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Volumn 13, Issue 9, 2002, Pages 431-439

Heme deficiency interferes with the Ras-mitogen-activated protein kinase signaling pathway and expression of a subset of neuronal genes

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; HEME; MITOGEN ACTIVATED PROTEIN KINASE; NERVE GROWTH FACTOR; NEUROFILAMENT PROTEIN; RAS PROTEIN;

EID: 0036741718     PISSN: 10449523     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (67)

References (55)
  • 1
    • 0000465203 scopus 로고
    • Regulation of heme biosynthesis in higher animals
    • H. A. Dailey (ed.), New York: Green Pub. Associates and Wiley-Interscience
    • Andrew, T. L., Riley, P. G., and Dailey, H. A. Regulation of heme biosynthesis in higher animals In: H. A. Dailey (ed.), Biosynthesis of Heme and Cholorophylls, pp. 183-232, New York: Green Pub. Associates and Wiley-Interscience, 1990.
    • (1990) Biosynthesis of Heme and Cholorophylls , pp. 183-232
    • Andrew, T.L.1    Riley, P.G.2    Dailey, H.A.3
  • 2
    • 0028935374 scopus 로고
    • Regulation of protein synthesis by heme-regulated elF-2α kinase
    • Chen, J. J., and London, I. M. Regulation of protein synthesis by heme-regulated elF-2α kinase. Trends Biochem. Sci., 20: 105-108, 1995.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 105-108
    • Chen, J.J.1    London, I.M.2
  • 3
    • 0032729833 scopus 로고    scopus 로고
    • Molecular mechanism of heme signaling in yeast: The transcriptional activator Hap1 serves as the key mediator
    • Zhang, L., and Hach, A. Molecular mechanism of heme signaling in yeast: the transcriptional activator Hap1 serves as the key mediator. Cell. Mol. Life. Sci., 56: 415-426, 1999.
    • (1999) Cell. Mol. Life. Sci. , vol.56 , pp. 415-426
    • Zhang, L.1    Hach, A.2
  • 4
    • 0029821892 scopus 로고    scopus 로고
    • Novel effects of heme and heme-related compounds in biological systems
    • Sassa, S. Novel effects of heme and heme-related compounds in biological systems. Curr. Med. Chem., 3: 273-290, 1996.
    • (1996) Curr. Med. Chem. , vol.3 , pp. 273-290
    • Sassa, S.1
  • 5
    • 0029960838 scopus 로고    scopus 로고
    • The role of heme in gene expression
    • Sassa, S., and Nagai, T. The role of heme in gene expression. Int. J. Hematol., 63: 167-178, 1996.
    • (1996) Int. J. Hematol. , vol.63 , pp. 167-178
    • Sassa, S.1    Nagai, T.2
  • 6
    • 0027360547 scopus 로고
    • Biochemistry of porphyria
    • Moore, M. R. Biochemistry of porphyria. Int. J. Biochem., 25: 1353-1368, 1993.
    • (1993) Int. J. Biochem. , vol.25 , pp. 1353-1368
    • Moore, M.R.1
  • 7
    • 0031940457 scopus 로고    scopus 로고
    • Acute porphyria: Treatment with heme
    • Tenhunen, R., and Mustajoki, P. Acute porphyria: treatment with heme. Semin. Liver Dis., 18: 53-55, 1998.
    • (1998) Semin. Liver Dis. , vol.18 , pp. 53-55
    • Tenhunen, R.1    Mustajoki, P.2
  • 8
    • 0031890977 scopus 로고    scopus 로고
    • Acute porphyrias: Pathogenesis of neurological manifestations
    • Meyer, U. A., Schuurmans, M. M., and Lindberg, R. L. Acute porphyrias: pathogenesis of neurological manifestations. Semin. Liver Dis., 18: 43-52, 1998.
    • (1998) Semin. Liver Dis. , vol.18 , pp. 43-52
    • Meyer, U.A.1    Schuurmans, M.M.2    Lindberg, R.L.3
  • 9
    • 0000016355 scopus 로고
    • The porphyrias
    • C. R. Scriver, A. L. Beaudt, W. S. Sly, and D. Valle (eds.), New York: The McGraw-Hill Companies, Inc..
    • Kappas, A., Sassa, S., Galbraith, R. A., and Nordmann, Y. The porphyrias. In: C. R. Scriver, A. L. Beaudt, W. S. Sly, and D. Valle (eds.), The Metabolic and Molecular Bases of Inherited Disease, 1995 Ed., 3 volumes, Vol. 2, pp. 2103-2160. New York: The McGraw-Hill Companies, Inc., 1995.
    • (1995) The Metabolic and Molecular Bases of Inherited Disease, 1995 Ed. , vol.2-3 , pp. 2103-2160
    • Kappas, A.1    Sassa, S.2    Galbraith, R.A.3    Nordmann, Y.4
  • 13
    • 0345704610 scopus 로고
    • Establishment of a noradrenergic clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor
    • Greene, L. A., and Tischler, A. S. 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.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 2424-2428
    • Greene, L.A.1    Tischler, A.S.2
  • 14
    • 0025350322 scopus 로고
    • NGF-dependent sprouting and regeneration in the hippocampus
    • Gage, F. H., Buzsaki, G., and Armstrong, D. M. NGF-dependent sprouting and regeneration in the hippocampus. Prog. Brain Res., 83: 357-370, 1990.
    • (1990) Prog. Brain Res. , vol.83 , pp. 357-370
    • Gage, F.H.1    Buzsaki, G.2    Armstrong, D.M.3
  • 16
    • 0021097734 scopus 로고
    • The effect of N-methylprotoporphyrin and succinyl-acetone on the regulation of heme biosynthesis in chicken hepatocytes in culture
    • De Matteis, F., and Marks, G. S. The effect of N-methylprotoporphyrin and succinyl-acetone on the regulation of heme biosynthesis in chicken hepatocytes in culture. FEBS Lett, 159: 127-131, 1983.
    • (1983) FEBS Lett. , vol.159 , pp. 127-131
    • De Matteis, F.1    Marks, G.S.2
  • 17
    • 0023656698 scopus 로고
    • Haem synthesis from exogenous 5-aminolaevulinate in cultured chick-embryo hepatocytes. Effects of inducers of cytochromes P-450
    • Shedlofsky, S. I., Sinclair, P. R., Bonkovsky, H, L., Healey, J. F., Swim, A. T., and Robinson, J. M. Haem synthesis from exogenous 5-aminolaevulinate in cultured chick-embryo hepatocytes. Effects of inducers of cytochromes P-450. Biochem. J., 248: 229-236, 1987.
    • (1987) Biochem. J. , vol.248 , pp. 229-236
    • Shedlofsky, S.I.1    Sinclair, P.R.2    Bonkovsky, H.L.3    Healey, J.F.4    Swim, A.T.5    Robinson, J.M.6
  • 18
    • 0032698075 scopus 로고    scopus 로고
    • Cell survival promoted by the Ras-MAPK signaling pathway by transcription-dependent and -independent mechanisms
    • Bonni, A., Brunet, A., West, A. E., Datta, S. R., Takasu, M. A., and Greenberg, M. E. Cell survival promoted by the Ras-MAPK signaling pathway by transcription-dependent and -independent mechanisms. Science (Wash. DC), 286: 1358-1362, 1999.
    • (1999) Science (Wash. DC) , vol.286 , pp. 1358-1362
    • Bonni, A.1    Brunet, A.2    West, A.E.3    Datta, S.R.4    Takasu, M.A.5    Greenberg, M.E.6
  • 19
    • 0028338460 scopus 로고
    • Nerve growth factor activates a Ras-dependent protein kinase that stimulates c-fos transcription via phosphorylation of CREB
    • Ginty, D. D., Bonni, A., and Greenberg, M. E. Nerve growth factor activates a Ras-dependent protein kinase that stimulates c-fos transcription via phosphorylation of CREB. Cell, 77: 713-725, 1994.
    • (1994) Cell , vol.77 , pp. 713-725
    • Ginty, D.D.1    Bonni, A.2    Greenberg, M.E.3
  • 20
    • 0030907924 scopus 로고    scopus 로고
    • Signal transduction by the neurotrophin receptors
    • Kaplan, D. R., and Miller, F. D. Signal transduction by the neurotrophin receptors. Curr. Opin. Cell Biol., 9: 213-221, 1997.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 213-221
    • Kaplan, D.R.1    Miller, F.D.2
  • 21
    • 0033563189 scopus 로고    scopus 로고
    • Trks: Signal transduction and intracellular pathways
    • Klesse, L. J., and Parada, L. F. Trks: signal transduction and intracellular pathways. Microsc. Res. Tech., 45: 210-216, 1999.
    • (1999) Microsc. Res. Tech. , vol.45 , pp. 210-216
    • Klesse, L.J.1    Parada, L.F.2
  • 23
    • 0029789643 scopus 로고    scopus 로고
    • Coupling of the RAS-MAPK pathway to gene activation by RSK2, a growth factor-regulated CREB kinase
    • Xing, J., Ginty, D. D., and Greenberg, M. E. Coupling of the RAS-MAPK pathway to gene activation by RSK2, a growth factor-regulated CREB kinase. Science (Wash. DC), 273: 959-963, 1996.
    • (1996) Science (Wash. DC) , vol.273 , pp. 959-963
    • Xing, J.1    Ginty, D.D.2    Greenberg, M.E.3
  • 24
    • 0032852479 scopus 로고    scopus 로고
    • CREB A stimulus-induced transcription factor activated by a diverse array of extracellular signals
    • Shaywitz, A. J., and Greenberg, M. E. CREB: A stimulus-induced transcription factor activated by a diverse array of extracellular signals. Annu. Rev. Biochem., 68: 821-861, 1999.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 821-861
    • Shaywitz, A.J.1    Greenberg, M.E.2
  • 25
    • 0040175067 scopus 로고    scopus 로고
    • Role and regulation of 90 kDa ribosomal S6 kinase (RSK) in signal transduction
    • Frodin, M., and Gammeltoft, S. Role and regulation of 90 kDa ribosomal S6 kinase (RSK) in signal transduction. Mol. Cell. Endocrinol., 151: 65-77, 1999.
    • (1999) Mol. Cell. Endocrinol. , vol.151 , pp. 65-77
    • Frodin, M.1    Gammeltoft, S.2
  • 26
    • 0042577160 scopus 로고    scopus 로고
    • Increased activity of eukaryotic initiation factor 2B in PC12 cells in response to differentiation by nerve growth factor
    • Munoz, F., Quevedo, C., Martin, M. E., Alcazar, A., Salinas, M., and Fando, J. L. Increased activity of eukaryotic initiation factor 2B in PC12 cells in response to differentiation by nerve growth factor. J. Neurochem., 71: 1905-1911, 1998.
    • (1998) J. Neurochem. , vol.71 , pp. 1905-1911
    • Munoz, F.1    Quevedo, C.2    Martin, M.E.3    Alcazar, A.4    Salinas, M.5    Fando, J.L.6
  • 27
    • 0026602898 scopus 로고
    • Concentration-dependent regulation of neuronal gene expression by nerve growth factor
    • Ma, Y., Campenot, R. B., and Miller, F. D. Concentration-dependent regulation of neuronal gene expression by nerve growth factor. J. Cell Biol., 117: 135-141, 1992.
    • (1992) J. Cell Biol. , vol.117 , pp. 135-141
    • Ma, Y.1    Campenot, R.B.2    Miller, F.D.3
  • 28
    • 0033136252 scopus 로고    scopus 로고
    • Nerve growth factor and epidermal growth factor stimulate clusterin gene expression in PC12 cells
    • Gutacker, C., Klock, G., Diel, P., and Koch-Brandt, C. Nerve growth factor and epidermal growth factor stimulate clusterin gene expression in PC12 cells. Biochem. J., 339: 759-766, 1999.
    • (1999) Biochem. J. , vol.339 , pp. 759-766
    • Gutacker, C.1    Klock, G.2    Diel, P.3    Koch-Brandt, C.4
  • 29
    • 0033620487 scopus 로고    scopus 로고
    • Heptahelical receptor signaling: Beyond the G protein paradigm
    • Hall, R. A., Premont, R. T., and Lefkowitz, R. J. Heptahelical receptor signaling: beyond the G protein paradigm. J. Cell Biol., 145: 927-932, 1999.
    • (1999) J. Cell Biol. , vol.145 , pp. 927-932
    • Hall, R.A.1    Premont, R.T.2    Lefkowitz, R.J.3
  • 30
    • 0031930873 scopus 로고    scopus 로고
    • The putative "switch 2" domain of the Ras-related GTPase. Rab1B, plays an essential role in the interaction with Rab escort protein
    • Overmeyer, J. H., Wilson, A. L., Erdman, R. A., and Maltese, W. A. The putative "switch 2" domain of the Ras-related GTPase. Rab1B, plays an essential role in the interaction with Rab escort protein. Mol. Biol. Cell, 9: 223-235, 1998.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 223-235
    • Overmeyer, J.H.1    Wilson, A.L.2    Erdman, R.A.3    Maltese, W.A.4
  • 31
    • 0033179137 scopus 로고    scopus 로고
    • Signalling through the JAK-STAT pathway in the developing brain
    • Cattaneo, E., Conti, L., and De-Fraja, C. Signalling through the JAK-STAT pathway in the developing brain. Trends Neurosci., 22: 365-369, 1999.
    • (1999) Trends Neurosci. , vol.22 , pp. 365-369
    • Cattaneo, E.1    Conti, L.2    De-Fraja, C.3
  • 32
    • 0034706070 scopus 로고    scopus 로고
    • In vivo localization and characterization of functional ciliary neurotrophic factor receptors which utilize JAK-STAT signaling
    • MacLennan, A. J., Neitzel, K. L., Devlin, B. K., Garcia, J., Hauptman, G. A., Gloaguen, I., Di Marco, A., Laufer, R., and Lee, N. In vivo localization and characterization of functional ciliary neurotrophic factor receptors which utilize JAK-STAT signaling. Neuroscience, 99: 761-772, 2000.
    • (2000) Neuroscience , vol.99 , pp. 761-772
    • MacLennan, A.J.1    Neitzel, K.L.2    Devlin, B.K.3    Garcia, J.4    Hauptman, G.A.5    Gloaguen, I.6    Di Marco, A.7    Laufer, R.8    Lee, N.9
  • 33
    • 0032555514 scopus 로고    scopus 로고
    • Characterization of the mechanism of regulation of Ca2+/calmodulin-dependent protein kinase I by calmodulin and by Ca2+/calmodulin-dependent protein kinase kinase
    • Matsushita, M., and Nairn, A. C. Characterization of the mechanism of regulation of Ca2+/calmodulin-dependent protein kinase I by calmodulin and by Ca2+/calmodulin-dependent protein kinase kinase. J. Biol. Chem., 273: 21473-21481, 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21473-21481
    • Matsushita, M.1    Nairn, A.C.2
  • 34
    • 0030271565 scopus 로고    scopus 로고
    • Structural organization and alternative splicing of the murine phosphoinositide 3-kinase p85α gene
    • Fruman, D. A., Cantley, L. C., and Carpenter, C. L. Structural organization and alternative splicing of the murine phosphoinositide 3-kinase p85α gene. Genomics, 37: 113-121, 1996.
    • (1996) Genomics , vol.37 , pp. 113-121
    • Fruman, D.A.1    Cantley, L.C.2    Carpenter, C.L.3
  • 35
    • 0027936755 scopus 로고
    • A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells
    • Han, J., Lee, J. D., Bibbs, L., and Ulevitch, R. J. A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells. Science (Wash. DC), 265: 808-811, 1994.
    • (1994) Science (Wash. DC) , vol.265 , pp. 808-811
    • Han, J.1    Lee, J.D.2    Bibbs, L.3    Ulevitch, R.J.4
  • 36
    • 0025838675 scopus 로고
    • Regulators and effectors of ras proteins
    • Bollag, G., and McCormick, F. Regulators and effectors of ras proteins. Annu. Rev. Cell. Biol., 7: 601-632, 1991.
    • (1991) Annu. Rev. Cell. Biol. , vol.7 , pp. 601-632
    • Bollag, G.1    McCormick, F.2
  • 37
    • 0030610847 scopus 로고    scopus 로고
    • rGbetal: A psychostimulant-regulated gene essential for establishing cocaine sensitization
    • Wang, X. B., Funada, M., Imai, Y., Revay, R. S., Ujike, H., Vandenbergh, D. J., and Uhl, G. R. rGbetal: a psychostimulant-regulated gene essential for establishing cocaine sensitization. J. Neurosci., 17: 5993-6000, 1997.
    • (1997) J. Neurosci. , vol.17 , pp. 5993-6000
    • Wang, X.B.1    Funada, M.2    Imai, Y.3    Revay, R.S.4    Ujike, H.5    Vandenbergh, D.J.6    Uhl, G.R.7
  • 38
    • 0030861630 scopus 로고    scopus 로고
    • A novel, nerve growth factor-activated pathway involving nitric oxide, p53, and p21WAF1 regulates neuronal differentiation of PC12 cells
    • Poluha, W., Schonhoff, C. M., Harrington, K. S., Lachyankar, M. B., Crosbie, N. E., Bulseco, D. A., and Ross, A. H. A novel, nerve growth factor-activated pathway involving nitric oxide, p53, and p21WAF1 regulates neuronal differentiation of PC12 cells. J. Biol. Chem., 272: 24002-24007, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24002-24007
    • Poluha, W.1    Schonhoff, C.M.2    Harrington, K.S.3    Lachyankar, M.B.4    Crosbie, N.E.5    Bulseco, D.A.6    Ross, A.H.7
  • 40
    • 0034674108 scopus 로고    scopus 로고
    • Neuropilin-2 and neuropilin-1 are receptors for the 165-amino acid form of vascular endothelial growth factor (VEGF) and of placenta growth factor-2, but only neuropilin-2 functions as a receptor for the 145-amino acid form of VEGF
    • Gluzman-Poltorak, Z., Cohen, T., Herzog, Y., and Neufeld, G. Neuropilin-2 and neuropilin-1 are receptors for the 165-amino acid form of vascular endothelial growth factor (VEGF) and of placenta growth factor-2, but only neuropilin-2 functions as a receptor for the 145-amino acid form of VEGF. J. Biol. Chem., 275: 18040-18045, 2000.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18040-18045
    • Gluzman-Poltorak, Z.1    Cohen, T.2    Herzog, Y.3    Neufeld, G.4
  • 41
    • 0033358605 scopus 로고    scopus 로고
    • Monoamine oxidase in neuropsychiatry and behavior
    • Shih, J. C., and Thompson, R. F. Monoamine oxidase in neuropsychiatry and behavior. Am. J. Hum. Genet., 65: 593-598, 1999.
    • (1999) Am. J. Hum. Genet. , vol.65 , pp. 593-598
    • Shih, J.C.1    Thompson, R.F.2
  • 42
    • 0030942844 scopus 로고    scopus 로고
    • The leptin receptor
    • Tartaglia, L. A. The leptin receptor. J. Biol. Chem., 272: 6093-6096, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6093-6096
    • Tartaglia, L.A.1
  • 43
    • 0026534571 scopus 로고
    • Ras is essential for nerve growth factor- and phorbol ester-induced tyrosine phosphorylation of MAP kinases
    • Thomas, S. M., DeMarco, M., D'Arcangelo, G., Halegoua, S., and Brugge, J. S. Ras is essential for nerve growth factor- and phorbol ester-induced tyrosine phosphorylation of MAP kinases. Cell, 68: 1031-1040, 1992.
    • (1992) Cell , vol.68 , pp. 1031-1040
    • Thomas, S.M.1    DeMarco, M.2    D'Arcangelo, G.3    Halegoua, S.4    Brugge, J.S.5
  • 44
    • 0032570802 scopus 로고    scopus 로고
    • Neurofilament (NF) assembly; divergent characteristics of human and rodent NF-L subunits
    • Carter, J., Gragerov, A., Konvicka, K., Elder, G., Weinstein, H., and Lazzarini, R. A. Neurofilament (NF) assembly; divergent characteristics of human and rodent NF-L subunits. J. Biol. Chem., 273: 5101-5108, 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5101-5108
    • Carter, J.1    Gragerov, A.2    Konvicka, K.3    Elder, G.4    Weinstein, H.5    Lazzarini, R.A.6
  • 45
    • 0034649781 scopus 로고    scopus 로고
    • MAP1B expression and microtubule stability in growing and regenerating axons
    • Gordon-Weeks, P. R., and Fischer, I. MAP1B expression and microtubule stability in growing and regenerating axons. Microsc. Res. Tech., 48: 63-74, 2000.
    • (2000) Microsc. Res. Tech. , vol.48 , pp. 63-74
    • Gordon-Weeks, P.R.1    Fischer, I.2
  • 46
    • 0032104055 scopus 로고    scopus 로고
    • Vesicular neurotransmitter transport and the presynaptic regulation of quantal size
    • Reimer, R. J., Fon, E. A., and Edwards, R. H. Vesicular neurotransmitter transport and the presynaptic regulation of quantal size. Curr. Opin. Neurobiol., 8: 405-412, 1998.
    • (1998) Curr. Opin. Neurobiol. , vol.8 , pp. 405-412
    • Reimer, R.J.1    Fon, E.A.2    Edwards, R.H.3
  • 47
    • 0021137263 scopus 로고
    • Porphyrin-heme biosynthesis in organotypic cultures of mouse dorsal root ganglia. Effects of heme and lead on porphyrin synthesis and peripheral myelin
    • Whetsell, W. O. J., Sassa, S., and Kappas, A. Porphyrin-heme biosynthesis in organotypic cultures of mouse dorsal root ganglia. Effects of heme and lead on porphyrin synthesis and peripheral myelin. J. Clin. Investig., 74: 600-607, 1984.
    • (1984) J. Clin. Investig. , vol.74 , pp. 600-607
    • Whetsell, W.O.J.1    Sassa, S.2    Kappas, A.3
  • 48
    • 0031017966 scopus 로고    scopus 로고
    • Transcriptional regulation of the ferritin heavy-chain gene: The activity of the CCAAT binding factor NF-Y is modulated in heme-treated Friend leukemia cells and during monocyte-to-macrophage differentiation
    • Marziali, G., Perrotti, E., Ilari, R., Testa, U., Coccia, E. M., and Battistini, A. Transcriptional regulation of the ferritin heavy-chain gene: the activity of the CCAAT binding factor NF-Y is modulated in heme-treated Friend leukemia cells and during monocyte-to-macrophage differentiation. Mol. Cell. Biol., 17: 1387-1395, 1997.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1387-1395
    • Marziali, G.1    Perrotti, E.2    Ilari, R.3    Testa, U.4    Coccia, E.M.5    Battistini, A.6
  • 49
    • 67650119996 scopus 로고    scopus 로고
    • Molecular actions of heme-regulatory proteins in eukaryotes
    • J. Fagan, N. Shimizu, and J. N. Davidson (eds.), Trivandrum, India: Research Signpost
    • Hon, T., Lee, H. C., and Zhang, L. Molecular actions of heme-regulatory proteins in eukaryotes In: J. Fagan, N. Shimizu, and J. N. Davidson (eds.), Recent Research Development in Molecular and Cellular Biology, Vol. 2, pp. 27-39, Trivandrum, India: Research Signpost, 2001.
    • (2001) Recent Research Development in Molecular and Cellular Biology , vol.2 , pp. 27-39
    • Hon, T.1    Lee, H.C.2    Zhang, L.3
  • 50
    • 0028821439 scopus 로고
    • Heme binds to a short sequence that serves a regulatory function in diverse proteins
    • Zhang, L., and Guarente, L. Heme binds to a short sequence that serves a regulatory function in diverse proteins. EMBO J., 14: 313-320, 1995.
    • (1995) EMBO J. , vol.14 , pp. 313-320
    • Zhang, L.1    Guarente, L.2
  • 51
    • 0033602364 scopus 로고    scopus 로고
    • Nerve growth factor induces survival and differentiation through two distinct signaling cascades in PC12 cells
    • Klesse, L. J., Meyers, K. A., Marshall, C. J., and Parada, L. F. Nerve growth factor induces survival and differentiation through two distinct signaling cascades in PC12 cells. Oncogene, 18: 2055-2068, 1999.
    • (1999) Oncogene , vol.18 , pp. 2055-2068
    • Klesse, L.J.1    Meyers, K.A.2    Marshall, C.J.3    Parada, L.F.4
  • 52
    • 0025267015 scopus 로고
    • The regulation and function of c-fos and other immediate early genes in the nervous system
    • Sheng, M., and Greenberg, M. E. The regulation and function of c-fos and other immediate early genes in the nervous system. Neuron, 4: 477-485, 1990.
    • (1990) Neuron , vol.4 , pp. 477-485
    • Sheng, M.1    Greenberg, M.E.2
  • 53
    • 0018427516 scopus 로고
    • Formation of cobalt protoporphyrin in the liver of rats. A mechanism for the inhibition of liver haem biosynthesis by inorganic cobalt
    • Sinclair, P., Gibbs, A. H., Sinclair, J. F., and de Matteis, F. Formation of cobalt protoporphyrin in the liver of rats. A mechanism for the inhibition of liver haem biosynthesis by inorganic cobalt. Biochem. J., 178: 529-538, 1979.
    • (1979) Biochem. J. , vol.178 , pp. 529-538
    • Sinclair, P.1    Gibbs, A.H.2    Sinclair, J.F.3    De Matteis, F.4
  • 54
    • 0032479977 scopus 로고    scopus 로고
    • Differential regulation of c-Jun by ERK and JNK during PC12 cell differentiation
    • Leppä, S., Saffrich, R., Ansorge, W., and Bohmann, D. Differential regulation of c-Jun by ERK and JNK during PC12 cell differentiation. EMBO J., 17:4404-4413, 1998.
    • (1998) EMBO J. , vol.17 , pp. 4404-4413
    • Leppä, S.1    Saffrich, R.2    Ansorge, W.3    Bohmann, D.4
  • 55
    • 0033614468 scopus 로고    scopus 로고
    • Heme initiates changes in the expression of a wide array of genes during the early erythroid differentiation stage
    • Zhu, Y., Hon, T., and Zhang, L. Heme initiates changes in the expression of a wide array of genes during the early erythroid differentiation stage. Biochem. Biophys. Res. Commun., 258: 87-93, 1999.
    • (1999) Biochem. Biophys. Res. Commun. , vol.258 , pp. 87-93
    • Zhu, Y.1    Hon, T.2    Zhang, L.3


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