메뉴 건너뛰기




Volumn 74, Issue 2-3, 2000, Pages 253-260

Neurotrophin receptor structure and interactions

Author keywords

Brain derived neurotrophic factor (BDNF); Neurotrophin 3 (NT 3); Neurotrophin 4 5 (NT 4); Neurotrophins; NGF; p75 receptor

Indexed keywords

BRAIN DERIVED NEUROTROPHIC FACTOR; CILIARY NEUROTROPHIC FACTOR; NERVE GROWTH FACTOR; NEUROTROPHIN 3; NEUROTROPHIN 4; NEUROTROPHIN RECEPTOR; PROTEIN TYROSINE KINASE;

EID: 0034085908     PISSN: 00316865     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0031-6865(99)00036-9     Document Type: Article
Times cited : (89)

References (76)
  • 1
    • 0015138902 scopus 로고
    • The amino acid sequence of 2.5S mouse submaxillary gland nerve growth factor
    • Angeletti R.H., Bradshaw R.A. The amino acid sequence of 2.5S mouse submaxillary gland nerve growth factor. Proc. Natl. Acad. Sci. 68:1971;2417-2420.
    • (1971) Proc. Natl. Acad. Sci. , vol.68 , pp. 2417-2420
    • Angeletti, R.H.1    Bradshaw, R.A.2
  • 3
    • 0032559622 scopus 로고    scopus 로고
    • The p75 neurotrophin receptor mediates neuronal apoptosis and is essential for naturally occurring sympathetic neuron death
    • Bamji S., Majdan M., Pozniak C.D., Belliveau D.J., Aloyz R J.K., Causing C.G., Miller F.D. The p75 neurotrophin receptor mediates neuronal apoptosis and is essential for naturally occurring sympathetic neuron death. J. Cell Biol. 140:1998;911-923.
    • (1998) J. Cell Biol. , vol.140 , pp. 911-923
    • Bamji, S.1    Majdan, M.2    Pozniak, C.D.3    Belliveau, D.J.4    Aloyz, R.J.K.5    Causing, C.G.6    Miller, F.D.7
  • 4
    • 0028090302 scopus 로고
    • The trk family of neurotrophin receptors
    • Barbacid M. The trk family of neurotrophin receptors. J. Neurobiol. 25:1994;1386-1403.
    • (1994) J. Neurobiol. , vol.25 , pp. 1386-1403
    • Barbacid, M.1
  • 5
    • 0024677597 scopus 로고
    • Trophic factors and neuronal survival
    • Barde Y.A. Trophic factors and neuronal survival. Neuron. 2:1989;1525-1534.
    • (1989) Neuron , vol.2 , pp. 1525-1534
    • Barde, Y.A.1
  • 6
    • 0027966170 scopus 로고
    • Disruption of NGF binding to the low-affinity neurotrophin receptor p75 reduces NGF binding to trkA on PC12 cells
    • Barker P.A., Shooter E.M. Disruption of NGF binding to the low-affinity neurotrophin receptor p75 reduces NGF binding to trkA on PC12 cells. Neuron. 13:1994;203-215.
    • (1994) Neuron , vol.13 , pp. 203-215
    • Barker, P.A.1    Shooter, E.M.2
  • 7
    • 0027183950 scopus 로고
    • Differential expression of nerve growth factor receptors leads to altered binding affinity and neurotrophin responsiveness
    • Benedetti M., Levi A., Chao M.V. Differential expression of nerve growth factor receptors leads to altered binding affinity and neurotrophin responsiveness. Proc. Natl. Acad. Sci. U.S.A. 90:1993;7859-7863.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 7859-7863
    • Benedetti, M.1    Levi, A.2    Chao, M.V.3
  • 8
    • 0025886463 scopus 로고
    • The low affinity nerve growth factor (NGF) receptor mediates NGF-induced tyrosine phosphorylation
    • Berg M.M., Sternberg D.W., Hempstead B.L., Chao M.V. The low affinity nerve growth factor (NGF) receptor mediates NGF-induced tyrosine phosphorylation. Proc. Natl. Acad. Sci. U.S.A. 88:1991;857-866.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 857-866
    • Berg, M.M.1    Sternberg, D.W.2    Hempstead, B.L.3    Chao, M.V.4
  • 9
    • 0026512998 scopus 로고
    • K-252a inhibits NGF-induced trk proto-oncogene tyrosine phosphorylation and kinase activity
    • Berg M.M., Sternberg D., Parada L.F., Chao M.V. K-252a inhibits NGF-induced trk proto-oncogene tyrosine phosphorylation and kinase activity. J. Biol. Chem. 267:1992;13-16.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13-16
    • Berg, M.M.1    Sternberg, D.2    Parada, L.F.3    Chao, M.V.4
  • 12
    • 0030606315 scopus 로고    scopus 로고
    • CAR1, a TNFR-related protein is a cellular receptor for cytopathic avian leukosis-sarcoma viruses and mediates apoptosis
    • Brojatsch J., Naughton J., Rolls M.M., Zingler K., Young J.A.T. CAR1, a TNFR-related protein is a cellular receptor for cytopathic avian leukosis-sarcoma viruses and mediates apoptosis. Cell. 87:1996;845-855.
    • (1996) Cell , vol.87 , pp. 845-855
    • Brojatsch, J.1    Naughton, J.2    Rolls, M.M.3    Zingler, K.4    Young, J.A.T.5
  • 14
    • 0029805770 scopus 로고    scopus 로고
    • Death of oligodendrocytes mediated by the interaction of nerve growth factor with its receptor p75
    • Casaccia-Bonnefil P., Carter B.D., Dobrowsky R.T., Chao M.V. Death of oligodendrocytes mediated by the interaction of nerve growth factor with its receptor p75. Nature. 383:1996;716-719.
    • (1996) Nature , vol.383 , pp. 716-719
    • Casaccia-Bonnefil, P.1    Carter, B.D.2    Dobrowsky, R.T.3    Chao, M.V.4
  • 15
    • 0031823035 scopus 로고    scopus 로고
    • Neurotrophins: The biological paradox of survival factors eliciting apoptosis
    • Casaccia-Bonnefil P., Kong H., Chao M.V. Neurotrophins: the biological paradox of survival factors eliciting apoptosis. Cell Death and Differentiation. 5:1998;357-364.
    • (1998) Cell Death and Differentiation , vol.5 , pp. 357-364
    • Casaccia-Bonnefil, P.1    Kong, H.2    Chao, M.V.3
  • 16
    • 0026730310 scopus 로고
    • Neurotrophin receptors: A window into neuronal differentiation
    • Chao M.V. Neurotrophin receptors: a window into neuronal differentiation. Neuron. 9:1992;583-593.
    • (1992) Neuron , vol.9 , pp. 583-593
    • Chao, M.V.1
  • 17
    • 0026578026 scopus 로고
    • Growth factor signaling: Where is the specificity?
    • Chao M.V. Growth factor signaling: where is the specificity? Cell. 68:1992;995-997.
    • (1992) Cell , vol.68 , pp. 995-997
    • Chao, M.V.1
  • 18
    • 0027942459 scopus 로고
    • The p75 neurotrophin receptor
    • Chao M.V. The p75 neurotrophin receptor. J. Neurobiol. 25:1994;1373-1385.
    • (1994) J. Neurobiol. , vol.25 , pp. 1373-1385
    • Chao, M.V.1
  • 20
    • 0029066697 scopus 로고
    • Contenders in FasL/TNF death signaling
    • Cleveland J.L., Ihle J.N. Contenders in FasL/TNF death signaling. Cell. 81:1995;479-482.
    • (1995) Cell , vol.81 , pp. 479-482
    • Cleveland, J.L.1    Ihle, J.N.2
  • 21
    • 0028388447 scopus 로고
    • Neurotrophic factors-switching neurotrophin dependence
    • Davies A.M. Neurotrophic factors-switching neurotrophin dependence. Curr. Biol. 4:1994;273-276.
    • (1994) Curr. Biol. , vol.4 , pp. 273-276
    • Davies, A.M.1
  • 22
    • 0030878081 scopus 로고    scopus 로고
    • The neurotrophin receptor p75 binds neurotrophin-3 on sympathetic neurons with high affinity and specificity
    • Dechant G., Barde Y.-A. The neurotrophin receptor p75 binds neurotrophin-3 on sympathetic neurons with high affinity and specificity. J. Neurosci. 17:1997;5281-5287.
    • (1997) J. Neurosci. , vol.17 , pp. 5281-5287
    • Dechant, G.1    Barde, Y.-A.2
  • 24
    • 0026634815 scopus 로고
    • The neurotrophins BDNF, NT-3 and NGF display distinct patterns of retrograde axonal-transport in peripheral and central neurons
    • Distefano P.S., Friedman B., Radziejewski C., Alexander C., Boland P., Schick C.M., Lindsay R.M., Wiegand S.J. The neurotrophins BDNF, NT-3 and NGF display distinct patterns of retrograde axonal-transport in peripheral and central neurons. Neuron. 8:1992;983-993.
    • (1992) Neuron , vol.8 , pp. 983-993
    • Distefano, P.S.1    Friedman, B.2    Radziejewski, C.3    Alexander, C.4    Boland, P.5    Schick, C.M.6    Lindsay, R.M.7    Wiegand, S.J.8
  • 25
    • 0028108788 scopus 로고
    • Activation of the sphingomyelin cycle through the low-affinity neurotrophin receptor
    • Dobrowsky R.T., Werner M.H., Castellino A.M., Chao M.V., Hannun Y.A. Activation of the sphingomyelin cycle through the low-affinity neurotrophin receptor. Science. 265:1994;1596-1599.
    • (1994) Science , vol.265 , pp. 1596-1599
    • Dobrowsky, R.T.1    Werner, M.H.2    Castellino, A.M.3    Chao, M.V.4    Hannun, Y.A.5
  • 26
    • 0029090337 scopus 로고
    • Neurotrophins induce sphingomyelin hydrolysis
    • Dobrowsky R.T., Jenkins G.M., Hannun Y.A. Neurotrophins induce sphingomyelin hydrolysis. J. Biol. Chem. 270:1995;22135-22142.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22135-22142
    • Dobrowsky, R.T.1    Jenkins, G.M.2    Hannun, Y.A.3
  • 28
    • 0029360415 scopus 로고
    • The death domain: A module shared by proteins with diverse cellular functions
    • Feinstein E., Kimchi A., Wallach D., Boldin M., Varfolomeev E. The death domain: a module shared by proteins with diverse cellular functions. TIBS. 20:1995;342-344.
    • (1995) TIBS , vol.20 , pp. 342-344
    • Feinstein, E.1    Kimchi, A.2    Wallach, D.3    Boldin, M.4    Varfolomeev, E.5
  • 29
    • 0029787071 scopus 로고    scopus 로고
    • Induction of cell death by endogenous nerve growth factor through its p75 receptor
    • Frade J.M., Rodriguez-Tebar A., Barde Y.-A. Induction of cell death by endogenous nerve growth factor through its p75 receptor. Nature. 383:1996;166-168.
    • (1996) Nature , vol.383 , pp. 166-168
    • Frade, J.M.1    Rodriguez-Tebar, A.2    Barde, Y.-A.3
  • 30
    • 0030863071 scopus 로고    scopus 로고
    • Modulation of nerve growth factor internalization by direct interaction between p75 and TrkA receptors
    • Gargano N., Levi A., Alema S. Modulation of nerve growth factor internalization by direct interaction between p75 and TrkA receptors. J. Neurosci. Res. 50:1997;1-12.
    • (1997) J. Neurosci. Res. , vol.50 , pp. 1-12
    • Gargano, N.1    Levi, A.2    Alema, S.3
  • 31
    • 15844369897 scopus 로고    scopus 로고
    • CD30 contains two binding sites with different specificities for members of the tumor necrosis factor receptor-associated factor family of signal transducing proteins
    • Gedrich R.W., Gilfillan M.C., Duckett C.S., Van Dongen J.L., Thompson C.B. CD30 contains two binding sites with different specificities for members of the tumor necrosis factor receptor-associated factor family of signal transducing proteins. J. Biol. Chem. 271:1996;12852-12858.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12852-12858
    • Gedrich, R.W.1    Gilfillan, M.C.2    Duckett, C.S.3    Van Dongen, J.L.4    Thompson, C.B.5
  • 32
    • 0022389934 scopus 로고
    • Characterization of the human melanoma nerve growth factor receptor
    • Grob P.M., Ross A.H., Koprowski H., Bothwell M. Characterization of the human melanoma nerve growth factor receptor. J. Biol. Chem. 260:1985;8044-8049.
    • (1985) J. Biol. Chem. , vol.260 , pp. 8044-8049
    • Grob, P.M.1    Ross, A.H.2    Koprowski, H.3    Bothwell, M.4
  • 34
    • 0027939697 scopus 로고
    • The low affinity NGF receptor, p75, can collaborate with each of the Trks to potentiate functional responses to the neurotrophins
    • Hantzopoulos P.A., Suri C., Glass D.J., Goldfarb M.P., Yancopoulos G.D. The low affinity NGF receptor, p75, can collaborate with each of the Trks to potentiate functional responses to the neurotrophins. Neuron. 13:1994;187-207.
    • (1994) Neuron , vol.13 , pp. 187-207
    • Hantzopoulos, P.A.1    Suri, C.2    Glass, D.J.3    Goldfarb, M.P.4    Yancopoulos, G.D.5
  • 35
    • 0025774207 scopus 로고
    • High-affinity NGF binding requires co-expression of the trk proto-oncogene and the low-affinity NGF receptor
    • Hempstead B.L., Martin-Zanca D., Kaplan D.R., Parada L.F., Chao M.V. High-affinity NGF binding requires co-expression of the trk proto-oncogene and the low-affinity NGF receptor. Nature. 350:1991;678-683.
    • (1991) Nature , vol.350 , pp. 678-683
    • Hempstead, B.L.1    Martin-Zanca, D.2    Kaplan, D.R.3    Parada, L.F.4    Chao, M.V.5
  • 36
    • 0026468503 scopus 로고
    • Overexpression of the trk tyrosine kinase rapidly accelerates nerve growth factor-induced differentiation
    • Hempstead B.L., Rabin S.J., Kaplan L., Reid S., Parada L.F., Kaplan D.R. Overexpression of the trk tyrosine kinase rapidly accelerates nerve growth factor-induced differentiation. Neurons. 9:1992;883-896.
    • (1992) Neurons , vol.9 , pp. 883-896
    • Hempstead, B.L.1    Rabin, S.J.2    Kaplan, L.3    Reid, S.4    Parada, L.F.5    Kaplan, D.R.6
  • 37
    • 0030032106 scopus 로고    scopus 로고
    • TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor-1 signal transduction pathways
    • Hsu H., Shu H.-B., Pan M.-P., Goeddel D.V. TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor-1 signal transduction pathways. Cell. 84:1996;299-308.
    • (1996) Cell , vol.84 , pp. 299-308
    • Hsu, H.1    Shu, H.-B.2    Pan, M.-P.3    Goeddel, D.V.4
  • 38
    • 0028916050 scopus 로고
    • A potential interaction of p75 and trkA NGF receptors revealed by affinity crosslinking and immunoprecipitation
    • Huber L.J., Chao M.V. A potential interaction of p75 and trkA NGF receptors revealed by affinity crosslinking and immunoprecipitation. J. Neurosci. Res. 40:1995;557-563.
    • (1995) J. Neurosci. Res. , vol.40 , pp. 557-563
    • Huber, L.J.1    Chao, M.V.2
  • 39
    • 0027050178 scopus 로고
    • Nerve growth-factor mediates signal transduction through trk homodimer receptors
    • Jing S.Q., Tapley P., Barbacid M. Nerve growth-factor mediates signal transduction through trk homodimer receptors. Neuron. 9:1992;1067-1079.
    • (1992) Neuron , vol.9 , pp. 1067-1079
    • Jing, S.Q.1    Tapley, P.2    Barbacid, M.3
  • 40
    • 0028177535 scopus 로고
    • Purification and characterization of a brain-derived neurotrophic factor neurotrophin-3 (bdnf/nt-3) heterodimer
    • Jungbluth S., Bailey K., Barde Y.A. Purification and characterization of a brain-derived neurotrophic factor neurotrophin-3 (bdnf/nt-3) heterodimer. Eur. J. Biochem. 221:1994;677-685.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 677-685
    • Jungbluth, S.1    Bailey, K.2    Barde, Y.A.3
  • 41
    • 0028115022 scopus 로고
    • Neurotrophin signal transduction by the trk receptor
    • Kaplan D.R., Stephens R.M. Neurotrophin signal transduction by the trk receptor. J. Neurobiol. 25:1994;1404-1417.
    • (1994) J. Neurobiol. , vol.25 , pp. 1404-1417
    • Kaplan, D.R.1    Stephens, R.M.2
  • 42
    • 0033613831 scopus 로고    scopus 로고
    • Association of TRAF6 with the p75 neurotrophin receptor
    • Khursigara G., Orlinick J.R., Chao M.V. Association of TRAF6 with the p75 neurotrophin receptor. J. Biol. Chem. 274:1999;2597-2600.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2597-2600
    • Khursigara, G.1    Orlinick, J.R.2    Chao, M.V.3
  • 43
    • 0030706168 scopus 로고    scopus 로고
    • A lipid-anchored Grb2-binding protein that links FGF-receptor activation to the Ras/MAPK signaling pathway
    • Kouhara H., Hadari Y.R., Spivak-Kroizman T., Schilling J., Bar-Sagi D., Lax I., Schlessinger J. A lipid-anchored Grb2-binding protein that links FGF-receptor activation to the Ras/MAPK signaling pathway. Cell. 89:1997;693-702.
    • (1997) Cell , vol.89 , pp. 693-702
    • Kouhara, H.1    Hadari, Y.R.2    Spivak-Kroizman, T.3    Schilling, J.4    Bar-Sagi, D.5    Lax, I.6    Schlessinger, J.7
  • 45
    • 0023236055 scopus 로고
    • The nerve growth factor: Thirty-five years later
    • Levi-Montalcini R. The nerve growth factor: thirty-five years later. Science. 237:1987;1154-1164.
    • (1987) Science , vol.237 , pp. 1154-1164
    • Levi-Montalcini, R.1
  • 46
    • 0030851905 scopus 로고    scopus 로고
    • NMR structure of the death domain of the p75 neurotrophin receptor
    • Liepinsh E., Ilag L.L., Otting G., Ibanez C.F. NMR structure of the death domain of the p75 neurotrophin receptor. EMBO J. 16:1997;4999-5005.
    • (1997) EMBO J. , vol.16 , pp. 4999-5005
    • Liepinsh, E.1    Ilag, L.L.2    Otting, G.3    Ibanez, C.F.4
  • 48
    • 0028217645 scopus 로고
    • High affinity nerve growth factor binding displays a faster rate of association than p140(trk) binding-implications for multisubunit polypeptide receptors
    • Mahadeo D., Kaplan L., Chao M.V., Hempstead B.L. High affinity nerve growth factor binding displays a faster rate of association than p140(trk) binding-implications for multisubunit polypeptide receptors. J. Biol. Chem. 269:1994;6884-6891.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6884-6891
    • Mahadeo, D.1    Kaplan, L.2    Chao, M.V.3    Hempstead, B.L.4
  • 50
    • 0027251256 scopus 로고
    • A new structural superfamily of growth factors defined by a cystine knot motif
    • McDonald N.Q., Hendrickson W.A. A new structural superfamily of growth factors defined by a cystine knot motif. Cell. 73:1993;421-424.
    • (1993) Cell , vol.73 , pp. 421-424
    • McDonald, N.Q.1    Hendrickson, W.A.2
  • 51
    • 0030136240 scopus 로고    scopus 로고
    • Deletions in the extracellular domain of rat trkA lead to an altered differentiative phenotype in neurotrophin responsive cells
    • McDonald J.I., Meakin S.O. Deletions in the extracellular domain of rat trkA lead to an altered differentiative phenotype in neurotrophin responsive cells. Mol. Cell. Neurosci. 7:1996;371-390.
    • (1996) Mol. Cell. Neurosci. , vol.7 , pp. 371-390
    • McDonald, J.I.1    Meakin, S.O.2
  • 52
    • 0025986121 scopus 로고
    • A new protein fold revealed by a 2.3 A resolution crystal structure of nerve growth factor
    • McDonald N.Q., Lapatto R., Murray-Rust J., Gunning J., Wlodawer A., Blundell T.L. A new protein fold revealed by a 2.3 A resolution crystal structure of nerve growth factor. Nature. 354:1991;411-414.
    • (1991) Nature , vol.354 , pp. 411-414
    • McDonald, N.Q.1    Lapatto, R.2    Murray-Rust, J.3    Gunning, J.4    Wlodawer, A.5    Blundell, T.L.6
  • 53
    • 0030298375 scopus 로고    scopus 로고
    • Herpes simplex virus-1 entry into cells mediated by a novel member of the TNF/NGF receptor family
    • Montgomery R.I., Warner M.S., Lum B.J., Spear P.G. Herpes simplex virus-1 entry into cells mediated by a novel member of the TNF/NGF receptor family. Cell. 87:1996;427-436.
    • (1996) Cell , vol.87 , pp. 427-436
    • Montgomery, R.I.1    Warner, M.S.2    Lum, B.J.3    Spear, P.G.4
  • 55
    • 0025938465 scopus 로고
    • Subunit promiscuity among hemopoietic growth factor receptors
    • Nicola N.A., Metcalf D. Subunit promiscuity among hemopoietic growth factor receptors. Cell. 67:1992;1-4.
    • (1992) Cell , vol.67 , pp. 1-4
    • Nicola, N.A.1    Metcalf, D.2
  • 56
    • 0027931786 scopus 로고
    • Neurotrophic factors: Two are better than one
    • Nishi R. Neurotrophic factors: two are better than one. Science. 265:1994;1052-1053.
    • (1994) Science , vol.265 , pp. 1052-1053
    • Nishi, R.1
  • 58
    • 0029017053 scopus 로고
    • NGF binding to the trk tyrosine kinase receptor requires the extracellular immunoglobulin-like domains
    • Perez P., Coll P.M., Hempstead B.L., Martin-Zanca D., Chao M.V. NGF binding to the trk tyrosine kinase receptor requires the extracellular immunoglobulin-like domains. Mol. Cell. Neurosci. 6:1995;97-105.
    • (1995) Mol. Cell. Neurosci. , vol.6 , pp. 97-105
    • Perez, P.1    Coll, P.M.2    Hempstead, B.L.3    Martin-Zanca, D.4    Chao, M.V.5
  • 59
    • 0032418850 scopus 로고    scopus 로고
    • Identification and characterization of novel substrates of Trk receptors in developing neurons
    • Qian X., Riccio A., Zhang Y., Ginty D.D. Identification and characterization of novel substrates of Trk receptors in developing neurons. Neuron. 21:1998;1017-1029.
    • (1998) Neuron , vol.21 , pp. 1017-1029
    • Qian, X.1    Riccio, A.2    Zhang, Y.3    Ginty, D.D.4
  • 60
    • 0026338953 scopus 로고
    • NGF and EGF rapidly activate p21ras in PC12 cells by distinct, convergent pathways involving tyrosine phosphorylation
    • Qui M.-S., Green S.H. NGF and EGF rapidly activate p21ras in PC12 cells by distinct, convergent pathways involving tyrosine phosphorylation. Neuron. 7:1991;937-946.
    • (1991) Neuron , vol.7 , pp. 937-946
    • Qui, M.-S.1    Green, S.H.2
  • 61
    • 0026733002 scopus 로고
    • PC12 cell neuronal differentiation is associated with prolonged p21ras activity and consequent prolonged ERK activity
    • Qui M.-S., Green S.H. PC12 cell neuronal differentiation is associated with prolonged p21ras activity and consequent prolonged ERK activity. Neuron. 9:1992;705-717.
    • (1992) Neuron , vol.9 , pp. 705-717
    • Qui, M.-S.1    Green, S.H.2
  • 63
    • 0027771130 scopus 로고
    • Heterodimers of the neurotrophic factors-formation, isolation and differential stability
    • Radziewjewski C., Robinson R.C. Heterodimers of the neurotrophic factors-formation, isolation and differential stability. Biochemistry. 32:1993;13350-13356.
    • (1993) Biochemistry , vol.32 , pp. 13350-13356
    • Radziewjewski, C.1    Robinson, R.C.2
  • 64
    • 0026608541 scopus 로고
    • Binding of neurotrophin-3 to its neuronal receptors and interactions with nerve growth-factor and brain-derived neurotrophic factor
    • Rodriguez-Tebar A., Dechant G., Gotz R., Barde Y.A. Binding of neurotrophin-3 to its neuronal receptors and interactions with nerve growth-factor and brain-derived neurotrophic factor. EMJO J. 11:1992;917-922.
    • (1992) EMJO J. , vol.11 , pp. 917-922
    • Rodriguez-Tebar, A.1    Dechant, G.2    Gotz, R.3    Barde, Y.A.4
  • 65
    • 0028124428 scopus 로고
    • A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor
    • Rothe M., Wong S.C., Henzel W.J., Goeddel D.V. A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor. Cell. 78:1994;681-692.
    • (1994) Cell , vol.78 , pp. 681-692
    • Rothe, M.1    Wong, S.C.2    Henzel, W.J.3    Goeddel, D.V.4
  • 66
    • 0028978626 scopus 로고
    • TRAF2-mediated activation of NF-kB by TNF receptor 2 and CD40
    • Rothe M., Sarma V., Dixit V.M., Goeddel D.V. TRAF2-mediated activation of NF-kB by TNF receptor 2 and CD40. Science. 269:1995;1424-1427.
    • (1995) Science , vol.269 , pp. 1424-1427
    • Rothe, M.1    Sarma, V.2    Dixit, V.M.3    Goeddel, D.V.4
  • 67
    • 0028353492 scopus 로고
    • The TNF receptor superfamily of cellular and viral proteins: Activation, costimulation and death
    • Smith C.A., Farrah T., Goodwin R.G. The TNF receptor superfamily of cellular and viral proteins: activation, costimulation and death. Cell. 76:1994;959-962.
    • (1994) Cell , vol.76 , pp. 959-962
    • Smith, C.A.1    Farrah, T.2    Goodwin, R.G.3
  • 68
    • 0018584222 scopus 로고
    • NGF receptors. Characterization of two distinct classes of binding sites on thick embryo sensory ganglia cells
    • Sutter A., Riopelle R.J., Harris-Warrick R.M., Shooter E.M. NGF receptors. Characterization of two distinct classes of binding sites on thick embryo sensory ganglia cells. J. Biol. Chem. 254:1979;5972-5982.
    • (1979) J. Biol. Chem. , vol.254 , pp. 5972-5982
    • Sutter, A.1    Riopelle, R.J.2    Harris-Warrick, R.M.3    Shooter, E.M.4
  • 69
    • 0028866230 scopus 로고
    • Neurotrophins and neuronal plasticity
    • Thoenen H. Neurotrophins and neuronal plasticity. Science. 270:1995;593-598.
    • (1995) Science , vol.270 , pp. 593-598
    • Thoenen, H.1
  • 70
    • 0029055577 scopus 로고
    • An immunoglobulin-like domain determines the specificity of neurotrophin receptors
    • Urfer R., Tsoulfas P., O'Connell L., Shelton D.L., Parada L.F., Presta L.G. An immunoglobulin-like domain determines the specificity of neurotrophin receptors. EMBO J. 14:1995;2795-2805.
    • (1995) EMBO J. , vol.14 , pp. 2795-2805
    • Urfer, R.1    Tsoulfas, P.2    O'Connell, L.3    Shelton, D.L.4    Parada, L.F.5    Presta, L.G.6
  • 73
    • 0028952568 scopus 로고
    • Interaction with trkA immobilizes gp75 in the high affinity nerve growth factor receptor complex
    • Wolf D.E., McKinnon C.A., Daou M.-C., Stephens R.M., Kaplan D.R., Ross A.H. Interaction with trkA immobilizes gp75 in the high affinity nerve growth factor receptor complex. J. Biol. Chem. 270:1995;2133-2138.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2133-2138
    • Wolf, D.E.1    McKinnon, C.A.2    Daou, M.-C.3    Stephens, R.M.4    Kaplan, D.R.5    Ross, A.H.6
  • 74
    • 0027332387 scopus 로고
    • Regulation of expression of mRNAs encoding the nerve growth factor receptors p75 and trkA mRNA in developing sensory neurons
    • Wyatt S., Davies A.M. Regulation of expression of mRNAs encoding the nerve growth factor receptors p75 and trkA mRNA in developing sensory neurons. Development. 119:1993;635-647.
    • (1993) Development , vol.119 , pp. 635-647
    • Wyatt, S.1    Davies, A.M.2
  • 75
    • 0028963084 scopus 로고
    • Requirement for phosphatidylinositol-3 kinase in the prevention of apoptosis by nerve growth factor
    • Yao R., Cooper G.M. Requirement for phosphatidylinositol-3 kinase in the prevention of apoptosis by nerve growth factor. Science. 267:1995;2003-2006.
    • (1995) Science , vol.267 , pp. 2003-2006
    • Yao, R.1    Cooper, G.M.2
  • 76
    • 0000326996 scopus 로고    scopus 로고
    • Competitive signaling between TrkA and p75 nerve growth factor receptors determines cell survival
    • Yoon S.O., Casaccia-Bonnefil P., Carter B., Chao M.V. Competitive signaling between TrkA and p75 nerve growth factor receptors determines cell survival. J. Neurosci. 18:1998;3273-3281.
    • (1998) J. Neurosci. , vol.18 , pp. 3273-3281
    • Yoon, S.O.1    Casaccia-Bonnefil, P.2    Carter, B.3    Chao, M.V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.