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Volumn 138, Issue 5, 1997, Pages 1089-1103

Nerve growth factor-specific regulation of protein methylation during neuronal differentiation of PC12 cells

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE DERIVATIVE; HOMOCYSTEINE; METHIONINE; NERVE GROWTH FACTOR; TRITIUM;

EID: 0030931409     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.138.5.1089     Document Type: Article
Times cited : (60)

References (64)
  • 1
    • 0031025092 scopus 로고    scopus 로고
    • A protein-arginine methyltransferase binds to the intracytoplasmic domain of the IFNAR1 chain in the type I interferon receptor
    • Abramovich, C., B. Yakobson, J. Chebath, and M. Revel. 1997. A protein-arginine methyltransferase binds to the intracytoplasmic domain of the IFNAR1 chain in the type I interferon receptor. EMBO (Eur. Mol. Biol. Organ.) J. 16:260-266.
    • (1997) EMBO (Eur. Mol. Biol. Organ.) J. , vol.16 , pp. 260-266
    • Abramovich, C.1    Yakobson, B.2    Chebath, J.3    Revel, M.4
  • 2
    • 0029808685 scopus 로고    scopus 로고
    • Phosphorylation of type III β-tubulin in PC12 cell neurites during NGF-induced process outgrowth
    • Aletta, J.M. 1996. Phosphorylation of type III β-tubulin in PC12 cell neurites during NGF-induced process outgrowth. J. Neurobiol. 31:461-475.
    • (1996) J. Neurobiol. , vol.31 , pp. 461-475
    • Aletta, J.M.1
  • 3
    • 0023376321 scopus 로고
    • Sequential phosphorylation of chartin microtubule-associated proteins is regulated by the presence of microtubules
    • Aletta, J.M., and L.A. Greene. 1987. Sequential phosphorylation of chartin microtubule-associated proteins is regulated by the presence of microtubules. J. Cell Biol. 105:277-290.
    • (1987) J. Cell Biol. , vol.105 , pp. 277-290
    • Aletta, J.M.1    Greene, L.A.2
  • 4
    • 0022990116 scopus 로고
    • Effects of the S-adenosylhomocysteine hydrolase inhibitors 3-deazaadenosine and 3-deazaaristeromycin on RNA methylation and synthesis
    • Backlund, P.S., Jr., D. Carotti, and G.L. Cantoni. 1986. Effects of the S-adenosylhomocysteine hydrolase inhibitors 3-deazaadenosine and 3-deazaaristeromycin on RNA methylation and synthesis. Eur. J. Biochem. 160:245-251.
    • (1986) Eur. J. Biochem. , vol.160 , pp. 245-251
    • Backlund Jr., P.S.1    Carotti, D.2    Cantoni, G.L.3
  • 5
    • 0021192752 scopus 로고
    • Differentiation of two mouse cell lines is associated with hypomethylation of their genomes
    • Bestor, T.H., S.R. Hellewell, and V.M. Ingram 1984. Differentiation of two mouse cell lines is associated with hypomethylation of their genomes. Mol. Cell. Biol. 4:1800-1806.
    • (1984) Mol. Cell. Biol. , vol.4 , pp. 1800-1806
    • Bestor, T.H.1    Hellewell, S.R.2    Ingram, V.M.3
  • 6
    • 0022515078 scopus 로고
    • Regulation of microtubule composition and stability during nerve growth factor-promoted neurite out-growth
    • Black, M.M., J.M. Aletta, and L.A. Greene. 1986. Regulation of microtubule composition and stability during nerve growth factor-promoted neurite out-growth. J. Cell Biol. 103:545-557.
    • (1986) J. Cell Biol. , vol.103 , pp. 545-557
    • Black, M.M.1    Aletta, J.M.2    Greene, L.A.3
  • 7
    • 0016203040 scopus 로고
    • A film detection method for tritium-labeled proteins and nucleic acids in polyacrylamide gels
    • Bonner, W.M., and R.A. Laskey. 1974. A film detection method for tritium-labeled proteins and nucleic acids in polyacrylamide gels. Eur. J. Biochem. 46:83-88.
    • (1974) Eur. J. Biochem. , vol.46 , pp. 83-88
    • Bonner, W.M.1    Laskey, R.A.2
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 9
    • 0343006620 scopus 로고
    • Evidence for RNA synthesis-dependent and independent pathways in stimulation of neurite outgrowth by nerve growth factor
    • Burstein, D.E., and L.A. Greene. 1978. Evidence for RNA synthesis-dependent and independent pathways in stimulation of neurite outgrowth by nerve growth factor. Proc. Natl. Acad Sci. USA. 75:6059-6063.
    • (1978) Proc. Natl. Acad Sci. USA , vol.75 , pp. 6059-6063
    • Burstein, D.E.1    Greene, L.A.2
  • 10
    • 0018700703 scopus 로고
    • Fluorographic detection of radioactivity in polyacrylamide gels with the water-soluble fluor, sodium salicylate
    • Chamberlain, J.P. 1979. Fluorographic detection of radioactivity in polyacrylamide gels with the water-soluble fluor, sodium salicylate. Anal. Biochem. 98:132-135.
    • (1979) Anal. Biochem. , vol.98 , pp. 132-135
    • Chamberlain, J.P.1
  • 11
    • 0026578026 scopus 로고
    • Growth factor signaling: Where is the specificity?
    • Chao, M.V. 1992. Growth factor signaling: where is the specificity? Cell. 68: 995-997.
    • (1992) Cell , vol.68 , pp. 995-997
    • Chao, M.V.1
  • 12
    • 0022388682 scopus 로고
    • Methyl-esterified proteins in a mammalian cell line
    • Chelsky, D., B. Ruskin, and D.E. Koshland. 1985. Methyl-esterified proteins in a mammalian cell line. Biochemistry. 24:6651-6658.
    • (1985) Biochemistry , vol.24 , pp. 6651-6658
    • Chelsky, D.1    Ruskin, B.2    Koshland, D.E.3
  • 13
    • 0017742252 scopus 로고
    • S-adenosyl-L-homocysteine hydrolase: Analogues of S-adenosyl-L-homocysteine as potential inhibitors
    • Chiang, P.K., H.H. Richards, and G.L. Cantoni. 1977. S-adenosyl-L-homocysteine hydrolase: analogues of S-adenosyl-L-homocysteine as potential inhibitors. Mol. Pharmacol. 13:939-947.
    • (1977) Mol. Pharmacol. , vol.13 , pp. 939-947
    • Chiang, P.K.1    Richards, H.H.2    Cantoni, G.L.3
  • 14
    • 0025000359 scopus 로고
    • Methionine and neural tube closure in cultured rat embryos: Morphological and biochemical analyses
    • Coelho, C.N.D., and N.W. Klein. 1990. Methionine and neural tube closure in cultured rat embryos: morphological and biochemical analyses. Teratology. 42:437-451.
    • (1990) Teratology , vol.42 , pp. 437-451
    • Coelho, C.N.D.1    Klein, N.W.2
  • 15
    • 70449254180 scopus 로고
    • The enzymatic synthesis of S-adenosyl-L-homocysteine from adenosine and homocysteine
    • De la Haba, G., and G.L. Cantoni. 1959. The enzymatic synthesis of S-adenosyl-L-homocysteine from adenosine and homocysteine. J. Biol. Chem. 234: 603-608.
    • (1959) J. Biol. Chem. , vol.234 , pp. 603-608
    • De La Haba, G.1    Cantoni, G.L.2
  • 16
    • 0028361380 scopus 로고
    • The catalytic subunit of protein phosphatase 2A is carboxyl-methylated in vivo
    • Favre, B., S. Zolnierowicz, P. Turowski, and B.A. Hemmings. 1994. The catalytic subunit of protein phosphatase 2A is carboxyl-methylated in vivo. J. Biol. Chem. 269:16311-16317.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16311-16317
    • Favre, B.1    Zolnierowicz, S.2    Turowski, P.3    Hemmings, B.A.4
  • 17
    • 0022255635 scopus 로고
    • Does phospholipid melhylation play a role in the primary mechanism of action of nerve growth factor?
    • Ferrari, G., and L.A. Greene. 1985. Does phospholipid melhylation play a role in the primary mechanism of action of nerve growth factor? J. Neurochem. 45:853-859.
    • (1985) J. Neurochem. , vol.45 , pp. 853-859
    • Ferrari, G.1    Greene, L.A.2
  • 18
    • 0021359709 scopus 로고
    • The importance of both early and delayed responses in the biological actions of nerve growth factor
    • Greene, L.A. 1984. The importance of both early and delayed responses in the biological actions of nerve growth factor. Trends Neurosci. 13:91-94.
    • (1984) Trends Neurosci. , vol.13 , pp. 91-94
    • Greene, L.A.1
  • 19
    • 0345704610 scopus 로고
    • Establishment of a noradrenergic clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor
    • Greene, L.A., and A.S. Tischler. 1976. Establishment of a noradrenergic clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor. Proc. Natl. Acad. Sci. USA. 73:2424-2428.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 2424-2428
    • Greene, L.A.1    Tischler, A.S.2
  • 20
    • 0020144469 scopus 로고
    • The role of transcription-dependent priming in nerve growth factor promoted neurite outgrowth
    • Greene, L.A. D.E. Burstein, and M.M. Black. 1982. The role of transcription-dependent priming in nerve growth factor promoted neurite outgrowth. Dev. Biol. 91:305-316.
    • (1982) Dev. Biol. , vol.91 , pp. 305-316
    • Greene, L.A.1    Burstein, D.E.2    Black, M.M.3
  • 21
    • 0023545249 scopus 로고
    • PC12 pheochromocytoma cells: Culture, nerve growth factor treatment, and experimental exploitation
    • Greene, L.A., J.M. Aletta, A. Rukenstein, and S.H. Green. 1987. PC12 pheochromocytoma cells: culture, nerve growth factor treatment, and experimental exploitation. Methods Enzymol. 147:207-216.
    • (1987) Methods Enzymol. , vol.147 , pp. 207-216
    • Greene, L.A.1    Aletta, J.M.2    Rukenstein, A.3    Green, S.H.4
  • 22
    • 0027505893 scopus 로고
    • Nerve growth factor induces a succession of increases in isoprenylated methylated small GTP-binding proteins of PC12-pheochromocytoma cells
    • Haklai, R., S. Lerner, and Y. Kloog. 1993. Nerve growth factor induces a succession of increases in isoprenylated methylated small GTP-binding proteins of PC12-pheochromocytoma cells. Neuropeplides. 24:11-25.
    • (1993) Neuropeplides , vol.24 , pp. 11-25
    • Haklai, R.1    Lerner, S.2    Kloog, Y.3
  • 23
    • 0019160447 scopus 로고
    • Nerve growth factor mediates phosphorylation of specific proteins
    • Halegoua, S., and J. Patrick. 1980. Nerve growth factor mediates phosphorylation of specific proteins. Cell. 22:571-581.
    • (1980) Cell , vol.22 , pp. 571-581
    • Halegoua, S.1    Patrick, J.2
  • 24
    • 0024366240 scopus 로고
    • Elucidation of the mechanism by which homocysteine potentiates the anti-vaccinia virus effects of the S-adenosylhomocysteine hydrolase inhibitor 9-(trans-2′, trans-3′-dihydroxycyclopent-4′-enyl) derivatives of adenine and 3-deazaadenine on the metabolism of S-adenosylhomocysteine in mouse L929 cells
    • Hasobe, M., J.G. McKee, H. Ishii, M. Cools, R.T. Borchardt, and E. DeClercq. 1989. Elucidation of the mechanism by which homocysteine potentiates the anti-vaccinia virus effects of the S-adenosylhomocysteine hydrolase inhibitor 9-(trans-2′, trans-3′-dihydroxycyclopent-4′-enyl) derivatives of adenine and 3-deazaadenine on the metabolism of S-adenosylhomocysteine in mouse L929 cells. Mol. Pharmacol. 36:490-496.
    • (1989) Mol. Pharmacol. , vol.36 , pp. 490-496
    • Hasobe, M.1    McKee, J.G.2    Ishii, H.3    Cools, M.4    Borchardt, R.T.5    DeClercq, E.6
  • 25
    • 0018355271 scopus 로고
    • Apparent suicide inactivation of human lymphoblast S-adenosylhomocysteine hydrolase by 2′-deoxyadenosine and adenosine arabinoside
    • Hershfield, M.S. 1979. Apparent suicide inactivation of human lymphoblast S-adenosylhomocysteine hydrolase by 2′-deoxyadenosine and adenosine arabinoside. J. Biol. Chem. 254:22-25.
    • (1979) J. Biol. Chem. , vol.254 , pp. 22-25
    • Hershfield, M.S.1
  • 26
    • 0015455045 scopus 로고
    • New syntheses of S-adenosyl homocysteine analogues, potential methyltransferase inhibitors
    • Hildeshein, J., R. Hildeshein, and E. Lederer. 1972. New syntheses of S-adenosyl homocysteine analogues, potential methyltransferase inhibitors. Biochimie (Paris). 54:989-995.
    • (1972) Biochimie (Paris) , vol.54 , pp. 989-995
    • Hildeshein, J.1    Hildeshein, R.2    Lederer, E.3
  • 27
    • 0027363447 scopus 로고
    • Modification of eukaryotic signaling proteins by COOH-terminal methylation reactions
    • Hrycyna, C.A., and S. Clarke. 1993. Modification of eukaryotic signaling proteins by COOH-terminal methylation reactions. Pharmacol. Ther. 59:281-300.
    • (1993) Pharmacol. Ther. , vol.59 , pp. 281-300
    • Hrycyna, C.A.1    Clarke, S.2
  • 28
    • 0019366764 scopus 로고
    • Nerve growth factor-induced alteration in the response of PC12 pheochromocytoma cells to epidermal growth factor
    • Huff, K., D. End, and G. Guroff. 1981. Nerve growth factor-induced alteration in the response of PC12 pheochromocytoma cells to epidermal growth factor. J. Cell Biol. 88:189-198.
    • (1981) J. Cell Biol. , vol.88 , pp. 189-198
    • Huff, K.1    End, D.2    Guroff, G.3
  • 29
    • 0028838971 scopus 로고
    • Protein kinases and phosphatases: The yin and yang of protein phosphorylation and signaling
    • Hunter, T. 1995. Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling. Cell. 80:225-236.
    • (1995) Cell , vol.80 , pp. 225-236
    • Hunter, T.1
  • 30
    • 0028115022 scopus 로고
    • Neurotrophin signal transduction by the Trk receptor
    • Kaplan, D.R., and R.M. Stephens. 1994. Neurotrophin signal transduction by the Trk receptor. J. Neurobiol. 25:1404-1417.
    • (1994) J. Neurobiol. , vol.25 , pp. 1404-1417
    • Kaplan, D.R.1    Stephens, R.M.2
  • 31
    • 0017717986 scopus 로고
    • Role of S-adenosylhomocysteine in adenosine mediated toxicity in cultured mouse T lymphoma cells
    • Kredich, N.M., and D.W. Martin, Jr. 1977. Role of S-adenosylhomocysteine in adenosine mediated toxicity in cultured mouse T lymphoma cells. Cell. 12: 931-938.
    • (1977) Cell , vol.12 , pp. 931-938
    • Kredich, N.M.1    Martin Jr., D.W.2
  • 32
    • 0027317444 scopus 로고
    • Early responses of PC12 cell to NGF and EGF: Effect of K252a and 5′-methylthioadenosine on gene expression and membrane protein methylation
    • Kujubu, D.A., J.B. Stimmel, R.E. Law, H.R. Herschman, and S. Clarke. 1993. Early responses of PC12 cell to NGF and EGF: effect of K252a and 5′-methylthioadenosine on gene expression and membrane protein methylation. J. Neurosci. Res. 36:58-65.
    • (1993) J. Neurosci. Res. , vol.36 , pp. 58-65
    • Kujubu, D.A.1    Stimmel, J.B.2    Law, R.E.3    Herschman, H.R.4    Clarke, S.5
  • 33
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature (Lond.). 222:680-685.
    • (1970) Nature (Lond.) , vol.222 , pp. 680-685
    • Laemmli, U.K.1
  • 34
  • 35
    • 0027184102 scopus 로고
    • Protein phosphatase 2A catalytic subunit is methylesterified at its carboxyl terminus by a novel methyltransferase
    • Lee, J., and J. Stock. 1993. Protein phosphatase 2A catalytic subunit is methylesterified at its carboxyl terminus by a novel methyltransferase. J. Biol. Chem. 268:19192-19195.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19192-19195
    • Lee, J.1    Stock, J.2
  • 36
    • 0029952559 scopus 로고    scopus 로고
    • A specific protein carboxyl methylesterase that demethylates phosphoprotein phosphatase 2A in bovine brain
    • Lee, J., Y. Chen, T. Tolstykh, and J. Stock. 1996. A specific protein carboxyl methylesterase that demethylates phosphoprotein phosphatase 2A in bovine brain. Proc. Natl. Acad. Sci. USA. 93:6043-6047.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6043-6047
    • Lee, J.1    Chen, Y.2    Tolstykh, T.3    Stock, J.4
  • 37
    • 17544370102 scopus 로고    scopus 로고
    • The mammalian immediate-early gene TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase
    • Lin, W.-J., J.D. Gary, M.C. Yang, S. Clarke, and H.R. Herschman. 1996. The mammalian immediate-early gene TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase. J. Biol. Chem. 271:15034-15044.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15034-15044
    • Lin, W.-J.1    Gary, J.D.2    Yang, M.C.3    Clarke, S.4    Herschman, H.R.5
  • 38
    • 0028957320 scopus 로고
    • In vivo and in vitro arginine methylation of RNA-binding proteins
    • Liu, Q., and G. Dreyfuss. 1995. In vivo and in vitro arginine methylation of RNA-binding proteins. Mol. Cell. Biol. 15:2800-2808.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2800-2808
    • Liu, Q.1    Dreyfuss, G.2
  • 39
    • 0026739034 scopus 로고
    • Rational approaches to the design of antiviral agents based on S-adenosyl-L-homocysteine hydrolase as a molecular target
    • Liu, S., M.S. Wolfe, and R.T. Borchardt. 1992. Rational approaches to the design of antiviral agents based on S-adenosyl-L-homocysteine hydrolase as a molecular target. Antivir. Res. 19:247-265.
    • (1992) Antivir. Res. , vol.19 , pp. 247-265
    • Liu, S.1    Wolfe, M.S.2    Borchardt, R.T.3
  • 40
    • 0030026182 scopus 로고    scopus 로고
    • Differential effects of the Rac GTPase on Purkinje cell axons and dendritic trunks and spines
    • Luo, L., T.K. Hensch, L. Ackerman, S. Barbel, L.Y. Jan, and Y.N. Jan. 1996. Differential effects of the Rac GTPase on Purkinje cell axons and dendritic trunks and spines. Nature (Lond.). 379:837-840.
    • (1996) Nature (Lond.) , vol.379 , pp. 837-840
    • Luo, L.1    Hensch, T.K.2    Ackerman, L.3    Barbel, S.4    Jan, L.Y.5    Jan, Y.N.6
  • 41
    • 0027418242 scopus 로고
    • Inhibition of the tyrosine kinase activity of fibroblast growth factor receptor by the methyltransferase inhibitor 5′-methylthioadenosine
    • Maher, P.A. 1993. Inhibition of the tyrosine kinase activity of fibroblast growth factor receptor by the methyltransferase inhibitor 5′-methylthioadenosine. J. Biol. Chem. 268:4244-4249.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4244-4249
    • Maher, P.A.1
  • 42
    • 0028872649 scopus 로고
    • Specificity of receptor tyrosine kinase signaling: Transient versus sustained extracellular signal-regulated kinase activation
    • Marshall, C.J. 1995. Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation. Cell. 80: 179-185.
    • (1995) Cell , vol.80 , pp. 179-185
    • Marshall, C.J.1
  • 43
    • 0026045006 scopus 로고
    • Tyrosine kinase activity coupled to the high-affinity nerve growth factor-receptor complex
    • Meakin, S.O., and E.M. Shooter. 1991. Tyrosine kinase activity coupled to the high-affinity nerve growth factor-receptor complex. Proc. Natl. Acad. Sci. USA. 88:5862-5866.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5862-5866
    • Meakin, S.O.1    Shooter, E.M.2
  • 44
    • 0027364367 scopus 로고
    • Modulation of insulin secretion from normal rat islets by inhibitors of the post-translational modifications of GTP binding proteins
    • Metz, S.A., M.E. Rubaglia, J.B. Stock, and A. Kowluru. 1993. Modulation of insulin secretion from normal rat islets by inhibitors of the post-translational modifications of GTP binding proteins. Biochem. J. 295:31-40.
    • (1993) Biochem. J. , vol.295 , pp. 31-40
    • Metz, S.A.1    Rubaglia, M.E.2    Stock, J.B.3    Kowluru, A.4
  • 46
    • 0017028064 scopus 로고
    • Characterization and isolation of proteolytically modified nerve growth factor
    • Mobley, W.C., A. Schenker, and E.M. Shooter. 1976. Characterization and isolation of proteolytically modified nerve growth factor. Biochemistry. 15: 5543-5552.
    • (1976) Biochemistry , vol.15 , pp. 5543-5552
    • Mobley, W.C.1    Schenker, A.2    Shooter, E.M.3
  • 47
    • 0031026635 scopus 로고    scopus 로고
    • Effects of methionine on the cytoplasmic distribution of actin and tubulin during neural tube closure in rat embryos
    • Moephuli, S.R., N.W. Klein, M.T. Baldwin, and H.M. Krider. 1997. Effects of methionine on the cytoplasmic distribution of actin and tubulin during neural tube closure in rat embryos. Proc. Natl. Acad. Sci. USA. 94:543-548.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 543-548
    • Moephuli, S.R.1    Klein, N.W.2    Baldwin, M.T.3    Krider, H.M.4
  • 48
    • 0025291029 scopus 로고
    • Diversity of methyl acceptor proteins in rat pheochromocytoma (PC12) cells revealed after treatment with adenosine dialdehyde
    • Najbauer, J., and D.W. Aswad. 1990. Diversity of methyl acceptor proteins in rat pheochromocytoma (PC12) cells revealed after treatment with adenosine dialdehyde. J. Biol. Chem. 265:12717-12721.
    • (1990) J. Biol. Chem. , vol.265 , pp. 12717-12721
    • Najbauer, J.1    Aswad, D.W.2
  • 49
    • 0029075550 scopus 로고
    • Functional significance of βγ-subunit carboxyl methylation for the activation of phospholipase C and phosphoinositide 3-kinase
    • Parish, C.A., A.V. Smrcka, and R.R. Rando. 1995. Functional significance of βγ-subunit carboxyl methylation for the activation of phospholipase C and phosphoinositide 3-kinase. Biochemistry. 34:7722-7727.
    • (1995) Biochemistry , vol.34 , pp. 7722-7727
    • Parish, C.A.1    Smrcka, A.V.2    Rando, R.R.3
  • 50
    • 0028859279 scopus 로고
    • Protein modules and signaling networks
    • Pawson, T. 1985. Protein modules and signaling networks. Nature (Lond.). 373: 573-580.
    • (1985) Nature (Lond.) , vol.373 , pp. 573-580
    • Pawson, T.1
  • 51
    • 0029082202 scopus 로고
    • Deletion of a conserved juxtamembrane sequence in trk abolishes NGF-promoted neuritogenesis
    • Peng, X., L.A. Greene, D.R. Kaplan, and R.M. Stephens. 1995. Deletion of a conserved juxtamembrane sequence in trk abolishes NGF-promoted neuritogenesis Neuron. 15:395-406.
    • (1995) Neuron , vol.15 , pp. 395-406
    • Peng, X.1    Greene, L.A.2    Kaplan, D.R.3    Stephens, R.M.4
  • 54
    • 0026733002 scopus 로고
    • ras activity and consequent prolonged ERK activity
    • ras activity and consequent prolonged ERK activity. Neuron. 9:705-717.
    • (1992) Neuron , vol.9 , pp. 705-717
    • Qui, M.-S.1    Green, S.H.2
  • 55
    • 0029978806 scopus 로고    scopus 로고
    • Chemical biology of protein isoprenylation/methylation
    • Rando, R.R. 1996. Chemical biology of protein isoprenylation/methylation. Biochim. Biophys. Acta. 1300:5-16.
    • (1996) Biochim. Biophys. Acta , vol.1300 , pp. 5-16
    • Rando, R.R.1
  • 56
    • 0025945632 scopus 로고
    • DNA methylation and gene expression
    • Razin, A., and H. Cedar. 1991. DNA methylation and gene expression. Microbiol. Rev. 55:451-458.
    • (1991) Microbiol. Rev. , vol.55 , pp. 451-458
    • Razin, A.1    Cedar, H.2
  • 57
    • 0025939423 scopus 로고
    • Multiple agents rescue PC12 cells from serum-free cell death by translation, and transcription-dependent mechanisms
    • Rukenstein, A., R.E. Rydel, and L.A. Greene. 1991. Multiple agents rescue PC12 cells from serum-free cell death by translation, and transcription-dependent mechanisms. J. Neurosci. 11:2557-2563.
    • (1991) J. Neurosci. , vol.11 , pp. 2557-2563
    • Rukenstein, A.1    Rydel, R.E.2    Greene, L.A.3
  • 58
    • 0021357849 scopus 로고
    • Differential inhibition of nerve growth factor and epidermal growth factor on the PC12 pheochromocytoma line
    • Seeley, P.J., A. Rukenstein, J.L. Connolly, and L.A. Greene. 1984. Differential inhibition of nerve growth factor and epidermal growth factor on the PC12 pheochromocytoma line. J. Cell Biol. 98:417-426.
    • (1984) J. Cell Biol. , vol.98 , pp. 417-426
    • Seeley, P.J.1    Rukenstein, A.2    Connolly, J.L.3    Greene, L.A.4
  • 59
    • 0028800723 scopus 로고
    • Contributions made by individual methylation sites of Escherichia coli aspartate receptor to chemotactic behavior
    • Shapiro, M.J., I. Chakrabarti, and D.E. Koshland. 1995. Contributions made by individual methylation sites of Escherichia coli aspartate receptor to chemotactic behavior. Proc. Natl. Acad. Sci. USA. 92:1053-1056.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1053-1056
    • Shapiro, M.J.1    Chakrabarti, I.2    Koshland, D.E.3
  • 60
    • 0022263028 scopus 로고
    • The role of estrogens on the proliferation of human breast tumor cells (MCF-7)
    • Soto, A.M., and C. Sonnenschein. 1985. The role of estrogens on the proliferation of human breast tumor cells (MCF-7). J. Steroid Biochem. 23:87-94.
    • (1985) J. Steroid Biochem. , vol.23 , pp. 87-94
    • Soto, A.M.1    Sonnenschein, C.2
  • 61
    • 0017855347 scopus 로고
    • Morphologic and cytochemical properties of a clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor
    • Tischler, A.S., and L.A. Greene. 1978. Morphologic and cytochemical properties of a clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor. Lab. Invest. 39:77-89.
    • (1978) Lab. Invest. , vol.39 , pp. 77-89
    • Tischler, A.S.1    Greene, L.A.2
  • 62
    • 0028940016 scopus 로고
    • Differential methylation and altered conformation of cytoplasmic and nuclear forms of protein phosphatase 2A during cell cycle progression
    • Turowski, P., A. Fernandez, B. Favre, N.J.C. Lamb, and B.A. Hemmings. 1995. Differential methylation and altered conformation of cytoplasmic and nuclear forms of protein phosphatase 2A during cell cycle progression. J. Cell Biol. 129:397-410.
    • (1995) J. Cell Biol. , vol.129 , pp. 397-410
    • Turowski, P.1    Fernandez, A.2    Favre, B.3    Lamb, N.J.C.4    Hemmings, B.A.5
  • 63
    • 0029145073 scopus 로고
    • Rho family members: Activators of MAP kinase cascades
    • Vojtek, A.B., and J.A. Cooper. 1995. Rho family members: activators of MAP kinase cascades. Cell. 82:527-529.
    • (1995) Cell , vol.82 , pp. 527-529
    • Vojtek, A.B.1    Cooper, J.A.2
  • 64
    • 0028154020 scopus 로고
    • Protein phosphatase 2A is reversibly modified by methyl esterification of its C-terminal leucine residue in bovine brain
    • Xie, H., and S. Clarke. 1994. Protein phosphatase 2A is reversibly modified by methyl esterification of its C-terminal leucine residue in bovine brain. J. Biol. Chem. 269:1981-1984.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1981-1984
    • Xie, H.1    Clarke, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.