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Volumn 120, Issue 2, 2014, Pages 51-63

Signalling pathways involved in paracetamol-induced hepatotoxicity: New insights on the role of protein tyrosine phosphatase 1B

Author keywords

Apoptosis; Hepatotoxicity; Necrosis; Oxidative stress; Paracetamol; Protein tyrosine phosphates 1B

Indexed keywords

PARACETAMOL; PROTEIN TYROSINE PHOSPHATASE 1B;

EID: 84910142073     PISSN: 13813455     EISSN: 17444160     Source Type: Journal    
DOI: 10.3109/13813455.2014.893365     Document Type: Article
Times cited : (11)

References (152)
  • 1
    • 0034708832 scopus 로고    scopus 로고
    • White MF. The C-Jun NH(2)-terminal kinase promotes insulin resistance during association with insulin receptor substrate-1 and phosphorylation of Ser(307)
    • Aguirre V, Uchida T, Yenush L, Davis R. (2000). White MF. The c-Jun NH(2)-terminal kinase promotes insulin resistance during association with insulin receptor substrate-1 and phosphorylation of Ser(307). J Biol Chem, 275:9047-54.
    • (2000) J Biol Chem , vol.275 , pp. 9047-9054
    • Aguirre, V.1    Uchida, T.2    Yenush, L.3    Davis, R.4
  • 2
    • 34250359779 scopus 로고    scopus 로고
    • Emerging role of Nrf2 in protecting against hepatic and gastrointestinal disease
    • Aleksunes LM, Manautou JE. (2007). Emerging role of Nrf2 in protecting against hepatic and gastrointestinal disease. Toxicol Path, 35:459-73.
    • (2007) Toxicol Path , vol.35 , pp. 459-473
    • Aleksunes, L.M.1    Manautou, J.E.2
  • 3
    • 74949101589 scopus 로고    scopus 로고
    • High Mobility Group Box-1 protein and Keratin-18, circulating serum proteins informative of acetaminophen-induced necrosis and apoptosis in vivo
    • Antoine DJ, Williams DP, Kipar A, et al. (2009). High Mobility Group Box-1 protein and Keratin-18, circulating serum proteins informative of acetaminophen-induced necrosis and apoptosis in vivo. Toxicol Sci, 112:521-31.
    • (2009) Toxicol Sci , vol.112 , pp. 521-531
    • Antoine, D.J.1    Williams, D.P.2    Kipar, A.3
  • 4
    • 84862776783 scopus 로고    scopus 로고
    • Molecular forms of HMGB1 and keratin-18 as mechanistic biomarkers for mode of cell death and prognosis during clinical acetaminophen hepatotoxicity
    • Antoine DJ, Jenkins RE, Dear JW, et al. (2012). Molecular forms of HMGB1 and keratin-18 as mechanistic biomarkers for mode of cell death and prognosis during clinical acetaminophen hepatotoxicity. J Hepatol, 56:1070-9.
    • (2012) J Hepatol , vol.56 , pp. 1070-1079
    • Antoine, D.J.1    Jenkins, R.E.2    Dear, J.W.3
  • 5
    • 0037155837 scopus 로고    scopus 로고
    • Direct activation of mitochondrial apoptosis machinery by c-Jun N-terminal kinase in adult cardiac myocytes
    • Aoki H, Kang PM, Hampe J, et al. (2002). Direct activation of mitochondrial apoptosis machinery by c-Jun N-terminal kinase in adult cardiac myocytes. J Biol Chem, 277:10244-50.
    • (2002) J Biol Chem , vol.277 , pp. 10244-10250
    • Aoki, H.1    Kang, P.M.2    Hampe, J.3
  • 6
    • 84884338770 scopus 로고    scopus 로고
    • Regulatory flexibility in the Nrf2-mediated stress response is conferred by conformational cycling of the Keap1-Nrf2 protein complex
    • Baird L, Llères D, Swift S, Dinkova-Kostova AT. (2013). Regulatory flexibility in the Nrf2-mediated stress response is conferred by conformational cycling of the Keap1-Nrf2 protein complex. Proc Natl Acad Sci USA, 110:15259-64.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 15259-15264
    • Baird, L.1    Llères, D.2    Swift, S.3    Dinkova-Kostova, A.T.4
  • 7
    • 0029782711 scopus 로고    scopus 로고
    • Regulated binding of PTP1Blike phosphatase to N-cadherin: Control of cadherin-mediated adhesion by dephosphorylation of beta-catenin
    • Balsamo J, Leung T, Ernst H, et al. (1996). Regulated binding of PTP1Blike phosphatase to N-cadherin: Control of cadherin-mediated adhesion by dephosphorylation of beta-catenin. J Cell Biol, 134:801-13.
    • (1996) J Cell Biol , vol.134 , pp. 801-813
    • Balsamo, J.1    Leung, T.2    Ernst, H.3
  • 8
    • 0031036223 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase 1B complexes with the insulin receptor in vivo and is tyrosine-phosphorylated in the presence of insulin
    • Bandyopadhyay D, Kusari A, Kenner KA, et al. (1997). Protein-tyrosine phosphatase 1B complexes with the insulin receptor in vivo and is tyrosine-phosphorylated in the presence of insulin. J Biol Chem, 272: 1639-45.
    • (1997) J Biol Chem , vol.272 , pp. 1639-1645
    • Bandyopadhyay, D.1    Kusari, A.2    Kenner, K.A.3
  • 9
    • 77956265378 scopus 로고    scopus 로고
    • Cytokeratin 18- based modification of the MELD score improves prediction of spontaneous survival after acute liver injury
    • Bechmann LP, Jochum C, Kocabayoglu P, et al. (2010). Cytokeratin 18- based modification of the MELD score improves prediction of spontaneous survival after acute liver injury. J Hepatol, 53:639-47.
    • (2010) J Hepatol , vol.53 , pp. 639-647
    • Bechmann, L.P.1    Jochum, C.2    Kocabayoglu, P.3
  • 10
    • 0035132183 scopus 로고    scopus 로고
    • Paracetamol (acetaminophen)- induced toxicity: Molecular and biochemical mechanisms, analogues and protective approaches
    • Bessems JG, Vermeulen NP. (2001). Paracetamol (acetaminophen)- induced toxicity: Molecular and biochemical mechanisms, analogues and protective approaches. Crit Rev Toxicol, 31:55-138.
    • (2001) Crit Rev Toxicol , vol.31 , pp. 55-138
    • Bessems, J.G.1    Vermeulen, N.P.2
  • 11
    • 0242666198 scopus 로고    scopus 로고
    • Phosphorylation of Nrf2 at Ser40 by protein kinase C in response to antioxidants leads to the release of Nrf2 from INrf2, but is not required for Nrf2 stabilization/accumulation in the nucleus and transcriptional activation of antioxidant response element-mediated NAD(P)H:quinone oxidoreductase-1 gene expression
    • Bloom DA, Jaiswal AK. (2003). Phosphorylation of Nrf2 at Ser40 by protein kinase C in response to antioxidants leads to the release of Nrf2 from INrf2, but is not required for Nrf2 stabilization/accumulation in the nucleus and transcriptional activation of antioxidant response element-mediated NAD(P)H:quinone oxidoreductase-1 gene expression. J Biol Chem, 278:44675-82.
    • (2003) J Biol Chem , vol.278 , pp. 44675-44682
    • Bloom, D.A.1    Jaiswal, A.K.2
  • 12
    • 33748942862 scopus 로고    scopus 로고
    • The isoform-specific functions of the c-Jun N-terminal Kinases (JNKs): Differences revealed by gene targeting
    • Bogoyevitch MA. (2006). The isoform-specific functions of the c-Jun N-terminal Kinases (JNKs): Differences revealed by gene targeting. Bioessays, 28:923-34.
    • (2006) Bioessays , vol.28 , pp. 923-934
    • Bogoyevitch, M.A.1
  • 13
    • 0031005579 scopus 로고    scopus 로고
    • Reperfusion after liver transplantation in rats differentially activates the mitogenactivated protein kinases
    • Bradham CA, Stachlewitz RF, Gao W, et al. (1997). Reperfusion after liver transplantation in rats differentially activates the mitogenactivated protein kinases. Hepatology, 25:1128-35.
    • (1997) Hepatology , vol.25 , pp. 1128-1135
    • Bradham, C.A.1    Stachlewitz, R.F.2    Gao, W.3
  • 14
    • 18144386564 scopus 로고    scopus 로고
    • No increase of apoptosis in regressing mouse liver after withdrawal of growth stimuli or food restriction
    • Bursch W, Wastl U, Hufnagl K, Schulte-Hermann R. (2005). No increase of apoptosis in regressing mouse liver after withdrawal of growth stimuli or food restriction. Toxicol Sci, 85:507-14.
    • (2005) Toxicol Sci , vol.85 , pp. 507-514
    • Bursch, W.1    Wastl, U.2    Hufnagl, K.3    Schulte-Hermann, R.4
  • 15
    • 1242336980 scopus 로고    scopus 로고
    • Apoptosis: The nexus of liver injury and fibrosis
    • Canbay A, Friedman S, Gores GJ. (2004). Apoptosis: The nexus of liver injury and fibrosis. Hepatology, 39:273-8.
    • (2004) Hepatology , vol.39 , pp. 273-278
    • Canbay, A.1    Friedman, S.2    Gores, G.J.3
  • 16
    • 0027365542 scopus 로고
    • Isolation of cDNA encoding the human NF-E2 protein
    • Chan JY, Han XL, Kan YW. (1993). Isolation of cDNA encoding the human NF-E2 protein. Proc Natl Acad Sci USA, 90:11366-70.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11366-11370
    • Chan, J.Y.1    Han, X.L.2    Kan, Y.W.3
  • 17
    • 0032536783 scopus 로고    scopus 로고
    • Targeted disruption of the ubiquitous CNC-bZIP transcription factor, Nrf-1, results in anemia and embryonic lethality in mice
    • Chan JY, Kwong M, Lu R, et al. (1998). Targeted disruption of the ubiquitous CNC-bZIP transcription factor, Nrf-1, results in anemia and embryonic lethality in mice. EMBO J, 17:1779-87.
    • (1998) EMBO J , vol.17 , pp. 1779-1787
    • Chan, J.Y.1    Kwong, M.2    Lu, R.3
  • 18
    • 0034672595 scopus 로고    scopus 로고
    • Impaired expression of glutathione synthetic enzyme genes in mice with targeted deletion of the Nrf2 basic-leucine zipper protein
    • Chan JY, Kwong M. (2000). Impaired expression of glutathione synthetic enzyme genes in mice with targeted deletion of the Nrf2 basic-leucine zipper protein. Biochim Biophys Acta, 1517:19-26.
    • (2000) Biochim Biophys Acta , vol.1517 , pp. 19-26
    • Chan, J.Y.1    Kwong, M.2
  • 19
    • 0030451213 scopus 로고    scopus 로고
    • Nrf2, a member of the NF-E2 family of transcription factors, is not essential for murine erythropoiesis, growth, and development
    • Chan K, Lu R, Chang JC, Kan YT. (1996). Nrf2, a member of the NF-E2 family of transcription factors, is not essential for murine erythropoiesis, growth, and development. Proc Natl Acad Sci USA, 93:13943-8.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13943-13948
    • Chan, K.1    Lu, R.2    Chang, J.C.3    Kan, Y.T.4
  • 20
    • 0038719671 scopus 로고    scopus 로고
    • JNK-dependent release of mitochondrial protein, Smac, during apoptosis in multiple myeloma (MM) cells
    • Chauhan D, Li G, Hideshima T, et al. (2003). JNK-dependent release of mitochondrial protein, Smac, during apoptosis in multiple myeloma (MM) cells. J Biol Chem, 278:17593-6.
    • (2003) J Biol Chem , vol.278 , pp. 17593-17596
    • Chauhan, D.1    Li, G.2    Hideshima, T.3
  • 21
    • 0038476526 scopus 로고    scopus 로고
    • Novel isoquinolinonederived inhibitors of poly (ADP-ribose) polymerase-1: Pharmacological characterization and neuroprotective effects in an in vitro model of cerebral ischemia
    • Chiarugi A, Meli E, Calvani M, et al. (2003). Novel isoquinolinonederived inhibitors of poly (ADP-ribose) polymerase-1: Pharmacological characterization and neuroprotective effects in an in vitro model of cerebral ischemia. J Pharmacol Exp Ther, 305: 943-9.
    • (2003) J Pharmacol Exp Ther , vol.305 , pp. 943-949
    • Chiarugi, A.1    Meli, E.2    Calvani, M.3
  • 22
    • 33751536492 scopus 로고    scopus 로고
    • Phospholipase C gamma1 negatively regulates growth hormone signalling by forming a ternary complex with Jak2 and protein tyrosine phosphatase-1B
    • Choi JH, Kim HS, Kim SH, et al. (2006). Phospholipase C gamma1 negatively regulates growth hormone signalling by forming a ternary complex with Jak2 and protein tyrosine phosphatase-1B. Nat Cell Biol, 8:1389-97.
    • (2006) Nat Cell Biol , vol.8 , pp. 1389-1397
    • Choi, J.H.1    Kim, H.S.2    Kim, S.H.3
  • 23
    • 0021955464 scopus 로고
    • Effects of N-acetylcysteine on acetaminophen covalent binding and hepatic necrosis in mice
    • Corcoran GB, Racz WJ, Smith CV, Mitchell JR. (1985). Effects of N-acetylcysteine on acetaminophen covalent binding and hepatic necrosis in mice. J Pharmacol Exp Ther, 232:864-72.
    • (1985) J Pharmacol Exp Ther , vol.232 , pp. 864-872
    • Corcoran, G.B.1    Racz, W.J.2    Smith, C.V.3    Mitchell, J.R.4
  • 24
    • 79961209077 scopus 로고    scopus 로고
    • Circulating apoptotic and necrotic cell death markers in patients with acute liver injury
    • Craig DG, Lee P, Pryde EA, et al. (2011). Circulating apoptotic and necrotic cell death markers in patients with acute liver injury. Liver Int, 31:1127-36.
    • (2011) Liver Int , vol.31 , pp. 1127-1136
    • Craig, D.G.1    Lee, P.2    Pryde, E.A.3
  • 25
    • 0141752795 scopus 로고    scopus 로고
    • Nrf2 is a direct PERK substrate and effector of PERK-dependent cell survival
    • Cullinan SB, Zhang D, Hannink M, et al. (2003). Nrf2 is a direct PERK substrate and effector of PERK-dependent cell survival. Mol Cell Biol, 23:7198-209.
    • (2003) Mol Cell Biol , vol.23 , pp. 7198-7209
    • Cullinan, S.B.1    Zhang, D.2    Hannink, M.3
  • 26
    • 4544294365 scopus 로고    scopus 로고
    • The Keap1-BTB protein is an adaptor that bridges Nrf2 to a Cul3-based E3 ligase: Oxidative stress sensing by a Cul3-Keap1 ligase
    • Cullinan SB, Gordan JD, Jin J, et al. (2004). The Keap1-BTB protein is an adaptor that bridges Nrf2 to a Cul3-based E3 ligase: Oxidative stress sensing by a Cul3-Keap1 ligase. Mol Cell Biol, 24:8477-86.
    • (2004) Mol Cell Biol , vol.24 , pp. 8477-8486
    • Cullinan, S.B.1    Gordan, J.D.2    Jin, J.3
  • 27
    • 35948979743 scopus 로고    scopus 로고
    • Cell signalling in oxidative stress-induced liver injury
    • Czaja MJ. (2007). Cell signalling in oxidative stress-induced liver injury. Semin Liver Dis, 27:378-89.
    • (2007) Semin Liver Dis , vol.27 , pp. 378-389
    • Czaja, M.J.1
  • 28
    • 33845914340 scopus 로고    scopus 로고
    • Regulation of protein tyrosine phosphatase 1B by sumoylation
    • Dadke SS, Cotteret SC, Yip ZM, et al. (2007). Regulation of protein tyrosine phosphatase 1B by sumoylation. Nat Cell Biol, 9:80-5.
    • (2007) Nat Cell Biol , vol.9 , pp. 80-85
    • Dadke, S.S.1    Cotteret, S.C.2    Yip, Z.M.3
  • 29
    • 0021345926 scopus 로고
    • N-acetyl-pbenzoquinone imine: A cytochrome P-450-mediated oxidation product of acetaminophen
    • Dahlin DC, Miwa GT, Lu AY, Nelson SD. (1984). N-acetyl-pbenzoquinone imine: A cytochrome P-450-mediated oxidation product of acetaminophen. Proc Natl Acad Sci USA, 81:1327-31.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 1327-1331
    • Dahlin, D.C.1    Miwa, G.T.2    Lu, A.Y.3    Nelson, S.D.4
  • 30
    • 0035963293 scopus 로고    scopus 로고
    • Functional characterization and role of INrf2 in antioxidant response element-mediated expression and antioxidant induction of NAD(P)H quinone oxidoreductase1 gene
    • Dhakshinamoorthy S, Jaiswal AK. (2001). Functional characterization and role of INrf2 in antioxidant response element-mediated expression and antioxidant induction of NAD(P)H quinone oxidoreductase1 gene. Oncogene, 20:3906-17.
    • (2001) Oncogene , vol.20 , pp. 3906-3917
    • Dhakshinamoorthy, S.1    Jaiswal, A.K.2
  • 31
    • 33947595809 scopus 로고    scopus 로고
    • Healthy animals and animal models of human disease(s) in safety assessment of human pharmaceuticals, including therapeutic antibodies
    • Dixit R, Boelsterli UA. (2007). Healthy animals and animal models of human disease(s) in safety assessment of human pharmaceuticals, including therapeutic antibodies. Drug Discov Today, 12:336-42.
    • (2007) Drug Discov Today , vol.12 , pp. 336-342
    • Dixit, R.1    Boelsterli, U.A.2
  • 32
    • 0033675833 scopus 로고    scopus 로고
    • Involvement of human cytochrome P450 2D6 in the bioactivation of acetaminophen
    • Dong H, Haining RL, Thummel KE, et al. (2000). Involvement of human cytochrome P450 2D6 in the bioactivation of acetaminophen. Drug Metab Dispos, 28:1397-400.
    • (2000) Drug Metab Dispos , vol.28 , pp. 1397-1400
    • Dong, H.1    Haining, R.L.2    Thummel, K.E.3
  • 33
    • 2942729545 scopus 로고    scopus 로고
    • Suramin inhibits death receptor-induced apoptosis in vitro and fulminant apoptotic liver damage in mice
    • Eichhorst ST, Krueger A, Muerkoster S, et al. (2004). Suramin inhibits death receptor-induced apoptosis in vitro and fulminant apoptotic liver damage in mice. Nat Med, 10:602-9.
    • (2004) Nat Med , vol.10 , pp. 602-609
    • Eichhorst, S.T.1    Krueger, A.2    Muerkoster, S.3
  • 34
    • 0035153227 scopus 로고    scopus 로고
    • High sensitivity of Nrf2 knockout mice to acetaminophen hepatotoxicity associated with decreased expression of ARE-regulated drug metabolizing enzymes and antioxidant genes
    • Enomoto A, Itoh K, Nagayoshi E, et al. (2001). High sensitivity of Nrf2 knockout mice to acetaminophen hepatotoxicity associated with decreased expression of ARE-regulated drug metabolizing enzymes and antioxidant genes. Toxicol Sci, 59:169-77.
    • (2001) Toxicol Sci , vol.59 , pp. 169-177
    • Enomoto, A.1    Itoh, K.2    Nagayoshi, E.3
  • 35
    • 34247602670 scopus 로고    scopus 로고
    • Survival and apoptosis: A dysregulated balance in liver cancer
    • Fabregat I, Roncero C, Fernandez M. (2007). Survival and apoptosis: A dysregulated balance in liver cancer. Liver Int, 27:155-62.
    • (2007) Liver Int , vol.27 , pp. 155-162
    • Fabregat, I.1    Roncero, C.2    Fernandez, M.3
  • 36
    • 57149127008 scopus 로고    scopus 로고
    • Anti-TNF alpha agents in elderly patients with rheumatoid arthritis: A study of a group of 105 over sixty five year old patients
    • Filippini M, Bazzani C, Zingarelli S, et al. (2008). Anti-TNF alpha agents in elderly patients with rheumatoid arthritis: A study of a group of 105 over sixty five year old patients. Reumatismo, 60:41-9.
    • (2008) Reumatismo , vol.60 , pp. 41-49
    • Filippini, M.1    Bazzani, C.2    Zingarelli, S.3
  • 37
    • 0027494395 scopus 로고
    • Calpain-catalyzed cleavage and subcellular relocation of protein phosphotyrosine phosphatase1B (PTP1B) in human platelets
    • Frangioni JV, Oda A, Smith M, et al. (1993). Calpain-catalyzed cleavage and subcellular relocation of protein phosphotyrosine phosphatase1B (PTP1B) in human platelets. EMBO J, 12:4843-56.
    • (1993) EMBO J , vol.12 , pp. 4843-4856
    • Frangioni, J.V.1    Oda, A.2    Smith, M.3
  • 38
    • 11144264663 scopus 로고    scopus 로고
    • BTB protein Keap1 targets antioxidant transcription factor Nrf2 for ubiquitination by the Cullin 3-Roc1 ligase
    • Furukawa M, Xiong Y. (2005). BTB protein Keap1 targets antioxidant transcription factor Nrf2 for ubiquitination by the Cullin 3-Roc1 ligase. Mol Cell Biol, 25:162-71.
    • (2005) Mol Cell Biol , vol.25 , pp. 162-171
    • Furukawa, M.1    Xiong, Y.2
  • 39
    • 0141750416 scopus 로고    scopus 로고
    • BTB/POZ domain proteins are putative substrate adaptors for cullin 3 ubiquitin ligases
    • Geyer R, Wee S, Anderson S, et al. (2003). BTB/POZ domain proteins are putative substrate adaptors for cullin 3 ubiquitin ligases. Mol Cell, 12:783-90.
    • (2003) Mol Cell , vol.12 , pp. 783-790
    • Geyer, R.1    Wee, S.2    Anderson, S.3
  • 40
    • 57649155739 scopus 로고    scopus 로고
    • Protection of acetaminophen induced mitochondrial dysfunctions and hepatic necrosis via Akt-NF-kappaB pathway: Role of a novel plant protein
    • Ghosh A, Sil PC. (2009). Protection of acetaminophen induced mitochondrial dysfunctions and hepatic necrosis via Akt-NF-kappaB pathway: Role of a novel plant protein. Chem Biol Interact, 177: 96-106.
    • (2009) Chem Biol Interact , vol.177 , pp. 96-106
    • Ghosh, A.1    Sil, P.C.2
  • 41
    • 0019764108 scopus 로고
    • Formation of chemically reactive metabolites of phenacetin and acetaminophen
    • Gillette JR, Nelson SD, Mulder GJ, et al. (1981). Formation of chemically reactive metabolites of phenacetin and acetaminophen. Adv Exp Med Biol, 136:931-50.
    • (1981) Adv Exp Med Biol , vol.136 , pp. 931-950
    • Gillette, J.R.1    Nelson, S.D.2    Mulder, G.J.3
  • 42
    • 34249879291 scopus 로고    scopus 로고
    • Levels of protein tyrosine phosphatase 1B determine susceptibility to apoptosis in serum-deprived hepatocytes
    • González-Rodr?́guez A, Escribano O, Alba J, et al. (2007). Levels of protein tyrosine phosphatase 1B determine susceptibility to apoptosis in serum-deprived hepatocytes. J Cell Physiol, 212:76-88.
    • (2007) J Cell Physiol , vol.212 , pp. 76-88
    • González-Rodŕguez, A.1    Escribano, O.2    Alba, J.3
  • 43
    • 2942529066 scopus 로고    scopus 로고
    • Reactive oxygen species in immune responses
    • Grisham MB. (2004). Reactive oxygen species in immune responses. Free Radic Biol Med, 36:1479-80.
    • (2004) Free Radic Biol Med , vol.36 , pp. 1479-1480
    • Grisham, M.B.1
  • 44
    • 33745758229 scopus 로고    scopus 로고
    • C-Jun N-terminal kinase plays a major role in murine acetaminophen hepatotoxicity
    • Gunawan BK, Liu ZX, Han D, et al. (2006). c-Jun N-terminal kinase plays a major role in murine acetaminophen hepatotoxicity. Gastroenterology, 131:165-78.
    • (2006) Gastroenterology , vol.131 , pp. 165-178
    • Gunawan, B.K.1    Liu, Z.X.2    Han, D.3
  • 45
    • 16244365903 scopus 로고    scopus 로고
    • Redox modulation of vascular tone: Focus of potassium channel mechanisms of dilation
    • Gutterman DD, Miura H, Liu Y. (2005). Redox modulation of vascular tone: Focus of potassium channel mechanisms of dilation. Arterioscler Thromb Vasc Biol, 25:671-8.
    • (2005) Arterioscler Thromb Vasc Biol , vol.25 , pp. 671-678
    • Gutterman, D.D.1    Miura, H.2    Liu, Y.3
  • 46
    • 0036500994 scopus 로고    scopus 로고
    • Imaging sites of receptor dephosphorylation by PTP1B on the surface of the endoplasmic reticulum
    • Haj FG, Verveer PJ, Squire A, et al. (2002). Imaging sites of receptor dephosphorylation by PTP1B on the surface of the endoplasmic reticulum. Science, 295:1708-11.
    • (2002) Science , vol.295 , pp. 1708-1711
    • Haj, F.G.1    Verveer, P.J.2    Squire, A.3
  • 47
    • 68949213938 scopus 로고    scopus 로고
    • Redox regulation of tumor necrosis factor signalling
    • Han D, Ybanez MD, Ahmadi S, et al. (2009). Redox regulation of tumor necrosis factor signalling. Antioxid Redox Signal, 11:2245-63.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 2245-2263
    • Han, D.1    Ybanez, M.D.2    Ahmadi, S.3
  • 48
    • 77949328370 scopus 로고    scopus 로고
    • Signal transduction pathways involved in drug-induced liver injury
    • Han D, Shinohara M, Ybanez MD, et al. (2010). Signal transduction pathways involved in drug-induced liver injury. Handb Exp Pharmacol, 196:267-310.
    • (2010) Handb Exp Pharmacol , vol.196 , pp. 267-310
    • Han, D.1    Shinohara, M.2    Ybanez, M.D.3
  • 49
    • 46649084880 scopus 로고    scopus 로고
    • Role of JNK translocation to mitochondria leading to inhibition of mitochondria bioenergetics in acetaminophen-induced liver injury
    • Hanawa N, Shinohara M, Saberi B, et al. (2008). Role of JNK translocation to mitochondria leading to inhibition of mitochondria bioenergetics in acetaminophen-induced liver injury. J Biol Chem, 283:13565-77.
    • (2008) J Biol Chem , vol.283 , pp. 13565-13577
    • Hanawa, N.1    Shinohara, M.2    Saberi, B.3
  • 50
    • 80053476859 scopus 로고    scopus 로고
    • Conformation-sensing antibodies stabilize the oxidized form of PTP1B and inhibit its phosphatase activity
    • Haque A, Andersen JN, Salmeen A, et al. (2011). Conformation-sensing antibodies stabilize the oxidized form of PTP1B and inhibit its phosphatase activity. Cell, 147:185-98.
    • (2011) Cell , vol.147 , pp. 185-198
    • Haque, A.1    Andersen, J.N.2    Salmeen, A.3
  • 51
    • 63549121490 scopus 로고    scopus 로고
    • Nrf2 and KEAP1 mutations: Permanent activation of an adaptive response in cancer
    • Hayes JD, McMahon M. (2009). Nrf2 and KEAP1 mutations: Permanent activation of an adaptive response in cancer. Trends Biochem Sci, 34: 176-88.
    • (2009) Trends Biochem Sci , vol.34 , pp. 176-188
    • Hayes, J.D.1    McMahon, M.2
  • 52
    • 34347234591 scopus 로고    scopus 로고
    • Critical role of c-jun (NH2) terminal kinase in paracetamol- induced acute liver failure
    • Henderson NC, Pollock KJ, Frew J, et al. (2007). Critical role of c-jun (NH2) terminal kinase in paracetamol- induced acute liver failure. Gut, 56:982-90.
    • (2007) Gut , vol.56 , pp. 982-990
    • Henderson, N.C.1    Pollock, K.J.2    Frew, J.3
  • 53
    • 0034656849 scopus 로고    scopus 로고
    • Reactive oxygen species, cell signalling, and cell injury
    • Hensley K, Robinson KA, Gabbita SP, et al. (2000). Reactive oxygen species, cell signalling, and cell injury. Free Radic Biol Med, 15: 1456-62.
    • (2000) Free Radic Biol Med , vol.15 , pp. 1456-1462
    • Hensley, K.1    Robinson, K.A.2    Gabbita, S.P.3
  • 54
    • 33646800165 scopus 로고    scopus 로고
    • ER-bound PTP1B is targeted to newly forming cell-matrix adhesions
    • Hernandez MV, Sala MG, Balsamo J, et al. (2006). ER-bound PTP1B is targeted to newly forming cell-matrix adhesions. J Cell Sci, 119: 1233-43.
    • (2006) J Cell Sci , vol.119 , pp. 1233-1243
    • Hernandez, M.V.1    Sala, M.G.2    Balsamo, J.3
  • 55
    • 0642375804 scopus 로고    scopus 로고
    • Chromosomal DNA fragmentation in apoptosis and necrosis induced by oxidative stress
    • Higuchi Y. (2003). Chromosomal DNA fragmentation in apoptosis and necrosis induced by oxidative stress. Biochem Pharmacol, 66: 1527-35.
    • (2003) Biochem Pharmacol , vol.66 , pp. 1527-1535
    • Higuchi, Y.1
  • 56
    • 0018965180 scopus 로고
    • 3-Hydroxyacetaminophen: A microsomal metabolite of acetaminophen. Evidence against an epoxide as the reactive metabolite of acetaminophen
    • Hinson JA, Pohl LR, Monks TJ, et al. (1980). 3-Hydroxyacetaminophen: A microsomal metabolite of acetaminophen. Evidence against an epoxide as the reactive metabolite of acetaminophen. Drug Metab Dispos, 8:289-94.
    • (1980) Drug Metab Dispos , vol.8 , pp. 289-294
    • Hinson, J.A.1    Pohl, L.R.2    Monks, T.J.3
  • 57
    • 0036908855 scopus 로고    scopus 로고
    • Protein kinase Cmediated desmin phosphorylation is related to myofibril disarray in cardiomyopathic hamster heart
    • Huang X, Li J, Foster D, Lemanski SL, et al. (2002). Protein kinase Cmediated desmin phosphorylation is related to myofibril disarray in cardiomyopathic hamster heart. Exp Biol Med, 227:1039-46.
    • (2002) Exp Biol Med , vol.227 , pp. 1039-1046
    • Huang, X.1    Li, J.2    Foster, D.3    Lemanski, S.L.4
  • 58
    • 70350743128 scopus 로고    scopus 로고
    • Reactive oxygen species (ROS) are essential mediators in epidermal growth factor (EGF)-stimulated corneal epithelial cell proliferation, adhesion, migration, and wound healing
    • Huo Y, Qiu WY, Pan Q, et al. (2009). Reactive oxygen species (ROS) are essential mediators in epidermal growth factor (EGF)-stimulated corneal epithelial cell proliferation, adhesion, migration, and wound healing. Exp Eye Res, 89:876-86.
    • (2009) Exp Eye Res , vol.89 , pp. 876-886
    • Huo, Y.1    Qiu, W.Y.2    Pan, Q.3
  • 59
    • 0028118492 scopus 로고
    • Regulation of transcription by dimerization of erythroid factor NF-E2 p45 with small Maf proteins
    • Igarashi K, Kataoka K, Itoh K, et al. (1994). Regulation of transcription by dimerization of erythroid factor NF-E2 p45 with small Maf proteins. Nature, 367:568-72.
    • (1994) Nature , vol.367 , pp. 568-572
    • Igarashi, K.1    Kataoka, K.2    Itoh, K.3
  • 60
    • 0025719104 scopus 로고
    • In vivo protein-DNA interactions at the betaglobin gene locus
    • Ikuta T, Kan YW. (1991). In vivo protein-DNA interactions at the betaglobin gene locus. Proc Natl Acad Sci USA, 88:10188-92.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 10188-10192
    • Ikuta, T.1    Kan, Y.W.2
  • 61
    • 0037438730 scopus 로고    scopus 로고
    • Biological significance of phospholipid hydroperoxide glutathione peroxidase (PHGPx, GPx4) in mammalian cells
    • Imai H, Nakagawa Y. (2003). Biological significance of phospholipid hydroperoxide glutathione peroxidase (PHGPx, GPx4) in mammalian cells. Free Radic Biol Med, 34:145-69.
    • (2003) Free Radic Biol Med , vol.34 , pp. 145-169
    • Imai, H.1    Nakagawa, Y.2
  • 62
    • 0031577292 scopus 로고    scopus 로고
    • An Nrf2/small Maf heterodimer mediates the induction of phase II detoxifying enzyme genes through antioxidant response elements
    • Itoh K, Chiba T, Takahashi S, et al. (1997). An Nrf2/small Maf heterodimer mediates the induction of phase II detoxifying enzyme genes through antioxidant response elements. Biochem Biophys Res Commun, 236:313-22.
    • (1997) Biochem Biophys Res Commun , vol.236 , pp. 313-322
    • Itoh, K.1    Chiba, T.2    Takahashi, S.3
  • 63
    • 0032953192 scopus 로고    scopus 로고
    • Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain
    • Itoh K, Wakabayashi N, Katoh Y, et al. (1999). Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain. Genes Dev, 13:76-86.
    • (1999) Genes Dev , vol.13 , pp. 76-86
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3
  • 64
    • 1942455887 scopus 로고    scopus 로고
    • Molecular mechanism activating Nrf2-Keap1 pathway in regulation of adaptive response to electrophiles
    • Itoh K, Tong KI, Yamamoto M. (2004). Molecular mechanism activating Nrf2-Keap1 pathway in regulation of adaptive response to electrophiles. Free Radic Biol Med, 15:1208-13.
    • (2004) Free Radic Biol Med , vol.15 , pp. 1208-1213
    • Itoh, K.1    Tong, K.I.2    Yamamoto, M.3
  • 65
    • 29544448331 scopus 로고    scopus 로고
    • Intracellular signalling mechanisms of acetaminophen-induced liver cell death
    • Jaeschke H, Bajt ML. (2006). Intracellular signalling mechanisms of acetaminophen-induced liver cell death. Toxicol Sci, 89:31-41.
    • (2006) Toxicol Sci , vol.89 , pp. 31-41
    • Jaeschke, H.1    Bajt, M.L.2
  • 66
    • 34447526197 scopus 로고    scopus 로고
    • GSK-3beta acts upstream of Fyn kinase in regulation of nuclear export and degradation of NF-E2 related factor 2
    • Jain AK, Jaiswal AK. (2007). GSK-3beta acts upstream of Fyn kinase in regulation of nuclear export and degradation of NF-E2 related factor 2. J Biol Chem, 282:16502-10.
    • (2007) J Biol Chem , vol.282 , pp. 16502-16510
    • Jain, A.K.1    Jaiswal, A.K.2
  • 68
    • 34547164540 scopus 로고    scopus 로고
    • The c-jun kinase/stress-activated pathway: Regulation, function and role in human disease
    • Johnson GL, Nakamura K. (2007). The c-jun kinase/stress-activated pathway: Regulation, function and role in human disease. Biochim Biophys Acta, 1773:1341-8.
    • (2007) Biochim Biophys Acta , vol.1773 , pp. 1341-1348
    • Johnson, G.L.1    Nakamura, K.2
  • 69
    • 0015754446 scopus 로고
    • Acetaminopheninduced hepatic necrosis II. Role of covalent binding in vivo
    • Jollow DJ, Mitchell JR, Potter WZ, et al. (1973). Acetaminopheninduced hepatic necrosis. II. Role of covalent binding in vivo. J Pharmacol Exp Ther, 187:195-202.
    • (1973) J Pharmacol Exp Ther , vol.187 , pp. 195-202
    • Jollow, D.J.1    Mitchell, J.R.2    Potter, W.Z.3
  • 70
    • 0016151122 scopus 로고
    • Bromobenzene-induced liver necrosis Protective role of glutathione and evidence for 3,4-bromobenzene oxide as the hepatotoxic metabolite
    • Jollow DJ, Mitchell JR, Zampaglione N, Gillette JR. (1974). Bromobenzene-induced liver necrosis. Protective role of glutathione and evidence for 3,4-bromobenzene oxide as the hepatotoxic metabolite. Pharmacology, 11:151-69.
    • (1974) Pharmacology , vol.11 , pp. 151-169
    • Jollow, D.J.1    Mitchell, J.R.2    Zampaglione, N.3    Gillette, J.R.4
  • 71
    • 1242274394 scopus 로고    scopus 로고
    • Scaffolding of Keap1 to the actin cytoskeleton controls the function of Nrf2 as key regulator of cytoprotective phase 2 genes
    • Kang MI, Kobayashi A, Wakabayashi N, et al. (2004). Scaffolding of Keap1 to the actin cytoskeleton controls the function of Nrf2 as key regulator of cytoprotective phase 2 genes. Proc Natl Acad Sci USA, 101:2046-51.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 2046-2051
    • Kang, M.I.1    Kobayashi, A.2    Wakabayashi, N.3
  • 72
    • 3042826208 scopus 로고    scopus 로고
    • Acetaminophen hepatoxicity: What do we know, what don't we know, and what do we do next?
    • Kaplowitz N. (2004). Acetaminophen hepatoxicity: What do we know, what don't we know, and what do we do next? Hepatology, 40:23-6.
    • (2004) Hepatology , vol.40 , pp. 23-26
    • Kaplowitz, N.1
  • 73
    • 20844444779 scopus 로고    scopus 로고
    • Idiosyncratic drug hepatotoxicity
    • Kaplowitz N. (2005). Idiosyncratic drug hepatotoxicity. Nat Rev Drug Discov, 4:489-99.
    • (2005) Nat Rev Drug Discov , vol.4 , pp. 489-499
    • Kaplowitz, N.1
  • 74
    • 53049104963 scopus 로고    scopus 로고
    • How to protect against acetaminophen: Don't ask for JUNK
    • Kaplowitz N, Shinohara M, Liu ZX, Han D. (2008). How to protect against acetaminophen: Don't ask for JUNK. Gastroenterology, 135: 1047-51.
    • (2008) Gastroenterology , vol.135 , pp. 1047-1051
    • Kaplowitz, N.1    Shinohara, M.2    Liu, Z.X.3    Han, D.4
  • 75
    • 70349843323 scopus 로고    scopus 로고
    • Nrf2:INrf2 (Keap1) signalling in oxidative stress
    • Kaspar JW, Niture SK, Jaiswal AK. (2009). Nrf2:INrf2 (Keap1) signalling in oxidative stress. Free Rad Biol Med, 47:1304-9.
    • (2009) Free Rad Biol Med , vol.47 , pp. 1304-1309
    • Kaspar, J.W.1    Niture, S.K.2    Jaiswal, A.K.3
  • 76
    • 0034752461 scopus 로고    scopus 로고
    • Two domains of Nrf2 cooperatively bind CBP, a CREB binding protein, and synergistically activate transcription
    • Katoh Y, Itoh K, Yoshida E, et al. (2001). Two domains of Nrf2 cooperatively bind CBP, a CREB binding protein, and synergistically activate transcription. Genes Cells, 6:857-68.
    • (2001) Genes Cells , vol.6 , pp. 857-868
    • Katoh, Y.1    Itoh, K.2    Yoshida, E.3
  • 77
    • 0033525730 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of a new Cap'n' collar family transcription factor Nrf3
    • Kobayashi A, Ito E, Toki T, et al. (1999). Molecular cloning and functional characterization of a new Cap'n' collar family transcription factor Nrf3. J Biol Chem, 274:6443-52.
    • (1999) J Biol Chem , vol.274 , pp. 6443-6452
    • Kobayashi, A.1    Ito, E.2    Toki, T.3
  • 78
    • 3543008924 scopus 로고    scopus 로고
    • Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2
    • Kobayashi A, Kang MI, Okawa H, et al. (2004). Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2. Mol Cell Biol, 24:7130-9.
    • (2004) Mol Cell Biol , vol.24 , pp. 7130-7139
    • Kobayashi, A.1    Kang, M.I.2    Okawa, H.3
  • 79
    • 33344469643 scopus 로고    scopus 로고
    • Oxidative and electrophilic stresses activate Nrf2 through inhibition of ubiquitination activity of Keap1
    • Kobayashi A, Kang MI, Watai Y, et al. (2006). Oxidative and electrophilic stresses activate Nrf2 through inhibition of ubiquitination activity of Keap1. Mol Cell Biol, 26:221-9.
    • (2006) Mol Cell Biol , vol.26 , pp. 221-229
    • Kobayashi, A.1    Kang, M.I.2    Watai, Y.3
  • 80
    • 34548258220 scopus 로고    scopus 로고
    • Double knockouts reveal that protein tyrosine phosphatase 1B is a physiological target of calpain-1 in platelets
    • Kuchay SM, Kim N, Grunz EA, et al. (2007). Double knockouts reveal that protein tyrosine phosphatase 1B is a physiological target of calpain-1 in platelets. Mol Cell Biol, 27:6038-52.
    • (2007) Mol Cell Biol , vol.27 , pp. 6038-6052
    • Kuchay, S.M.1    Kim, N.2    Grunz, E.A.3
  • 81
    • 0037507299 scopus 로고    scopus 로고
    • NADPH oxidase AtrbohD and AtrbohF genes function in ROS-dependent ABA signalling in Arabidopsis
    • Kwak JM, Mori IC, Pei ZM, et al. (2003). NADPH oxidase AtrbohD and AtrbohF genes function in ROS-dependent ABA signalling in Arabidopsis. EMBO J, 22:2623-33.
    • (2003) EMBO J , vol.22 , pp. 2623-2633
    • Kwak, J.M.1    Mori, I.C.2    Pei, Z.M.3
  • 82
    • 0035260034 scopus 로고    scopus 로고
    • Role of transcription factor Nrf2 in the induction of hepatic phase 2 and antioxidative enzymes in vivo by the cancer chemoprotective agent, 3H-1, 2-dimethiole-3-thione
    • Kwak MK, Itoh K, Yamamoto M, et al. (2001). Role of transcription factor Nrf2 in the induction of hepatic phase 2 and antioxidative enzymes in vivo by the cancer chemoprotective agent, 3H-1, 2-dimethiole-3-thione. Mol Med, 7:135-45.
    • (2001) Mol Med , vol.7 , pp. 135-145
    • Kwak, M.K.1    Itoh, K.2    Yamamoto, M.3
  • 83
    • 0038433303 scopus 로고    scopus 로고
    • J und mediates survival signalling by the JNK signal transduction pathway
    • Lamb JA, Ventura JJ, Hess P, et al. (2003). J unD mediates survival signalling by the JNK signal transduction pathway. Mol Cell, 11: 1479-89.
    • (2003) Mol Cell , vol.11 , pp. 1479-1489
    • Lamb, J.A.1    Ventura, J.J.2    Hess, P.3
  • 84
    • 32644474169 scopus 로고    scopus 로고
    • Acetaminophen-induced acute liver failure: Results of a United States multicenter, prospective study
    • Larson AM, Polson J, Fontana RJ, et al. (2005). Acetaminophen-induced acute liver failure: Results of a United States multicenter, prospective study. Hepatology, 42:1364-72.
    • (2005) Hepatology , vol.42 , pp. 1364-1372
    • Larson, A.M.1    Polson, J.2    Fontana, R.J.3
  • 85
    • 33847750361 scopus 로고    scopus 로고
    • Mitochondrial protection by the JNK inhibitor leflunomide rescues mice from acetaminophen-induced liver injury
    • Latchoumycandane C, Goh CW, Ong MM, Boelsterli UA. (2007). Mitochondrial protection by the JNK inhibitor leflunomide rescues mice from acetaminophen-induced liver injury. Hepatology, 45: 412-21.
    • (2007) Hepatology , vol.45 , pp. 412-421
    • Latchoumycandane, C.1    Goh, C.W.2    Ong, M.M.3    Boelsterli, U.A.4
  • 86
    • 3042738919 scopus 로고    scopus 로고
    • Acetaminophen and the U.S. Acute Liver Failure Study Group: Lowering the risks of hepatic failure
    • Lee WM. (2004). Acetaminophen and the U.S. Acute Liver Failure Study Group: Lowering the risks of hepatic failure. Hepatology, 40: 6-9.
    • (2004) Hepatology , vol.40 , pp. 6-9
    • Lee, W.M.1
  • 87
    • 36349004846 scopus 로고    scopus 로고
    • Acetaminophen toxicity: Changing perceptions on a social/medical issue
    • Lee WM. (2007). Acetaminophen toxicity: Changing perceptions on a social/medical issue. Hepatology, 46:966-70.
    • (2007) Hepatology , vol.46 , pp. 966-970
    • Lee, W.M.1
  • 88
    • 11144244006 scopus 로고    scopus 로고
    • Crystal structure of the Kelch domain of human Keap1
    • Li X, Zhang D, Hannink M, Beamer LJ. (2004). Crystal structure of the Kelch domain of human Keap1. J Biol Chem, 24:54750-8.
    • (2004) J Biol Chem , vol.24 , pp. 54750-54758
    • Li, X.1    Zhang, D.2    Hannink, M.3    Beamer, L.J.4
  • 89
    • 0036009411 scopus 로고    scopus 로고
    • NF-kappaB inhibition sensitizes hepatocytes to TNF-induced apoptosis through a sustained activation of JNK and c-Jun
    • Liu H, Lo CR, Czaja MJ. (2002). NF-kappaB inhibition sensitizes hepatocytes to TNF-induced apoptosis through a sustained activation of JNK and c-Jun. Hepatology, 35:772-8.
    • (2002) Hepatology , vol.35 , pp. 772-778
    • Liu, H.1    Lo, C.R.2    Czaja, M.J.3
  • 90
    • 84867847425 scopus 로고    scopus 로고
    • Acetaminophen-induced liver injury in rats and mice: Comparison of protein adducts mitochondrial dysfunction, and oxidative stress in the mechanism of toxicity
    • McGill MR, Williams CD, Xie Y, et al. (2012). Acetaminophen-induced liver injury in rats and mice: Comparison of protein adducts mitochondrial dysfunction, and oxidative stress in the mechanism of toxicity. Toxicol Appl Pharmacol, 264:387-94.
    • (2012) Toxicol Appl Pharmacol , vol.264 , pp. 387-394
    • McGill, M.R.1    Williams, C.D.2    Xie, Y.3
  • 92
    • 3843104763 scopus 로고    scopus 로고
    • Redox-regulated turnover of Nrf2 is determined by at least two separate protein domains, the redox-sensitive Neh2 degron and the redox-insensitive Neh6 degron
    • McMahon M, Thomas N, Itoh K, et al. (2004). Redox-regulated turnover of Nrf2 is determined by at least two separate protein domains, the redox-sensitive Neh2 degron and the redox-insensitive Neh6 degron. J Biol Chem, 279:31556-67.
    • (2004) J Biol Chem , vol.279 , pp. 31556-31567
    • McMahon, M.1    Thomas, N.2    Itoh, K.3
  • 93
    • 0345528139 scopus 로고    scopus 로고
    • Analysis of the regulation of protein tyrosine phosphatases in vivo by reversible oxidation
    • Meng TC, Tonks NK. (2003). Analysis of the regulation of protein tyrosine phosphatases in vivo by reversible oxidation. Methods Enzymol, 366:304-18.
    • (2003) Methods Enzymol , vol.366 , pp. 304-318
    • Meng, T.C.1    Tonks, N.K.2
  • 95
    • 0015733053 scopus 로고
    • Acetaminopheninduced hepatic necrosis IV. Protective role of glutathione
    • Mitchell JR, Jollow DJ, Potter WZ, et al. (1973b). Acetaminopheninduced hepatic necrosis. IV. Protective role of glutathione. J Pharmacol Exp Ther, 187:211-17.
    • (1973) J Pharmacol Exp Ther , vol.187 , pp. 211-217
    • Mitchell, J.R.1    Jollow, D.J.2    Potter, W.Z.3
  • 96
    • 84879407019 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase 1B modulates GSK3beta/Nrf2 and IGFIR signalling pathways in acetaminophen-induced hepatotoxicity
    • Mobasher MA, González-Rodr?́guez A, Santamaria B, et al. (2013). Protein tyrosine phosphatase 1B modulates GSK3beta/Nrf2 and IGFIR signalling pathways in acetaminophen-induced hepatotoxicity. Cell Death Dis, 4:1-13.
    • (2013) Cell Death Dis , vol.4 , pp. 1-13
    • Mobasher, M.A.1    González-Rodŕguez, A.2    Santamaria, B.3
  • 97
    • 0025242796 scopus 로고
    • Synergistic enhancement of globin gene expression by activator protein-1-like proteins
    • Moi P, Kan YW. (1990). Synergistic enhancement of globin gene expression by activator protein-1-like proteins. Proc Natl Acad Sci USA, 87:9000-4.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 9000-9004
    • Moi, P.1    Kan, Y.W.2
  • 98
    • 0028061444 scopus 로고
    • Isolation of NF-E2-related factor 2 (Nrf2), a NF-E2-like basic leucine zipper transcriptional activator that binds to the tandem NF-E2/AP1 repeat of the beta-globin locus control region
    • Moi P, Chan K, Asunis I, et al. (1994). Isolation of NF-E2-related factor 2 (Nrf2), a NF-E2-like basic leucine zipper transcriptional activator that binds to the tandem NF-E2/AP1 repeat of the beta-globin locus control region. Proc Natl Acad Sci USA, 91:9926-30.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 9926-9930
    • Moi, P.1    Chan, K.2    Asunis, I.3
  • 99
    • 0032189224 scopus 로고    scopus 로고
    • Identification of Bach2 as a B-cell-specific partner for small maf proteins that negatively regulate the immunoglobulin heavy chain gene 30 enhancer
    • Muto A, Hoshino H, Madisen L, et al. (1998). Identification of Bach2 as a B-cell-specific partner for small maf proteins that negatively regulate the immunoglobulin heavy chain gene 30 enhancer. EMBO J, 17:5734-43.
    • (1998) EMBO J , vol.17 , pp. 5734-5743
    • Muto, A.1    Hoshino, H.2    Madisen, L.3
  • 100
    • 53049105071 scopus 로고    scopus 로고
    • Deletion of apoptosis signal-regulating kinase 1 attenuates acetaminophen-induced liver injury by inhibiting c-Jun N-terminal kinase activation
    • Nakagawa H, Maeda S, Hikiba Y, et al. (2008). Deletion of apoptosis signal-regulating kinase 1 attenuates acetaminophen-induced liver injury by inhibiting c-Jun N-terminal kinase activation. Gastroenterology, 135:1311-21.
    • (2008) Gastroenterology , vol.135 , pp. 1311-1321
    • Nakagawa, H.1    Maeda, S.2    Hikiba, Y.3
  • 101
    • 0013282861 scopus 로고    scopus 로고
    • Increased protein stability as a mechanism that enhances Nrf2-mediated transcriptional activation of the antioxidant response element Degradation of Nrf2 by the 26 S proteasome
    • Nguyen T, Sherratt PJ, Huang HC, et al. (2003). Increased protein stability as a mechanism that enhances Nrf2-mediated transcriptional activation of the antioxidant response element. Degradation of Nrf2 by the 26 S proteasome. J Biol Chem, 278:4536-41.
    • (2003) J Biol Chem , vol.278 , pp. 4536-4541
    • Nguyen, T.1    Sherratt, P.J.2    Huang, H.C.3
  • 102
    • 28544450507 scopus 로고    scopus 로고
    • The carboxy-terminal Neh3 domain of Nrf2 is required for transcriptional activation
    • Nioi P, Nguyen T, Sherratt PJ, Pickett CB. (2005). The carboxy-terminal Neh3 domain of Nrf2 is required for transcriptional activation. Mol Cell Biol, 25:10895-906.
    • (2005) Mol Cell Biol , vol.25 , pp. 10895-10906
    • Nioi, P.1    Nguyen, T.2    Sherratt, P.J.3    Pickett, C.B.4
  • 103
    • 67649415378 scopus 로고    scopus 로고
    • Prothymosin-alpha mediates nuclear import of the INrf2/Cul3 Rbx1 complex to degrade nuclear Nrf2
    • Niture SK, Jaiswal AK. (2009). Prothymosin-alpha mediates nuclear import of the INrf2/Cul3 Rbx1 complex to degrade nuclear Nrf2. J Biol Chem, 284:13856-68.
    • (2009) J Biol Chem , vol.284 , pp. 13856-13868
    • Niture, S.K.1    Jaiswal, A.K.2
  • 104
    • 80051690439 scopus 로고    scopus 로고
    • Src subfamily kinases regulate nuclear export and degradation of transcription factor Nrf2 to switch off Nrf2-mediated antioxidant activation of cytoprotective gene expression
    • Niture SK, Jain AK, Shelton PM, Jaiswal AK. (2011). Src subfamily kinases regulate nuclear export and degradation of transcription factor Nrf2 to switch off Nrf2-mediated antioxidant activation of cytoprotective gene expression. J Biol Chem, 286:28821-32.
    • (2011) J Biol Chem , vol.286 , pp. 28821-28832
    • Niture, S.K.1    Jain, A.K.2    Shelton, P.M.3    Jaiswal, A.K.4
  • 105
    • 0035034541 scopus 로고    scopus 로고
    • Apoptosis and liver diseases: Recent concepts of mechanism and significance
    • Ockner RK. (2001). Apoptosis and liver diseases: Recent concepts of mechanism and significance. J Gastroenterol Hepatol, 16: 248-60.
    • (2001) J Gastroenterol Hepatol , vol.16 , pp. 248-260
    • Ockner, R.K.1
  • 106
    • 84860850926 scopus 로고    scopus 로고
    • Protein-tyrosine Phosphatase 1B (PTP1B) Deficiency confers resistance to transforming growth factor-beta (TGF-beta)-induced suppressor effects in hepatocytes
    • Ortiz C, Caja L, Bertran E, et al. (2012). Protein-tyrosine Phosphatase 1B (PTP1B) Deficiency confers resistance to transforming growth factor-beta (TGF-beta)-induced suppressor effects in hepatocytes. J Biol Chem, 287:15263-74.
    • (2012) J Biol Chem , vol.287 , pp. 15263-15274
    • Ortiz, C.1    Caja, L.2    Bertran, E.3
  • 107
    • 0037126649 scopus 로고    scopus 로고
    • Results of a prospective study of acute liver failure at 17 tertiary care centers in the United States
    • Ostapowicz G, Fontana RJ, Schiodt FV, et al. (2002). Results of a prospective study of acute liver failure at 17 tertiary care centers in the United States. Ann Intern Med, 137:947-54.
    • (2002) Ann Intern Med , vol.137 , pp. 947-954
    • Ostapowicz, G.1    Fontana, R.J.2    Schiodt, F.V.3
  • 108
    • 0029805130 scopus 로고    scopus 로고
    • Bach proteins belong to a novel family of BTB-basic leucine zipper transcription factors that interact with MafK and regulate transcription through the NF-E2 site
    • Oyake T, Itoh K, Motohashi H, et al. (1996). Bach proteins belong to a novel family of BTB-basic leucine zipper transcription factors that interact with MafK and regulate transcription through the NF-E2 site. Mol Cell Biol, 16:6083-95.
    • (1996) Mol Cell Biol , vol.16 , pp. 6083-6095
    • Oyake, T.1    Itoh, K.2    Motohashi, H.3
  • 109
    • 0033611564 scopus 로고    scopus 로고
    • Differential expression and translocation of protein tyrosine phosphatase 1B-related proteins in ME-180 tumor cells expressing apoptotic sensitivity and resistance to tumor necrosis factor: Potential interaction with epidermal growth factor receptor
    • Perez M, Haschke B, Donato NJ. (1999). Differential expression and translocation of protein tyrosine phosphatase 1B-related proteins in ME-180 tumor cells expressing apoptotic sensitivity and resistance to tumor necrosis factor: Potential interaction with epidermal growth factor receptor. Oncogene, 18:967-78.
    • (1999) Oncogene , vol.18 , pp. 967-978
    • Perez, M.1    Haschke, B.2    Donato, N.J.3
  • 110
    • 0017714304 scopus 로고
    • Treating acute acetaminophen poisoning with acetylcysteine
    • Peterson RG, Rumack BH. (1977). Treating acute acetaminophen poisoning with acetylcysteine. JAMA, 237:2406-7.
    • (1977) JAMA , vol.237 , pp. 2406-2407
    • Peterson, R.G.1    Rumack, B.H.2
  • 111
    • 0017084677 scopus 로고
    • Reversal of experimental paracetamol toxicosis with N-acetylcysteine
    • Piperno E, Berssenbruegge DA. (1976). Reversal of experimental paracetamol toxicosis with N-acetylcysteine. Lancet, 2:738-9.
    • (1976) Lancet , vol.2 , pp. 738-739
    • Piperno, E.1    Berssenbruegge, D.A.2
  • 112
    • 0023103693 scopus 로고
    • Mechanisms of acetaminophen oxidation to N-acetyl-P-benzoquinone imine by horseradish peroxidase and cytochrome P-450
    • Potter DW, Hinson JA. (1987). Mechanisms of acetaminophen oxidation to N-acetyl-P-benzoquinone imine by horseradish peroxidase and cytochrome P-450. J Biol Chem, 262:966-73.
    • (1987) J Biol Chem , vol.262 , pp. 966-973
    • Potter, D.W.1    Hinson, J.A.2
  • 113
    • 0015738695 scopus 로고
    • Acetaminopheninduced hepatic necrosis 3. Cytochrome P-450-mediated covalent binding in vitro
    • Potter WZ, Davis DC, Mitchell JR, et al. (1973). Acetaminopheninduced hepatic necrosis. 3. Cytochrome P-450-mediated covalent binding in vitro. J Pharmacol Exp Ther, 187:203-10.
    • (1973) J Pharmacol Exp Ther , vol.187 , pp. 203-210
    • Potter, W.Z.1    Davis, D.C.2    Mitchell, J.R.3
  • 114
    • 0017372818 scopus 로고
    • Iatrogenic complications of drug overdosage and poisoning
    • Prescott LF. (1977). Iatrogenic complications of drug overdosage and poisoning. Acta Pharmacol Toxicol, 41:2-64.
    • (1977) Acta Pharmacol Toxicol , vol.41 , pp. 2-64
    • Prescott, L.F.1
  • 115
    • 0019218676 scopus 로고
    • Hepatotoxicity of mild analgesics
    • Prescott LF. (1980). Hepatotoxicity of mild analgesics. Br J Clin Pharmacol, 2:373-9.
    • (1980) Br J Clin Pharmacol , vol.2 , pp. 373-379
    • Prescott, L.F.1
  • 116
    • 0020600559 scopus 로고
    • Paracetamol overdosage Pharmacological considerations and clinical management
    • Prescott LF. (1983). Paracetamol overdosage. Pharmacological considerations and clinical management. Drugs, 25:290-14.
    • (1983) Drugs , vol.25 , pp. 290-214
    • Prescott, L.F.1
  • 117
    • 79952256187 scopus 로고    scopus 로고
    • SCF/{beta}-TrCP promotes glycogen synthase kinase 3-dependent degradation of the Nrf2 transcription factor in a Keap1-independent manner
    • Rada P, Rojo AI, Chowdhry S, et al. (2011). SCF/{beta}-TrCP promotes glycogen synthase kinase 3-dependent degradation of the Nrf2 transcription factor in a Keap1-independent manner. Mol Cell Biol, 31:1121-33.
    • (2011) Mol Cell Biol , vol.31 , pp. 1121-1133
    • Rada, P.1    Rojo, A.I.2    Chowdhry, S.3
  • 118
    • 84866283856 scopus 로고    scopus 로고
    • Structural and functional characterization of Nrf2 degradation by the glycogen synthase kinase 3/b-TrCP axis
    • Rada P, Rojo AI, Evrard-Todeschi N, et al. (2012). Structural and functional characterization of Nrf2 degradation by the glycogen synthase kinase 3/b-TrCP axis. Mol Cell Biol, 32:3486-99.
    • (2012) Mol Cell Biol , vol.32 , pp. 3486-3499
    • Rada, P.1    Rojo, A.I.2    Evrard-Todeschi, N.3
  • 119
    • 67649221506 scopus 로고    scopus 로고
    • Histological patterns in drug-induced liver disease
    • Ramachandran R, Kakar S. (2009). Histological patterns in drug-induced liver disease. J Clin Pathol, 62:481-92.
    • (2009) J Clin Pathol , vol.62 , pp. 481-492
    • Ramachandran, R.1    Kakar, S.2
  • 120
    • 0024401849 scopus 로고
    • Acetaminophen activation by human liver cytochromes P450IIE1 and P450IA2
    • Raucy JL, Lasker JM, Lieber CS, Black M. (1989). Acetaminophen activation by human liver cytochromes P450IIE1 and P450IA2. Arch Biochem Biophys, 271:270-83.
    • (1989) Arch Biochem Biophys , vol.271 , pp. 270-283
    • Raucy, J.L.1    Lasker, J.M.2    Lieber, C.S.3    Black, M.4
  • 121
    • 0035793592 scopus 로고    scopus 로고
    • Protein kinase C-zeta phosphorylates insulin receptor substrate-1 and impairs its ability to activate phosphatidylinositol 3-kinase in response to insulin
    • Ravichandran LV, Esposito DL, Chen J, Quan MJ. (2001). Protein kinase C-zeta phosphorylates insulin receptor substrate-1 and impairs its ability to activate phosphatidylinositol 3-kinase in response to insulin. J Biol Chem, 276:3543-9.
    • (2001) J Biol Chem , vol.276 , pp. 3543-3549
    • Ravichandran, L.V.1    Esposito, D.L.2    Chen, J.3    Quan, M.J.4
  • 122
    • 13244292321 scopus 로고    scopus 로고
    • Mechanisms of acetaminophen-induced hepatotoxicity: Role of oxidative stress and mitochondrial permeability transition in freshly isolated mouse hepatocytes
    • Reid AB, Kurten RC, McCullough SS, et al. (2005). Mechanisms of acetaminophen-induced hepatotoxicity: Role of oxidative stress and mitochondrial permeability transition in freshly isolated mouse hepatocytes. J Pharmacol Exp Ther, 312:509-16.
    • (2005) J Pharmacol Exp Ther , vol.312 , pp. 509-516
    • Reid, A.B.1    Kurten, R.C.2    McCullough, S.S.3
  • 123
    • 0019430214 scopus 로고
    • Acetaminophen overdose 662 cases with evaluation of oral acetylcysteine treatment
    • Rumack BH, Peterson RC, Koch GG, Amara IA. (1981). Acetaminophen overdose. 662 cases with evaluation of oral acetylcysteine treatment. Arch Intern Med, 141:380-5.
    • (1981) Arch Intern Med , vol.141 , pp. 380-385
    • Rumack, B.H.1    Peterson, R.C.2    Koch, G.G.3    Amara, I.A.4
  • 124
    • 52749091386 scopus 로고    scopus 로고
    • Regulation of H(2)O(2)-induced necrosis by PKC and AMP-activated kinase signalling in primary cultured hepatocytes
    • Saberi B, Shinohara M, Ybanez MD, et al. (2008). Regulation of H(2)O(2)-induced necrosis by PKC and AMP-activated kinase signalling in primary cultured hepatocytes. Am J Physiol Cell Physiol, 295:50-63.
    • (2008) Am J Physiol Cell Physiol , vol.295 , pp. 50-63
    • Saberi, B.1    Shinohara, M.2    Ybanez, M.D.3
  • 125
    • 33744950387 scopus 로고    scopus 로고
    • Glycogen synthase kinase- 3beta inhibits the xenobiotic and antioxidant cell response by direct phosphorylation and nuclear exclusion of the transcription factor Nrf2
    • Salazar M, Rojo AI, Velasco D, et al. (2006). Glycogen synthase kinase- 3beta inhibits the xenobiotic and antioxidant cell response by direct phosphorylation and nuclear exclusion of the transcription factor Nrf2. J Biol Chem, 281:14841-51.
    • (2006) J Biol Chem , vol.281 , pp. 14841-14851
    • Salazar, M.1    Rojo, A.I.2    Velasco, D.3
  • 126
    • 33644858301 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase 1B deficiency protects against Fas-induced hepatic failure
    • Sangwan V, Paliouras GN, Cheng A, et al. (2006). Protein-tyrosine phosphatase 1B deficiency protects against Fas-induced hepatic failure. J Biol Chem, 281:221-8.
    • (2006) J Biol Chem , vol.281 , pp. 221-228
    • Sangwan, V.1    Paliouras, G.N.2    Cheng, A.3
  • 127
    • 33644813043 scopus 로고    scopus 로고
    • JNK1 but not JNK2 promotes the development of steatohepatitis in mice
    • Schattenberg JM, Singh R, Wang Y, et al. (2006). JNK1 but not JNK2 promotes the development of steatohepatitis in mice. Hepatology, 43: 163-72.
    • (2006) Hepatology , vol.43 , pp. 163-172
    • Schattenberg, J.M.1    Singh, R.2    Wang, Y.3
  • 128
  • 129
    • 84873469216 scopus 로고    scopus 로고
    • The transcription factor NF-E2-related factor 2 (Nrf2): A protooncogene
    • Shelton P, Jaiswal AK. (2013). The transcription factor NF-E2-related factor 2 (Nrf2): A protooncogene. FASEB J, 27:414-23.
    • (2013) FASEB J , vol.27 , pp. 414-423
    • Shelton, P.1    Jaiswal, A.K.2
  • 130
    • 39749180445 scopus 로고    scopus 로고
    • Tyrosine kinases Btk and Tec regulate osteoclast differentiation by linking RANK and ITAM signals
    • Shinohara M, Koga T, Okamoto K, et al. (2008). Tyrosine kinases Btk and Tec regulate osteoclast differentiation by linking RANK and ITAM signals. Cell, 132:794-806.
    • (2008) Cell , vol.132 , pp. 794-806
    • Shinohara, M.1    Koga, T.2    Okamoto, K.3
  • 131
    • 77950886196 scopus 로고    scopus 로고
    • Silencing glycogen synthase kinase-3beta inhibits acetaminophen hepatotoxicity and attenuates JNK activation and loss of glutamate cysteine ligase and myeloid cell leukemia sequence 1
    • Shinohara M, Ybanez MD, Win S, et al. (2010). Silencing glycogen synthase kinase-3beta inhibits acetaminophen hepatotoxicity and attenuates JNK activation and loss of glutamate cysteine ligase and myeloid cell leukemia sequence 1. J Biol Chem, 285:8244-55.
    • (2010) J Biol Chem , vol.285 , pp. 8244-8255
    • Shinohara, M.1    Ybanez, M.D.2    Win, S.3
  • 132
    • 0028015606 scopus 로고
    • Loss of CYP2E1 and CYP1A2 activity as a function of acetaminophen dose: Relation to toxicity
    • Snawder JE, Roe AL, Benson RW, Roberts DW. (1994). Loss of CYP2E1 and CYP1A2 activity as a function of acetaminophen dose: Relation to toxicity. Biochem Biophys Res Commun, 203:532-9.
    • (1994) Biochem Biophys Res Commun , vol.203 , pp. 532-539
    • Snawder, J.E.1    Roe, A.L.2    Benson, R.W.3    Roberts, D.W.4
  • 133
    • 0037462651 scopus 로고    scopus 로고
    • Degradation of transcription factor Nrf2 via the ubiquitin-proteasome pathway and stabilization by cadmium
    • Stewart D, Killeen E, Naquin R, et al. (2003). Degradation of transcription factor Nrf2 via the ubiquitin-proteasome pathway and stabilization by cadmium. J Biol Chem, 278:2396-402.
    • (2003) J Biol Chem , vol.278 , pp. 2396-2402
    • Stewart, D.1    Killeen, E.2    Naquin, R.3
  • 134
    • 2342480474 scopus 로고    scopus 로고
    • Drug-induced liver injury: What you need to know
    • Thames G. (2004). Drug-induced liver injury: What you need to know. Gastroenterol Nurs, 27:31-3.
    • (2004) Gastroenterol Nurs , vol.27 , pp. 31-33
    • Thames, G.1
  • 135
    • 49649098815 scopus 로고    scopus 로고
    • C-Jun N-terminal kinase 2 promotes graft injury via the mitochondrial permeability transition after mouse liver transplantation
    • Theruvath TP, Czerny C, Ramshesh VK, et al. (2008). C-Jun N-terminal kinase 2 promotes graft injury via the mitochondrial permeability transition after mouse liver transplantation. Am J Transplant, 8: 1819-28.
    • (2008) Am J Transplant , vol.8 , pp. 1819-1828
    • Theruvath, T.P.1    Czerny, C.2    Ramshesh, V.K.3
  • 136
    • 0027253615 scopus 로고
    • Oxidation of acetaminophen to N-acetyl-p-aminobenzoquinone imine by human CYP3A4
    • Thummel KE, Lee CA, Kunze KL, et al. (1993). Oxidation of acetaminophen to N-acetyl-p-aminobenzoquinone imine by human CYP3A4. Biochem Pharmacol, 45:1563-9.
    • (1993) Biochem Pharmacol , vol.45 , pp. 1563-1569
    • Thummel, K.E.1    Lee, C.A.2    Kunze, K.L.3
  • 137
    • 33344463325 scopus 로고    scopus 로고
    • Keap1 recruits Neh2 through binding to ETGE and DLG motifs: Characterization of the two-site molecular recognition model
    • Tong KI, Katoh Y, Kusunoki H, et al. (2006a). Keap1 recruits Neh2 through binding to ETGE and DLG motifs: Characterization of the two-site molecular recognition model. Mol Cell Biol, 26:2887-900.
    • (2006) Mol Cell Biol , vol.26 , pp. 2887-2900
    • Tong, K.I.1    Katoh, Y.2    Kusunoki, H.3
  • 138
    • 33750613056 scopus 로고    scopus 로고
    • Two-site substrate recognition model for the Keap1-Mrf2 system: A hinge and latch mechanism
    • Tong KI, Kobayashi A, Katsuoka F, Yamamoto M. (2006b). Two-site substrate recognition model for the Keap1-Mrf2 system: A hinge and latch mechanism. Biol Chem, 387:1311-20.
    • (2006) Biol Chem , vol.387 , pp. 1311-1320
    • Tong, K.I.1    Kobayashi, A.2    Katsuoka, F.3    Yamamoto, M.4
  • 139
    • 0023924803 scopus 로고
    • Purification of proteintyrosine phosphatases from human placenta
    • Tonks NK, Diltz CD, Fischer EH. (1988). Purification of proteintyrosine phosphatases from human placenta. J Biol Che, 263:6722-30.
    • (1988) J Biol Che , vol.263 , pp. 6722-6730
    • Tonks, N.K.1    Diltz, C.D.2    Fischer, E.H.3
  • 140
    • 38949104743 scopus 로고    scopus 로고
    • Idiosyncratic drug reactions: Past, present, and future
    • Uetrecht J. (2008). Idiosyncratic drug reactions: Past, present, and future. Chem Res Toxicol, 21:84-92.
    • (2008) Chem Res Toxicol , vol.21 , pp. 84-92
    • Uetrecht, J.1
  • 141
    • 43949097304 scopus 로고    scopus 로고
    • Caspase activation is associated with spontaneous recovery from acute liver failure
    • Volkmann X, Ansteatt M, Hadem J, et al. (2008). Caspase activation is associated with spontaneous recovery from acute liver failure. Hepatology, 47:1624-33.
    • (2008) Hepatology , vol.47 , pp. 1624-1633
    • Volkmann, X.1    Ansteatt, M.2    Hadem, J.3
  • 142
    • 0242329881 scopus 로고    scopus 로고
    • Keap1-null mutation leads to postnatal lethality due to constitutive Nrf2 activation
    • Wakabayashi N, Itoh K, Wakabayashi J, et al. (2003). Keap1-null mutation leads to postnatal lethality due to constitutive Nrf2 activation. Nat Genet, 35:238-45.
    • (2003) Nat Genet , vol.35 , pp. 238-245
    • Wakabayashi, N.1    Itoh, K.2    Wakabayashi, J.3
  • 143
    • 33744956373 scopus 로고    scopus 로고
    • Tumor necrosis factorinduced toxic liver injury results from JNK2-dependent activation of caspase-8 and the mitochondrial death pathway
    • Wang Y, Singh R, Lefkowitch JH, et al. (2006). Tumor necrosis factorinduced toxic liver injury results from JNK2-dependent activation of caspase-8 and the mitochondrial death pathway. J Biol Chem, 281: 15258-67.
    • (2006) J Biol Chem , vol.281 , pp. 15258-15267
    • Wang, Y.1    Singh, R.2    Lefkowitch, J.H.3
  • 144
    • 84877846556 scopus 로고    scopus 로고
    • RXRa inhibits the NRF2-ARE signaling pathway through a direct interaction with the Neh7 domain of NRF2
    • Wang H, Liu K, Geng M, et al. (2013). RXRa inhibits the NRF2-ARE signaling pathway through a direct interaction with the Neh7 domain of NRF2. Cancer Res, 73:3097-108.
    • (2013) Cancer Res , vol.73 , pp. 3097-3108
    • Wang, H.1    Liu, K.2    Geng, M.3
  • 145
    • 21144438395 scopus 로고    scopus 로고
    • Proteomic identification of potential susceptibility factors in drug-induced liver disease
    • Welch KD, Wen B, Goodlett DR, et al. (2005). Proteomic identification of potential susceptibility factors in drug-induced liver disease. Chem Res Toxicol, 18:924-33.
    • (2005) Chem Res Toxicol , vol.18 , pp. 924-933
    • Welch, K.D.1    Wen, B.2    Goodlett, D.R.3
  • 146
    • 33644512085 scopus 로고    scopus 로고
    • Genomic identification of potential risk factors during acetaminophen-induced liver disease in susceptible and resistant strains of mice
    • Welch KD, Reilly TP, Bourdi M, et al. (2006). Genomic identification of potential risk factors during acetaminophen-induced liver disease in susceptible and resistant strains of mice. Chem Res Toxicol, 19: 223-33.
    • (2006) Chem Res Toxicol , vol.19 , pp. 223-233
    • Welch, K.D.1    Reilly, T.P.2    Bourdi, M.3
  • 148
    • 15244359632 scopus 로고    scopus 로고
    • Liver-specific inactivation of the Nrf1 gene in adult mouse leads to nonalcoholic steatohepatitis and hepatic neoplasia
    • Xu ZR, Chen LY, Leung L, et al. (2005). Liver-specific inactivation of the Nrf1 gene in adult mouse leads to nonalcoholic steatohepatitis and hepatic neoplasia. Proc Natl Acad Sci USA, 102:4120-5.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 4120-4125
    • Xu, Z.R.1    Chen, L.Y.2    Leung, L.3
  • 149
    • 6744219613 scopus 로고    scopus 로고
    • Long range interacation of cis-DNA elements mediates by architectural transcription factor Bach1
    • Yoshida C, Tokumasu F, Hohmura KI. (1999). Long range interacation of cis-DNA elements mediates by architectural transcription factor Bach1. Genes Cells, 4:643-55.
    • (1999) Genes Cells , vol.4 , pp. 643-655
    • Yoshida, C.1    Tokumasu, F.2    Hohmura, K.I.3
  • 150
    • 24044466764 scopus 로고    scopus 로고
    • Ubiquitination of Keap1, a BTBKelch substrate adaptor protein for Cul3, targets Keap1 for degradation by a proteasome-independent pathway
    • Zhang DD, Lo SC, Sun Z, et al. (2005). Ubiquitination of Keap1, a BTBKelch substrate adaptor protein for Cul3, targets Keap1 for degradation by a proteasome-independent pathway. J Biol Chem, 280: 30091-9.
    • (2005) J Biol Chem , vol.280 , pp. 30091-30099
    • Zhang, D.D.1    Lo, S.C.2    Sun, Z.3
  • 151
    • 33845442925 scopus 로고    scopus 로고
    • Mechanistic studies of the Nrf2-Keap1 signalling pathway
    • Zhang DD. (2006). Mechanistic studies of the Nrf2-Keap1 signalling pathway. Drug Metab Rev, 38:769-89.
    • (2006) Drug Metab Rev , vol.38 , pp. 769-789
    • Zhang, D.D.1
  • 152
    • 37349081929 scopus 로고    scopus 로고
    • C-Jun N-terminal kinase regulates mitochondrial bioenergetics by modulating pyruvate dehydrogenase activity in primary cortical neurons
    • Zhou Q, Lam PY, Han D, Cadenas E. (2008). c-Jun N-terminal kinase regulates mitochondrial bioenergetics by modulating pyruvate dehydrogenase activity in primary cortical neurons. J Neurochem, 104:325-35.
    • (2008) J Neurochem , vol.104 , pp. 325-335
    • Zhou, Q.1    Lam, P.Y.2    Han, D.3    Cadenas, E.4


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