • Peyrl, A.1    Weitzdoerfer, R.2    Gulesserian, T.3    Fountoulakis, M.4    Lubec, G.5
  • 37
    • 3042636436 scopus 로고    scopus 로고
    • JAB1 participates in unfolded protein responses by association and dissociation with IRE1
    • Oono K, Yoneda T, Manabe T, Yamagishi S, Matsuda S, et al.(2004) JAB1 participates in unfolded protein responses by association and dissociation with IRE1. Neurochem Int 45: 765-772.
    • (2004) Neurochem Int , vol.45 , pp. 765-772
    • Oono, K.1    Yoneda, T.2    Manabe, T.3    Yamagishi, S.4    Matsuda, S.5
  • 38
    • 0037312293 scopus 로고    scopus 로고
    • NEDD8 protein is involved in ubiquitinated inclusion bodies
    • Dil Kuazi A, Kito K, Abe Y, Shin RW, Kamitani T, et al.(2003) NEDD8 protein is involved in ubiquitinated inclusion bodies. J Pathol 199: 259-266.
    • (2003) J Pathol , vol.199 , pp. 259-266
    • Dil Kuazi, A.1    Kito, K.2    Abe, Y.3    Shin, R.W.4    Kamitani, T.5
  • 39
    • 13544270760 scopus 로고    scopus 로고
    • Accumulation of NEDD8 in neuronal and glial inclusions of neurodegenerative disorders
    • Mori F, Nishie M, Piao YS, Kito K, Kamitani T, et al.(2005) Accumulation of NEDD8 in neuronal and glial inclusions of neurodegenerative disorders. Neuropathol Appl Neurobiol 31: 53-61.
    • (2005) Neuropathol Appl Neurobiol , vol.31 , pp. 53-61
    • Mori, F.1    Nishie, M.2    Piao, Y.S.3    Kito, K.4    Kamitani, T.5
  • 40
    • 33846639529 scopus 로고    scopus 로고
    • Mutations in CUL4B, which encodes a ubiquitin E3 ligase subunit, cause an X-linked mental retardation syndrome associated with aggressive outbursts, seizures, relative macrocephaly, central obesity, hypogonadism, pes cavus, and tremor
    • Tarpey PS, Raymond FL, O'Meara S, Edkins S, Teague J, et al.(2007) Mutations in CUL4B, which encodes a ubiquitin E3 ligase subunit, cause an X-linked mental retardation syndrome associated with aggressive outbursts, seizures, relative macrocephaly, central obesity, hypogonadism, pes cavus, and tremor. Am J Hum Genet 80: 345-352.
    • (2007) Am J Hum Genet , vol.80 , pp. 345-352
    • Tarpey, P.S.1    Raymond, F.L.2    O'Meara, S.3    Edkins, S.4    Teague, J.5
  • 41
    • 33847216248 scopus 로고    scopus 로고
    • Mutation in CUL4B, which encodes a member of cullin-RING ubiquitin ligase complex, causes X-linked mental retardation
    • Zou Y, Liu Q, Chen B, Zhang X, Guo C, et al.(2007) Mutation in CUL4B, which encodes a member of cullin-RING ubiquitin ligase complex, causes X-linked mental retardation. Am J Hum Genet 80: 561-566.
    • (2007) Am J Hum Genet , vol.80 , pp. 561-566
    • Zou, Y.1    Liu, Q.2    Chen, B.3    Zhang, X.4    Guo, C.5
  • 42
    • 34547674622 scopus 로고    scopus 로고
    • Mechanisms that regulate establishment, maintenance, and remodeling of dendritic fields
    • Parrish JZ, Emoto K, Kim MD, Jan YN, (2007) Mechanisms that regulate establishment, maintenance, and remodeling of dendritic fields. Annu Rev Neurosci 30: 399-423.
    • (2007) Annu Rev Neurosci , vol.30 , pp. 399-423
    • Parrish, J.Z.1    Emoto, K.2    Kim, M.D.3    Jan, Y.N.4
  • 43
    • 0033103536 scopus 로고    scopus 로고
    • Mosaic analysis with a repressible cell marker for studies of gene function in neuronal morphogenesis
    • Lee T, Luo L, (1999) Mosaic analysis with a repressible cell marker for studies of gene function in neuronal morphogenesis. Neuron 22: 451-461.
    • (1999) Neuron , vol.22 , pp. 451-461
    • Lee, T.1    Luo, L.2
  • 44
    • 0036082991 scopus 로고    scopus 로고
    • Genetic manipulation of single neurons in vivo reveals specific roles of flamingo in neuronal morphogenesis
    • Sweeney NT, Li W, Gao FB, (2002) Genetic manipulation of single neurons in vivo reveals specific roles of flamingo in neuronal morphogenesis. Dev Biol 247: 76-88.
    • (2002) Dev Biol , vol.247 , pp. 76-88
    • Sweeney, N.T.1    Li, W.2    Gao, F.B.3
  • 45
    • 0141750416 scopus 로고    scopus 로고
    • BTB/POZ domain proteins are putative substrate adaptors for cullin 3 ubiquitin ligases
    • Geyer R, Wee S, Anderson S, Yates J, Wolf DA, (2003) BTB/POZ domain proteins are putative substrate adaptors for cullin 3 ubiquitin ligases. Mol Cell 12: 783-790.
    • (2003) Mol Cell , vol.12 , pp. 783-790
    • Geyer, R.1    Wee, S.2    Anderson, S.3    Yates, J.4    Wolf, D.A.5
  • 46
    • 0141493447 scopus 로고    scopus 로고
    • BTB proteins are substrate-specific adaptors in an SCF-like modular ubiquitin ligase containing CUL-3
    • Xu L, Wei Y, Reboul J, Vaglio P, Shin TH, et al.(2003) BTB proteins are substrate-specific adaptors in an SCF-like modular ubiquitin ligase containing CUL-3. Nature 425: 316-321.
    • (2003) Nature , vol.425 , pp. 316-321
    • Xu, L.1    Wei, Y.2    Reboul, J.3    Vaglio, P.4    Shin, T.H.5
  • 47
    • 0242575197 scopus 로고    scopus 로고
    • Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin ligases
    • Furukawa M, He YJ, Borchers C, Xiong Y, (2003) Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin ligases. Nat Cell Biol 5: 1001-1007.
    • (2003) Nat Cell Biol , vol.5 , pp. 1001-1007
    • Furukawa, M.1    He, Y.J.2    Borchers, C.3    Xiong, Y.4
  • 48
    • 0141493448 scopus 로고    scopus 로고
    • The BTB protein MEL-26 is a substrate-specific adaptor of the CUL-3 ubiquitin-ligase
    • Pintard L, Willis JH, Willems A, Johnson JL, Srayko M, et al.(2003) The BTB protein MEL-26 is a substrate-specific adaptor of the CUL-3 ubiquitin-ligase. Nature 425: 311-316.
    • (2003) Nature , vol.425 , pp. 311-316
    • Pintard, L.1    Willis, J.H.2    Willems, A.3    Johnson, J.L.4    Srayko, M.5
  • 49
    • 0037447261 scopus 로고    scopus 로고
    • Dendrites of distinct classes of Drosophila sensory neurons show different capacities for homotypic repulsion
    • Grueber WB, Ye B, Moore AW, Jan LY, Jan YN, (2003) Dendrites of distinct classes of Drosophila sensory neurons show different capacities for homotypic repulsion. Curr Biol 13: 618-626.
    • (2003) Curr Biol , vol.13 , pp. 618-626
    • Grueber, W.B.1    Ye, B.2    Moore, A.W.3    Jan, L.Y.4    Jan, Y.N.5
  • 50
    • 0030757226 scopus 로고    scopus 로고
    • Drosophila kelch is an oligomeric ring canal actin organizer
    • Robinson DN, Cooley L, (1997) Drosophila kelch is an oligomeric ring canal actin organizer. J Cell Biol 138: 799-810.
    • (1997) J Cell Biol , vol.138 , pp. 799-810
    • Robinson, D.N.1    Cooley, L.2
  • 51
    • 23244445819 scopus 로고    scopus 로고
    • Src64 is involved in fusome development and karyosome formation during Drosophila oogenesis
    • Djagaeva I, Doronkin S, Beckendorf SK, (2005) Src64 is involved in fusome development and karyosome formation during Drosophila oogenesis. Dev Biol 284: 143-156.
    • (2005) Dev Biol , vol.284 , pp. 143-156
    • Djagaeva, I.1    Doronkin, S.2    Beckendorf, S.K.3
  • 52
    • 0026337934 scopus 로고
    • Female sterile mutations on the second chromosome of Drosophila melanogaster. II. Mutations blocking oogenesis or altering egg morphology
    • Schupbach T, Wieschaus E, (1991) Female sterile mutations on the second chromosome of Drosophila melanogaster. II. Mutations blocking oogenesis or altering egg morphology. Genetics 129: 1119-1136.
    • (1991) Genetics , vol.129 , pp. 1119-1136
    • Schupbach, T.1    Wieschaus, E.2
  • 53
    • 0030972377 scopus 로고    scopus 로고
    • Examination of the function of two kelch proteins generated by stop codon suppression
    • Robinson DN, Cooley L, (1997) Examination of the function of two kelch proteins generated by stop codon suppression. Development 124: 1405-1417.
    • (1997) Development , vol.124 , pp. 1405-1417
    • Robinson, D.N.1    Cooley, L.2
  • 54
    • 0036333568 scopus 로고    scopus 로고
    • Tiling of the Drosophila epidermis by multidendritic sensory neurons
    • Grueber WB, Jan LY, Jan YN, (2002) Tiling of the Drosophila epidermis by multidendritic sensory neurons. Development 129: 2867-2878.
    • (2002) Development , vol.129 , pp. 2867-2878
    • Grueber, W.B.1    Jan, L.Y.2    Jan, Y.N.3
  • 56
    • 54949144402 scopus 로고    scopus 로고
    • The autistic neuron: troubled translation?
    • Kelleher RJ 3rd, Bear MF, (2008) The autistic neuron: troubled translation? Cell 135: 401-406.
    • (2008) Cell , vol.135 , pp. 401-406
    • Kelleher 3rd, R.J.1    Bear, M.F.2
  • 57
    • 0033763056 scopus 로고    scopus 로고
    • The gene encoding gigaxonin, a new member of the cytoskeletal BTB/kelch repeat family, is mutated in giant axonal neuropathy
    • Bomont P, Cavalier L, Blondeau F, Ben Hamida C, Belal S, et al.(2000) The gene encoding gigaxonin, a new member of the cytoskeletal BTB/kelch repeat family, is mutated in giant axonal neuropathy. Nat Genet 26: 370-374.
    • (2000) Nat Genet , vol.26 , pp. 370-374
    • Bomont, P.1    Cavalier, L.2    Blondeau, F.3    Ben Hamida, C.4    Belal, S.5
  • 58
    • 58149232639 scopus 로고    scopus 로고
    • Nuclear erythroid 2-related factor 2-antioxidative response element signaling pathway in motor cortex and spinal cord in amyotrophic lateral sclerosis
    • Sarlette A, Krampfl K, Grothe C, Neuhoff N, Dengler R, et al.(2008) Nuclear erythroid 2-related factor 2-antioxidative response element signaling pathway in motor cortex and spinal cord in amyotrophic lateral sclerosis. J Neuropathol Exp Neurol 67: 1055-1062.
    • (2008) J Neuropathol Exp Neurol , vol.67 , pp. 1055-1062
    • Sarlette, A.1    Krampfl, K.2    Grothe, C.3    Neuhoff, N.4    Dengler, R.5
  • 59
    • 0037163043 scopus 로고    scopus 로고
    • Actinfilin, a brain-specific actin-binding protein in postsynaptic density
    • Chen Y, Derin R, Petralia RS, Li M, (2002) Actinfilin, a brain-specific actin-binding protein in postsynaptic density. J Biol Chem 277: 30495-30501.
    • (2002) J Biol Chem , vol.277 , pp. 30495-30501
    • Chen, Y.1    Derin, R.2    Petralia, R.S.3    Li, M.4
  • 60
    • 33749170168 scopus 로고    scopus 로고
    • Targeted deletion of a single Sca8 ataxia locus allele in mice causes abnormal gait, progressive loss of motor coordination, and Purkinje cell dendritic deficits
    • He Y, Zu T, Benzow KA, Orr HT, Clark HB, et al.(2006) Targeted deletion of a single Sca8 ataxia locus allele in mice causes abnormal gait, progressive loss of motor coordination, and Purkinje cell dendritic deficits. J Neurosci 26: 9975-9982.
    • (2006) J Neurosci , vol.26 , pp. 9975-9982
    • He, Y.1    Zu, T.2    Benzow, K.A.3    Orr, H.T.4    Clark, H.B.5
  • 61
    • 0027160708 scopus 로고
    • Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
    • Brand AH, Perrimon N, (1993) Targeted gene expression as a means of altering cell fates and generating dominant phenotypes. Development 118: 401-415.
    • (1993) Development , vol.118 , pp. 401-415
    • Brand, A.H.1    Perrimon, N.2
  • 62
    • 28844498390 scopus 로고    scopus 로고
    • New techniques for imaging, digitization and analysis of three-dimensional neural morphology on multiple scales
    • Wearne SL, Rodriguez A, Ehlenberger DB, Rocher AB, Henderson SC, et al.(2005) New techniques for imaging, digitization and analysis of three-dimensional neural morphology on multiple scales. Neuroscience 136: 661-680.
    • (2005) Neuroscience , vol.136 , pp. 661-680
    • Wearne, S.L.1    Rodriguez, A.2    Ehlenberger, D.B.3    Rocher, A.B.4    Henderson, S.C.5
  • 63
    • 70449558124 scopus 로고    scopus 로고
    • Dual regulation of dendritic morphogenesis in Drosophila by the COP9 signalosome
    • In Press
    • Djagaeva I, Doronkin S, (2009) Dual regulation of dendritic morphogenesis in Drosophila by the COP9 signalosome. PLoS ONE. In press.
    • (2009) PLoS ONE
    • Djagaeva, I.1    Doronkin, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.