메뉴 건너뛰기




Volumn 12, Issue 2, 2014, Pages

Contribution of Orb2A Stability in Regulated Amyloid-Like Oligomerization of Drosophila Orb2

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; CYTOPLASMIC POLYADENYLATION ELEMENT BINDING PROTEIN; LIM KINASE; ORB2A PROTEIN; PHOSPHOPROTEIN PHOSPHATASE 2A; TRANSDUCER OF ERB B2; UNCLASSIFIED DRUG;

EID: 84895445770     PISSN: 15449173     EISSN: 15457885     Source Type: Journal    
DOI: 10.1371/journal.pbio.1001786     Document Type: Article
Times cited : (50)

References (63)
  • 1
    • 33749077101 scopus 로고    scopus 로고
    • Dendritic protein synthesis, synaptic plasticity, and memory
    • Sutton MA, Schuman EM, (2006) Dendritic protein synthesis, synaptic plasticity, and memory. Cell 127: 49-58.
    • (2006) Cell , vol.127 , pp. 49-58
    • Sutton, M.A.1    Schuman, E.M.2
  • 2
    • 58149485508 scopus 로고    scopus 로고
    • Making synaptic plasticity and memory last: mechanisms of translational regulation
    • Richter JD, Klann E, (2009) Making synaptic plasticity and memory last: mechanisms of translational regulation. Genes Dev 23: 1-11.
    • (2009) Genes Dev , vol.23 , pp. 1-11
    • Richter, J.D.1    Klann, E.2
  • 3
    • 36448958766 scopus 로고    scopus 로고
    • Function of the Drosophila CPEB protein Orb2 in long-term courtship memory
    • Keleman K, Kruttner S, Alenius M, Dickson BJ, (2007) Function of the Drosophila CPEB protein Orb2 in long-term courtship memory. Nat Neurosci 10: 1587-1593.
    • (2007) Nat Neurosci , vol.10 , pp. 1587-1593
    • Keleman, K.1    Kruttner, S.2    Alenius, M.3    Dickson, B.J.4
  • 4
    • 84867725756 scopus 로고    scopus 로고
    • Drosophila CPEB Orb2A mediates memory independent of its RNA-binding domain
    • Kruttner S, Stepien B, Noordermeer JN, Mommaas MA, Mechtler K, et al. (2012) Drosophila CPEB Orb2A mediates memory independent of its RNA-binding domain. Neuron 76: 383-395.
    • (2012) Neuron , vol.76 , pp. 383-395
    • Kruttner, S.1    Stepien, B.2    Noordermeer, J.N.3    Mommaas, M.A.4    Mechtler, K.5
  • 5
    • 84862776939 scopus 로고    scopus 로고
    • Critical role of amyloid-like oligomers of Drosophila Orb2 in the persistence of memory
    • Majumdar A, Cesario WC, White-Grindley E, Jiang H, Ren F, et al. (2012) Critical role of amyloid-like oligomers of Drosophila Orb2 in the persistence of memory. Cell 148: 515-529.
    • (2012) Cell , vol.148 , pp. 515-529
    • Majumdar, A.1    Cesario, W.C.2    White-Grindley, E.3    Jiang, H.4    Ren, F.5
  • 6
    • 75749134925 scopus 로고    scopus 로고
    • Aplysia CPEB can form prion-like multimers in sensory neurons that contribute to long-term facilitation
    • Si K, Choi YB, White-Grindley E, Majumdar A, Kandel ER, (2010) Aplysia CPEB can form prion-like multimers in sensory neurons that contribute to long-term facilitation. Cell 140: 421-435.
    • (2010) Cell , vol.140 , pp. 421-435
    • Si, K.1    Choi, Y.B.2    White-Grindley, E.3    Majumdar, A.4    Kandel, E.R.5
  • 7
    • 0346186101 scopus 로고    scopus 로고
    • A neuronal isoform of CPEB regulates local protein synthesis and stabilizes synapse-specific long-term facilitation in aplysia
    • Si K, Giustetto M, Etkin A, Hsu R, Janisiewicz AM, et al. (2003) A neuronal isoform of CPEB regulates local protein synthesis and stabilizes synapse-specific long-term facilitation in aplysia. Cell 115: 893-904.
    • (2003) Cell , vol.115 , pp. 893-904
    • Si, K.1    Giustetto, M.2    Etkin, A.3    Hsu, R.4    Janisiewicz, A.M.5
  • 8
    • 0035894857 scopus 로고    scopus 로고
    • A role for the cytoplasmic polyadenylation element in NMDA receptor-regulated mRNA translation in neurons
    • Wells DG, Dong X, Quinlan EM, Huang YS, Bear MF, et al. (2001) A role for the cytoplasmic polyadenylation element in NMDA receptor-regulated mRNA translation in neurons. J Neurosci 21: 9541-9548.
    • (2001) J Neurosci , vol.21 , pp. 9541-9548
    • Wells, D.G.1    Dong, X.2    Quinlan, E.M.3    Huang, Y.S.4    Bear, M.F.5
  • 9
    • 0032215079 scopus 로고    scopus 로고
    • CPEB-mediated cytoplasmic polyadenylation and the regulation of experience-dependent translation of alpha-CaMKII mRNA at synapses
    • Wu L, Wells D, Tay J, Mendis D, Abbott MA, et al. (1998) CPEB-mediated cytoplasmic polyadenylation and the regulation of experience-dependent translation of alpha-CaMKII mRNA at synapses. Neuron 21: 1129-1139.
    • (1998) Neuron , vol.21 , pp. 1129-1139
    • Wu, L.1    Wells, D.2    Tay, J.3    Mendis, D.4    Abbott, M.A.5
  • 10
    • 52249104915 scopus 로고    scopus 로고
    • Sustained CPEB-dependent local protein synthesis is required to stabilize synaptic growth for persistence of long-term facilitation in Aplysia
    • Miniaci MC, Kim JH, Puthanveettil SV, Si K, Zhu H, et al. (2008) Sustained CPEB-dependent local protein synthesis is required to stabilize synaptic growth for persistence of long-term facilitation in Aplysia. Neuron 59: 1024-1036.
    • (2008) Neuron , vol.59 , pp. 1024-1036
    • Miniaci, M.C.1    Kim, J.H.2    Puthanveettil, S.V.3    Si, K.4    Zhu, H.5
  • 12
    • 79952578947 scopus 로고    scopus 로고
    • Protein-only mechanism induces self-perpetuating changes in the activity of neuronal Aplysia cytoplasmic polyadenylation element binding protein (CPEB)
    • Heinrich SU, Lindquist S, (2011) Protein-only mechanism induces self-perpetuating changes in the activity of neuronal Aplysia cytoplasmic polyadenylation element binding protein (CPEB). Proc Natl Acad Sci U S A 108: 2999-3004.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 2999-3004
    • Heinrich, S.U.1    Lindquist, S.2
  • 14
    • 58149386438 scopus 로고    scopus 로고
    • Coupled phosphatase and kinase switches produce the tristability required for long-term potentiation and long-term depression
    • Pi HJ, Lisman JE, (2008) Coupled phosphatase and kinase switches produce the tristability required for long-term potentiation and long-term depression. J Neurosci 28: 13132-13138.
    • (2008) J Neurosci , vol.28 , pp. 13132-13138
    • Pi, H.J.1    Lisman, J.E.2
  • 15
    • 31144479591 scopus 로고    scopus 로고
    • A brain-specific microRNA regulates dendritic spine development
    • Schratt GM, Tuebing F, Nigh EA, Kane CG, Sabatini ME, et al. (2006) A brain-specific microRNA regulates dendritic spine development. Nature 439: 283-289.
    • (2006) Nature , vol.439 , pp. 283-289
    • Schratt, G.M.1    Tuebing, F.2    Nigh, E.A.3    Kane, C.G.4    Sabatini, M.E.5
  • 16
    • 79953803635 scopus 로고    scopus 로고
    • Anti-proliferative protein Tob negatively regulates CPEB3 target by recruiting Caf1 deadenylase
    • Hosoda N, Funakoshi Y, Hirasawa M, Yamagishi R, Asano Y, et al. (2011) Anti-proliferative protein Tob negatively regulates CPEB3 target by recruiting Caf1 deadenylase. EMBO J 30: 1311-1323.
    • (2011) EMBO J , vol.30 , pp. 1311-1323
    • Hosoda, N.1    Funakoshi, Y.2    Hirasawa, M.3    Yamagishi, R.4    Asano, Y.5
  • 17
    • 33750699996 scopus 로고    scopus 로고
    • Analyzing chromatin remodeling complexes using shotgun proteomics and normalized spectral abundance factors
    • Florens L, Carozza MJ, Swanson SK, Fournier M, Coleman MK, et al. (2006) Analyzing chromatin remodeling complexes using shotgun proteomics and normalized spectral abundance factors. Methods 40: 303-311.
    • (2006) Methods , vol.40 , pp. 303-311
    • Florens, L.1    Carozza, M.J.2    Swanson, S.K.3    Fournier, M.4    Coleman, M.K.5
  • 18
    • 0036375529 scopus 로고    scopus 로고
    • Antiproliferative proteins of the BTG/Tob family are degraded by the ubiquitin-proteasome system
    • Sasajima H, Nakagawa K, Yokosawa H, (2002) Antiproliferative proteins of the BTG/Tob family are degraded by the ubiquitin-proteasome system. Eur J Biochem 269: 3596-3604.
    • (2002) Eur J Biochem , vol.269 , pp. 3596-3604
    • Sasajima, H.1    Nakagawa, K.2    Yokosawa, H.3
  • 19
    • 0036594619 scopus 로고    scopus 로고
    • Phosphorylation of three regulatory serines of Tob by Erk1 and Erk2 is required for Ras-mediated cell proliferation and transformation
    • Suzuki T, J KT, Ajima R, Nakamura T, Yoshida Y, et al. (2002) Phosphorylation of three regulatory serines of Tob by Erk1 and Erk2 is required for Ras-mediated cell proliferation and transformation. Genes Dev 16: 1356-1370.
    • (2002) Genes Dev , vol.16 , pp. 1356-1370
    • Suzuki, T.1    Ajima, R.2    Nakamura, T.3    Yoshida, Y.4
  • 20
    • 0035947157 scopus 로고    scopus 로고
    • In search of a function for the TIS21/PC3/BTG1/TOB family
    • Matsuda S, Rouault J, Magaud J, Berthet C, (2001) In search of a function for the TIS21/PC3/BTG1/TOB family. FEBS Lett 497: 67-72.
    • (2001) FEBS Lett , vol.497 , pp. 67-72
    • Matsuda, S.1    Rouault, J.2    Magaud, J.3    Berthet, C.4
  • 21
    • 20944439879 scopus 로고    scopus 로고
    • The negative cell cycle regulator, Tob (transducer of ErbB-2), is a multifunctional protein involved in hippocampus-dependent learning and memory
    • Jin M, Wang XM, Tu Y, Zhang XH, Gao X, et al. (2005) The negative cell cycle regulator, Tob (transducer of ErbB-2), is a multifunctional protein involved in hippocampus-dependent learning and memory. Neuroscience 131: 647-659.
    • (2005) Neuroscience , vol.131 , pp. 647-659
    • Jin, M.1    Wang, X.M.2    Tu, Y.3    Zhang, X.H.4    Gao, X.5
  • 22
    • 0030050820 scopus 로고    scopus 로고
    • Tob, a novel protein that interacts with p185erbB2, is associated with anti-proliferative activity
    • Matsuda S, Kawamura-Tsuzuku J, Ohsugi M, Yoshida M, Emi M, et al. (1996) Tob, a novel protein that interacts with p185erbB2, is associated with anti-proliferative activity. Oncogene 12: 705-713.
    • (1996) Oncogene , vol.12 , pp. 705-713
    • Matsuda, S.1    Kawamura-Tsuzuku, J.2    Ohsugi, M.3    Yoshida, M.4    Emi, M.5
  • 23
    • 17744389965 scopus 로고    scopus 로고
    • Negative regulation of BMP/Smad signaling by Tob in osteoblasts
    • Yoshida Y, Tanaka S, Umemori H, Minowa O, Usui M, et al. (2000) Negative regulation of BMP/Smad signaling by Tob in osteoblasts. Cell 103: 1085-1097.
    • (2000) Cell , vol.103 , pp. 1085-1097
    • Yoshida, Y.1    Tanaka, S.2    Umemori, H.3    Minowa, O.4    Usui, M.5
  • 24
    • 0347475689 scopus 로고    scopus 로고
    • Tob proteins enhance inhibitory Smad-receptor interactions to repress BMP signaling
    • Yoshida Y, von Bubnoff A, Ikematsu N, Blitz IL, Tsuzuku JK, et al. (2003) Tob proteins enhance inhibitory Smad-receptor interactions to repress BMP signaling. Mech Dev 120: 629-637.
    • (2003) Mech Dev , vol.120 , pp. 629-637
    • Yoshida, Y.1    von Bubnoff, A.2    Ikematsu, N.3    Blitz, I.L.4    Tsuzuku, J.K.5
  • 25
    • 36049016095 scopus 로고    scopus 로고
    • Human TOB, an antiproliferative transcription factor, is a poly(A)-binding protein-dependent positive regulator of cytoplasmic mRNA deadenylation
    • Ezzeddine N, Chang TC, Zhu W, Yamashita A, Chen CY, et al. (2007) Human TOB, an antiproliferative transcription factor, is a poly(A)-binding protein-dependent positive regulator of cytoplasmic mRNA deadenylation. Mol Cell Biol 27: 7791-7801.
    • (2007) Mol Cell Biol , vol.27 , pp. 7791-7801
    • Ezzeddine, N.1    Chang, T.C.2    Zhu, W.3    Yamashita, A.4    Chen, C.Y.5
  • 26
    • 36849079370 scopus 로고    scopus 로고
    • Mechanism of mRNA deadenylation: evidence for a molecular interplay between translation termination factor eRF3 and mRNA deadenylases
    • Funakoshi Y, Doi Y, Hosoda N, Uchida N, Osawa M, et al. (2007) Mechanism of mRNA deadenylation: evidence for a molecular interplay between translation termination factor eRF3 and mRNA deadenylases. Genes Dev 21: 3135-3148.
    • (2007) Genes Dev , vol.21 , pp. 3135-3148
    • Funakoshi, Y.1    Doi, Y.2    Hosoda, N.3    Uchida, N.4    Osawa, M.5
  • 27
    • 41349114842 scopus 로고    scopus 로고
    • Interaction of antiproliferative protein Tob with the CCR4-NOT deadenylase complex
    • Miyasaka T, Morita M, Ito K, Suzuki T, Fukuda H, et al. (2008) Interaction of antiproliferative protein Tob with the CCR4-NOT deadenylase complex. Cancer Sci 99: 755-761.
    • (2008) Cancer Sci , vol.99 , pp. 755-761
    • Miyasaka, T.1    Morita, M.2    Ito, K.3    Suzuki, T.4    Fukuda, H.5
  • 28
    • 20444485379 scopus 로고    scopus 로고
    • xBtg-x regulates Wnt/beta-Catenin signaling during early Xenopus development
    • Wessely O, Kim JI, Tran U, Fuentealba L, De Robertis EM, (2005) xBtg-x regulates Wnt/beta-Catenin signaling during early Xenopus development. Dev Biol 283: 17-28.
    • (2005) Dev Biol , vol.283 , pp. 17-28
    • Wessely, O.1    Kim, J.I.2    Tran, U.3    Fuentealba, L.4    De Robertis, E.M.5
  • 29
    • 47049101429 scopus 로고    scopus 로고
    • An internal thermal sensor controlling temperature preference in Drosophila
    • Hamada FN, Rosenzweig M, Kang K, Pulver SR, Ghezzi A, et al. (2008) An internal thermal sensor controlling temperature preference in Drosophila. Nature 454: 217-220.
    • (2008) Nature , vol.454 , pp. 217-220
    • Hamada, F.N.1    Rosenzweig, M.2    Kang, K.3    Pulver, S.R.4    Ghezzi, A.5
  • 30
    • 79959341475 scopus 로고    scopus 로고
    • Phosphorylation state of a Tob/BTG protein, FOG-3, regulates initiation and maintenance of the Caenorhabditis elegans sperm fate program
    • Lee MH, Kim KW, Morgan CT, Morgan DE, Kimble J, (2011) Phosphorylation state of a Tob/BTG protein, FOG-3, regulates initiation and maintenance of the Caenorhabditis elegans sperm fate program. Proc Natl Acad Sci U S A 108: 9125-9130.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 9125-9130
    • Lee, M.H.1    Kim, K.W.2    Morgan, C.T.3    Morgan, D.E.4    Kimble, J.5
  • 31
    • 0037020164 scopus 로고    scopus 로고
    • Identification of the anti-proliferative protein Tob as a MAPK substrate
    • Maekawa M, Nishida E, Tanoue T, (2002) Identification of the anti-proliferative protein Tob as a MAPK substrate. J Biol Chem 277: 37783-37787.
    • (2002) J Biol Chem , vol.277 , pp. 37783-37787
    • Maekawa, M.1    Nishida, E.2    Tanoue, T.3
  • 32
    • 0035071742 scopus 로고    scopus 로고
    • A serine/threonine kinase p90rsk1 phosphorylates the anti-proliferative protein Tob
    • Suzuki T, Matsuda S, Tsuzuku JK, Yoshida Y, Yamamoto T, (2001) A serine/threonine kinase p90rsk1 phosphorylates the anti-proliferative protein Tob. Genes Cells 6: 131-138.
    • (2001) Genes Cells , vol.6 , pp. 131-138
    • Suzuki, T.1    Matsuda, S.2    Tsuzuku, J.K.3    Yoshida, Y.4    Yamamoto, T.5
  • 33
    • 20444377630 scopus 로고    scopus 로고
    • Bidirectional regulation of cytoplasmic polyadenylation element-binding protein phosphorylation by Ca2+/calmodulin-dependent protein kinase II and protein phosphatase 1 during hippocampal long-term potentiation
    • Atkins CM, Davare MA, Oh MC, Derkach V, Soderling TR, (2005) Bidirectional regulation of cytoplasmic polyadenylation element-binding protein phosphorylation by Ca2+/calmodulin-dependent protein kinase II and protein phosphatase 1 during hippocampal long-term potentiation. J Neurosci 25: 5604-5610.
    • (2005) J Neurosci , vol.25 , pp. 5604-5610
    • Atkins, C.M.1    Davare, M.A.2    Oh, M.C.3    Derkach, V.4    Soderling, T.R.5
  • 34
    • 0033634850 scopus 로고    scopus 로고
    • Phosphorylation of CPEB by Eg2 mediates the recruitment of CPSF into an active cytoplasmic polyadenylation complex
    • Mendez R, Murthy KG, Ryan K, Manley JL, Richter JD, (2000) Phosphorylation of CPEB by Eg2 mediates the recruitment of CPSF into an active cytoplasmic polyadenylation complex. Mol Cell 6: 1253-1259.
    • (2000) Mol Cell , vol.6 , pp. 1253-1259
    • Mendez, R.1    Murthy, K.G.2    Ryan, K.3    Manley, J.L.4    Richter, J.D.5
  • 35
    • 84864311586 scopus 로고    scopus 로고
    • Bidirectional control of mRNA translation and synaptic plasticity by the cytoplasmic polyadenylation complex
    • Udagawa T, Swanger SA, Takeuchi K, Kim JH, Nalavadi V, et al. (2012) Bidirectional control of mRNA translation and synaptic plasticity by the cytoplasmic polyadenylation complex. Mol Cell 47: 253-266.
    • (2012) Mol Cell , vol.47 , pp. 253-266
    • Udagawa, T.1    Swanger, S.A.2    Takeuchi, K.3    Kim, J.H.4    Nalavadi, V.5
  • 36
    • 2342589413 scopus 로고    scopus 로고
    • Recognition of phosphate monoester dianion by an alkoxide-bridged dinuclear zinc(II) complex
    • Kinoshita E, Takahashi M, Takeda H, Shiro M, Koike T, (2004) Recognition of phosphate monoester dianion by an alkoxide-bridged dinuclear zinc(II) complex. Dalton Trans pp. 1189-1193.
    • (2004) Dalton Trans , pp. 1189-1193
    • Kinoshita, E.1    Takahashi, M.2    Takeda, H.3    Shiro, M.4    Koike, T.5
  • 38
    • 0025635610 scopus 로고
    • Tautomycin from the bacterium Streptomyces verticillatus. Another potent and specific inhibitor of protein phosphatases 1 and 2A
    • MacKintosh C, Klumpp S, (1990) Tautomycin from the bacterium Streptomyces verticillatus. Another potent and specific inhibitor of protein phosphatases 1 and 2A. FEBS Lett 277: 137-140.
    • (1990) FEBS Lett , vol.277 , pp. 137-140
    • MacKintosh, C.1    Klumpp, S.2
  • 39
    • 0027202187 scopus 로고
    • Expression, purification, crystallization, and biochemical characterization of a recombinant protein phosphatase
    • Zhuo S, Clemens JC, Hakes DJ, Barford D, Dixon JE, (1993) Expression, purification, crystallization, and biochemical characterization of a recombinant protein phosphatase. J Biol Chem 268: 17754-17761.
    • (1993) J Biol Chem , vol.268 , pp. 17754-17761
    • Zhuo, S.1    Clemens, J.C.2    Hakes, D.J.3    Barford, D.4    Dixon, J.E.5
  • 40
    • 23944519706 scopus 로고    scopus 로고
    • LIM Kinase1 controls synaptic stability downstream of the type II BMP receptor
    • Eaton BA, Davis GW, (2005) LIM Kinase1 controls synaptic stability downstream of the type II BMP receptor. Neuron 47: 695-708.
    • (2005) Neuron , vol.47 , pp. 695-708
    • Eaton, B.A.1    Davis, G.W.2
  • 41
    • 0141656297 scopus 로고    scopus 로고
    • Direct signaling by the BMP type II receptor via the cytoskeletal regulator LIMK1
    • Foletta VC, Lim MA, Soosairajah J, Kelly AP, Stanley EG, et al. (2003) Direct signaling by the BMP type II receptor via the cytoskeletal regulator LIMK1. J Cell Biol 162: 1089-1098.
    • (2003) J Cell Biol , vol.162 , pp. 1089-1098
    • Foletta, V.C.1    Lim, M.A.2    Soosairajah, J.3    Kelly, A.P.4    Stanley, E.G.5
  • 42
    • 67349090396 scopus 로고    scopus 로고
    • LIMK1 acts downstream of BMP signaling in developing retinal ganglion cell axons but not dendrites
    • Hocking JC, Hehr CL, Bertolesi G, Funakoshi H, Nakamura T, et al. (2009) LIMK1 acts downstream of BMP signaling in developing retinal ganglion cell axons but not dendrites. Dev Biol 330: 273-285.
    • (2009) Dev Biol , vol.330 , pp. 273-285
    • Hocking, J.C.1    Hehr, C.L.2    Bertolesi, G.3    Funakoshi, H.4    Nakamura, T.5
  • 43
    • 11244313831 scopus 로고    scopus 로고
    • Activation of LIMK1 by binding to the BMP receptor, BMPRII, regulates BMP-dependent dendritogenesis
    • Lee-Hoeflich ST, Causing CG, Podkowa M, Zhao X, Wrana JL, et al. (2004) Activation of LIMK1 by binding to the BMP receptor, BMPRII, regulates BMP-dependent dendritogenesis. Embo J 23: 4792-4801.
    • (2004) Embo J , vol.23 , pp. 4792-4801
    • Lee-Hoeflich, S.T.1    Causing, C.G.2    Podkowa, M.3    Zhao, X.4    Wrana, J.L.5
  • 44
    • 34347374867 scopus 로고    scopus 로고
    • BMP gradients steer nerve growth cones by a balancing act of LIM kinase and Slingshot phosphatase on ADF/cofilin
    • Wen Z, Han L, Bamburg JR, Shim S, Ming GL, et al. (2007) BMP gradients steer nerve growth cones by a balancing act of LIM kinase and Slingshot phosphatase on ADF/cofilin. J Cell Biol 178: 107-119.
    • (2007) J Cell Biol , vol.178 , pp. 107-119
    • Wen, Z.1    Han, L.2    Bamburg, J.R.3    Shim, S.4    Ming, G.L.5
  • 45
    • 33745004382 scopus 로고    scopus 로고
    • Lim kinase regulates the development of olfactory and neuromuscular synapses
    • Ang LH, Chen W, Yao Y, Ozawa R, Tao E, et al. (2006) Lim kinase regulates the development of olfactory and neuromuscular synapses. Dev Biol 293: 178-190.
    • (2006) Dev Biol , vol.293 , pp. 178-190
    • Ang, L.H.1    Chen, W.2    Yao, Y.3    Ozawa, R.4    Tao, E.5
  • 46
    • 18444372636 scopus 로고    scopus 로고
    • Abnormal spine morphology and enhanced LTP in LIMK-1 knockout mice
    • Meng Y, Zhang Y, Tregoubov V, Janus C, Cruz L, et al. (2002) Abnormal spine morphology and enhanced LTP in LIMK-1 knockout mice. Neuron 35: 121-133.
    • (2002) Neuron , vol.35 , pp. 121-133
    • Meng, Y.1    Zhang, Y.2    Tregoubov, V.3    Janus, C.4    Cruz, L.5
  • 47
    • 0028360968 scopus 로고
    • The mating of a fly
    • Hall JC, (1994) The mating of a fly. Science 264: 1702-1714.
    • (1994) Science , vol.264 , pp. 1702-1714
    • Hall, J.C.1
  • 48
    • 0034724897 scopus 로고    scopus 로고
    • Localization of a short-term memory in Drosophila
    • Zars T, Fischer M, Schulz R, Heisenberg M, (2000) Localization of a short-term memory in Drosophila. Science 288: 672-675.
    • (2000) Science , vol.288 , pp. 672-675
    • Zars, T.1    Fischer, M.2    Schulz, R.3    Heisenberg, M.4
  • 49
    • 27944476273 scopus 로고    scopus 로고
    • A role for protein phosphatases 1, 2A, and 2B in cerebellar long-term potentiation
    • Belmeguenai A, Hansel C, (2005) A role for protein phosphatases 1, 2A, and 2B in cerebellar long-term potentiation. J Neurosci 25: 10768-10772.
    • (2005) J Neurosci , vol.25 , pp. 10768-10772
    • Belmeguenai, A.1    Hansel, C.2
  • 50
    • 0242493699 scopus 로고    scopus 로고
    • Kinetic simulation of signal transduction system in hippocampal long-term potentiation with dynamic modeling of protein phosphatase 2A
    • Kikuchi S, Fujimoto K, Kitagawa N, Fuchikawa T, Abe M, et al. (2003) Kinetic simulation of signal transduction system in hippocampal long-term potentiation with dynamic modeling of protein phosphatase 2A. Neural Netw 16: 1389-1398.
    • (2003) Neural Netw , vol.16 , pp. 1389-1398
    • Kikuchi, S.1    Fujimoto, K.2    Kitagawa, N.3    Fuchikawa, T.4    Abe, M.5
  • 51
    • 0027432518 scopus 로고
    • An essential role for protein phosphatases in hippocampal long-term depression
    • Mulkey RM, Herron CE, Malenka RC, (1993) An essential role for protein phosphatases in hippocampal long-term depression. Science 261: 1051-1055.
    • (1993) Science , vol.261 , pp. 1051-1055
    • Mulkey, R.M.1    Herron, C.E.2    Malenka, R.C.3
  • 52
    • 77955389691 scopus 로고    scopus 로고
    • Drosophila Orb2 targets genes involved in neuronal growth, synapse formation, and protein turnover
    • Mastushita-Sakai T, White-Grindley E, Samuelson J, Seidel C, Si K, (2010) Drosophila Orb2 targets genes involved in neuronal growth, synapse formation, and protein turnover. Proc Natl Acad Sci U S A 107: 11987-11992.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 11987-11992
    • Mastushita-Sakai, T.1    White-Grindley, E.2    Samuelson, J.3    Seidel, C.4    Si, K.5
  • 53
    • 70350176190 scopus 로고    scopus 로고
    • Genetic modifiers of dFMR1 encode RNA granule components in Drosophila
    • Cziko AM, McCann CT, Howlett IC, Barbee SA, Duncan RP, et al. (2009) Genetic modifiers of dFMR1 encode RNA granule components in Drosophila. Genetics 182: 1051-1060.
    • (2009) Genetics , vol.182 , pp. 1051-1060
    • Cziko, A.M.1    McCann, C.T.2    Howlett, I.C.3    Barbee, S.A.4    Duncan, R.P.5
  • 54
    • 0033539924 scopus 로고    scopus 로고
    • Tob2, a novel anti-proliferative Tob/BTG1 family member, associates with a component of the CCR4 transcriptional regulatory complex capable of binding cyclin-dependent kinases
    • Ikematsu N, Yoshida Y, Kawamura-Tsuzuku J, Ohsugi M, Onda M, et al. (1999) Tob2, a novel anti-proliferative Tob/BTG1 family member, associates with a component of the CCR4 transcriptional regulatory complex capable of binding cyclin-dependent kinases. Oncogene 18: 7432-7441.
    • (1999) Oncogene , vol.18 , pp. 7432-7441
    • Ikematsu, N.1    Yoshida, Y.2    Kawamura-Tsuzuku, J.3    Ohsugi, M.4    Onda, M.5
  • 55
    • 41949099124 scopus 로고    scopus 로고
    • The BTG2 protein is a general activator of mRNA deadenylation
    • Mauxion F, Faux C, Seraphin B, (2008) The BTG2 protein is a general activator of mRNA deadenylation. Embo J 27: 1039-1048.
    • (2008) Embo J , vol.27 , pp. 1039-1048
    • Mauxion, F.1    Faux, C.2    Seraphin, B.3
  • 56
    • 33746751550 scopus 로고    scopus 로고
    • Tob1 controls dorsal development of zebrafish embryos by antagonizing maternal beta-catenin transcriptional activity
    • Xiong B, Rui Y, Zhang M, Shi K, Jia S, et al. (2006) Tob1 controls dorsal development of zebrafish embryos by antagonizing maternal beta-catenin transcriptional activity. Dev Cell 11: 225-238.
    • (2006) Dev Cell , vol.11 , pp. 225-238
    • Xiong, B.1    Rui, Y.2    Zhang, M.3    Shi, K.4    Jia, S.5
  • 57
    • 0037075207 scopus 로고    scopus 로고
    • wishful thinking encodes a BMP type II receptor that regulates synaptic growth in Drosophila
    • Aberle H, Haghighi AP, Fetter RD, McCabe BD, Magalhaes TR, et al. (2002) wishful thinking encodes a BMP type II receptor that regulates synaptic growth in Drosophila. Neuron 33: 545-558.
    • (2002) Neuron , vol.33 , pp. 545-558
    • Aberle, H.1    Haghighi, A.P.2    Fetter, R.D.3    McCabe, B.D.4    Magalhaes, T.R.5
  • 58
    • 3843118935 scopus 로고    scopus 로고
    • Synaptic strengthening mediated by bone morphogenetic protein-dependent retrograde signaling in the Drosophila CNS
    • Baines RA, (2004) Synaptic strengthening mediated by bone morphogenetic protein-dependent retrograde signaling in the Drosophila CNS. J Neurosci 24: 6904-6911.
    • (2004) J Neurosci , vol.24 , pp. 6904-6911
    • Baines, R.A.1
  • 59
    • 12144289951 scopus 로고    scopus 로고
    • Highwire regulates presynaptic BMP signaling essential for synaptic growth
    • McCabe BD, Hom S, Aberle H, Fetter RD, Marques G, et al. (2004) Highwire regulates presynaptic BMP signaling essential for synaptic growth. Neuron 41: 891-905.
    • (2004) Neuron , vol.41 , pp. 891-905
    • McCabe, B.D.1    Hom, S.2    Aberle, H.3    Fetter, R.D.4    Marques, G.5
  • 60
    • 0042964820 scopus 로고    scopus 로고
    • The BMP homolog Gbb provides a retrograde signal that regulates synaptic growth at the Drosophila neuromuscular junction
    • McCabe BD, Marques G, Haghighi AP, Fetter RD, Crotty ML, et al. (2003) The BMP homolog Gbb provides a retrograde signal that regulates synaptic growth at the Drosophila neuromuscular junction. Neuron 39: 241-254.
    • (2003) Neuron , vol.39 , pp. 241-254
    • McCabe, B.D.1    Marques, G.2    Haghighi, A.P.3    Fetter, R.D.4    Crotty, M.L.5
  • 61
    • 0029089595 scopus 로고
    • Subdivision of the Drosophila mushroom bodies by enhancer-trap expression patterns
    • Yang MY, Armstrong JD, Vilinsky I, Strausfeld NJ, Kaiser K, (1995) Subdivision of the Drosophila mushroom bodies by enhancer-trap expression patterns. Neuron 15: 45-54.
    • (1995) Neuron , vol.15 , pp. 45-54
    • Yang, M.Y.1    Armstrong, J.D.2    Vilinsky, I.3    Strausfeld, N.J.4    Kaiser, K.5
  • 62
    • 0035940416 scopus 로고    scopus 로고
    • A conditional tissue-specific transgene expression system using inducible GAL4
    • Osterwalder T, Yoon KS, White BH, Keshishian H, (2001) A conditional tissue-specific transgene expression system using inducible GAL4. Proc Natl Acad Sci U S A 98: 12596-12601.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 12596-12601
    • Osterwalder, T.1    Yoon, K.S.2    White, B.H.3    Keshishian, H.4
  • 63
    • 0033378174 scopus 로고    scopus 로고
    • Mushroom body ablation impairs short-term memory and long-term memory of courtship conditioning in Drosophila melanogaster
    • McBride SM, Giuliani G, Choi C, Krause P, Correale D, et al. (1999) Mushroom body ablation impairs short-term memory and long-term memory of courtship conditioning in Drosophila melanogaster. Neuron 24: 967-977.
    • (1999) Neuron , vol.24 , pp. 967-977
    • McBride, S.M.1    Giuliani, G.2    Choi, C.3    Krause, P.4    Correale, D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.