메뉴 건너뛰기




Volumn 4, Issue 10, 2009, Pages

Dual regulation of dendritic morphogenesis in Drosophila by the COP9 signalosome

Author keywords

[No Author keywords available]

Indexed keywords

COP9 SIGNALOSOME; CULLIN; F BOX PROTEIN; NEDD8 PROTEIN; CSN5 PROTEIN, DROSOPHILA; DROSOPHILA PROTEIN; MULTIPROTEIN COMPLEX; NEDD8 PROTEIN, DROSOPHILA; PEPTIDE HYDROLASE; SIGNAL PEPTIDE; UBIQUITIN;

EID: 70449558124     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0007577     Document Type: Article
Times cited : (13)

References (59)
  • 1
    • 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
  • 2
    • 5344277556 scopus 로고    scopus 로고
    • Deciphering the molecular basis of memory failure in Alzheimer's disease
    • Walsh DM, Selkoe DJ (2004) Deciphering the molecular basis of memory failure in Alzheimer's disease. Neuron 44: 181-193.
    • (2004) Neuron , vol.44 , pp. 181-193
    • Walsh, D.M.1    Selkoe, D.J.2
  • 3
    • 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
  • 4
    • 0026320986 scopus 로고
    • Proliferative and degenerative changes in striatal spiny neurons in Huntington's disease: A combined study using the section-Golgi method and calbindin D28k immunocytochemistry
    • Ferrante RJ, Kowall NW, Richardson EP, Jr. (1991) Proliferative and degenerative changes in striatal spiny neurons in Huntington's disease: a combined study using the section-Golgi method and calbindin D28k immunocytochemistry. J Neurosci 11: 3877-3887.
    • (1991) J Neurosci , vol.11 , pp. 3877-3887
    • Ferrante, R.J.1    Kowall, N.W.2    Richardson Jr., E.P.3
  • 5
    • 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
  • 6
    • 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
  • 7
    • 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
  • 8
    • 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
  • 10
    • 33846974037 scopus 로고    scopus 로고
    • Transmitting on actin: Synaptic control of dendritic architecture
    • Schubert V, Dotti CG (2007) Transmitting on actin: synaptic control of dendritic architecture. J Cell Sci 120: 205-212.
    • (2007) J Cell Sci , vol.120 , pp. 205-212
    • Schubert, V.1    Dotti, C.G.2
  • 12
    • 0033279836 scopus 로고    scopus 로고
    • SCF and Cullin/Ring H2-based ubiquitin ligases
    • Deshaies RJ (1999) SCF and Cullin/Ring H2-based ubiquitin ligases. Annu Rev Cell Dev Biol 15: 435-467.
    • (1999) Annu Rev Cell Dev Biol , vol.15 , pp. 435-467
    • Deshaies, R.J.1
  • 13
    • 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
  • 14
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman MH, Ciechanover A (2002) The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev 82: 373-428.
    • (2002) Physiol Rev , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 15
    • 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
  • 16
    • 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
  • 17
    • 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
  • 18
    • 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
  • 20
    • 0036848655 scopus 로고    scopus 로고
    • CSN5/Jab1 mutations affect axis formation in the Drosophila oocyte by activating a meiotic checkpoint
    • Doronkin S, Djagaeva I, Beckendorf SK (2002) CSN5/Jab1 mutations affect axis formation in the Drosophila oocyte by activating a meiotic checkpoint. Development 129: 5053-5064.
    • (2002) Development , vol.129 , pp. 5053-5064
    • Doronkin, S.1    Djagaeva, I.2    Beckendorf, S.K.3
  • 21
    • 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
  • 22
    • 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
  • 23
    • 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
  • 24
    • 0035907047 scopus 로고    scopus 로고
    • Interactions of the COP9 signalosome with the E3 ubiquitin ligase SCFTIRI in mediating auxin response
    • Schwechheimer C, Serino G, Callis J, Crosby WL, Lyapina S, et al. (2001) Interactions of the COP9 signalosome with the E3 ubiquitin ligase SCFTIRI in mediating auxin response. Science 292: 1379-1382.
    • (2001) Science , vol.292 , pp. 1379-1382
    • Schwechheimer, C.1    Serino, G.2    Callis, J.3    Crosby, W.L.4    Lyapina, S.5
  • 25
    • 29944435762 scopus 로고    scopus 로고
    • The emerging role of the COP9 signalosome in cancer
    • Richardson KS, Zundel W (2005) The emerging role of the COP9 signalosome in cancer. Mol Cancer Res 3: 645-653.
    • (2005) Mol Cancer Res , vol.3 , pp. 645-653
    • Richardson, K.S.1    Zundel, W.2
  • 26
    • 0037012075 scopus 로고    scopus 로고
    • Drosophila JAB1/CSN5 acts in photoreceptor cells to induce glial cells
    • Suh GS, Poeck B, Chouard T, Oron E, Segal D, et al. (2002) Drosophila JAB1/CSN5 acts in photoreceptor cells to induce glial cells. Neuron 33: 35-46.
    • (2002) Neuron , vol.33 , pp. 35-46
    • Suh, G.S.1    Poeck, B.2    Chouard, T.3    Oron, E.4    Segal, D.5
  • 27
    • 59649121965 scopus 로고    scopus 로고
    • The COP9 signalosome is required for light-dependent timeless degradation and Drosophila clock resetting
    • Knowles A, Koh K, Wu JT, Chien CT, Chamovitz DA, et al. (2009) The COP9 signalosome is required for light-dependent timeless degradation and Drosophila clock resetting. J Neurosci 29: 1152-1162.
    • (2009) J Neurosci , vol.29 , pp. 1152-1162
    • Knowles, A.1    Koh, K.2    Wu, J.T.3    Chien, C.T.4    Chamovitz, D.A.5
  • 28
    • 33846559388 scopus 로고    scopus 로고
    • COP9 signalosome subunit 5 (CSN5/Jab1) regulates the development of the Drosophila immune system: Effects on Cactus, Dorsal and hematopoiesis
    • Harari-Steinberg O, Cantera R, Denti S, Bianchi E, Oron E, et al. (2007) COP9 signalosome subunit 5 (CSN5/Jab1) regulates the development of the Drosophila immune system: effects on Cactus, Dorsal and hematopoiesis. Genes Cells 12: 183-195.
    • (2007) Genes Cells , vol.12 , pp. 183-195
    • Harari-Steinberg, O.1    Cantera, R.2    Denti, S.3    Bianchi, E.4    Oron, E.5
  • 29
    • 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
  • 30
    • 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
  • 31
    • 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
  • 32
    • 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
  • 33
    • 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
  • 34
    • 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
  • 35
    • 0037434075 scopus 로고    scopus 로고
    • Implication of Trip15/CSN2 in early stage of neuronal differentiation of P19 embryonal carcinoma cells
    • Akiyama H, Sugiyama A, Uzawa K, Fujisawa N, Tashiro Y, et al. (2003) Implication of Trip15/CSN2 in early stage of neuronal differentiation of P19 embryonal carcinoma cells. Brain Res Dev Brain Res 140: 45-56.
    • (2003) Brain Res Dev Brain Res , vol.140 , pp. 45-56
    • Akiyama, H.1    Sugiyama, A.2    Uzawa, K.3    Fujisawa, N.4    Tashiro, Y.5
  • 36
    • 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
  • 37
    • 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
  • 38
    • 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
  • 39
    • 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
  • 40
    • 53049095816 scopus 로고    scopus 로고
    • Drosophila orthologues to human disease genes: An update on progress
    • Doronkin S, Reiter LT (2008) Drosophila orthologues to human disease genes: an update on progress. Prog Nucleic Acid Res Mol Biol 82: 1-32.
    • (2008) Prog Nucleic Acid Res Mol Biol , vol.82 , pp. 1-32
    • Doronkin, S.1    Reiter, L.T.2
  • 41
    • 29444455075 scopus 로고    scopus 로고
    • Drosophila as a model for human neurodegenerative disease
    • Bilen J, Bonini NM (2005) Drosophila as a model for human neurodegenerative disease. Annu Rev Genet 39: 153-171.
    • (2005) Annu Rev Genet , vol.39 , pp. 153-171
    • Bilen, J.1    Bonini, N.M.2
  • 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
    • 3543144446 scopus 로고
    • Dendritic organization in the neurons of the visual and motor cortices of the cat
    • Sholl DA (1953) Dendritic organization in the neurons of the visual and motor cortices of the cat. J Anat 87: 387-406.
    • (1953) J Anat , vol.87 , pp. 387-406
    • Sholl, D.A.1
  • 45
    • 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
  • 46
    • 0033602475 scopus 로고    scopus 로고
    • HOS, a human homolog of Slimb, forms an SCF complex with Skp1 and Cullin1 and targets the phosphorylation-dependent degradation of IkappaB and beta-catenin
    • Fuchs SY, Chen A, Xiong Y, Pan ZQ, Ronai Z (1999) HOS, a human homolog of Slimb, forms an SCF complex with Skp1 and Cullin1 and targets the phosphorylation-dependent degradation of IkappaB and beta-catenin. Oncogene 18: 2039-2046.
    • (1999) Oncogene , vol.18 , pp. 2039-2046
    • Fuchs, S.Y.1    Chen, A.2    Xiong, Y.3    Pan, Z.Q.4    Ronai, Z.5
  • 47
    • 0032576777 scopus 로고    scopus 로고
    • Regulation of the Hedgehog and Wingless signalling pathways by the F-box/WD40-repeat protein Slimb
    • Jiang J, Struhl G (1998) Regulation of the Hedgehog and Wingless signalling pathways by the F-box/WD40-repeat protein Slimb. Nature 391: 493-496.
    • (1998) Nature , vol.391 , pp. 493-496
    • Jiang, J.1    Struhl, G.2
  • 48
    • 30044442183 scopus 로고    scopus 로고
    • Processing of the Drosophila hedgehog signaling effector Ci-155 to the repressor Ci-75 is mediated by direct binding to the SCF component Slimb
    • Smelkinson MG, Kalderon D (2006) Processing of the Drosophila hedgehog signaling effector Ci-155 to the repressor Ci-75 is mediated by direct binding to the SCF component Slimb. Curr Biol 16: 110-116.
    • (2006) Curr Biol , vol.16 , pp. 110-116
    • Smelkinson, M.G.1    Kalderon, D.2
  • 49
    • 0242384747 scopus 로고    scopus 로고
    • Beta-catenin is critical for dendritic morphogenesis
    • Yu X, Malenka RC (2003) Beta-catenin is critical for dendritic morphogenesis. Nat Neurosci 6: 1169-1177.
    • (2003) Nat Neurosci , vol.6 , pp. 1169-1177
    • Yu, X.1    Malenka, R.C.2
  • 50
    • 2942738996 scopus 로고    scopus 로고
    • The Hedgehog response network: Sensors, switches, and routers
    • Lum L, Beachy PA (2004) The Hedgehog response network: sensors, switches, and routers. Science 304: 1755-1759.
    • (2004) Science , vol.304 , pp. 1755-1759
    • Lum, L.1    Beachy, P.A.2
  • 51
    • 28844478864 scopus 로고    scopus 로고
    • The mechanism of hedgehog signal transduction
    • Kalderon D (2005) The mechanism of hedgehog signal transduction. Biochem Soc Trans 33: 1509-1512.
    • (2005) Biochem Soc Trans , vol.33 , pp. 1509-1512
    • Kalderon, D.1
  • 52
    • 33645514645 scopus 로고    scopus 로고
    • Genome-wide analyses identify transcription factors required for proper morphogenesis of Drosophila sensory neuron dendrites
    • Parrish JZ, Kim MD, Jan LY, Jan YN (2006) Genome-wide analyses identify transcription factors required for proper morphogenesis of Drosophila sensory neuron dendrites. Genes Dev 20: 820-835.
    • (2006) Genes Dev , vol.20 , pp. 820-835
    • Parrish, J.Z.1    Kim, M.D.2    Jan, L.Y.3    Jan, Y.N.4
  • 53
    • 0027817446 scopus 로고
    • Genetic analysis of hedgehog signalling in the Drosophila embryo
    • Forbes AJ, Nakano Y, Taylor AM, Ingham PW (1993) Genetic analysis of hedgehog signalling in the Drosophila embryo. Dev Suppl. pp 115-124.
    • (1993) Dev Suppl , pp. 115-124
    • Forbes, A.J.1    Nakano, Y.2    Taylor, A.M.3    Ingham, P.W.4
  • 54
    • 0029858774 scopus 로고    scopus 로고
    • Transcriptional activation of hedgehog target genes in Drosophila is mediated directly by the cubitus interruptus protein, a member of the GLI family of zinc finger DNA-binding proteins
    • Alexandre C, Jacinto A, Ingham PW (1996) Transcriptional activation of hedgehog target genes in Drosophila is mediated directly by the cubitus interruptus protein, a member of the GLI family of zinc finger DNA-binding proteins. Genes Dev 10: 2003-2013.
    • (1996) Genes Dev , vol.10 , pp. 2003-2013
    • Alexandre, C.1    Jacinto, A.2    Ingham, P.W.3
  • 55
    • 0029896212 scopus 로고    scopus 로고
    • Sending and receiving the hedgehog signal: Control by the Drosophila Gli protein Cubitus interruptus
    • Dominguez M, Brunner M, Hafen E, Basler K (1996) Sending and receiving the hedgehog signal: control by the Drosophila Gli protein Cubitus interruptus. Science 272: 1621-1625.
    • (1996) Science , vol.272 , pp. 1621-1625
    • Dominguez, M.1    Brunner, M.2    Hafen, E.3    Basler, K.4
  • 56
    • 0031040287 scopus 로고    scopus 로고
    • Drosophila cubitus interruptus forms a negative feedback loop with patched and regulates expression of Hedgehog target genes
    • Hepker J, Wang QT, Motzny CK, Holmgren R, Orenic TV (1997) Drosophila cubitus interruptus forms a negative feedback loop with patched and regulates expression of Hedgehog target genes. Development 124: 549-558.
    • (1997) Development , vol.124 , pp. 549-558
    • Hepker, J.1    Wang, Q.T.2    Motzny, C.K.3    Holmgren, R.4    Orenic, T.V.5
  • 57
    • 0001466654 scopus 로고    scopus 로고
    • GLI3 mutations in human disorders mimic Drosophila cubitus interruptus protein functions and localization
    • Shin SH, Kogerman P, Lindstrom E, Toftgard R, Biesecker LG (1999) GLI3 mutations in human disorders mimic Drosophila cubitus interruptus protein functions and localization. Proc Natl Acad Sci U S A 96: 2880-2884.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 2880-2884
    • Shin, S.H.1    Kogerman, P.2    Lindstrom, E.3    Toftgard, R.4    Biesecker, L.G.5
  • 58
    • 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
  • 59
    • 77949322235 scopus 로고    scopus 로고
    • COP9 limits dendritic branching via Cullin3-dependent degradation of the actin-crosslinking BTB-domain protein Kelch. PLoS ONE
    • In press
    • Djagaeva I, Doronkin S (2009) COP9 limits dendritic branching via Cullin3-dependent degradation of the actin-crosslinking BTB-domain protein Kelch. PLoS ONE, In press.
    • (2009)
    • Djagaeva, I.1    Doronkin, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.