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Volumn 19, Issue 9, 1999, Pages 6427-6440

Functional analysis of H-Ryk, an atypical member of the receptor tyrosine kinase family

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; GLYCINE; LYSINE; PHENYLALANINE; PROTEIN TYROSINE KINASE; RECOMBINANT NERVE GROWTH FACTOR;

EID: 0032812687     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.19.9.6427     Document Type: Article
Times cited : (64)

References (84)
  • 1
    • 0026510312 scopus 로고
    • The nerve growth-factor receptor a multi-component system that mediates the actions of the neurotrophin family of proteins
    • Barker, P. A., and R. A. Murphy. 1992. The nerve growth-factor receptor a multi-component system that mediates the actions of the neurotrophin family of proteins. Mol. Cell. Biol. 110:1-15.
    • (1992) Mol. Cell. Biol. , vol.110 , pp. 1-15
    • Barker, P.A.1    Murphy, R.A.2
  • 2
    • 0027412196 scopus 로고
    • "ALSCRIPT" - A tool to format multiple sequence alignments
    • Barton, G. J. 1993. "ALSCRIPT" - a tool to format multiple sequence alignments. Protein Eng. 6:47-50.
    • (1993) Protein Eng. , vol.6 , pp. 47-50
    • Barton, G.J.1
  • 3
    • 0025303764 scopus 로고
    • Protein multiple sequence alignment and flexible pattern matching
    • Barton, G. J. 1990. Protein multiple sequence alignment and flexible pattern matching. Methods Enzymol. 183:403-428.
    • (1990) Methods Enzymol. , vol.183 , pp. 403-428
    • Barton, G.J.1
  • 7
    • 0029837284 scopus 로고    scopus 로고
    • Derailed is required for muscle attachment site selection in Drosophila
    • Callahan, C. A., J. L. Bonkovsky, A. L. Scully, and B. J. Thomas. 1996. derailed is required for muscle attachment site selection in Drosophila. Development 127:2761-2767.
    • (1996) Development , vol.127 , pp. 2761-2767
    • Callahan, C.A.1    Bonkovsky, J.L.2    Scully, A.L.3    Thomas, B.J.4
  • 8
    • 0028998860 scopus 로고
    • Control of neuronal pathway selection by a drosophila receptor protein-tyrosine kinase family member
    • Callahan, C. A., M. G. Muralidhar, S. E. Lundgren, A. L. Scully, and J. B. Thomas. 1995. Control of neuronal pathway selection by a drosophila receptor protein-tyrosine kinase family member. Nature 376:171-174.
    • (1995) Nature , vol.376 , pp. 171-174
    • Callahan, C.A.1    Muralidhar, M.G.2    Lundgren, S.E.3    Scully, A.L.4    Thomas, J.B.5
  • 9
    • 0028949081 scopus 로고
    • Heregulin stimulates mitogenesis and phosphatidylinositol 3-kinase in mouse fibroblasts transfected with erbb2/neu and erbb3
    • Carraway, K. L., S. P. Soltoff, A. J. Diamonti, and L. C. Cantley. 1995. Heregulin stimulates mitogenesis and phosphatidylinositol 3-kinase in mouse fibroblasts transfected with erbb2/neu and erbb3. J. Biol. Chem. 270:7111-7116.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7111-7116
    • Carraway, K.L.1    Soltoff, S.P.2    Diamonti, A.J.3    Cantley, L.C.4
  • 10
    • 0023392945 scopus 로고
    • High-efficiency transformation of mammalian cells by plasmid DNA
    • Chen, C., and H. Okayama. 1987. High-efficiency transformation of mammalian cells by plasmid DNA. Mol. Cell. Biol. 7:2745-2752.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2745-2752
    • Chen, C.1    Okayama, H.2
  • 11
    • 0023711798 scopus 로고
    • A high efficient system for stably transforming cells with plasmid DNA
    • Chen, C., and H. Okayama. 1988. A high efficient system for stably transforming cells with plasmid DNA. BioTechniques 6:632-638.
    • (1988) BioTechniques , vol.6 , pp. 632-638
    • Chen, C.1    Okayama, H.2
  • 12
    • 0030720269 scopus 로고    scopus 로고
    • Mutational analysis of Cak1p, an essential protein kinase that regulates cell cycle progression
    • Chun, K. T., and M. G. Goebl. 1997. Mutational analysis of Cak1p, an essential protein kinase that regulates cell cycle progression. Mol. Gen. Genet. 256:365-375.
    • (1997) Mol. Gen. Genet. , vol.256 , pp. 365-375
    • Chun, K.T.1    Goebl, M.G.2
  • 13
    • 0032524629 scopus 로고    scopus 로고
    • PDZ proteins organize synaptic signaling pathways
    • Craven, S., and D. Bredt. 1998. PDZ proteins organize synaptic signaling pathways. Cell 93:495-498.
    • (1998) Cell , vol.93 , pp. 495-498
    • Craven, S.1    Bredt, D.2
  • 14
    • 0028177590 scopus 로고
    • P56lck interacts via its src homology 2 domain with the ZAP-70 kinase
    • Duplay, P., M. Thome, F. Herve, and O. Acuto. 1994. p56lck interacts via its src homology 2 domain with the ZAP-70 kinase. J. Exp. Med. 179:1163-1172.
    • (1994) J. Exp. Med. , vol.179 , pp. 1163-1172
    • Duplay, P.1    Thome, M.2    Herve, F.3    Acuto, O.4
  • 15
    • 0033593325 scopus 로고    scopus 로고
    • The CDK-activating kinase (Cak1p) from budding yeast has an unusual ATP-binding pocket
    • Enke, D. A., P. Kaldis, J. K. Holmes, and M. J. Solomon. 1999. The CDK-activating kinase (Cak1p) from budding yeast has an unusual ATP-binding pocket. J. Biol. Chem. 274:1949-1956.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1949-1956
    • Enke, D.A.1    Kaldis, P.2    Holmes, J.K.3    Solomon, M.J.4
  • 16
    • 0027184473 scopus 로고
    • Required for Raf and MAP kinase function during the meiotic maturation of Xenopus oocytes
    • Fabian, J. R., D. K. Morrison, and I. O. Daar. 1993. Required for Raf and MAP kinase function during the meiotic maturation of Xenopus oocytes. J. Cell Biol. 122:645-652.
    • (1993) J. Cell Biol. , vol.122 , pp. 645-652
    • Fabian, J.R.1    Morrison, D.K.2    Daar, I.O.3
  • 17
    • 0028341334 scopus 로고
    • A single amino acid change in Raf-1 inhibits Ras binding and alters Raf-1 function
    • Fabian, J. R., A. B. Vojtek, J. A. Cooper, and D. K. Morrison. 1994. A single amino acid change in Raf-1 inhibits Ras binding and alters Raf-1 function. Proc. Natl. Acad. Sci. USA 91:5982-5986.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5982-5986
    • Fabian, J.R.1    Vojtek, A.B.2    Cooper, J.A.3    Morrison, D.K.4
  • 18
    • 0028120910 scopus 로고
    • Efficient coupling with phosphatidylinositol 3-kinase, but not phospholipase C gamma or GTPase-activating protein, distinguishes ErbB-3 signaling from that of other ErbB/EGFR family members
    • Fedi, P., J. H. Pierce, P. P. di Fiore, and M. H. Kraus. 1994. Efficient coupling with phosphatidylinositol 3-kinase, but not phospholipase C gamma or GTPase-activating protein, distinguishes ErbB-3 signaling from that of other ErbB/EGFR family members. Mol. Cell. Biol 14:492-500.
    • (1994) Mol. Cell. Biol , vol.14 , pp. 492-500
    • Fedi, P.1    Pierce, J.H.2    Di Fiore, P.P.3    Kraus, M.H.4
  • 20
    • 0025834693 scopus 로고
    • Identification of electrostatic interactions that determine the phosphorylation site specificity of the cAMP-dependent protein kinase
    • Gibbs, C. S., and M. J. Zoller. 1991. Identification of electrostatic interactions that determine the phosphorylation site specificity of the cAMP-dependent protein kinase. Biochemistry 30:5329-5334.
    • (1991) Biochemistry , vol.30 , pp. 5329-5334
    • Gibbs, C.S.1    Zoller, M.J.2
  • 21
    • 0029278868 scopus 로고
    • Localization of two mouse genes encoding the protein tyrosine kinase receptor-related protein RYK
    • Gough, N. M., S. Rakar, C. M. Hovens, and A Wilks. 1995. Localization of two mouse genes encoding the protein tyrosine kinase receptor-related protein RYK. Mamm. Genome 6:255-256.
    • (1995) Mamm. Genome , vol.6 , pp. 255-256
    • Gough, N.M.1    Rakar, S.2    Hovens, C.M.3    Wilks, A.4
  • 22
    • 0029780534 scopus 로고    scopus 로고
    • A new member of the Eph family of receptors that lacks protein tyrosine kinase activity
    • Gurniak, C. B., and L. J. Berg. 1996. A new member of the Eph family of receptors that lacks protein tyrosine kinase activity. Oncogene 13:777-786.
    • (1996) Oncogene , vol.13 , pp. 777-786
    • Gurniak, C.B.1    Berg, L.J.2
  • 23
    • 0029020282 scopus 로고
    • The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification
    • Hanks, S. K., and T. Hunter. 1995. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J. 9:576-596.
    • (1995) FASEB J. , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 24
    • 0023885305 scopus 로고
    • Conserved features and deduced phylogeny of the catalytic domains
    • Hanks, S. K., A. M. Quinn, and T. Hunter. 1988. Conserved features and deduced phylogeny of the catalytic domains. Science 241:42-52.
    • (1988) Science , vol.241 , pp. 42-52
    • Hanks, S.K.1    Quinn, A.M.2    Hunter, T.3
  • 25
    • 0030859238 scopus 로고    scopus 로고
    • Role of the glycine triad in the ATP-binding site of cAMP-dependent protein kinase
    • Hemmer, W., M. McGlone, I. Tsigelny, and S. S. Taylor. 1997. Role of the glycine triad in the ATP-binding site of cAMP-dependent protein kinase. J. Biol. Chem. 272:16946-16954.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16946-16954
    • Hemmer, W.1    McGlone, M.2    Tsigelny, I.3    Taylor, S.S.4
  • 26
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., H. D. Hunt, R. M. Horton, J. K. Pullen, and L. R. Pease. 1989. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77:51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 28
    • 0030067804 scopus 로고    scopus 로고
    • The C. elegans vulval induction gene lin-2 encodes a member of the MAGUK family of cell junction proteins
    • Hoskins, R., A. Hajnal, S. Harp, and S. Kim. 1996. The C. elegans vulval induction gene lin-2 encodes a member of the MAGUK family of cell junction proteins. Development 122:97-111.
    • (1996) Development , vol.122 , pp. 97-111
    • Hoskins, R.1    Hajnal, A.2    Harp, S.3    Kim, S.4
  • 30
    • 0030766163 scopus 로고    scopus 로고
    • Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog
    • Hubbard, S. R. 1997. Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog. EMBO J. 16:5572-5581.
    • (1997) EMBO J. , vol.16 , pp. 5572-5581
    • Hubbard, S.R.1
  • 31
    • 0028582185 scopus 로고
    • Crystal structure of the tyrosine kinase domain of the human insulin receptor
    • Hubbard, S. R., L. Wei, L. Ellis, and W. A. Hendrickson. 1994. Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature 372:746-754.
    • (1994) Nature , vol.372 , pp. 746-754
    • Hubbard, S.R.1    Wei, L.2    Ellis, L.3    Hendrickson, W.A.4
  • 32
    • 0028916050 scopus 로고
    • A potential interaction of p75 and Trka NGF receptors revealed by affinity cross-linking and immunoprecipitation
    • Huber, L. J., and M. V. Chao. 1995. A potential interaction of p75 and Trka NGF receptors revealed by affinity cross-linking and immunoprecipitation. J. Neurosci. Res. 40:557-563.
    • (1995) J. Neurosci. Res. , vol.40 , pp. 557-563
    • Huber, L.J.1    Chao, M.V.2
  • 33
    • 0028206124 scopus 로고
    • Molecular cloning of a novel receptor tyrosine kinase gene, STK, derived from enriched hematopoietic stem cells
    • Iwama, A., K. Okano, T. Sudo, Y. Matsuda, and T. Suda. 1994. Molecular cloning of a novel receptor tyrosine kinase gene, STK, derived from enriched hematopoietic stem cells. Blood 83:3160-3169.
    • (1994) Blood , vol.83 , pp. 3160-3169
    • Iwama, A.1    Okano, K.2    Sudo, T.3    Matsuda, Y.4    Suda, T.5
  • 34
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: Structural basis for regulation
    • Johnson, L. N., M. E. Noble, and D. J. Owen. 1996. Active and inactive protein kinases: structural basis for regulation. Cell 85:149-158.
    • (1996) Cell , vol.85 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.2    Owen, D.J.3
  • 35
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W., and C. Sander. 1983. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 36
    • 0033563245 scopus 로고    scopus 로고
    • Overexpression of H-Ryk in mouse fibroblasts confers transforming ability in vitro and in vivo: Correlation with up-regulation in epithelial ovarian cancer
    • Katso, R., S. Manek, S. Biddolph, R. Whittaker, F. Charnock, M. Wells, and T. Ganesan. 1999. Overexpression of H-Ryk in mouse fibroblasts confers transforming ability in vitro and in vivo: correlation with up-regulation in epithelial ovarian cancer. Cancer Res. 59:2265-2270.
    • (1999) Cancer Res. , vol.59 , pp. 2265-2270
    • Katso, R.1    Manek, S.2    Biddolph, S.3    Whittaker, R.4    Charnock, F.5    Wells, M.6    Ganesan, T.7
  • 37
    • 0027447550 scopus 로고
    • The murine vik gene (chromosome 9) encodes a putative receptor with unique protein kinase motifs
    • Kelman, Z., D. Simon-Chazottes, J. L. Guénet, and Y. Yarden. 1993. The murine vik gene (chromosome 9) encodes a putative receptor with unique protein kinase motifs. Oncogene 8:37-44.
    • (1993) Oncogene , vol.8 , pp. 37-44
    • Kelman, Z.1    Simon-Chazottes, D.2    Guénet, J.L.3    Yarden, Y.4
  • 38
  • 39
    • 0025857391 scopus 로고
    • The trk proto-oncogene encodes a receptor for nerve growth factor
    • Klein, R., S. Jing, V. Nanduri, E. O'Rourke, and M. Barbacid. 1991. The trk proto-oncogene encodes a receptor for nerve growth factor. Cell 65:189-197.
    • (1991) Cell , vol.65 , pp. 189-197
    • Klein, R.1    Jing, S.2    Nanduri, V.3    O'Rourke, E.4    Barbacid, M.5
  • 41
    • 0028284689 scopus 로고
    • Isolation of tyrosine kinase related genes expressed in the early hematopoietic system
    • Larsson-Blomberg, L., and E. Dzierzak. 1994. Isolation of tyrosine kinase related genes expressed in the early hematopoietic system. FEBS Lett. 348: 119-125.
    • (1994) FEBS Lett. , vol.348 , pp. 119-125
    • Larsson-Blomberg, L.1    Dzierzak, E.2
  • 42
    • 0030009196 scopus 로고    scopus 로고
    • Potent human p140-TrkA agonists derived from an anti-receptor monoclonal antibody
    • LeSauteur, L., S. Maliartchouk, H. Le Jeune, R. Quirion, and H. U. Saragovi. 1996. Potent human p140-TrkA agonists derived from an anti-receptor monoclonal antibody. J. Neurosci. 16:1308-1316.
    • (1996) J. Neurosci. , vol.16 , pp. 1308-1316
    • LeSauteur, L.1    Maliartchouk, S.2    Le Jeune, H.3    Quirion, R.4    Saragovi, H.U.5
  • 44
    • 0028152333 scopus 로고
    • MAP kinase kinase kinase, MAP kinase kinase and MAP kinase
    • Marshall, C. J. 1994. MAP kinase kinase kinase, MAP kinase kinase and MAP kinase. Curr. Opin. Genet. Dev. 4:82-89.
    • (1994) Curr. Opin. Genet. Dev. , vol.4 , pp. 82-89
    • Marshall, C.J.1
  • 46
    • 0027074850 scopus 로고
    • A novel family of cell surface receptors with tyrosine kinase-like domain
    • Masiakowski, P., and D. Carroll. 1992. A novel family of cell surface receptors with tyrosine kinase-like domain. J. Biol. Chem. 267:26181-26190.
    • (1992) J. Biol. Chem. , vol.267 , pp. 26181-26190
    • Masiakowski, P.1    Carroll, D.2
  • 47
    • 0030598848 scopus 로고    scopus 로고
    • Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism
    • Mohammadi, M., J. Schlessinger, and S. R. Hubbard. 1996. Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism. Cell 86:577-587.
    • (1996) Cell , vol.86 , pp. 577-587
    • Mohammadi, M.1    Schlessinger, J.2    Hubbard, S.R.3
  • 48
    • 0024273702 scopus 로고
    • Mutational analysis of a phosphotransfer motif essential for v-fps tyrosine kinase activity
    • Moran, M. F., C. A. Koch, I. Sadowski, and T. Pawson. 1988. Mutational analysis of a phosphotransfer motif essential for v-fps tyrosine kinase activity. Oncogene 3:665-672.
    • (1988) Oncogene , vol.3 , pp. 665-672
    • Moran, M.F.1    Koch, C.A.2    Sadowski, I.3    Pawson, T.4
  • 49
    • 0028880074 scopus 로고
    • Colon carcinoma kinase-4 defines a new subclass of the receptor tyrosine kinase family
    • Mossie, K., B. Jallal, F. Alves, I. Sures, G. D. Plowman, and A. Ullrich. 1995. Colon carcinoma kinase-4 defines a new subclass of the receptor tyrosine kinase family. Oncogene 11:2179-2184.
    • (1995) Oncogene , vol.11 , pp. 2179-2184
    • Mossie, K.1    Jallal, B.2    Alves, F.3    Sures, I.4    Plowman, G.D.5    Ullrich, A.6
  • 50
    • 0028943531 scopus 로고
    • Tyrosine kinase-activity of a chimeric insulin-like-growth-factor-1 receptor-containing the insulin-receptor C-terminal domain - Comparison with the tyrosine kinase-activities of the insulin and insulin-like-growth-factor-1 receptors using a cell-free system
    • Mothe, I., S. Tartare, A. Kowalskichauvel, P. Kaliman, E. Vanobberghen, and R. Ballotti. 1995. Tyrosine kinase-activity of a chimeric insulin-like-growth-factor-1 receptor-containing the insulin-receptor C-terminal domain - comparison with the tyrosine kinase-activities of the insulin and insulin-like-growth-factor-1 receptors using a cell-free system. Eur. J. Biochem. 228:842-848.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 842-848
    • Mothe, I.1    Tartare, S.2    Kowalskichauvel, A.3    Kaliman, P.4    Vanobberghen, E.5    Ballotti, R.6
  • 51
    • 0028332830 scopus 로고
    • Tyrosines 1148 and 1173 of activated human epidermal growth factor receptors are binding sites of Shc in intact cells
    • Okabayashi, Y., Y. Kido, T. Okutani, Y. Sugimoto, K. Sakaguchi, and M. Kasuga. 1994. Tyrosines 1148 and 1173 of activated human epidermal growth factor receptors are binding sites of Shc in intact cells. J. Biol. Chem. 269:18674-18678.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18674-18678
    • Okabayashi, Y.1    Kido, Y.2    Okutani, T.3    Sugimoto, Y.4    Sakaguchi, K.5    Kasuga, M.6
  • 54
    • 0026484261 scopus 로고
    • SH2 and SH3 domains-from structure to function
    • Pawson, T., and G. D. Gish. 1992. SH2 and SH3 domains-from structure to function. Cell 71:359-362.
    • (1992) Cell , vol.71 , pp. 359-362
    • Pawson, T.1    Gish, G.D.2
  • 55
    • 0029004590 scopus 로고
    • Protein modelling by E-mail
    • Peitsch, M. C. 1995. Protein modelling by E-mail. BioTechnology 13:658-660.
    • (1995) BioTechnology , vol.13 , pp. 658-660
    • Peitsch, M.C.1
  • 56
    • 0028221043 scopus 로고
    • Signalling pathways initiated by receptor protein tyrosine kinases in Drosophila
    • Perrimon, N. 1994. Signalling pathways initiated by receptor protein tyrosine kinases in Drosophila. Curr. Opin. Cell Biol. 6:260-266.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 260-266
    • Perrimon, N.1
  • 57
    • 0023155210 scopus 로고
    • Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes
    • Ponder, J. W., and F. M. Richards. 1987. Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes. J. Mol. Biol. 193:775-791.
    • (1987) J. Mol. Biol. , vol.193 , pp. 775-791
    • Ponder, J.W.1    Richards, F.M.2
  • 58
    • 0029904190 scopus 로고    scopus 로고
    • Expression of protein tyrosine kinases in the murine thymus stroma
    • Potworowski, E. F., and C. Beauchemin. 1996. Expression of protein tyrosine kinases in the murine thymus stroma. Immunol. Lett. 50:65-69.
    • (1996) Immunol. Lett. , vol.50 , pp. 65-69
    • Potworowski, E.F.1    Beauchemin, C.2
  • 59
    • 0027466903 scopus 로고
    • Insulin-induced phosphorylation of the 46- And 52-kDa Shc proteins
    • Pronk, G. J., J. Mcglades, G. Pelicci, T. Pawson, and J. L. Bos. 1993. Insulin-induced phosphorylation of the 46- and 52-kDa Shc proteins. J. Biol. Chem. 268:5748-5753.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5748-5753
    • Pronk, G.J.1    Mcglades, J.2    Pelicci, G.3    Pawson, T.4    Bos, J.L.5
  • 60
    • 0027955433 scopus 로고
    • The adapter protein Shc interacts with the interleukin-2 (IL-2) receptor upon IL-2 stimulation
    • Ravichandran, K. S., and S. J. Burakoff. 1994. The adapter protein Shc interacts with the interleukin-2 (IL-2) receptor upon IL-2 stimulation. J. Biol. Chem. 269:1599-1602.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1599-1602
    • Ravichandran, K.S.1    Burakoff, S.J.2
  • 61
    • 0028204991 scopus 로고
    • Elucidation of the role of breathless, a Drosophila FGF receptor homolog, in tracheal cell migration
    • Reichman, F. M., B. Dickson, E. Hafen, and B. Z. Shilo. 1994. Elucidation of the role of breathless, a Drosophila FGF receptor homolog, in tracheal cell migration. Genes Dev. 8:428-439.
    • (1994) Genes Dev. , vol.8 , pp. 428-439
    • Reichman, F.M.1    Dickson, B.2    Hafen, E.3    Shilo, B.Z.4
  • 62
    • 0026743174 scopus 로고
    • Multiple protein sequence alignment from tertiary structure comparison: Assignment of global and residue confidence levels
    • Russell, R. B., and G. J. Barton. 1992. Multiple protein sequence alignment from tertiary structure comparison: assignment of global and residue confidence levels. Proteins Struct. Funct. Genet. 14:309-323.
    • (1992) Proteins Struct. Funct. Genet. , vol.14 , pp. 309-323
    • Russell, R.B.1    Barton, G.J.2
  • 64
    • 0032585638 scopus 로고    scopus 로고
    • Ryk is expressed in a differentiation-specific manner in epithelial tissues and is strongly induced in decidualizing uterine stroma
    • Serfas, M. S., and A. L. Tyner. 1998. Ryk is expressed in a differentiation-specific manner in epithelial tissues and is strongly induced in decidualizing uterine stroma. Oncogene 17:3435-3444.
    • (1998) Oncogene , vol.17 , pp. 3435-3444
    • Serfas, M.S.1    Tyner, A.L.2
  • 66
    • 0028797388 scopus 로고
    • The receptor tyrosine kinase-related gene (ryk) demonstrates lineage and stage-specific expression in hematopoietic cells
    • Simoneaux, D. K., F. A. Fletcher, R. Jurecic, H. G. Shilling, N. T. Van, P. Patel, and J. W. Belmont 1995. The receptor tyrosine kinase-related gene (ryk) demonstrates lineage and stage-specific expression in hematopoietic cells. J. Immunol. 154:1157-1166.
    • (1995) J. Immunol. , vol.154 , pp. 1157-1166
    • Simoneaux, D.K.1    Fletcher, F.A.2    Jurecic, R.3    Shilling, H.G.4    Van, N.T.5    Patel, P.6    Belmont, J.W.7
  • 67
    • 0029993728 scopus 로고    scopus 로고
    • Let-23 receptor localisation by the cell junction protein LIN-7 during C. elegans vulval induction
    • Simske, J., S. Kaech, S. Harp, and S. Kim. 1996. Let-23 receptor localisation by the cell junction protein LIN-7 during C. elegans vulval induction. Cell 85:195-204.
    • (1996) Cell , vol.85 , pp. 195-204
    • Simske, J.1    Kaech, S.2    Harp, S.3    Kim, S.4
  • 68
    • 0028241935 scopus 로고
    • Tyrosine kinase gene expression in the mouse small intestine
    • Siyanova, E. Y., M. S. Serfas, I. A. Mazo, and A. L. Tyner. 1994. Tyrosine kinase gene expression in the mouse small intestine. Oncogene 9:2053-2057.
    • (1994) Oncogene , vol.9 , pp. 2053-2057
    • Siyanova, E.Y.1    Serfas, M.S.2    Mazo, I.A.3    Tyner, A.L.4
  • 69
    • 0027288587 scopus 로고
    • The sh2 sh3 domain-containing protein grb2 interacts with tyrosine-phosphorylated irs1 and shc - Implications for insulin control of ras signaling
    • Skolnik, E. Y., C. H. Lee, A. Batzer, L. M. Vicentini, M. Zhou, R. Daly, M. J. Myers, J. M. Backer, A. Ullrich, and M. F. White. 1993. The sh2 sh3 domain-containing protein grb2 interacts with tyrosine-phosphorylated irs1 and shc - implications for insulin control of ras signaling. EMBO J. 12:1929-1936.
    • (1993) EMBO J. , vol.12 , pp. 1929-1936
    • Skolnik, E.Y.1    Lee, C.H.2    Batzer, A.3    Vicentini, L.M.4    Zhou, M.5    Daly, R.6    Myers, M.J.7    Backer, J.M.8    Ullrich, A.9    White, M.F.10
  • 70
    • 0027318314 scopus 로고
    • Molecular cloning and chromosomal localisation of the human homologue of a receptor related to tyrosine kinases (RYK)
    • Stacker, S. A., C. M. Hovens, A. Vitali, M. A. Pritchard, E. Baker, G. R. Sutherland, and A. F. Wilks. 1993. Molecular cloning and chromosomal localisation of the human homologue of a receptor related to tyrosine kinases (RYK). Oncogene 8:1347-1356.
    • (1993) Oncogene , vol.8 , pp. 1347-1356
    • Stacker, S.A.1    Hovens, C.M.2    Vitali, A.3    Pritchard, M.A.4    Baker, E.5    Sutherland, G.R.6    Wilks, A.F.7
  • 71
    • 0026044779 scopus 로고
    • FGFR-4, a new member of the fibroblast growth factor receptor family, expressed in the definitive endoderm and skeletal muscle lineages of the mouse
    • Stark, K. L., J. A. McMahon, and A. P. McMahon. 1991. FGFR-4, a new member of the fibroblast growth factor receptor family, expressed in the definitive endoderm and skeletal muscle lineages of the mouse. Development 113:641-651.
    • (1991) Development , vol.113 , pp. 641-651
    • Stark, K.L.1    McMahon, J.A.2    McMahon, A.P.3
  • 72
    • 0027204285 scopus 로고
    • The human ryk cDNa sequence predicts a protein containing two putative transmembrane segments and a tyrosine kinase catalytic domain
    • Tamagnone, L., J. Partanen, E. Armstrong, J. Lasota, K. Ohgami, T. Tazunoki, S. LaForgia, K. Huebner, and K. Alitalo. 1993. The human ryk cDNA sequence predicts a protein containing two putative transmembrane segments and a tyrosine kinase catalytic domain. Oncogene 8:2009-2014.
    • (1993) Oncogene , vol.8 , pp. 2009-2014
    • Tamagnone, L.1    Partanen, J.2    Armstrong, E.3    Lasota, J.4    Ohgami, K.5    Tazunoki, T.6    LaForgia, S.7    Huebner, K.8    Alitalo, K.9
  • 74
    • 0022591495 scopus 로고
    • The classification of amino acid conservation
    • Taylor, W. R. 1986. The classification of amino acid conservation. J. Theor. Biol. 119:205-208.
    • (1986) J. Theor. Biol. , vol.119 , pp. 205-208
    • Taylor, W.R.1
  • 75
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 76
    • 0030598908 scopus 로고    scopus 로고
    • Civ1 (CAK in vivo), a novel Cdk-activating kinase
    • Thuret, J. Y., J. G. Valay, G. Faye, and C. Mann. 1996. Civ1 (CAK in vivo), a novel Cdk-activating kinase. Cell 86:565-576.
    • (1996) Cell , vol.86 , pp. 565-576
    • Thuret, J.Y.1    Valay, J.G.2    Faye, G.3    Mann, C.4
  • 77
    • 0031309902 scopus 로고    scopus 로고
    • The discoidin domain receptor tyrosine kinases are activated by collagen
    • Vogel, W., G. D. Gish, F. Alves, and T. Pawson. 1997. The discoidin domain receptor tyrosine kinases are activated by collagen. Mol. Cell 1:13-23.
    • (1997) Mol. Cell , vol.1 , pp. 13-23
    • Vogel, W.1    Gish, G.D.2    Alves, F.3    Pawson, T.4
  • 79
    • 0030485340 scopus 로고    scopus 로고
    • Pediatric brain tumors express multiple receptor tyrosine kinases including novel cell adhesion kinases
    • Weiner, H. L., M. Rothman, D. C. Miller, and E. B. Ziff. 1996. Pediatric brain tumors express multiple receptor tyrosine kinases including novel cell adhesion kinases. Pediatr. Neurosurg. 25:64-71.
    • (1996) Pediatr. Neurosurg. , vol.25 , pp. 64-71
    • Weiner, H.L.1    Rothman, M.2    Miller, D.C.3    Ziff, E.B.4
  • 80
    • 12044249985 scopus 로고
    • Cytokine signal transduction and the Jak family of protein tyrosine kinases
    • Wilks, A., and A. Harpur. 1994. Cytokine signal transduction and the Jak family of protein tyrosine kinases. Bioessays 16:313-319.
    • (1994) Bioessays , vol.16 , pp. 313-319
    • Wilks, A.1    Harpur, A.2
  • 81
    • 0027205387 scopus 로고
    • Dror, apotential neurotrophic receptor gene, encodes a Drosophila homolog of the vertebrate Ror family of Trk-related receptor tyrosine kinases
    • Wilson, C., C. I. Goberdhan, and H. Steller. 1993. Dror, apotential neurotrophic receptor gene, encodes a Drosophila homolog of the vertebrate Ror family of Trk-related receptor tyrosine kinases. Proc. Natl. Acad. Sci. USA 90:7190-7113.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7190-17113
    • Wilson, C.1    Goberdhan, C.I.2    Steller, H.3
  • 82
    • 0027312775 scopus 로고
    • Isolation of a novel receptor tyrosine kinase cDNa expressed by developing erythroid progenitors
    • Yee, K., T. R. Bishop, C. Mather, and L. I. Zon. 1993. Isolation of a novel receptor tyrosine kinase cDNA expressed by developing erythroid progenitors. Blood 82:1335-1343.
    • (1993) Blood , vol.82 , pp. 1335-1343
    • Yee, K.1    Bishop, T.R.2    Mather, C.3    Zon, L.I.4
  • 83
    • 0029860520 scopus 로고    scopus 로고
    • Regulation and interaction of pp90rsk isoforms with mitogen activated protein kinases
    • Zhao, Y., C. Bjorbaek, and D. Moller. 1996. Regulation and interaction of pp90rsk isoforms with mitogen activated protein kinases. J. Biol. Chem. 271:29773-29779.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29773-29779
    • Zhao, Y.1    Bjorbaek, C.2    Moller, D.3
  • 84
    • 0029007314 scopus 로고
    • rsk isoform with a unique N-terminal sequence: Growth factor-stimulated kinase function and nuclear translocation
    • rsk isoform with a unique N-terminal sequence: growth factor-stimulated kinase function and nuclear translocation. Mol. Cell. Biol. 15:4353-4363.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4353-4363
    • Zhao, Y.1    Bjorbaek, C.2    Weremowicz, S.3    Morton, C.4    Moller, D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.