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Volumn 292, Issue 5, 2007, Pages

Mitochondrial nitric oxide in the signaling of cell integrated responses

Author keywords

Hydrogen peroxide; Mitochondrial nitric oxide synthase; Mitogen activated protein kinase; Peroxynitrite

Indexed keywords

CYTOCHROME C OXIDASE; HYDROGEN PEROXIDE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE P38; NITRIC OXIDE; OXYGEN; SUPEROXIDE DISMUTASE; MITOGEN ACTIVATED PROTEIN KINASE; NITRIC OXIDE SYNTHASE; PEROXYNITROUS ACID; REACTIVE OXYGEN METABOLITE;

EID: 34250635065     PISSN: 03636143     EISSN: 15221563     Source Type: Journal    
DOI: 10.1152/ajpcell.00248.2006     Document Type: Review
Times cited : (115)

References (146)
  • 3
  • 4
    • 0035341719 scopus 로고    scopus 로고
    • 2 induce apoptosis through Fenton chemistry independent of the cellular thiol state
    • 2 induce apoptosis through Fenton chemistry independent of the cellular thiol state. Free Radic Biol Med 30: 1008-1018, 2001.
    • (2001) Free Radic Biol Med , vol.30 , pp. 1008-1018
    • Antunes, F.1    Cadenas, E.2
  • 5
    • 10044230387 scopus 로고    scopus 로고
    • On the mechanism and biology of cytochrome oxidase inhibition by nitric oxide
    • Antunes F, Boveris A, Cadenas E. On the mechanism and biology of cytochrome oxidase inhibition by nitric oxide. Proc Natl Acad Sci USA 101: 16774-16779, 2004.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 16774-16779
    • Antunes, F.1    Boveris, A.2    Cadenas, E.3
  • 6
    • 0008824942 scopus 로고    scopus 로고
    • The domains of death: Evolution of the apoptosis machinery
    • Aravind L, Dixit VM, Koonin EV. The domains of death: evolution of the apoptosis machinery. Trends Biochem Sci 24: 47-53, 1999.
    • (1999) Trends Biochem Sci , vol.24 , pp. 47-53
    • Aravind, L.1    Dixit, V.M.2    Koonin, E.V.3
  • 8
    • 0033922278 scopus 로고    scopus 로고
    • Cell cycle control during liver development in the rat: Evidence indicating a role for cyclin D1 posttranscriptional regulation
    • Awad MM, Grappuso PA. Cell cycle control during liver development in the rat: evidence indicating a role for cyclin D1 posttranscriptional regulation. Cell Growth Differ 11: 325-334, 2000.
    • (2000) Cell Growth Differ , vol.11 , pp. 325-334
    • Awad, M.M.1    Grappuso, P.A.2
  • 10
    • 0033521019 scopus 로고    scopus 로고
    • Roles of superoxide radical anion in signal transduction mediated by reversible regulation of protein-tyrosine phosphatase 1B
    • Barrett WC, DeGnore P, Keng YF, Zhang ZY, Yim MB, Chock PB. Roles of superoxide radical anion in signal transduction mediated by reversible regulation of protein-tyrosine phosphatase 1B. J Biol Chem 274: 34543-34546, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 34543-34546
    • Barrett, W.C.1    DeGnore, P.2    Keng, Y.F.3    Zhang, Z.Y.4    Yim, M.B.5    Chock, P.B.6
  • 11
    • 0034483987 scopus 로고    scopus 로고
    • Reactive oxygen and nitrogen species: Efficient, selective, and interactive signals during intercellular induction of apoptosis
    • Bauer G. Reactive oxygen and nitrogen species: efficient, selective, and interactive signals during intercellular induction of apoptosis. Anticancer Res 20: 4115-4139, 2000.
    • (2000) Anticancer Res , vol.20 , pp. 4115-4139
    • Bauer, G.1
  • 15
    • 0029153913 scopus 로고
    • Apoptosis and necrosis: Two distinct events induced, respectively, by mild and intense insults with N-methyl-D-aspartate or nitric oxide/superoxide in cortical cell cultures
    • Bonfoco E, Krainc D, Ankarcrona M, Nicotera P, Lipton SA. Apoptosis and necrosis: two distinct events induced, respectively, by mild and intense insults with N-methyl-D-aspartate or nitric oxide/superoxide in cortical cell cultures. Proc Natl Acad Sci USA 92: 7162-7166, 1995.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7162-7166
    • Bonfoco, E.1    Krainc, D.2    Ankarcrona, M.3    Nicotera, P.4    Lipton, S.A.5
  • 16
    • 0029963244 scopus 로고    scopus 로고
    • Rapid reduction of nitric oxide by mitochondria, and reversible inhibition of mitochondrial respiration by nitric oxide
    • Borutaite V, Brown GC. Rapid reduction of nitric oxide by mitochondria, and reversible inhibition of mitochondrial respiration by nitric oxide. Biochem J 315: 295-299, 1996.
    • (1996) Biochem J , vol.315 , pp. 295-299
    • Borutaite, V.1    Brown, G.C.2
  • 17
    • 0002889135 scopus 로고    scopus 로고
    • Cellular sources and steady state of reactive oxygen species
    • edited by Biadasz Clerch L and Massaro DJ. New York: Marcell Dekker
    • Boveris A, Cadenas E. Cellular sources and steady state of reactive oxygen species. In: Oxygen, Gene Expression and Cellular Function, edited by Biadasz Clerch L and Massaro DJ. New York: Marcell Dekker, 1997, p. 3-27.
    • (1997) Oxygen, Gene Expression and Cellular Function , pp. 3-27
    • Boveris, A.1    Cadenas, E.2
  • 18
    • 0002767020 scopus 로고    scopus 로고
    • Regulation of oxygen uptake by nitric oxide
    • edited by Ignarro L. San Diego, CA: Academic
    • Boveris A, Poderoso JJ. Regulation of oxygen uptake by nitric oxide. In Nitric Oxide. Biology and Pathobiology, edited by Ignarro L. San Diego, CA: Academic, 2000, p. 355-368.
    • (2000) In Nitric Oxide. Biology and Pathobiology , pp. 355-368
    • Boveris, A.1    Poderoso, J.J.2
  • 19
    • 0031740358 scopus 로고    scopus 로고
    • Regulation of mitochondrial respiration by adenosine phosphate, oxygen, and nitric oxide
    • Boveris A, Costa L, Cadenas E, Poderoso JJ. Regulation of mitochondrial respiration by adenosine phosphate, oxygen, and nitric oxide. Methods Enzymol 301: 188-198, 1999.
    • (1999) Methods Enzymol , vol.301 , pp. 188-198
    • Boveris, A.1    Costa, L.2    Cadenas, E.3    Poderoso, J.J.4
  • 21
    • 0344827270 scopus 로고    scopus 로고
    • Enalapril increases mitochondrial nitric oxide synthase activity in heart and liver
    • Boveris A, D'Amico G, Lores-Arnaiz S, Costa LE. Enalapril increases mitochondrial nitric oxide synthase activity in heart and liver. Antioxid Redox Signal 5: 691-697, 2003.
    • (2003) Antioxid Redox Signal , vol.5 , pp. 691-697
    • Boveris, A.1    D'Amico, G.2    Lores-Arnaiz, S.3    Costa, L.E.4
  • 22
    • 0015363173 scopus 로고
    • The cellular production of hydrogen peroxide
    • Boveris A, Oshino N, Chance B. The cellular production of hydrogen peroxide. Biochem J 128: 617-630, 1972.
    • (1972) Biochem J , vol.128 , pp. 617-630
    • Boveris, A.1    Oshino, N.2    Chance, B.3
  • 24
    • 0028134892 scopus 로고
    • Nanomolar concentrations of nitric oxide reversibly inhibit synaptosomal respiration by competing with oxygen at cytochrome oxidase
    • Brown GC, Cooper CE. Nanomolar concentrations of nitric oxide reversibly inhibit synaptosomal respiration by competing with oxygen at cytochrome oxidase. FEBS Lett 356: 295-298, 1994.
    • (1994) FEBS Lett , vol.356 , pp. 295-298
    • Brown, G.C.1    Cooper, C.E.2
  • 25
    • 0029161636 scopus 로고
    • Nitric oxide regulates mitochondrial respiration and cell functions by inhibiting cytochrome oxidase
    • Brown GC. Nitric oxide regulates mitochondrial respiration and cell functions by inhibiting cytochrome oxidase. FEBS Lett 369: 136-9, 1995.
    • (1995) FEBS Lett , vol.369 , pp. 136-139
    • Brown, G.C.1
  • 26
    • 14444268768 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis. Insights from genetics
    • Brown RH Jr. Amyotrophic lateral sclerosis. Insights from genetics. Arch Neurol 54: 1246-1250, 1997.
    • (1997) Arch Neurol , vol.54 , pp. 1246-1250
    • Brown Jr., R.H.1
  • 27
    • 0018264539 scopus 로고
    • Peroxide removal by selenium-dependent and selenium-independent gluthatione peroxidases in hemoglobin-free perfused rat liver
    • Burk RF, Nishiki K, Lawrence RA, Chance B. Peroxide removal by selenium-dependent and selenium-independent gluthatione peroxidases in hemoglobin-free perfused rat liver. J Biol Chem 253: 43-46, 1978.
    • (1978) J Biol Chem , vol.253 , pp. 43-46
    • Burk, R.F.1    Nishiki, K.2    Lawrence, R.A.3    Chance, B.4
  • 29
    • 0034655602 scopus 로고    scopus 로고
    • Nitric oxide production and mitochondrial dysfunction during rat thymocyte apoptosis
    • Bustamante J, Bersier G, Romero M, Badin RA, Boveris A. Nitric oxide production and mitochondrial dysfunction during rat thymocyte apoptosis. Arch Biochem Biophys 376: 239-47, 2000.
    • (2000) Arch Biochem Biophys , vol.376 , pp. 239-247
    • Bustamante, J.1    Bersier, G.2    Romero, M.3    Badin, R.A.4    Boveris, A.5
  • 30
    • 0034467521 scopus 로고    scopus 로고
    • Analysis of the pathways of nitric oxide utilization in mitochondria
    • Cadenas E, Poderoso JJ, Antunes F, Boveris A. Analysis of the pathways of nitric oxide utilization in mitochondria. Free Radic Res 33: 747-756, 2000.
    • (2000) Free Radic Res , vol.33 , pp. 747-756
    • Cadenas, E.1    Poderoso, J.J.2    Antunes, F.3    Boveris, A.4
  • 31
    • 0036478928 scopus 로고    scopus 로고
    • The Apaf-1 apoptosome: A large caspase-activating complex
    • Cain K, Bratton SB, Cohen GM. The Apaf-1 apoptosome: a large caspase-activating complex. Biochimie 84: 203-214, 2002.
    • (2002) Biochimie , vol.84 , pp. 203-214
    • Cain, K.1    Bratton, S.B.2    Cohen, G.M.3
  • 35
    • 0029843160 scopus 로고    scopus 로고
    • Measurements of nitric oxide and hydrogen peroxide production from human neutrophils
    • Carreras MC, Poderoso JJ, Cadenas E, Boveris A. Measurements of nitric oxide and hydrogen peroxide production from human neutrophils. Methods Enzymol 269: 65-75, 1996.
    • (1996) Methods Enzymol , vol.269 , pp. 65-75
    • Carreras, M.C.1    Poderoso, J.J.2    Cadenas, E.3    Boveris, A.4
  • 36
    • 1642422748 scopus 로고    scopus 로고
    • Nitric oxide, complex I, and the modulation of mitochondrial reactive species in biology and disease
    • Carreras MC, Franco MC, Peralta JG, Poderoso JJ. Nitric oxide, complex I, and the modulation of mitochondrial reactive species in biology and disease. Mol Aspects Med 25: 125-139, 2004.
    • (2004) Mol Aspects Med , vol.25 , pp. 125-139
    • Carreras, M.C.1    Franco, M.C.2    Peralta, J.G.3    Poderoso, J.J.4
  • 38
    • 0029998238 scopus 로고    scopus 로고
    • Differential inhibitory action of nitric oxide and peroxynitrite on mitochondrial electron transport
    • Cassina A, Radi R. Differential inhibitory action of nitric oxide and peroxynitrite on mitochondrial electron transport. Arch Biochem Biophys 328: 309-316, 1996.
    • (1996) Arch Biochem Biophys , vol.328 , pp. 309-316
    • Cassina, A.1    Radi, R.2
  • 39
    • 33645560710 scopus 로고    scopus 로고
    • Mitochondrial cytochrome oxidase produces nitric oxide under hypoxic conditions: Implications for oxygen sensing and hypoxic signaling in eukaryotes
    • Castello PR, David PS, McClure T, Crook Z, Poyton RO. Mitochondrial cytochrome oxidase produces nitric oxide under hypoxic conditions: implications for oxygen sensing and hypoxic signaling in eukaryotes. Cell Metab 3: 277-287, 2006.
    • (2006) Cell Metab , vol.3 , pp. 277-287
    • Castello, P.R.1    David, P.S.2    McClure, T.3    Crook, Z.4    Poyton, R.O.5
  • 40
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • Chance B, Sies H, Boveris A. Hydroperoxide metabolism in mammalian organs. Physiol Rev 59: 527-605, 1979.
    • (1979) Physiol Rev , vol.59 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 41
    • 0035282334 scopus 로고    scopus 로고
    • Mammalian MAP kinase signaling cascades
    • Chang L, Karin M. Mammalian MAP kinase signaling cascades. Nature 410: 37-40, 2001.
    • (2001) Nature , vol.410 , pp. 37-40
    • Chang, L.1    Karin, M.2
  • 42
    • 0032900439 scopus 로고    scopus 로고
    • New insights into the role of nuclear factor-κB, a ubiquitous transcription factor in the initiation of diseases
    • Chen F, Castranova V, Shi X, Demers LM. New insights into the role of nuclear factor-κB, a ubiquitous transcription factor in the initiation of diseases. Clin Chem 45: 7-17, 1999.
    • (1999) Clin Chem , vol.45 , pp. 7-17
    • Chen, F.1    Castranova, V.2    Shi, X.3    Demers, L.M.4
  • 44
    • 0037063110 scopus 로고    scopus 로고
    • The reciprocal dance between cancer and development
    • Chodosh LA. The reciprocal dance between cancer and development. N Engl J Med 347: 134-136, 2002.
    • (2002) N Engl J Med , vol.347 , pp. 134-136
    • Chodosh, L.A.1
  • 45
    • 0030734267 scopus 로고    scopus 로고
    • Nitric oxide in excitable tissues: Physiological roles and disease
    • Christopherson KS, Bredt D. Nitric oxide in excitable tissues: physiological roles and disease. J Clin Invest 100: 2424-2429, 1997.
    • (1997) J Clin Invest , vol.100 , pp. 2424-2429
    • Christopherson, K.S.1    Bredt, D.2
  • 48
    • 28044464985 scopus 로고
    • Reversible inhibition of cytochrome c oxidase, the terminal enzyme of the mitochondrial respiratory chain, by nitric oxide
    • Cleeter MWJ, Cooper JM, Darley-Usmar VM, Moncada S, Schapira AHV. Reversible inhibition of cytochrome c oxidase, the terminal enzyme of the mitochondrial respiratory chain, by nitric oxide. FEBS Lett 345: 50-54, 1994.
    • (1994) FEBS Lett , vol.345 , pp. 50-54
    • Cleeter, M.W.J.1    Cooper, J.M.2    Darley-Usmar, V.M.3    Moncada, S.4    Schapira, A.H.V.5
  • 49
    • 0032560572 scopus 로고    scopus 로고
    • Persistent inhibition of cell respiration by nitric oxide: Cruxial role of s-nitrosylation of mitochondrial complex I and protective action of glutathione
    • Clementi E, Brown GC, Feelish M, Moncada S. Persistent inhibition of cell respiration by nitric oxide: cruxial role of s-nitrosylation of mitochondrial complex I and protective action of glutathione. Proc Natl Acad Sci USA 95: 7631-7636, 1998.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 7631-7636
    • Clementi, E.1    Brown, G.C.2    Feelish, M.3    Moncada, S.4
  • 50
    • 0030768150 scopus 로고    scopus 로고
    • Oxygen dependence of mitochondrial function measured by high-resolution respirometry in long-term hypoxic rats
    • Costa LE, Mendez G, Boveris A. Oxygen dependence of mitochondrial function measured by high-resolution respirometry in long-term hypoxic rats. Am J Physiol Cell Physiol 273: C852-C858, 1997.
    • (1997) Am J Physiol Cell Physiol , vol.273
    • Costa, L.E.1    Mendez, G.2    Boveris, A.3
  • 51
    • 0030579089 scopus 로고    scopus 로고
    • Nitric oxide inhibits DNA synthesis and induces activation of poly(ADP-ribose) polymerase in cultured rat hepatocytes
    • Dalmau M, Joaquin M, Nakamura T, Bartrons R, Gil J. Nitric oxide inhibits DNA synthesis and induces activation of poly(ADP-ribose) polymerase in cultured rat hepatocytes. Exp Cell Res 228: 14-18, 1996.
    • (1996) Exp Cell Res , vol.228 , pp. 14-18
    • Dalmau, M.1    Joaquin, M.2    Nakamura, T.3    Bartrons, R.4    Gil, J.5
  • 52
    • 0032694302 scopus 로고    scopus 로고
    • The broad spectrum of responses to oxidants in proliferating cells: A new paradigm for oxidative stress
    • Davies KJ. The broad spectrum of responses to oxidants in proliferating cells: a new paradigm for oxidative stress. IUBMB Life 48: 41-47, 2000.
    • (2000) IUBMB Life , vol.48 , pp. 41-47
    • Davies, K.J.1
  • 53
    • 0033802982 scopus 로고    scopus 로고
    • Nitric oxide-dependent activation of p53 suppresses bleomycin-induced apoptosis in the lung
    • Davis DW, Weidner DA, Holian A, McConkey DJ. Nitric oxide-dependent activation of p53 suppresses bleomycin-induced apoptosis in the lung. J Exp Med 192: 857-869, 2000.
    • (2000) J Exp Med , vol.192 , pp. 857-869
    • Davis, D.W.1    Weidner, D.A.2    Holian, A.3    McConkey, D.J.4
  • 54
    • 4844226180 scopus 로고    scopus 로고
    • Ubiquitination and degradation of neuronal nitric oxide synthase in vitro: Dimer stabilization protects the enzyme proteolysis
    • Dumbar AY, Kamada Y, Jenkins GJ, Lowe ER, Billecke SS, Osawa Y. Ubiquitination and degradation of neuronal nitric oxide synthase in vitro: dimer stabilization protects the enzyme proteolysis. Mol Pharmacol 66: 964-969, 2004.
    • (2004) Mol Pharmacol , vol.66 , pp. 964-969
    • Dumbar, A.Y.1    Kamada, Y.2    Jenkins, G.J.3    Lowe, E.R.4    Billecke, S.S.5    Osawa, Y.6
  • 55
    • 0032842491 scopus 로고    scopus 로고
    • Induction of apoptosis and caspase activation in cell obtained from familial haemophagocytic lymphohistiocytosis patients
    • Fadeel B, Orrenius S, Henter JI. Induction of apoptosis and caspase activation in cell obtained from familial haemophagocytic lymphohistiocytosis patients. Br J Haematol 106: 406-415, 1999.
    • (1999) Br J Haematol , vol.106 , pp. 406-415
    • Fadeel, B.1    Orrenius, S.2    Henter, J.I.3
  • 56
    • 0015842752 scopus 로고
    • Superoxide dismutase: A comparison of rate constants
    • Forman HJ, Fridovich I. Superoxide dismutase: a comparison of rate constants. Arch Biochem Biophys 150: 396-400, 1973.
    • (1973) Arch Biochem Biophys , vol.150 , pp. 396-400
    • Forman, H.J.1    Fridovich, I.2
  • 58
    • 0141988685 scopus 로고    scopus 로고
    • Bal de Kier Joffé E, Carreras MC, Poderoso JJ. Decreased mitochondrial nitric oxide synthase activity and hydrogen peroxide relate persistent tumoral proliferation to embryonic behavior
    • Galli S, Labato MI, Bal de Kier Joffé E, Carreras MC, Poderoso JJ. Decreased mitochondrial nitric oxide synthase activity and hydrogen peroxide relate persistent tumoral proliferation to embryonic behavior. Cancer Res 63: 6370-6377, 2003.
    • (2003) Cancer Res , vol.63 , pp. 6370-6377
    • Galli, S.1    Labato, M.I.2
  • 59
    • 0000367869 scopus 로고    scopus 로고
    • Molecular regulation of inducible nitric oxide synthase
    • edited by Ignarro L. San Diego, CA: Academic
    • Ganster R, Geller D. Molecular regulation of inducible nitric oxide synthase. In: Nitric Oxide. Biology and Pathobiology, edited by Ignarro L. San Diego, CA: Academic, 2000, 129-156.
    • (2000) Nitric Oxide. Biology and Pathobiology , pp. 129-156
    • Ganster, R.1    Geller, D.2
  • 60
    • 0030697859 scopus 로고    scopus 로고
    • Nitric oxide synthase activity in mitochondria
    • Ghafourifar P, Richter C. Nitric oxide synthase activity in mitochondria. FEBS Lett 418: 291-296, 1997.
    • (1997) FEBS Lett , vol.418 , pp. 291-296
    • Ghafourifar, P.1    Richter, C.2
  • 62
    • 0030460014 scopus 로고    scopus 로고
    • On the mechanism of inhibition of cytochrome c oxidase by nitric oxide
    • Giuffre A, Sarti P, D'Itri E, Buse G, Soulimane T, Brunori M. On the mechanism of inhibition of cytochrome c oxidase by nitric oxide. J Biol Chem 271: 33404-33408, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 33404-33408
    • Giuffre, A.1    Sarti, P.2    D'Itri, E.3    Buse, G.4    Soulimane, T.5    Brunori, M.6
  • 63
    • 0032079478 scopus 로고    scopus 로고
    • Production of nitric oxide by mitochondria
    • Giulivi C, Poderoso JJ, Boveris A. Production of nitric oxide by mitochondria. J Biol Chem 273: 11038-11043, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 11038-11043
    • Giulivi, C.1    Poderoso, J.J.2    Boveris, A.3
  • 64
    • 0032526039 scopus 로고    scopus 로고
    • Functional implications of nitric oxide produced by mitochondria in mitochondrial metabolism
    • Giulivi C. Functional implications of nitric oxide produced by mitochondria in mitochondrial metabolism. Biochem J 332: 673-679, 1998.
    • (1998) Biochem J , vol.332 , pp. 673-679
    • Giulivi, C.1
  • 65
    • 0032052209 scopus 로고    scopus 로고
    • Mitochondrial oxygen affinity, respiratory flux control and excess capacity of cytochrome c oxidase
    • Gnaiger E, Lassnig B, Kuznetsov A, Rieger G, Margreiter R. Mitochondrial oxygen affinity, respiratory flux control and excess capacity of cytochrome c oxidase. J Exp Biol 201: 1129-1139, 1998.
    • (1998) J Exp Biol , vol.201 , pp. 1129-1139
    • Gnaiger, E.1    Lassnig, B.2    Kuznetsov, A.3    Rieger, G.4    Margreiter, R.5
  • 66
    • 0032422402 scopus 로고    scopus 로고
    • Redox regulation of the caspases during apoptosis
    • Hampton MB, Fadeel B, Orrenius S. Redox regulation of the caspases during apoptosis. Ann NY Acad Sci 854: 328-335, 1998.
    • (1998) Ann NY Acad Sci , vol.854 , pp. 328-335
    • Hampton, M.B.1    Fadeel, B.2    Orrenius, S.3
  • 67
    • 0032808057 scopus 로고    scopus 로고
    • Nitric oxide induces tyrosine nitration and release of cytochrome c preceding an increase of mitochondrial transmembrane potential in macrophages
    • Hortelano S, Alvarez AM, Bosca L. Nitric oxide induces tyrosine nitration and release of cytochrome c preceding an increase of mitochondrial transmembrane potential in macrophages. FASEB J 13: 2311-2317, 1999.
    • (1999) FASEB J , vol.13 , pp. 2311-2317
    • Hortelano, S.1    Alvarez, A.M.2    Bosca, L.3
  • 69
    • 0034116561 scopus 로고    scopus 로고
    • Prolonged activation of the mitogen-activated protein kinase pathway is required for macrophage-like differentiation of a human myeloid leukemic cell line
    • Hu X, Moscinski LC, Valkov NI, Fisher AB, Hill BJ, Zuckerman KS. Prolonged activation of the mitogen-activated protein kinase pathway is required for macrophage-like differentiation of a human myeloid leukemic cell line. Cell Growth Differ 11: 191-200, 2000.
    • (2000) Cell Growth Differ , vol.11 , pp. 191-200
    • Hu, X.1    Moscinski, L.C.2    Valkov, N.I.3    Fisher, A.B.4    Hill, B.J.5    Zuckerman, K.S.6
  • 70
    • 28444442671 scopus 로고    scopus 로고
    • Effect of nitric oxide-cGMP-dependent protein kinase activation on advanced glycation end-product-induced proliferation in renal fibroblasts
    • Huang JS, Chuang LY, Guh JY, Chen CJ, Yang YL, Chiang TA, Hung MY, Liao TN. Effect of nitric oxide-cGMP-dependent protein kinase activation on advanced glycation end-product-induced proliferation in renal fibroblasts. J Am Soc Nephrol 16: 2318-2329, 2005.
    • (2005) J Am Soc Nephrol , vol.16 , pp. 2318-2329
    • Huang, J.S.1    Chuang, L.Y.2    Guh, J.Y.3    Chen, C.J.4    Yang, Y.L.5    Chiang, T.A.6    Hung, M.Y.7    Liao, T.N.8
  • 71
    • 0034699513 scopus 로고    scopus 로고
    • Superoxide dismutase as a target for the selective killing of cancer cells
    • Huang P, Feng L, Oldham EA, Keating MJ, Plunkett W. Superoxide dismutase as a target for the selective killing of cancer cells. Nature 407: 390-395, 2000.
    • (2000) Nature , vol.407 , pp. 390-395
    • Huang, P.1    Feng, L.2    Oldham, E.A.3    Keating, M.J.4    Plunkett, W.5
  • 72
    • 0017120213 scopus 로고
    • The influence of thyroid hormones on the structure and function of mitochondrial membranes
    • Hulbert AJ, Augee ML, Raison JK. The influence of thyroid hormones on the structure and function of mitochondrial membranes. Biochim Biophys Acta 455: 597-601, 1976.
    • (1976) Biochim Biophys Acta , vol.455 , pp. 597-601
    • Hulbert, A.J.1    Augee, M.L.2    Raison, J.K.3
  • 73
    • 0033301259 scopus 로고    scopus 로고
    • 2-induced activation of SAPK/JNK but not for that of p38 and ERK in Chinese hamster V79 cells
    • 2-induced activation of SAPK/JNK but not for that of p38 and ERK in Chinese hamster V79 cells. Antioxid Redox Signal 1: 501-508, 1999.
    • (1999) Antioxid Redox Signal , vol.1 , pp. 501-508
    • Inanami, O.1    Ohta, T.2    Ito, S.3    Kuwabara, M.4
  • 77
    • 0030662226 scopus 로고    scopus 로고
    • Nitric oxide inhibits apoptosis by preventing increases in caspase-3-like activity via two distinct mechanisms
    • Kim YM, Talanian RV, Billiar TR. Nitric oxide inhibits apoptosis by preventing increases in caspase-3-like activity via two distinct mechanisms. J Biol Chem 272: 31138-31148, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 31138-31148
    • Kim, Y.M.1    Talanian, R.V.2    Billiar, T.R.3
  • 78
    • 0030716481 scopus 로고    scopus 로고
    • Kinetics of the inhibition of mitochondrial respiration by
    • Koivisto A, Matthias A, Bronnkov G, Nedergaard J. Kinetics of the inhibition of mitochondrial respiration by NO. FEBS Lett 417: 75-80, 1997.
    • (1997) FEBS Lett , vol.417 , pp. 75-80
    • Koivisto, A.1    Matthias, A.2    Bronnkov, G.3    Nedergaard, J.4
  • 79
    • 0038486928 scopus 로고    scopus 로고
    • Protein interactions with nitric oxide synthases: Controlling the right time, the right place, and the right amount of nitric oxide
    • Kone BC, Kuncewicz T, Zhang W, Yu ZY. Protein interactions with nitric oxide synthases: controlling the right time, the right place, and the right amount of nitric oxide. Am J Physiol Renal Physiol 285: F178-F190, 2003.
    • (2003) Am J Physiol Renal Physiol , vol.285
    • Kone, B.C.1    Kuncewicz, T.2    Zhang, W.3    Yu, Z.Y.4
  • 80
    • 0032171425 scopus 로고    scopus 로고
    • The basic chemistry of nitrogen monoxide and peroxynitrite
    • Koppenol WH. The basic chemistry of nitrogen monoxide and peroxynitrite. Free Radic Biol Med 25: 381-391, 1998.
    • (1998) Free Radic Biol Med , vol.25 , pp. 381-391
    • Koppenol, W.H.1
  • 81
    • 0034604540 scopus 로고    scopus 로고
    • Selective activation of p38 MAPK cascade and mitotic arrest caused by low level oxidative stress
    • Kurata S. Selective activation of p38 MAPK cascade and mitotic arrest caused by low level oxidative stress. J Biol Chem 275: 23413-23416, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 23413-23416
    • Kurata, S.1
  • 82
    • 0026623110 scopus 로고
    • Endothelial nitric oxide synthase: Molecular cloning and characterization of a distinct enzyme isoform
    • Lamas S, Marsden PA, Lee GK, Tempst P, Michel T. Endothelial nitric oxide synthase: molecular cloning and characterization of a distinct enzyme isoform. Proc Natl Acad Sci USA 89: 6348-6352, 1992.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 6348-6352
    • Lamas, S.1    Marsden, P.A.2    Lee, G.K.3    Tempst, P.4    Michel, T.5
  • 83
    • 33646103893 scopus 로고    scopus 로고
    • Caspases leave the beaten track: Caspase-mediated activation of NF-κB
    • Lamkanfi M, Declercq W, Vanden Berghe T, Vandenabeele P. Caspases leave the beaten track: caspase-mediated activation of NF-κB. J Cell Biol 173: 166-171, 2003.
    • (2003) J Cell Biol , vol.173 , pp. 166-171
    • Lamkanfi, M.1    Declercq, W.2    Vanden Berghe, T.3    Vandenabeele, P.4
  • 85
    • 0034724668 scopus 로고    scopus 로고
    • Cyclic nucleotides suppress tumor necrosis factor alpha-mediated apoptosis by inhibiting caspase activation and cytochrome c release in primary hepatocytes via a mechanism independent of Akt activation
    • Li J, Yang S, Billiar TR. Cyclic nucleotides suppress tumor necrosis factor alpha-mediated apoptosis by inhibiting caspase activation and cytochrome c release in primary hepatocytes via a mechanism independent of Akt activation. J Biol Chem 275: 13026-13034, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 13026-13034
    • Li, J.1    Yang, S.2    Billiar, T.R.3
  • 86
    • 33645533784 scopus 로고    scopus 로고
    • Immunoregulatory and antimicrobial effects of nitrogen oxides
    • Mannick JB. Immunoregulatory and antimicrobial effects of nitrogen oxides. Proc Am Thorac Soc 3: 161-165, 2006.
    • (2006) Proc Am Thorac Soc , vol.3 , pp. 161-165
    • Mannick, J.B.1
  • 87
    • 0035852845 scopus 로고    scopus 로고
    • Inhibition of NF-κB by S-nitrosylation
    • Marshall HE, Stamler JS. Inhibition of NF-κB by S-nitrosylation. Biochemistry 40: 1688-1693, 2001.
    • (2001) Biochemistry , vol.40 , pp. 1688-1693
    • Marshall, H.E.1    Stamler, J.S.2
  • 88
    • 0037072883 scopus 로고    scopus 로고
    • Nitrosative stress-induced apoptosis through inhibition of NF-κB
    • Marshall HE, Stamler JS. Nitrosative stress-induced apoptosis through inhibition of NF-κB. J Biol Chem 277: 34223-34228, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 34223-34228
    • Marshall, H.E.1    Stamler, J.S.2
  • 90
    • 33645456241 scopus 로고    scopus 로고
    • 2+ and calmodulin/MAP kinase kinase/extracellular signal-regulated protein kinase signalling pathway in the mitogenic and antimitogenic effect of nitric oxide in glia- and neurone-derived cell lines
    • 2+ and calmodulin/MAP kinase kinase/extracellular signal-regulated protein kinase signalling pathway in the mitogenic and antimitogenic effect of nitric oxide in glia- and neurone-derived cell lines. Eur J Neurosci 23: 1690-1700, 2006.
    • (2006) Eur J Neurosci , vol.23 , pp. 1690-1700
    • Meini, A.1    Garcia, J.B.2    Pessina, G.P.3    Aldinucci, C.4    Frosini, M.5    Palmi, M.6
  • 91
    • 0029812216 scopus 로고    scopus 로고
    • Nitric oxide-induced apoptosis: P53-dependent and p53-independent signaling pathways
    • Messmer UK. Nitric oxide-induced apoptosis: p53-dependent and p53-independent signaling pathways. Biochem J 319: 299-305. 1996.
    • (1996) Biochem J , vol.319 , pp. 299-305
    • Messmer, U.K.1
  • 92
    • 0030711558 scopus 로고    scopus 로고
    • Nitric oxide synthases: Which, where, why?
    • Michel T, Feron O. Nitric oxide synthases: which, where, why? J Clin Invest 100: 2146-2152, 1997.
    • (1997) J Clin Invest , vol.100 , pp. 2146-2152
    • Michel, T.1    Feron, O.2
  • 93
    • 33744940003 scopus 로고    scopus 로고
    • Nitric oxide and p38 MAP kinase mediate shear stress-dependent inhibition of MMP-2 production in microvascular endothelial cells
    • Milkiewicz M, Kelland C, Colgan S, Haas TL. Nitric oxide and p38 MAP kinase mediate shear stress-dependent inhibition of MMP-2 production in microvascular endothelial cells. J Cell Physiol 208: 229-237, 2006.
    • (2006) J Cell Physiol , vol.208 , pp. 229-237
    • Milkiewicz, M.1    Kelland, C.2    Colgan, S.3    Haas, T.L.4
  • 94
    • 0034634441 scopus 로고    scopus 로고
    • Mechanism of nitric oxide-induced apoptosis in human neuroblastoma SH-SY5Y cells
    • Moriya R, Uehara T, Nomura Y. Mechanism of nitric oxide-induced apoptosis in human neuroblastoma SH-SY5Y cells. FEBS Lett 484: 253-260, 2000.
    • (2000) FEBS Lett , vol.484 , pp. 253-260
    • Moriya, R.1    Uehara, T.2    Nomura, Y.3
  • 97
    • 0030774585 scopus 로고    scopus 로고
    • Role of glutathione and nitric oxide in the energy metabolism of rat liver mitochondria
    • Nishikawa M, Sato EF, Kuroki T, Inoue M. Role of glutathione and nitric oxide in the energy metabolism of rat liver mitochondria. FEBS Lett 415: 341-345, 1997.
    • (1997) FEBS Lett , vol.415 , pp. 341-345
    • Nishikawa, M.1    Sato, E.F.2    Kuroki, T.3    Inoue, M.4
  • 99
    • 0036170886 scopus 로고    scopus 로고
    • Thyroid status is a key regulator of both flux and efficiency of oxidative phosphorylation in rat hepatocytes
    • Nogueira V, Walter L, Av'eret N, Fontaine E, Rigoulet M, Leverve XM. Thyroid status is a key regulator of both flux and efficiency of oxidative phosphorylation in rat hepatocytes. J Bioenerg Biomembr 34: 55-66, 2002.
    • (2002) J Bioenerg Biomembr , vol.34 , pp. 55-66
    • Nogueira, V.1    Walter, L.2    Av'eret, N.3    Fontaine, E.4    Rigoulet, M.5    Leverve, X.M.6
  • 101
    • 14044254869 scopus 로고    scopus 로고
    • Impaired vasodilation by red blood cells in sickle cell disease
    • Pawloski JR, Hess DT, Stamler JS. Impaired vasodilation by red blood cells in sickle cell disease. Proc Natl Acad Sci USA 102: 2531-2536, 2005.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 2531-2536
    • Pawloski, J.R.1    Hess, D.T.2    Stamler, J.S.3
  • 102
    • 0032529218 scopus 로고    scopus 로고
    • Inducible nitric oxide: An autoregulatory feedback inhibitor of vascular inflammation
    • Peng HB, Spiecker M, Liao JK. Inducible nitric oxide: an autoregulatory feedback inhibitor of vascular inflammation. J Immunol 161: 1970-1976, 1998.
    • (1998) J Immunol , vol.161 , pp. 1970-1976
    • Peng, H.B.1    Spiecker, M.2    Liao, J.K.3
  • 104
    • 0035853035 scopus 로고    scopus 로고
    • Nitric oxide-induced cytostasis and cell cycle arrest of a human breast cancer cell line (MDA-MB-231): Potential role of cyclin D1
    • Pervin S, Singh R, Chaudhuri G. Nitric oxide-induced cytostasis and cell cycle arrest of a human breast cancer cell line (MDA-MB-231): potential role of cyclin D1. Proc Natl Acad Sci USA 98: 3583-3588, 2001.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 3583-3588
    • Pervin, S.1    Singh, R.2    Chaudhuri, G.3
  • 105
    • 0033304945 scopus 로고    scopus 로고
    • The cyclins and cyclin-dependent kinase inhibitors in hormonal regulation of proliferation and differentiation
    • Pestell RG, Albanese C, Reutens AT, Segall JE, Lee RJ, Arnold A. The cyclins and cyclin-dependent kinase inhibitors in hormonal regulation of proliferation and differentiation. Endocr Rev 20: 501-534, 1999.
    • (1999) Endocr Rev , vol.20 , pp. 501-534
    • Pestell, R.G.1    Albanese, C.2    Reutens, A.T.3    Segall, J.E.4    Lee, R.J.5    Arnold, A.6
  • 106
    • 0037276437 scopus 로고    scopus 로고
    • The CD95 (APO-1/Fas) DISC and beyond
    • Peter ME, Krammer PH. The CD95 (APO-1/Fas) DISC and beyond. Cell Death Differ 10: 26-35, 2003.
    • (2003) Cell Death Differ , vol.10 , pp. 26-35
    • Peter, M.E.1    Krammer, P.H.2
  • 108
    • 0029986691 scopus 로고    scopus 로고
    • Nitric oxide inhibits electron transfer and increases superoxide radical production in rat heart mitochondria and submitochondrial particles
    • Poderoso JJ, Carreras MC, Lisdero C, Riobó N, Schöpfer F, Boveris A. Nitric oxide inhibits electron transfer and increases superoxide radical production in rat heart mitochondria and submitochondrial particles. Arch Biochem Biophys 328: 85-92, 1996.
    • (1996) Arch Biochem Biophys , vol.328 , pp. 85-92
    • Poderoso, J.J.1    Carreras, M.C.2    Lisdero, C.3    Riobó, N.4    Schöpfer, F.5    Boveris, A.6
  • 110
  • 113
    • 0035937771 scopus 로고    scopus 로고
    • 2 by catalase inhibits the proliferation of HER-2 Neu-transformed Rat-1 fibroblasts through the induction of a stress response
    • 2 by catalase inhibits the proliferation of HER-2 Neu-transformed Rat-1 fibroblasts through the induction of a stress response. J Biol Chem 276: 9558-9564, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 9558-9564
    • Preston, T.J.1    Muller, F.J.2    Singh, G.3
  • 117
    • 0033038403 scopus 로고    scopus 로고
    • Thyroid hormone and other regulators of uncoupling proteins
    • Reitman ML, He Y, Gong DW. Thyroid hormone and other regulators of uncoupling proteins. Int J Obes 23: S56-S59, 1999.
    • (1999) Int J Obes , vol.23
    • Reitman, M.L.1    He, Y.2    Gong, D.W.3
  • 119
    • 0037044724 scopus 로고    scopus 로고
    • The modulation of mitochondrial nitric oxide synthase activity in rat brain development
    • Riobó N, Melani M, Sanjuán N, Carreras MC, Cadenas E, Poderoso JJ. The modulation of mitochondrial nitric oxide synthase activity in rat brain development. J Biol Chem 277: 42447-42455, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 42447-42455
    • Riobó, N.1    Melani, M.2    Sanjuán, N.3    Carreras, M.C.4    Cadenas, E.5    Poderoso, J.J.6
  • 120
    • 0035477926 scopus 로고    scopus 로고
    • Nitric oxide inhibits mitochondrial NADH-ubiquinone reductase activity through peroxynitrite formation
    • Riobó NA, Clementi E, Melani M, Boveris A, Cadenas E, Moncada S, Poderoso JJ. Nitric oxide inhibits mitochondrial NADH-ubiquinone reductase activity through peroxynitrite formation. Biochem J 359: 39-45, 2001.
    • (2001) Biochem J , vol.359 , pp. 39-45
    • Riobó, N.A.1    Clementi, E.2    Melani, M.3    Boveris, A.4    Cadenas, E.5    Moncada, S.6    Poderoso, J.J.7
  • 121
    • 0034693227 scopus 로고    scopus 로고
    • Distinct pathways for stimulation of cytochrome c release by etoposide
    • Robertson JD, Gogvadze V, Zhivotovsky, Orrenius S. Distinct pathways for stimulation of cytochrome c release by etoposide. J Biol Chem 275: 32438-32443, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 32438-32443
    • Robertson, J.D.1    Gogvadze, V.2    Zhivotovsky3    Orrenius, S.4
  • 123
    • 0035978743 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis
    • Rowland LP, Shneider NA. Amyotrophic lateral sclerosis. N Engl J Med 344: 1688-1700, 2001.
    • (2001) N Engl J Med , vol.344 , pp. 1688-1700
    • Rowland, L.P.1    Shneider, N.A.2
  • 126
    • 0031552931 scopus 로고    scopus 로고
    • Cardiolipin synthase from mammalian mitochondria
    • Schlame M, Hostetler KY. Cardiolipin synthase from mammalian mitochondria. Biochim Biophys Acta 1348: 207-213, 1997.
    • (1997) Biochim Biophys Acta , vol.1348 , pp. 207-213
    • Schlame, M.1    Hostetler, K.Y.2
  • 127
    • 0038381423 scopus 로고    scopus 로고
    • Nitrosylation of cytochrome c during apoptosis
    • Schonhoff CM, Gaston B, Mannick JB. Nitrosylation of cytochrome c during apoptosis. J Biol Chem 278: 18265-18270, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 18265-18270
    • Schonhoff, C.M.1    Gaston, B.2    Mannick, J.B.3
  • 130
    • 0028061310 scopus 로고
    • Role of nitric oxide in the regulation of oxygen consumption in conscious dogs
    • Shen W, Xu X, Ochoa M, Zhao G, Wolin M, Hintze TH. Role of nitric oxide in the regulation of oxygen consumption in conscious dogs. Circ Res 75: 1086-1095, 1994.
    • (1994) Circ Res , vol.75 , pp. 1086-1095
    • Shen, W.1    Xu, X.2    Ochoa, M.3    Zhao, G.4    Wolin, M.5    Hintze, T.H.6
  • 131
    • 8644219655 scopus 로고    scopus 로고
    • Living with or without cyclins and cyclin-dependent kinases
    • Sherr CJ, Roberts JM. Living with or without cyclins and cyclin-dependent kinases. Genes Dev 18: 2699-2711, 2004.
    • (2004) Genes Dev , vol.18 , pp. 2699-2711
    • Sherr, C.J.1    Roberts, J.M.2
  • 133
    • 0033914409 scopus 로고    scopus 로고
    • Astrocyte-derived nitric oxide causes both reversible and irreversible damage to the neuronal mitochondrial respiratory chain
    • Stewart VC, Sharpe MA, Clark JB, Heales JR. Astrocyte-derived nitric oxide causes both reversible and irreversible damage to the neuronal mitochondrial respiratory chain. J Neurochem 75: 694-700, 2000.
    • (2000) J Neurochem , vol.75 , pp. 694-700
    • Stewart, V.C.1    Sharpe, M.A.2    Clark, J.B.3    Heales, J.R.4
  • 134
    • 0023766145 scopus 로고
    • Insulin-stimulated MAP-2 kinase phosphorylates and activates ribosomal protein S6 kinase II
    • Sturgill TW, Ray LB, Erikson E, Maller JL. Insulin-stimulated MAP-2 kinase phosphorylates and activates ribosomal protein S6 kinase II. Nature 334: 715-718, 1988.
    • (1988) Nature , vol.334 , pp. 715-718
    • Sturgill, T.W.1    Ray, L.B.2    Erikson, E.3    Maller, J.L.4
  • 137
    • 0028875182 scopus 로고
    • Oxygen-dependent regulation of mitochondrial energy metabolism by nitric oxide
    • Takehara Y, Kanno T, Yoshioka T, Inoue M, Utsumi K. Oxygen-dependent regulation of mitochondrial energy metabolism by nitric oxide. Arch Biochem Biophys 323: 27-32, 1995.
    • (1995) Arch Biochem Biophys , vol.323 , pp. 27-32
    • Takehara, Y.1    Kanno, T.2    Yoshioka, T.3    Inoue, M.4    Utsumi, K.5
  • 138
    • 0034712704 scopus 로고    scopus 로고
    • Nitric oxide modulates expression of cell cycle regulatory proteins. A cytostatic strategy for inhibition of human vascular smooth muscle cell proliferation
    • Tanner FC, Meier P, Greutert H, Champion C, Nabel EG, Lüscher TF. Nitric oxide modulates expression of cell cycle regulatory proteins. A cytostatic strategy for inhibition of human vascular smooth muscle cell proliferation. Circulation 101: 1982-1989, 2000.
    • (2000) Circulation , vol.101 , pp. 1982-1989
    • Tanner, F.C.1    Meier, P.2    Greutert, H.3    Champion, C.4    Nabel, E.G.5    Lüscher, T.F.6
  • 139
    • 0028885796 scopus 로고
    • Inhibition of cytochrome c oxidase in turnover by nitric oxide: Mechanism and implications for control of respiration
    • Torres J, Darley-Usmar V, Wilson MT. Inhibition of cytochrome c oxidase in turnover by nitric oxide: mechanism and implications for control of respiration. Biochem J 312: 169-173, 1995.
    • (1995) Biochem J , vol.312 , pp. 169-173
    • Torres, J.1    Darley-Usmar, V.2    Wilson, M.T.3
  • 140
    • 0002361408 scopus 로고    scopus 로고
    • Nitric oxide, oxidative stress, and signal transduction
    • edited by Ignarro L. San Diego, CA: Academic
    • Torres M, Forman HJ. Nitric oxide, oxidative stress, and signal transduction. In Nitric Oxide. Biology and Pathobiology, edited by Ignarro L. San Diego, CA: Academic, 2000, p. 329-342.
    • (2000) In Nitric Oxide. Biology and Pathobiology , pp. 329-342
    • Torres, M.1    Forman, H.J.2
  • 141
    • 0022869401 scopus 로고
    • Increased spontaneous chemiluminescence from liver homogenates and isolated hepatocytes upon inhibition of superoxide and hydrogen peroxide utilization
    • Turrens JF, Giulivi C, Boveris A. Increased spontaneous chemiluminescence from liver homogenates and isolated hepatocytes upon inhibition of superoxide and hydrogen peroxide utilization. Free Radic Biol Med 2: 153-140, 1986.
    • (1986) Free Radic Biol Med , vol.2 , pp. 153-140
    • Turrens, J.F.1    Giulivi, C.2    Boveris, A.3
  • 143
    • 20644464245 scopus 로고
    • Diffusion of nitric oxide
    • Wise DL, Houghton G. Diffusion of nitric oxide. Chem Eng Sci 26: 453-460, 1968.
    • (1968) Chem Eng Sci , vol.26 , pp. 453-460
    • Wise, D.L.1    Houghton, G.2
  • 144
    • 0035139792 scopus 로고    scopus 로고
    • Therapeutic potential of inhibition of the NF-κB pathway in the treatment of inflammation and cancer
    • Yamamoto Y, Gaynor RB. Therapeutic potential of inhibition of the NF-κB pathway in the treatment of inflammation and cancer. J Clin Invest 107: 135-142, 2001.
    • (2001) J Clin Invest , vol.107 , pp. 135-142
    • Yamamoto, Y.1    Gaynor, R.B.2


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