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Volumn 107, Issue 5, 2008, Pages 1248-1260

A food-derived synergist of NGF signaling: Identification of protein tyrosine phosphatase 1B as a key regulator of NGF receptor-initiated signal transduction

Author keywords

Isothiocyanate; Nerve growth factor; Neuritogenesis; Protein tyrosine phosphatase; TrkA

Indexed keywords

6 METHYLSULFINYLHEXYLISOTHIOCYANATE; BRASSICA EXTRACT; ISOTHIOCYANIC ACID DERIVATIVE; MITOGEN ACTIVATED PROTEIN KINASE; NERVE GROWTH FACTOR; NERVE GROWTH FACTOR RECEPTOR; PROTEIN TYROSINE KINASE A; PROTEIN TYROSINE PHOSPHATASE 1B; SULFORAPHANE; UNCLASSIFIED DRUG;

EID: 55849150237     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2008.05686.x     Document Type: Article
Times cited : (29)

References (59)
  • 1
    • 0034671546 scopus 로고    scopus 로고
    • A cytosolic protein-tyrosine phosphatase PTP1B specifically dephosphorylates and deactivates prolactin-activated STAT5a and STAT5b
    • Aoki N. Matsuda T. (2000) A cytosolic protein-tyrosine phosphatase PTP1B specifically dephosphorylates and deactivates prolactin-activated STAT5a and STAT5b. J. Biol. Chem. 275, 39718 39726.
    • (2000) J. Biol. Chem. , vol.275 , pp. 39718-39726
    • Aoki, N.1    Matsuda, T.2
  • 2
    • 0036138705 scopus 로고    scopus 로고
    • A nuclear protein tyrosine phosphatase TC-PTP is a potential negative regulator of the PRL-mediated signaling pathway: Dephosphorylation and deactivation of signal transducer and activator of transcription 5a and 5b by TC-PTP in nucleus
    • Aoki N. Matsuda T. (2002) A nuclear protein tyrosine phosphatase TC-PTP is a potential negative regulator of the PRL-mediated signaling pathway: dephosphorylation and deactivation of signal transducer and activator of transcription 5a and 5b by TC-PTP in nucleus. Mol. Endocrinol. 16, 58 69.
    • (2002) Mol. Endocrinol. , vol.16 , pp. 58-69
    • Aoki, N.1    Matsuda, T.2
  • 3
    • 0029800248 scopus 로고    scopus 로고
    • The novel protein-tyrosine phosphatase PTP20 is a positive regulator of PC12 cell neuronal differentiation
    • Aoki N., Yamaguchi-Aoki Y. Ullrich A. (1996) The novel protein-tyrosine phosphatase PTP20 is a positive regulator of PC12 cell neuronal differentiation. J. Biol. Chem. 271, 29422 29426.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29422-29426
    • Aoki, N.1    Yamaguchi-Aoki, Y.2    Ullrich, A.3
  • 4
    • 0033549893 scopus 로고    scopus 로고
    • The selective and inducible activation of endogenous PI 3-kinase in PC12 cells results in efficient NGF-mediated survival but defective neurite outgrowth
    • Ashcroft M., Stephens R. M., Hallberg B., Downward J. Kaplan D. R. (1999) The selective and inducible activation of endogenous PI 3-kinase in PC12 cells results in efficient NGF-mediated survival but defective neurite outgrowth. Oncogene 18, 4586 4597.
    • (1999) Oncogene , vol.18 , pp. 4586-4597
    • Ashcroft, M.1    Stephens, R.M.2    Hallberg, B.3    Downward, J.4    Kaplan, D.R.5
  • 6
    • 0033521019 scopus 로고    scopus 로고
    • Roles of superoxide radical anion in signal transduction mediated by reversible regulation of protein-tyrosine phosphatase 1B
    • Barrett W. C., DeGnore J. P., Keng Y. F., Zhang Z. Y., Yim M. B. Chock P. B. (1999a) Roles of superoxide radical anion in signal transduction mediated by reversible regulation of protein-tyrosine phosphatase 1B. J. Biol. Chem. 274, 34543 34546.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34543-34546
    • Barrett, W.C.1    Degnore, J.P.2    Keng, Y.F.3    Zhang, Z.Y.4    Yim, M.B.5    Chock, P.B.6
  • 8
    • 28244495389 scopus 로고    scopus 로고
    • Natural antioxidants and neurodegenerative diseases
    • Bastianetto S. Quirion R. (2004) Natural antioxidants and neurodegenerative diseases. Front. Biosci. 9, 3447 3452.
    • (2004) Front. Biosci. , vol.9 , pp. 3447-3452
    • Bastianetto, S.1    Quirion, R.2
  • 10
    • 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
    • 0028228616 scopus 로고
    • Activation of MAP kinase kinase is necessary and sufficient for PC12 differentiation and for transformation of NIH 3T3 cells
    • Cowley S., Paterson H., Kemp P. Marshall C. J. (1994) Activation of MAP kinase kinase is necessary and sufficient for PC12 differentiation and for transformation of NIH 3T3 cells. Cell 77, 841 852.
    • (1994) Cell , vol.77 , pp. 841-852
    • Cowley, S.1    Paterson, H.2    Kemp, P.3    Marshall, C.J.4
  • 13
    • 0031791274 scopus 로고    scopus 로고
    • Identification of the oxidation states of the active site cysteine in a recombinant protein tyrosine phosphatase by electrospray mass spectrometry using on-line desalting
    • DeGnore J. P., Konig S., Barrett W. C., Chock P. B. Fales H. M. (1998) Identification of the oxidation states of the active site cysteine in a recombinant protein tyrosine phosphatase by electrospray mass spectrometry using on-line desalting. Rapid Commun. Mass Spectrom. 12, 1457 1462.
    • (1998) Rapid Commun. Mass Spectrom. , vol.12 , pp. 1457-1462
    • Degnore, J.P.1    Konig, S.2    Barrett, W.C.3    Chock, P.B.4    Fales, H.M.5
  • 14
    • 0032176512 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: Mechanisms of catalysis and regulation
    • Denu J. M. Dixon J. E. (1998) Protein tyrosine phosphatases: mechanisms of catalysis and regulation. Curr. Opin. Chem. Biol. 2, 633 641.
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 633-641
    • Denu, J.M.1    Dixon, J.E.2
  • 15
    • 0032554611 scopus 로고    scopus 로고
    • Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: Evidence for a sulfenic acid intermediate and implications for redox regulation
    • Denu J. M. Tanner K. G. (1998) Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation. Biochemistry 37, 5633 5642.
    • (1998) Biochemistry , vol.37 , pp. 5633-5642
    • Denu, J.M.1    Tanner, K.G.2
  • 16
    • 0037155862 scopus 로고    scopus 로고
    • Detection, quantitation, purification, and identification of cardiac proteins S-thiolated during ischemia and reperfusion
    • Eaton P., Byers H. L., Leeds N., Ward M. A. Shattock M. J. (2002) Detection, quantitation, purification, and identification of cardiac proteins S-thiolated during ischemia and reperfusion. J. Biol. Chem. 277, 9806 9811.
    • (2002) J. Biol. Chem. , vol.277 , pp. 9806-9811
    • Eaton, P.1    Byers, H.L.2    Leeds, N.3    Ward, M.A.4    Shattock, M.J.5
  • 17
    • 0033525870 scopus 로고    scopus 로고
    • Structure of protein tyrosine phosphatase 1B in complex with inhibitors bearing two phosphotyrosine mimetics
    • Elchebly M., Payette P., Michaliszyn E. et al. (1999) Structure of protein tyrosine phosphatase 1B in complex with inhibitors bearing two phosphotyrosine mimetics. Science 283, 1544 1548.
    • (1999) Science , vol.283 , pp. 1544-1548
    • Elchebly, M.1    Payette, P.2    Michaliszyn, E.3
  • 19
    • 0030931522 scopus 로고    scopus 로고
    • Broccoli sprouts: An exceptionally rich source of inducers of enzymes that protect against chemical carcinogens
    • Fahey J. W., Zhang Y. Talalay P. (1997) Broccoli sprouts: an exceptionally rich source of inducers of enzymes that protect against chemical carcinogens. Proc. Natl Acad. Sci. USA 94, 10367 10372.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 10367-10372
    • Fahey, J.W.1    Zhang, Y.2    Talalay, P.3
  • 20
    • 35548930637 scopus 로고    scopus 로고
    • PTPσ binds and dephosphorylates neurotrophin receptors and can suppress NGF-dependent neurite outgrowth from sensory neurons
    • Faux C., Hawadle M., Nixon J., Wallace A., Lee S., Murray S. Stoker A. (2007) PTPσ binds and dephosphorylates neurotrophin receptors and can suppress NGF-dependent neurite outgrowth from sensory neurons. Biochim. Biophys. Acta 1773, 1689 1700.
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 1689-1700
    • Faux, C.1    Hawadle, M.2    Nixon, J.3    Wallace, A.4    Lee, S.5    Murray, S.6    Stoker, A.7
  • 21
    • 0028791689 scopus 로고
    • Delayed treatment with intravenous basic fibroblast growth factor reduces infarct size following permanent focal cerebral ischemia in rats
    • Fisher M., Meadows M. E., Do T., Weise J., Trubetskoy V., Charette M. Finklestein S. P. (1995) Delayed treatment with intravenous basic fibroblast growth factor reduces infarct size following permanent focal cerebral ischemia in rats. J. Cereb. Blood Flow Metab. 15, 953 959.
    • (1995) J. Cereb. Blood Flow Metab. , vol.15 , pp. 953-959
    • Fisher, M.1    Meadows, M.E.2    Do, T.3    Weise, J.4    Trubetskoy, V.5    Charette, M.6    Finklestein, S.P.7
  • 23
    • 0035502381 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase 1B (PTP1B): A novel therapeutic target for type 2 diabetes mellitus, obesity and related states of insulin resistance
    • Goldstein B. J. (2001) Protein-tyrosine phosphatase 1B (PTP1B): a novel therapeutic target for type 2 diabetes mellitus, obesity and related states of insulin resistance. Curr. Drug. Targets Immune Endocr. Metabol. Disord. 1, 265 275.
    • (2001) Curr. Drug. Targets Immune Endocr. Metabol. Disord. , vol.1 , pp. 265-275
    • Goldstein, B.J.1
  • 24
    • 0345704610 scopus 로고
    • Establishment of a noradrenergic clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor
    • Greene L. A. Tischler A. S. (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
  • 26
    • 36349037272 scopus 로고    scopus 로고
    • Chemical knockdown of protein-tyrosine phosphatase 1B by 1,2-naphthoquinone through covalent modification causes persistent transactivation of epidermal growth factor receptor
    • Iwamoto N., Sumi D., Ishii T., Uchida K., Cho A. K., Froines J. R. Kumagai Y. (2007) Chemical knockdown of protein-tyrosine phosphatase 1B by 1,2-naphthoquinone through covalent modification causes persistent transactivation of epidermal growth factor receptor. J. Biol. Chem. 282, 33396 33404.
    • (2007) J. Biol. Chem. , vol.282 , pp. 33396-33404
    • Iwamoto, N.1    Sumi, D.2    Ishii, T.3    Uchida, K.4    Cho, A.K.5    Froines, J.R.6    Kumagai, Y.7
  • 27
    • 11144278530 scopus 로고    scopus 로고
    • Redox regulation of nerve growth factor-induced neuronal differentiation of PC12 cells through modulation of the nerve growth factor receptor, TrkA
    • Kamata H., Oka S., Shibukawa Y., Kakuta J. Hirata H. (2005) Redox regulation of nerve growth factor-induced neuronal differentiation of PC12 cells through modulation of the nerve growth factor receptor, TrkA. Arch. Biochem. Biophys. 434, 16 25.
    • (2005) Arch. Biochem. Biophys. , vol.434 , pp. 16-25
    • Kamata, H.1    Oka, S.2    Shibukawa, Y.3    Kakuta, J.4    Hirata, H.5
  • 28
    • 0025735392 scopus 로고
    • The trk proto-oncogene product: A signal transducing receptor for nerve growth factor
    • Kaplan D. R., Hempstead B. L., Martin-Zanca D., Chao M. V. Parada L. F. (1991a) The trk proto-oncogene product: a signal transducing receptor for nerve growth factor. Science 252, 554 558.
    • (1991) Science , vol.252 , pp. 554-558
    • Kaplan, D.R.1    Hempstead, B.L.2    Martin-Zanca, D.3    Chao, M.V.4    Parada, L.F.5
  • 29
    • 0025797396 scopus 로고
    • Tyrosine phosphorylation and tyrosine kinase activity of the trk proto-oncogene product induced by NGF
    • Kaplan D. R., Martin-Zanca D. Parada L. F. (1991b) Tyrosine phosphorylation and tyrosine kinase activity of the trk proto-oncogene product induced by NGF. Nature 350, 158 160.
    • (1991) Nature , vol.350 , pp. 158-160
    • Kaplan, D.R.1    Martin-Zanca, D.2    Parada, L.F.3
  • 30
    • 0033942614 scopus 로고    scopus 로고
    • Increased energy expenditure, decreased adiposity, and tissue-specific insulin sensitivity in protein-tyrosine phosphatase 1B-deficient mice
    • Klaman L. D., Boss O., Peroni O. D. et al. (2000) Increased energy expenditure, decreased adiposity, and tissue-specific insulin sensitivity in protein-tyrosine phosphatase 1B-deficient mice. Mol. Cell. Biol. 20, 5479 5489.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5479-5489
    • Klaman, L.D.1    Boss, O.2    Peroni, O.D.3
  • 31
    • 0023067115 scopus 로고
    • Nerve growth factor treatment after brain injury prevents neuronal death
    • Kromer L. F. (1987) Nerve growth factor treatment after brain injury prevents neuronal death. Science 235, 214 216.
    • (1987) Science , vol.235 , pp. 214-216
    • Kromer, L.F.1
  • 32
    • 0642316039 scopus 로고    scopus 로고
    • Nerve growth factor: Structure, function and therapeutic implications for Alzheimer's disease
    • Lad S. P., Neet K. E. Mufson E. J. (2003) Nerve growth factor: structure, function and therapeutic implications for Alzheimer's disease. Curr. Drug Target CNS Neurol. Disord. 2, 315 334.
    • (2003) Curr. Drug Target CNS Neurol. Disord. , vol.2 , pp. 315-334
    • Lad, S.P.1    Neet, K.E.2    Mufson, E.J.3
  • 33
    • 0032546955 scopus 로고    scopus 로고
    • Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor
    • Lee S. R., Kwon K. S., Kim S. R. Rhee S. G. (1998) Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor. J. Biol. Chem. 273, 15366 15372.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15366-15372
    • Lee, S.R.1    Kwon, K.S.2    Kim, S.R.3    Rhee, S.G.4
  • 34
    • 0023236055 scopus 로고
    • The nerve growth factor 35 years later
    • Levi-Montalcini R. (1987) The nerve growth factor 35 years later. Science 237, 1154 1162.
    • (1987) Science , vol.237 , pp. 1154-1162
    • Levi-Montalcini, R.1
  • 36
    • 0035877633 scopus 로고    scopus 로고
    • Insulin-stimulated hydrogen peroxide reversibly inhibits protein-tyrosine phosphatase 1b in vivo and enhances the early insulin action cascade
    • Mahadev K., Zilbering A., Zhu L. Goldstein B. J. (2001) Insulin-stimulated hydrogen peroxide reversibly inhibits protein-tyrosine phosphatase 1b in vivo and enhances the early insulin action cascade. J. Biol. Chem. 276, 21938 21942.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21938-21942
    • Mahadev, K.1    Zilbering, A.2    Zhu, L.3    Goldstein, B.J.4
  • 37
    • 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
  • 38
    • 33750159449 scopus 로고    scopus 로고
    • Neurohormetic phytochemicals: Low-dose toxins that induce adaptive neuronal stress responses
    • Mattson M. P. Cheng A. (2006) Neurohormetic phytochemicals: low-dose toxins that induce adaptive neuronal stress responses. Trends Neurosci. 29, 632 639.
    • (2006) Trends Neurosci. , vol.29 , pp. 632-639
    • Mattson, M.P.1    Cheng, A.2
  • 39
    • 0036184190 scopus 로고    scopus 로고
    • Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo
    • Meng T. C., Fukada T. Tonks N. K. (2002) Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo. Mol. Cell 9, 387 399.
    • (2002) Mol. Cell , vol.9 , pp. 387-399
    • Meng, T.C.1    Fukada, T.2    Tonks, N.K.3
  • 40
    • 0038749600 scopus 로고    scopus 로고
    • Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B
    • van Montfort R. L. M., Congreve M., Tisi D., Carr R. Jhoti H. (2003) Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B. Nature 423, 773 777.
    • (2003) Nature , vol.423 , pp. 773-777
    • Van Montfort, R.L.M.1    Congreve, M.2    Tisi, D.3    Carr, R.4    Jhoti, H.5
  • 41
    • 0036479330 scopus 로고    scopus 로고
    • A sulforaphane analogue that potently activates the Nrf2-dependent detoxification pathway
    • Morimitsu Y., Nakagawa Y., Hayashi K. et al. (2002) A sulforaphane analogue that potently activates the Nrf2-dependent detoxification pathway. J. Biol. Chem. 277, 3456 3463.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3456-3463
    • Morimitsu, Y.1    Nakagawa, Y.2    Hayashi, K.3
  • 42
    • 0030953448 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases in signal transduction
    • Neel B. G. Tonks N. K. (1997) Protein tyrosine phosphatases in signal transduction. Curr. Opin. Cell Biol. 9, 193 204.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 193-204
    • Neel, B.G.1    Tonks, N.K.2
  • 43
    • 0027410497 scopus 로고
    • The MAP kinase cascade is essential for diverse signal transduction pathways
    • Nishida E. Gotoh Y. (1993) The MAP kinase cascade is essential for diverse signal transduction pathways. Trends Biochem. Sci. 18, 128 131.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 128-131
    • Nishida, E.1    Gotoh, Y.2
  • 44
    • 0028293929 scopus 로고
    • Neuronal differentiation signals are controlled by nerve growth factor receptor/Trk binding sites for SHC and PLC gamma
    • Obermeier A., Bradshaw R. A., Seedorf K., Choidas A., Schlessinger J. Ullrich A. (1994) Neuronal differentiation signals are controlled by nerve growth factor receptor/Trk binding sites for SHC and PLC gamma. EMBO J. 13, 1585 1590.
    • (1994) EMBO J. , vol.13 , pp. 1585-1590
    • Obermeier, A.1    Bradshaw, R.A.2    Seedorf, K.3    Choidas, A.4    Schlessinger, J.5    Ullrich, A.6
  • 45
    • 0029034774 scopus 로고
    • Inhibition of MAP kinase kinase blocks the differentiation of PC-12 cells induced by nerve growth factor
    • Pang L., Sawada T., Decker S. J. Saltiel A. R. (1995) Inhibition of MAP kinase kinase blocks the differentiation of PC-12 cells induced by nerve growth factor. J. Biol. Chem. 270, 13585 13588.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13585-13588
    • Pang, L.1    Sawada, T.2    Decker, S.J.3    Saltiel, A.R.4
  • 46
    • 0033057286 scopus 로고    scopus 로고
    • The staurosporine-like compound L-753,000 (NB-506) potentiates the neurotrophic effects of neurotrophin-3 by acting selectively at the TrkA receptor
    • Pollack S., Young L., Bilsland J., Wilkie N., Ellis S., Hefti F., Broughton H. Harper S. (1999) The staurosporine-like compound L-753,000 (NB-506) potentiates the neurotrophic effects of neurotrophin-3 by acting selectively at the TrkA receptor. Mol. Pharmacol. 56, 185 195.
    • (1999) Mol. Pharmacol. , vol.56 , pp. 185-195
    • Pollack, S.1    Young, L.2    Bilsland, J.3    Wilkie, N.4    Ellis, S.5    Hefti, F.6    Broughton, H.7    Harper, S.8
  • 47
    • 0026733002 scopus 로고
    • PC12 cell neuronal differentiation is associated with prolonged p21ras activity and consequent prolonged ERK activity
    • Qui M. S. Green S. H. (1992) PC12 cell neuronal differentiation is associated with prolonged p21ras 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
  • 49
    • 0026678172 scopus 로고
    • Association of the Shc and Grb2/Sem5 SH2-containing proteins is implicated in activation of the Ras pathway by tyrosine kinases
    • Rozakis-Adcock M., McGlade J., Mbamalu G. et al. (1992) Association of the Shc and Grb2/Sem5 SH2-containing proteins is implicated in activation of the Ras pathway by tyrosine kinases. Nature 360, 689 692.
    • (1992) Nature , vol.360 , pp. 689-692
    • Rozakis-Adcock, M.1    McGlade, J.2    Mbamalu, G.3
  • 50
    • 0030951213 scopus 로고    scopus 로고
    • Intraventricular brain-derived neurotrophic factor reduces infarct size after focal cerebral ischemia in rats
    • Schabitz W. R., Schwab S., Spranger M. Hacke W. (1997) Intraventricular brain-derived neurotrophic factor reduces infarct size after focal cerebral ischemia in rats. J. Cereb. Blood Flow Metab. 17, 500 506.
    • (1997) J. Cereb. Blood Flow Metab. , vol.17 , pp. 500-506
    • Schabitz, W.R.1    Schwab, S.2    Spranger, M.3    Hacke, W.4
  • 52
    • 0034607872 scopus 로고    scopus 로고
    • Nerve growth factor-induced neuronal differentiation requires generation of Rac1-regulated reactive oxygen species
    • Suzukawa K., Miura K., Mitsushita J., Resau J., Hirose K., Crystal R. Kamata T. (2000) Nerve growth factor-induced neuronal differentiation requires generation of Rac1-regulated reactive oxygen species. J. Biol. Chem. 275, 13175 13178.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13175-13178
    • Suzukawa, K.1    Miura, K.2    Mitsushita, J.3    Resau, J.4    Hirose, K.5    Crystal, R.6    Kamata, T.7
  • 53
    • 0035170990 scopus 로고    scopus 로고
    • Phytochemicals from cruciferous plants protect against cancer by modulating carcinogen metabolism
    • Talalay P. Fahey J. W. (2001) Phytochemicals from cruciferous plants protect against cancer by modulating carcinogen metabolism. J. Nutr. 131, 3027S 3033S.
    • (2001) J. Nutr. , vol.131
    • Talalay, P.1    Fahey, J.W.2
  • 54
    • 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. Brugge J. S. (1992) Ras is essential for nerve growth factor- and phorbol ester-induced tyrosine phosphorylation of MAP kinases. Cell 68, 1031 1040.
    • (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
  • 55
    • 0026486878 scopus 로고
    • Sustained activation of the mitogen-activated protein (MAP) kinase cascade may be required for differentiation of PC12 cells. Comparison of the effects of nerve growth factor and epidermal growth factor
    • Traverse S., Gomez N., Paterson H., Marshall C. Cohen P. (1992) Sustained activation of the mitogen-activated protein (MAP) kinase cascade may be required for differentiation of PC12 cells. Comparison of the effects of nerve growth factor and epidermal growth factor. Biochem. J. 288, 351 355.
    • (1992) Biochem. J. , vol.288 , pp. 351-355
    • Traverse, S.1    Gomez, N.2    Paterson, H.3    Marshall, C.4    Cohen, P.5
  • 56
    • 0035793027 scopus 로고    scopus 로고
    • Nerve growth factor and glial cell line-derived neurotrophic factor restore the cholinergic neuronal phenotype in organotypic brain slices of the basal nucleus of Meynert
    • Weis C., Marksteiner J. Humpel C. (2001) Nerve growth factor and glial cell line-derived neurotrophic factor restore the cholinergic neuronal phenotype in organotypic brain slices of the basal nucleus of Meynert. Neuroscience 102, 129 138.
    • (2001) Neuroscience , vol.102 , pp. 129-138
    • Weis, C.1    Marksteiner, J.2    Humpel, C.3
  • 57
    • 0026523559 scopus 로고
    • Ras mediates nerve growth factor receptor modulation of three signal-transducing protein kinases: MAP kinase, Raf-1, and RSK
    • Wood K. W., Sarnecki C., Roberts T. M. Blenis J. (1992) Ras mediates nerve growth factor receptor modulation of three signal-transducing protein kinases: MAP kinase, Raf-1, and RSK. Cell 68, 1041 1050.
    • (1992) Cell , vol.68 , pp. 1041-1050
    • Wood, K.W.1    Sarnecki, C.2    Roberts, T.M.3    Blenis, J.4
  • 58
    • 0028326168 scopus 로고
    • Anticarcinogenic activities of organic isothiocyanates: Chemistry and mechanisms
    • Zhang Y. Talalay P. (1994) Anticarcinogenic activities of organic isothiocyanates: chemistry and mechanisms. Cancer Res. 54, 1976s 1981s.
    • (1994) Cancer Res. , vol.54
    • Zhang, Y.1    Talalay, P.2
  • 59
    • 0026577605 scopus 로고
    • A major inducer of anticarcinogenic protective enzymes from broccoli: Isolation and elucidation of structure
    • Zhang Y., Talalay P., Cho C. G. Posner G. H. (1992) A major inducer of anticarcinogenic protective enzymes from broccoli: isolation and elucidation of structure. Proc. Natl Acad. Sci. USA 89, 2399 2403.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 2399-2403
    • Zhang, Y.1    Talalay, P.2    Cho, C.G.3    Posner, G.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.