메뉴 건너뛰기




Volumn 46, Issue 2, 2011, Pages 483-497

F-spondin regulates neuronal survival through activation of disabled-1 in the chicken ciliary ganglion

Author keywords

APP; Ciliary ganglion; Disabled 1; Extracellular matrix; F spondin; Programmed cell death; Transforming growth factor beta

Indexed keywords

BLOCKING ANTIBODY; MEMBRANE PROTEIN; PROTEIN DISABLED 1; PROTEIN F SPONDIN; RECEPTOR; REELIN; THROMBOSPONDIN; THROMBOSPONDIN 1; TRANSFORMING GROWTH FACTOR BETA; UNCLASSIFIED DRUG;

EID: 78751704969     PISSN: 10447431     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mcn.2010.12.001     Document Type: Article
Times cited : (13)

References (90)
  • 1
    • 0028328817 scopus 로고
    • An assay for transforming growth factor-beta using cells transfected with a plasminogen activator inhibitor-1 promoter-luciferase construct
    • Abe M., Harpel J.G., Metz C.N., Nunes I., Loskutoff D.J., Rifkin D.B. An assay for transforming growth factor-beta using cells transfected with a plasminogen activator inhibitor-1 promoter-luciferase construct. Anal. Biochem. 1994, 216:276-284.
    • (1994) Anal. Biochem. , vol.216 , pp. 276-284
    • Abe, M.1    Harpel, J.G.2    Metz, C.N.3    Nunes, I.4    Loskutoff, D.J.5    Rifkin, D.B.6
  • 2
    • 0037439630 scopus 로고    scopus 로고
    • Making sense of latent TGFbeta activation
    • Annes J.P., Munger J.S., Rifkin D.B. Making sense of latent TGFbeta activation. J. Cell Sci. 2003, 116:217-224.
    • (2003) J. Cell Sci. , vol.116 , pp. 217-224
    • Annes, J.P.1    Munger, J.S.2    Rifkin, D.B.3
  • 3
    • 0025514410 scopus 로고
    • Survival effect of ciliary neurotrophic factor (CNTF) on chick embryonic motoneurons in culture: comparison with other neurotrophic factors and cytokines
    • Arakawa Y., Sendtner M., Thoenen H. Survival effect of ciliary neurotrophic factor (CNTF) on chick embryonic motoneurons in culture: comparison with other neurotrophic factors and cytokines. J. Neurosci. 1990, 10:3507-3515.
    • (1990) J. Neurosci. , vol.10 , pp. 3507-3515
    • Arakawa, Y.1    Sendtner, M.2    Thoenen, H.3
  • 5
    • 0021686832 scopus 로고
    • Purification of the chick eye ciliary neuronotrophic factor
    • Barbin G., Manthorpe M., Varon S. Purification of the chick eye ciliary neuronotrophic factor. J. Neurochem. 1984, 43:1468-1478.
    • (1984) J. Neurochem. , vol.43 , pp. 1468-1478
    • Barbin, G.1    Manthorpe, M.2    Varon, S.3
  • 7
    • 0018865660 scopus 로고
    • Selective survival of neurons from chick embryo sensory ganglionic dissociates utilizing serum-free supplemented medium
    • Bottenstein J.E., Skaper S.D., Varon S.S., Sato G.H. Selective survival of neurons from chick embryo sensory ganglionic dissociates utilizing serum-free supplemented medium. Exp. Cell Res. 1980, 125:183-190.
    • (1980) Exp. Cell Res. , vol.125 , pp. 183-190
    • Bottenstein, J.E.1    Skaper, S.D.2    Varon, S.S.3    Sato, G.H.4
  • 8
    • 0033773180 scopus 로고    scopus 로고
    • The transforming growth factor-betas: structure, signaling, and roles in nervous system development and functions
    • Böttner M., Krieglstein K., Unsicker K. The transforming growth factor-betas: structure, signaling, and roles in nervous system development and functions. J. Neurochem. 2000, 75:2227-2240.
    • (2000) J. Neurochem. , vol.75 , pp. 2227-2240
    • Böttner, M.1    Krieglstein, K.2    Unsicker, K.3
  • 9
    • 0032211047 scopus 로고    scopus 로고
    • Accumulation of F-spondin in injured peripheral nerve promotes the outgrowth of sensory axons
    • Burstyn-Cohen T., Frumkin A., Xu Y.T., Scherer S.S., Klar A. Accumulation of F-spondin in injured peripheral nerve promotes the outgrowth of sensory axons. J. Neurosci. 1998, 18:8875-8885.
    • (1998) J. Neurosci. , vol.18 , pp. 8875-8885
    • Burstyn-Cohen, T.1    Frumkin, A.2    Xu, Y.T.3    Scherer, S.S.4    Klar, A.5
  • 10
    • 0033151663 scopus 로고    scopus 로고
    • F-Spondin is required for accurate pathfinding of commissural axons at the floor plate
    • Burstyn-Cohen T., Tzarfaty V., Frumkin A., Feinstein Y., Stoeckli E., Klar A. F-Spondin is required for accurate pathfinding of commissural axons at the floor plate. Neuron 1999, 23:233-246.
    • (1999) Neuron , vol.23 , pp. 233-246
    • Burstyn-Cohen, T.1    Tzarfaty, V.2    Frumkin, A.3    Feinstein, Y.4    Stoeckli, E.5    Klar, A.6
  • 11
    • 33747869352 scopus 로고    scopus 로고
    • Adaptive roles of programmed cell death during nervous system development
    • Buss R.R., Sun W., Oppenheim R.W. Adaptive roles of programmed cell death during nervous system development. Annu. Rev. Neurosci. 2006, 29:1-35.
    • (2006) Annu. Rev. Neurosci. , vol.29 , pp. 1-35
    • Buss, R.R.1    Sun, W.2    Oppenheim, R.W.3
  • 13
    • 0026793958 scopus 로고
    • Molecular cloning and DNA sequence analysis of cDNA encoding chicken homologue of the Bcl-2 oncoprotein
    • Cazals-Hatem D.L., Louie D.C., Tanaka S., Reed J.C. Molecular cloning and DNA sequence analysis of cDNA encoding chicken homologue of the Bcl-2 oncoprotein. Biochim. Biophys. Acta 1992, 1132:109-113.
    • (1992) Biochim. Biophys. Acta , vol.1132 , pp. 109-113
    • Cazals-Hatem, D.L.1    Louie, D.C.2    Tanaka, S.3    Reed, J.C.4
  • 14
    • 0028940096 scopus 로고
    • A protein related to extracellular matrix proteins deleted in the mouse mutant reeler
    • D'Arcangelo G., Miao G.G., Chen S.C., Soares H.D., Morgan J.I., Curran T. A protein related to extracellular matrix proteins deleted in the mouse mutant reeler. Nature 1995, 374:719-723.
    • (1995) Nature , vol.374 , pp. 719-723
    • D'Arcangelo, G.1    Miao, G.G.2    Chen, S.C.3    Soares, H.D.4    Morgan, J.I.5    Curran, T.6
  • 16
    • 0030702123 scopus 로고    scopus 로고
    • Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
    • Datta S.R., Dudek H., Tao X., Masters S., Fu H., Gotoh Y., Greenberg M.E. Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell 1997, 91:231-241.
    • (1997) Cell , vol.91 , pp. 231-241
    • Datta, S.R.1    Dudek, H.2    Tao, X.3    Masters, S.4    Fu, H.5    Gotoh, Y.6    Greenberg, M.E.7
  • 17
    • 0038201542 scopus 로고    scopus 로고
    • Regulation of neuronal survival and death by extracellular signals during development
    • Davies A.M. Regulation of neuronal survival and death by extracellular signals during development. EMBO J. 2003, 22:2537-2545.
    • (2003) EMBO J. , vol.22 , pp. 2537-2545
    • Davies, A.M.1
  • 18
    • 33748932378 scopus 로고    scopus 로고
    • The extracellular matrix and synapses
    • Dityatev A., Schachner M. The extracellular matrix and synapses. Cell Tissue Res. 2006, 326:647-654.
    • (2006) Cell Tissue Res. , vol.326 , pp. 647-654
    • Dityatev, A.1    Schachner, M.2
  • 19
    • 0026585737 scopus 로고
    • Changes in the electrical properties of chick ciliary ganglion neurones during embryonic development
    • Dourado M.M., Dryer S.E. Changes in the electrical properties of chick ciliary ganglion neurones during embryonic development. J. Physiol. 1992, 449:411-428.
    • (1992) J. Physiol. , vol.449 , pp. 411-428
    • Dourado, M.M.1    Dryer, S.E.2
  • 20
    • 1342321750 scopus 로고    scopus 로고
    • PI 3-kinase. Akt and cell survival
    • Downward J. PI 3-kinase. Akt and cell survival. Semin. Cell Dev. Biol. 2004, 15:177-182.
    • (2004) Semin. Cell Dev. Biol. , vol.15 , pp. 177-182
    • Downward, J.1
  • 21
    • 0032484019 scopus 로고    scopus 로고
    • CREB is a regulatory target for the proteinkinase Akt/PKB
    • Du K., Montminy M. CREB is a regulatory target for the proteinkinase Akt/PKB. J. Biol. Chem. 1998, 273:32377-32379.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32377-32379
    • Du, K.1    Montminy, M.2
  • 22
    • 58149175555 scopus 로고    scopus 로고
    • The life of a cell: apoptosis regulation by the PI3K/PKB pathway
    • Duronio V. The life of a cell: apoptosis regulation by the PI3K/PKB pathway. Biochem. J. 2008, 415:333-344.
    • (2008) Biochem. J. , vol.415 , pp. 333-344
    • Duronio, V.1
  • 23
    • 0343237235 scopus 로고
    • The heparin-binding domain of laminin is responsible for its effects on neurite outgrowth and neuronal survival
    • Edgar D., Timpl R., Thoenen H. The heparin-binding domain of laminin is responsible for its effects on neurite outgrowth and neuronal survival. EMBO J. 1984, 3:1463-1468.
    • (1984) EMBO J. , vol.3 , pp. 1463-1468
    • Edgar, D.1    Timpl, R.2    Thoenen, H.3
  • 24
    • 0026640706 scopus 로고
    • Isolation and characterization of the chicken bcl-2 gene: expression in a variety of tissues including lymphoid and neuronal organs in adult and embryo
    • Eguchi Y., Ewert D.L., Tsujimoto Y. Isolation and characterization of the chicken bcl-2 gene: expression in a variety of tissues including lymphoid and neuronal organs in adult and embryo. Nucleic Acids Res. 1992, 20:4187-4192.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 4187-4192
    • Eguchi, Y.1    Ewert, D.L.2    Tsujimoto, Y.3
  • 25
    • 0026638915 scopus 로고
    • Early stages of motor neuron differentiation revealed by expression of homeobox gene Islet-1
    • Ericson J., Thor S., Edlund T., Jessell T.M., Yamada T. Early stages of motor neuron differentiation revealed by expression of homeobox gene Islet-1. Science 1992, 256:1555-1560.
    • (1992) Science , vol.256 , pp. 1555-1560
    • Ericson, J.1    Thor, S.2    Edlund, T.3    Jessell, T.M.4    Yamada, T.5
  • 26
    • 0031437818 scopus 로고    scopus 로고
    • The developmental expression of choline acetyltransferase (ChAT) and the neuropeptide VIP in chick sympathetic neurons: evidence for different regulatory events in cholinergic differentiation
    • Ernsberger U., Patzke H., Rohrer H. The developmental expression of choline acetyltransferase (ChAT) and the neuropeptide VIP in chick sympathetic neurons: evidence for different regulatory events in cholinergic differentiation. Mech. Dev. 1997, 68:115-126.
    • (1997) Mech. Dev. , vol.68 , pp. 115-126
    • Ernsberger, U.1    Patzke, H.2    Rohrer, H.3
  • 27
    • 16544366593 scopus 로고    scopus 로고
    • The neuronal class 2 TSR proteins F-spondin and Mindin: a small family with divergent biological activities
    • Feinstein Y., Klar A. The neuronal class 2 TSR proteins F-spondin and Mindin: a small family with divergent biological activities. Int. J. Biochem. Cell Biol. 2004, 36:975-980.
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 975-980
    • Feinstein, Y.1    Klar, A.2
  • 29
    • 0029963838 scopus 로고    scopus 로고
    • Expression of a chicken ciliary neurotrophic factor in targets of ciliary ganglion neurons during and after the cell-death phase
    • Finn T.P., Nishi R. Expression of a chicken ciliary neurotrophic factor in targets of ciliary ganglion neurons during and after the cell-death phase. J. Comp. Neurol. 1996, 366:559-571.
    • (1996) J. Comp. Neurol. , vol.366 , pp. 559-571
    • Finn, T.P.1    Nishi, R.2
  • 30
    • 79961211320 scopus 로고    scopus 로고
    • The Crosstalk of RAS with the TGF-beta Family during Carcinoma Progression and its Implications for Targeted Cancer Therapy
    • 20718708
    • Grusch M., Petz M., Metzner T., Oztürk D., Schneller D., Mikulits W. The Crosstalk of RAS with the TGF-beta Family during Carcinoma Progression and its Implications for Targeted Cancer Therapy. Curr. Cancer Drug Targets PMID 2010, 20718708.
    • (2010) Curr. Cancer Drug Targets PMID
    • Grusch, M.1    Petz, M.2    Metzner, T.3    Oztürk, D.4    Schneller, D.5    Mikulits, W.6
  • 31
    • 0034772594 scopus 로고    scopus 로고
    • GDNF and neurturin are target-derived factors essential for cranial parasympathetic neuron development
    • Hashino E., Shero M., Junghans D., Rohrer H., Milbrandt J., Johnson E.M. GDNF and neurturin are target-derived factors essential for cranial parasympathetic neuron development. Development 2001, 128:3773-3782.
    • (2001) Development , vol.128 , pp. 3773-3782
    • Hashino, E.1    Shero, M.2    Junghans, D.3    Rohrer, H.4    Milbrandt, J.5    Johnson, E.M.6
  • 32
    • 0031885706 scopus 로고    scopus 로고
    • Lost caps in histological counting methods
    • Hedreen J.C. Lost caps in histological counting methods. Anat. Rec. 1998, 250:366-372.
    • (1998) Anat. Rec. , vol.250 , pp. 366-372
    • Hedreen, J.C.1
  • 33
    • 33750333569 scopus 로고    scopus 로고
    • Reelin, lipoprotein receptors and synaptic plasticity
    • Herz J., Chen Y. Reelin, lipoprotein receptors and synaptic plasticity. Nat. Rev. Neurosci. 2006, 7:850-859.
    • (2006) Nat. Rev. Neurosci. , vol.7 , pp. 850-859
    • Herz, J.1    Chen, Y.2
  • 34
    • 0025786502 scopus 로고
    • 39-kDa protein modulates binding of ligands to low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor
    • Herz J., Goldstein J.L., Strickland D.K., Ho Y.K., Brown M.S. 39-kDa protein modulates binding of ligands to low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor. J. Biol. Chem. 1991, 266:21232-21238.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21232-21238
    • Herz, J.1    Goldstein, J.L.2    Strickland, D.K.3    Ho, Y.K.4    Brown, M.S.5
  • 35
    • 0033213319 scopus 로고    scopus 로고
    • Direct binding of Reelin to VLDL receptor and ApoE receptor 2 induces tyrosine phosphorylation of disabled-1 and modulates tau phosphorylation
    • Hiesberger T., Trommsdorff M., Howell B.W., Goffinet A., Mumby M.C., Cooper J.A., Herz J. Direct binding of Reelin to VLDL receptor and ApoE receptor 2 induces tyrosine phosphorylation of disabled-1 and modulates tau phosphorylation. Neuron 1999, 24:481-489.
    • (1999) Neuron , vol.24 , pp. 481-489
    • Hiesberger, T.1    Trommsdorff, M.2    Howell, B.W.3    Goffinet, A.4    Mumby, M.C.5    Cooper, J.A.6    Herz, J.7
  • 36
    • 1442306058 scopus 로고    scopus 로고
    • Binding of F-spondin to amyloid-beta precursor protein: a candidate amyloid-beta precursor protein ligand that modulates amyloid-beta precursor protein cleavage
    • Ho A., Südhof T.C. Binding of F-spondin to amyloid-beta precursor protein: a candidate amyloid-beta precursor protein ligand that modulates amyloid-beta precursor protein cleavage. Proc. Natl Acad. Sci. USA 2004, 101:2548-2553.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 2548-2553
    • Ho, A.1    Südhof, T.C.2
  • 37
    • 50849122319 scopus 로고    scopus 로고
    • Functional interactions of APP with the apoE receptor family
    • Hoe H.S., Rebeck G.W. Functional interactions of APP with the apoE receptor family. J. Neurochem. 2008, 106:2263-2271.
    • (2008) J. Neurochem. , vol.106 , pp. 2263-2271
    • Hoe, H.S.1    Rebeck, G.W.2
  • 38
    • 27144504391 scopus 로고    scopus 로고
    • F-spondin interaction with the apolipoprotein E receptor ApoEr2 affects processing of amyloid precursor protein
    • Hoe H.S., Wessner D., Beffert U., Becker A.G., Matsuoka Y., Rebeck G.W. F-spondin interaction with the apolipoprotein E receptor ApoEr2 affects processing of amyloid precursor protein. Mol. Cell. Biol. 2005, 25:9259-9268.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 9259-9268
    • Hoe, H.S.1    Wessner, D.2    Beffert, U.3    Becker, A.G.4    Matsuoka, Y.5    Rebeck, G.W.6
  • 39
    • 0033198295 scopus 로고    scopus 로고
    • Disabled-1 binds to the cytoplasmic domain of amyloid precursor-like protein 1
    • Homayouni R., Rice D.S., Sheldon M., Curran T. Disabled-1 binds to the cytoplasmic domain of amyloid precursor-like protein 1. J. Neurosci. 1999, 19:7507-7515.
    • (1999) J. Neurosci. , vol.19 , pp. 7507-7515
    • Homayouni, R.1    Rice, D.S.2    Sheldon, M.3    Curran, T.4
  • 40
    • 0033066680 scopus 로고    scopus 로고
    • The disabled 1 phosphotyrosine-binding domain binds to the internalization signals of transmembrane glycoproteins and to phospholipids
    • Howell B.W., Lanier L.M., Frank R., Gertler F.B., Cooper J.A. The disabled 1 phosphotyrosine-binding domain binds to the internalization signals of transmembrane glycoproteins and to phospholipids. Mol. Cell. Biol. 1999, 19:5179-5188.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5179-5188
    • Howell, B.W.1    Lanier, L.M.2    Frank, R.3    Gertler, F.B.4    Cooper, J.A.5
  • 41
    • 0041488911 scopus 로고    scopus 로고
    • Trk receptors: roles in neuronal signal transduction
    • Huang E.J., Reichardt L.F. Trk receptors: roles in neuronal signal transduction. Annu. Rev. Biochem. 2003, 72:609-642.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 609-642
    • Huang, E.J.1    Reichardt, L.F.2
  • 43
    • 2442596967 scopus 로고    scopus 로고
    • Alternative splicing modulates Disabled-1 (Dab1) function in the developing chick retina
    • Katyal S., Godbout R. Alternative splicing modulates Disabled-1 (Dab1) function in the developing chick retina. Embo J. 2004, 23:1878-1888.
    • (2004) Embo J. , vol.23 , pp. 1878-1888
    • Katyal, S.1    Godbout, R.2
  • 44
    • 0035844278 scopus 로고    scopus 로고
    • Identification of reelin-induced sites of tyrosyl phosphorylation on disabled 1
    • Keshvara L., Benhayon D., Magdaleno S., Curran T. Identification of reelin-induced sites of tyrosyl phosphorylation on disabled 1. J. Biol. Chem. 2001, 276:16008-16014.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16008-16014
    • Keshvara, L.1    Benhayon, D.2    Magdaleno, S.3    Curran, T.4
  • 45
    • 0026770381 scopus 로고
    • F-spondin: a gene expressed at high levels in the floor plate encodes a secreted protein that promotes neural cell adhesion and neurite extension
    • Klar A., Baldassare M., Jessell T.M. F-spondin: a gene expressed at high levels in the floor plate encodes a secreted protein that promotes neural cell adhesion and neurite extension. Cell 1992, 69:95-110.
    • (1992) Cell , vol.69 , pp. 95-110
    • Klar, A.1    Baldassare, M.2    Jessell, T.M.3
  • 46
    • 0027195615 scopus 로고
    • The neurotrophic factor concept: a reexamination
    • Korsching S. The neurotrophic factor concept: a reexamination. J. Neurosci. 1993, 13:2739-2748.
    • (1993) J. Neurosci. , vol.13 , pp. 2739-2748
    • Korsching, S.1
  • 47
    • 0031794123 scopus 로고    scopus 로고
    • TGF-beta regulates the survival of ciliary ganglionic neurons synergistically with ciliary neurotrophic factor and neurotrophins
    • Krieglstein K., Farkas L., Unsicker K. TGF-beta regulates the survival of ciliary ganglionic neurons synergistically with ciliary neurotrophic factor and neurotrophins. J. Neurobiol. 1998, 37:563-572.
    • (1998) J. Neurobiol. , vol.37 , pp. 563-572
    • Krieglstein, K.1    Farkas, L.2    Unsicker, K.3
  • 48
    • 0032403377 scopus 로고    scopus 로고
    • Glial cell line-derived neurotrophic factor requires transforming growth factor-beta for exerting its full neurotrophic potential on peripheral and CNS neurons
    • Krieglstein K., Henheik P., Farkas L., Jaszai J., Galter D., Krohn K., Unsicker K. Glial cell line-derived neurotrophic factor requires transforming growth factor-beta for exerting its full neurotrophic potential on peripheral and CNS neurons. J. Neurosci. 1998, 18:9822-9834.
    • (1998) J. Neurosci. , vol.18 , pp. 9822-9834
    • Krieglstein, K.1    Henheik, P.2    Farkas, L.3    Jaszai, J.4    Galter, D.5    Krohn, K.6    Unsicker, K.7
  • 50
    • 0028070847 scopus 로고
    • Trophic factors from chromaffin granules promote survival of peripheral and central nervous system neurons
    • Lachmund A., Gehrke D., Krieglstein K., Unsicker K. Trophic factors from chromaffin granules promote survival of peripheral and central nervous system neurons. Neuroscience 1994, 62:361-370.
    • (1994) Neuroscience , vol.62 , pp. 361-370
    • Lachmund, A.1    Gehrke, D.2    Krieglstein, K.3    Unsicker, K.4
  • 51
    • 0016283634 scopus 로고
    • Synaptic transmission and cell death during normal ganglionic development
    • Landmesser L., Pilar G. Synaptic transmission and cell death during normal ganglionic development. J. Physiol. 1974, 241:737-749.
    • (1974) J. Physiol. , vol.241 , pp. 737-749
    • Landmesser, L.1    Pilar, G.2
  • 52
    • 0022335318 scopus 로고
    • Conversion of a high molecular weight latent beta-TGF from chicken embryo fibroblasts into a low molecular weight active beta-TGF under acidic conditions
    • Lawrence D.A., Pircher R., Jullien P. Conversion of a high molecular weight latent beta-TGF from chicken embryo fibroblasts into a low molecular weight active beta-TGF under acidic conditions. Biochem. Biophys. Res. Commun. 1985, 133:1026-1034.
    • (1985) Biochem. Biophys. Res. Commun. , vol.133 , pp. 1026-1034
    • Lawrence, D.A.1    Pircher, R.2    Jullien, P.3
  • 53
    • 0033558875 scopus 로고    scopus 로고
    • Role of Nr13 in regulation of programmed cell death in the bursa of Fabricius
    • Lee R.M., Gillet G., Burnside J., Thomas S.J., Neiman P. Role of Nr13 in regulation of programmed cell death in the bursa of Fabricius. Genes Dev. 1999, 13:718-728.
    • (1999) Genes Dev. , vol.13 , pp. 718-728
    • Lee, R.M.1    Gillet, G.2    Burnside, J.3    Thomas, S.J.4    Neiman, P.5
  • 54
    • 0035873538 scopus 로고    scopus 로고
    • Cell death and neuronal replacement during formation of the avian ciliary ganglion
    • Lee V.M., Smiley G.G., Nishi R. Cell death and neuronal replacement during formation of the avian ciliary ganglion. Dev. Biol. 2001, 233:437-448.
    • (2001) Dev. Biol. , vol.233 , pp. 437-448
    • Lee, V.M.1    Smiley, G.G.2    Nishi, R.3
  • 55
    • 50549180370 scopus 로고
    • Essential role of the nerve growth factor in the survival and maintenance of dissociated sensory and sympathetic embryonic nerve cells in vitro
    • Levi-Montalcini R., Angeletti P.U. Essential role of the nerve growth factor in the survival and maintenance of dissociated sensory and sympathetic embryonic nerve cells in vitro. Dev. Biol. 1963, 7:653-659.
    • (1963) Dev. Biol. , vol.7 , pp. 653-659
    • Levi-Montalcini, R.1    Angeletti, P.U.2
  • 56
    • 34250788809 scopus 로고    scopus 로고
    • AKT/PKB signaling: navigating downstream
    • Manning B.D., Cantley L.C. AKT/PKB signaling: navigating downstream. Cell 2007, 129:1261-1274.
    • (2007) Cell , vol.129 , pp. 1261-1274
    • Manning, B.D.1    Cantley, L.C.2
  • 57
    • 0021926560 scopus 로고
    • Purified proteins acting on cultured chick embryo ciliary ganglion neurons
    • Manthorpe M., Davis G.E., Varon S. Purified proteins acting on cultured chick embryo ciliary ganglion neurons. Fed. Proc. 1985, 44:2753-2759.
    • (1985) Fed. Proc. , vol.44 , pp. 2753-2759
    • Manthorpe, M.1    Davis, G.E.2    Varon, S.3
  • 58
    • 0015235748 scopus 로고
    • Characterization of two ganglion cell populations in avian ciliary ganglia
    • Marwitt R., Pilar G., Weakly J.N. Characterization of two ganglion cell populations in avian ciliary ganglia. Brain Res. 1971, 25:317-334.
    • (1971) Brain Res. , vol.25 , pp. 317-334
    • Marwitt, R.1    Pilar, G.2    Weakly, J.N.3
  • 59
    • 0023492085 scopus 로고
    • Cholinergic innervation of the smooth muscle cells in the choroid coat of the chick eye and its development
    • Meriney S.D., Pilar G. Cholinergic innervation of the smooth muscle cells in the choroid coat of the chick eye and its development. J. Neurosci. 1987, 7:3827-3839.
    • (1987) J. Neurosci. , vol.7 , pp. 3827-3839
    • Meriney, S.D.1    Pilar, G.2
  • 60
    • 0026663993 scopus 로고
    • The amyloid protein precursor of Alzheimer's disease is a mediator of the effects of nerve growth factor on neurite outgrowth
    • Milward E.A., Papadopoulos R., Fuller S.J., Moir R.D., Small D., Beyreuther K., Masters C.L. The amyloid protein precursor of Alzheimer's disease is a mediator of the effects of nerve growth factor on neurite outgrowth. Neuron 1992, 9:129-137.
    • (1992) Neuron , vol.9 , pp. 129-137
    • Milward, E.A.1    Papadopoulos, R.2    Fuller, S.J.3    Moir, R.D.4    Small, D.5    Beyreuther, K.6    Masters, C.L.7
  • 61
    • 0033562740 scopus 로고    scopus 로고
    • Identification of a potent neurotrophic substance for ciliary ganglionic neurons in fetal calf serum as insulin-like growth factor II
    • Motoike T., Unsicker K. Identification of a potent neurotrophic substance for ciliary ganglionic neurons in fetal calf serum as insulin-like growth factor II. J. Neurosci. Res. 1999, 56:386-396.
    • (1999) J. Neurosci. Res. , vol.56 , pp. 386-396
    • Motoike, T.1    Unsicker, K.2
  • 62
    • 0026697724 scopus 로고
    • NeuN, a neuronal specific nuclear protein in vertebrates
    • Mullen R.J., Buck C.R., Smith A.M. NeuN, a neuronal specific nuclear protein in vertebrates. Development 1992, 116:201-211.
    • (1992) Development , vol.116 , pp. 201-211
    • Mullen, R.J.1    Buck, C.R.2    Smith, A.M.3
  • 63
    • 0034109215 scopus 로고    scopus 로고
    • Activation of latent TGF-beta by thrombospondin-1: mechanisms and physiology
    • Murphy-Ullrich J.E., Poczatek M. Activation of latent TGF-beta by thrombospondin-1: mechanisms and physiology. Cytokine Growth Factor Rev. 2000, 11:59-69.
    • (2000) Cytokine Growth Factor Rev. , vol.11 , pp. 59-69
    • Murphy-Ullrich, J.E.1    Poczatek, M.2
  • 64
    • 0037960223 scopus 로고    scopus 로고
    • Upregulation and antiapoptotic role of endogenous Alzheimer amyloid precursor protein in dorsal root ganglion neurons
    • Nishimura I., Takazaki R., Kuwako K., Enokido Y., Yoshikawa K. Upregulation and antiapoptotic role of endogenous Alzheimer amyloid precursor protein in dorsal root ganglion neurons. Exp. Cell Res. 2003, 286:241-251.
    • (2003) Exp. Cell Res. , vol.286 , pp. 241-251
    • Nishimura, I.1    Takazaki, R.2    Kuwako, K.3    Enokido, Y.4    Yoshikawa, K.5
  • 65
    • 0026058318 scopus 로고
    • Cell death during development of the nervous system
    • Oppenheim R.W. Cell death during development of the nervous system. Annu. Rev. Neurosci. 1991, 14:453-501.
    • (1991) Annu. Rev. Neurosci. , vol.14 , pp. 453-501
    • Oppenheim, R.W.1
  • 67
    • 0037078123 scopus 로고    scopus 로고
    • TGFbeta induces GDNF responsiveness in neurons by recruitment of GFRalpha1 to the plasma membrane
    • Peterziel H., Unsicker K., Krieglstein K. TGFbeta induces GDNF responsiveness in neurons by recruitment of GFRalpha1 to the plasma membrane. J. Cell Biol. 2002, 159:157-167.
    • (2002) J. Cell Biol. , vol.159 , pp. 157-167
    • Peterziel, H.1    Unsicker, K.2    Krieglstein, K.3
  • 68
    • 36448966008 scopus 로고    scopus 로고
    • Specificity in the crosstalk of TGFbeta/GDNF family members is determined by distinct GFR alpha receptors
    • Peterziel H., Paech T., Strelau J., Unsicker K., Krieglstein K. Specificity in the crosstalk of TGFbeta/GDNF family members is determined by distinct GFR alpha receptors. J. Neurochem. 2007, 103:2491-2504.
    • (2007) J. Neurochem. , vol.103 , pp. 2491-2504
    • Peterziel, H.1    Paech, T.2    Strelau, J.3    Unsicker, K.4    Krieglstein, K.5
  • 69
    • 0017228158 scopus 로고
    • Ultrastructural differences during embryonic cell death in normal and peripherally deprived ciliary ganglia
    • Pilar G., Landmesser L. Ultrastructural differences during embryonic cell death in normal and peripherally deprived ciliary ganglia. J. Cell Biol. 1976, 68:339-356.
    • (1976) J. Cell Biol. , vol.68 , pp. 339-356
    • Pilar, G.1    Landmesser, L.2
  • 70
    • 33644803381 scopus 로고    scopus 로고
    • Depolarization promotes survival of ciliary ganglion neurons by BDNF-dependent and -independent mechanisms
    • Pugh P.C., Zhou X., Jayakar S.S., Margiotta J.F. Depolarization promotes survival of ciliary ganglion neurons by BDNF-dependent and -independent mechanisms. Dev. Biol. 2006, 291:182-191.
    • (2006) Dev. Biol. , vol.291 , pp. 182-191
    • Pugh, P.C.1    Zhou, X.2    Jayakar, S.S.3    Margiotta, J.F.4
  • 71
    • 0033532054 scopus 로고    scopus 로고
    • The activation sequence of thrombospondin-1 interacts with the latency-associated peptide to regulate activation of latent transforming growth factor-beta
    • Ribeiro S.M., Poczatek M., Schultz-Cherry S., Villain M., Murphy-Ullrich J.E. The activation sequence of thrombospondin-1 interacts with the latency-associated peptide to regulate activation of latent transforming growth factor-beta. J. Biol. Chem. 1999, 274:13586-13593.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13586-13593
    • Ribeiro, S.M.1    Poczatek, M.2    Schultz-Cherry, S.3    Villain, M.4    Murphy-Ullrich, J.E.5
  • 72
    • 0031658384 scopus 로고    scopus 로고
    • Disabled-1 acts downstream of Reelin in a signaling pathway that controls laminar organization in the mammalian brain
    • Rice D.S., Sheldon M., D'Arcangelo G., Nakajima K., Goldowitz D., Curran T. Disabled-1 acts downstream of Reelin in a signaling pathway that controls laminar organization in the mammalian brain. Development 1998, 125:3719-3729.
    • (1998) Development , vol.125 , pp. 3719-3729
    • Rice, D.S.1    Sheldon, M.2    D'Arcangelo, G.3    Nakajima, K.4    Goldowitz, D.5    Curran, T.6
  • 74
    • 0033559397 scopus 로고    scopus 로고
    • Glial cell line-derived neurotrophic factor rescues target-deprived sympathetic spinal cord neurons but requires transforming growth factor-beta as cofactor in vivo
    • Schober A., Hertel R., Arumae U., Farkas L., Jaszai J., Krieglstein K., Saarma M., Unsicker K. Glial cell line-derived neurotrophic factor rescues target-deprived sympathetic spinal cord neurons but requires transforming growth factor-beta as cofactor in vivo. J. Neurosci. 1999, 19:2008-2015.
    • (1999) J. Neurosci. , vol.19 , pp. 2008-2015
    • Schober, A.1    Hertel, R.2    Arumae, U.3    Farkas, L.4    Jaszai, J.5    Krieglstein, K.6    Saarma, M.7    Unsicker, K.8
  • 77
    • 0042357460 scopus 로고    scopus 로고
    • Selectivity in neurotrophin signaling: theme and variations
    • Segal R.A. Selectivity in neurotrophin signaling: theme and variations. Annu. Rev. Neurosci. 2003, 26:299-330.
    • (2003) Annu. Rev. Neurosci. , vol.26 , pp. 299-330
    • Segal, R.A.1
  • 79
    • 0028213567 scopus 로고
    • A heparin-binding domain in the amyloid protein precursor of Alzheimer's disease is involved in the regulation of neurite outgrowth
    • Small D.H., Nurcombe V., Reed G., Clarris H., Moir R., Beyreuther K., Masters C.L. A heparin-binding domain in the amyloid protein precursor of Alzheimer's disease is involved in the regulation of neurite outgrowth. J. Neurosci. 1994, 14:2117-2127.
    • (1994) J. Neurosci. , vol.14 , pp. 2117-2127
    • Small, D.H.1    Nurcombe, V.2    Reed, G.3    Clarris, H.4    Moir, R.5    Beyreuther, K.6    Masters, C.L.7
  • 81
    • 0035836639 scopus 로고    scopus 로고
    • F-spondin is a contact-repellent molecule for embryonic motor neurons
    • Tzarfati-Majar V., Burstyn-Cohen T., Klar A. F-spondin is a contact-repellent molecule for embryonic motor neurons. Proc. Natl Acad. Sci. USA 2001, 98:4722-4727.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 4722-4727
    • Tzarfati-Majar, V.1    Burstyn-Cohen, T.2    Klar, A.3
  • 83
    • 0000950755 scopus 로고    scopus 로고
    • Neurotrophic roles of GDNF and related factors
    • Springer, Chapter 8, F. Hefti (Ed.) Handbook of Experimental Pharmacology
    • Unsicker K., Suter-Crazzolara C., Krieglstein K. Neurotrophic roles of GDNF and related factors. Neurotrophic Factors 1999, vol. 134:189-224. Springer, Chapter 8. F. Hefti (Ed.).
    • (1999) Neurotrophic Factors , vol.134 , pp. 189-224
    • Unsicker, K.1    Suter-Crazzolara, C.2    Krieglstein, K.3
  • 84
    • 0034105456 scopus 로고    scopus 로고
    • Co-activation of TGF-ss and cytokine signaling pathways are required for neurotrophic functions
    • Unsicker K., Krieglstein K. Co-activation of TGF-ss and cytokine signaling pathways are required for neurotrophic functions. Cytokine Growth Factor Rev. 2000, 11:97-102.
    • (2000) Cytokine Growth Factor Rev. , vol.11 , pp. 97-102
    • Unsicker, K.1    Krieglstein, K.2
  • 86
    • 54949132875 scopus 로고    scopus 로고
    • Bcl-2 family proteins and cancer
    • Yip K.W., Reed J.C. Bcl-2 family proteins and cancer. Oncogene 2008, 27:6398-6406.
    • (2008) Oncogene , vol.27 , pp. 6398-6406
    • Yip, K.W.1    Reed, J.C.2
  • 87
    • 37549040612 scopus 로고    scopus 로고
    • A critical function for beta-amyloid precursor protein in neuronal migration revealed by in utero RNA interference
    • Young-Pearse T.L., Bai J., Chang R., Zheng J.B., LoTurco J.J., Selkoe D.J. A critical function for beta-amyloid precursor protein in neuronal migration revealed by in utero RNA interference. J. Neurosci. 2007, 27:14459-14469.
    • (2007) J. Neurosci. , vol.27 , pp. 14459-14469
    • Young-Pearse, T.L.1    Bai, J.2    Chang, R.3    Zheng, J.B.4    LoTurco, J.J.5    Selkoe, D.J.6
  • 88
    • 0030584088 scopus 로고    scopus 로고
    • Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)
    • Zha J., Harada H., Yang E., Jockel J., Korsmeyer S.J. Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L). Cell 1996, 87:619-628.
    • (1996) Cell , vol.87 , pp. 619-628
    • Zha, J.1    Harada, H.2    Yang, E.3    Jockel, J.4    Korsmeyer, S.J.5
  • 89
    • 0034284864 scopus 로고    scopus 로고
    • Evolutionarily conserved Bok proteins in the Bcl-2 family
    • Zhang H., Holzgreve W., De Geyter C. Evolutionarily conserved Bok proteins in the Bcl-2 family. FEBS Lett. 2000, 480:311-313.
    • (2000) FEBS Lett. , vol.480 , pp. 311-313
    • Zhang, H.1    Holzgreve, W.2    De Geyter, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.