메뉴 건너뛰기




Volumn 6, Issue , 2015, Pages 552-564

Critical role of c-jun N-terminal protein kinase in promoting mitochondrial dysfunction and acute liver injury

Author keywords

Acute liver injury; Carbon tetrachloride; Differential proteomics; JNK; Mitochondria; Protein phosphorylation

Indexed keywords

ALANINE AMINOTRANSFERASE; ALDEHYDE DEHYDROGENASE; ANTHRA[1,9 CD]PYRAZOL 6(2H) ONE; ANTIOXIDANT; BI 78D3; CARBON TETRACHLORIDE; CYTOCHROME P450 2E1; MITOCHONDRIAL PROTEIN; OXOGLUTARATE DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); STRESS ACTIVATED PROTEIN KINASE; STRESS ACTIVATED PROTEIN KINASE INHIBITOR; SU 3327; UNCLASSIFIED DRUG; [2 (2,2,6,6 TETRAMETHYLPIPERIDINE 1 OXYL 4 YLAMINO) 2 OXOETHYL]TRIPPHENYLPHOSPHENIUM CHLORIDE; BAX PROTEIN, MOUSE; PROTEIN BAX;

EID: 84944740153     PISSN: 22132317     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.redox.2015.09.040     Document Type: Article
Times cited : (47)

References (59)
  • 1
    • 3042738919 scopus 로고    scopus 로고
    • Acetaminophen and the U.S. acute liver failure study group: lowering the risks of hepatic failure
    • Lee W.M. Acetaminophen and the U.S. acute liver failure study group: lowering the risks of hepatic failure. Hepatology 2004, 40:6-9.
    • (2004) Hepatology , vol.40 , pp. 6-9
    • Lee, W.M.1
  • 3
    • 0018857260 scopus 로고
    • Potentiation of acetaminophen hepatotoxicity by alcohol
    • McClain C.J., Kromhout J.P., Peterson F.J., Holtzman J.L. Potentiation of acetaminophen hepatotoxicity by alcohol. JAMA 1980, 244:251-253.
    • (1980) JAMA , vol.244 , pp. 251-253
    • McClain, C.J.1    Kromhout, J.P.2    Peterson, F.J.3    Holtzman, J.L.4
  • 6
    • 0037256608 scopus 로고    scopus 로고
    • Hepatotoxicity and mechanism of action of haloalkanes: carbon tetrachloride as a toxicological model
    • Weber L., Boll M., Stampfl A. Hepatotoxicity and mechanism of action of haloalkanes: carbon tetrachloride as a toxicological model. Crit. Rev. Toxicol. 2003, 33:105-136.
    • (2003) Crit. Rev. Toxicol. , vol.33 , pp. 105-136
    • Weber, L.1    Boll, M.2    Stampfl, A.3
  • 7
    • 0030751667 scopus 로고    scopus 로고
    • Prooxidant-initiated lipid peroxidation in isolated rat hepatocytes: detection of 4-hydroxynonenal- and malondialdehyde-protein adducts
    • Hartley D.P., Kroll D.J., Petersen D.R. Prooxidant-initiated lipid peroxidation in isolated rat hepatocytes: detection of 4-hydroxynonenal- and malondialdehyde-protein adducts. Chem. Res. Toxicol. 1997, 10:895-905.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 895-905
    • Hartley, D.P.1    Kroll, D.J.2    Petersen, D.R.3
  • 8
    • 0032531047 scopus 로고    scopus 로고
    • Nitric oxide protection of rat liver from lipid peroxidation, collagen accumulation, and liver damage induced by carbon tetrachloride
    • Muriel P. Nitric oxide protection of rat liver from lipid peroxidation, collagen accumulation, and liver damage induced by carbon tetrachloride. Biochem. Pharmacol. 1998, 56:773-779.
    • (1998) Biochem. Pharmacol. , vol.56 , pp. 773-779
    • Muriel, P.1
  • 9
    • 17944391477 scopus 로고    scopus 로고
    • Resistance to carbon tetrachloride-induced hepatotoxicity in mice which lack CYP2E1 expression
    • Wong F.W.Y., Chan W.Y., SST Lee Resistance to carbon tetrachloride-induced hepatotoxicity in mice which lack CYP2E1 expression. Toxicol. Appl. Pharmacol. 1998, 153:109-118.
    • (1998) Toxicol. Appl. Pharmacol. , vol.153 , pp. 109-118
    • Wong, F.W.Y.1    Chan, W.Y.2    SST, L.3
  • 10
    • 0028880006 scopus 로고
    • Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis
    • Xia Z., Dickens M., Raingeaud J., Davis R.J., Greenberg M.E. Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis. Science 1995, 270:1326-1331.
    • (1995) Science , vol.270 , pp. 1326-1331
    • Xia, Z.1    Dickens, M.2    Raingeaud, J.3    Davis, R.J.4    Greenberg, M.E.5
  • 11
    • 84864198388 scopus 로고    scopus 로고
    • A liver full of JNK: signaling in regulation of cell function and disease pathogenesis, and clinical approaches
    • Seki E., Brenner D.A., Karin M. A liver full of JNK: signaling in regulation of cell function and disease pathogenesis, and clinical approaches. Gastroenterology 2012, 143:307-320.
    • (2012) Gastroenterology , vol.143 , pp. 307-320
    • Seki, E.1    Brenner, D.A.2    Karin, M.3
  • 12
  • 14
    • 0034802130 scopus 로고    scopus 로고
    • Acetaminophen induces apoptosis of C6 glioma cells by activating the c-Jun NH2-terminal protein kinase-related cell death pathway
    • Bae M.A., Pie J.E., Song B.J. Acetaminophen induces apoptosis of C6 glioma cells by activating the c-Jun NH2-terminal protein kinase-related cell death pathway. Mol. Pharmacol. 2001, 60:847-856.
    • (2001) Mol. Pharmacol. , vol.60 , pp. 847-856
    • Bae, M.A.1    Pie, J.E.2    Song, B.J.3
  • 15
    • 33746379603 scopus 로고    scopus 로고
    • JNK- and p38 kinase-mediated phosphorylation of Bax leads to its activation and mitochondrial translocation and to apoptosis of human hepatoma HepG2 cells
    • Kim B.J., Ryu S.W., Song B.J. JNK- and p38 kinase-mediated phosphorylation of Bax leads to its activation and mitochondrial translocation and to apoptosis of human hepatoma HepG2 cells. J. Biol. Chem. 2006, 281:21256-21265.
    • (2006) J. Biol. Chem. , vol.281 , pp. 21256-21265
    • Kim, B.J.1    Ryu, S.W.2    Song, B.J.3
  • 17
    • 0029803923 scopus 로고    scopus 로고
    • Independent regulation of JNK/p38 mitogen-activated protein kinases by metabolic oxidative stress in the liver
    • Mendelson K.G., Contois L.R., Tevosian S.G., Davis R.J., Paulson K.E. Independent regulation of JNK/p38 mitogen-activated protein kinases by metabolic oxidative stress in the liver. Proc. Nat. Acad. Sci. USA 1996, 93:12908-12913.
    • (1996) Proc. Nat. Acad. Sci. USA , vol.93 , pp. 12908-12913
    • Mendelson, K.G.1    Contois, L.R.2    Tevosian, S.G.3    Davis, R.J.4    Paulson, K.E.5
  • 18
    • 73449119542 scopus 로고    scopus 로고
    • Inhibition of hepatic mitochondrial aldehyde dehydrogenase by carbon tetrachloride through JNK-mediated phosphorylation
    • Moon K.H., Lee Y.M., Song B.J. Inhibition of hepatic mitochondrial aldehyde dehydrogenase by carbon tetrachloride through JNK-mediated phosphorylation. Free Radic. Biol. Med. 2010, 48:391-398.
    • (2010) Free Radic. Biol. Med. , vol.48 , pp. 391-398
    • Moon, K.H.1    Lee, Y.M.2    Song, B.J.3
  • 19
    • 0038677013 scopus 로고    scopus 로고
    • C-Jun N-terminal kinase (JNK)-mediated modulation of brain mitochondria function: new target proteins for JNK signalling in mitochondrion-dependent apoptosis
    • Schroeter H., Boyd C.S., Ahmed R., Spencer J.P., Duncan R.F., Rice-Evans C., Cadenas E. c-Jun N-terminal kinase (JNK)-mediated modulation of brain mitochondria function: new target proteins for JNK signalling in mitochondrion-dependent apoptosis. Biochem. J. 2003, 372:359-369.
    • (2003) Biochem. J. , vol.372 , pp. 359-369
    • Schroeter, H.1    Boyd, C.S.2    Ahmed, R.3    Spencer, J.P.4    Duncan, R.F.5    Rice-Evans, C.6    Cadenas, E.7
  • 20
    • 64549143360 scopus 로고    scopus 로고
    • Design, synthesis, and structure- activity relationship of substrate competitive, selective, and in vivo active triazole and thiadiazole inhibitors of the c-Jun N-terminal kinase
    • De S.K., Stebbins J.L., Chen L.H., Riel-Mehan M., Machleidt T., Dahl R., Yuan H., Emdadi A., Barile E., Chen V., Murphy R., Pellecchia M. Design, synthesis, and structure- activity relationship of substrate competitive, selective, and in vivo active triazole and thiadiazole inhibitors of the c-Jun N-terminal kinase. J. Med. Chem. 2009, 52:1943-1952.
    • (2009) J. Med. Chem. , vol.52 , pp. 1943-1952
    • De, S.K.1    Stebbins, J.L.2    Chen, L.H.3    Riel-Mehan, M.4    Machleidt, T.5    Dahl, R.6    Yuan, H.7    Emdadi, A.8    Barile, E.9    Chen, V.10    Murphy, R.11    Pellecchia, M.12
  • 25
    • 53549125568 scopus 로고    scopus 로고
    • Mechanism of 3,4-methylenedioxymethamphetamine (MDMA, ecstasy)-mediated mitochondrial dysfunction in rat liver
    • Moon K.H., Upreti V.V., Yu L.R., Lee I.J., Ye X., Eddington N.D., Veenstra T.D., Song B.J. Mechanism of 3,4-methylenedioxymethamphetamine (MDMA, ecstasy)-mediated mitochondrial dysfunction in rat liver. Proteomics 2008, 8:3906-3918.
    • (2008) Proteomics , vol.8 , pp. 3906-3918
    • Moon, K.H.1    Upreti, V.V.2    Yu, L.R.3    Lee, I.J.4    Ye, X.5    Eddington, N.D.6    Veenstra, T.D.7    Song, B.J.8
  • 27
    • 78751611793 scopus 로고    scopus 로고
    • Distinct roles of GCN5/PCAF-mediated H3K9ac and CBP/p300-mediated H3K18/27ac in nuclear receptor transactivation
    • Jin Q., Yu L.R., Wang L., Zhang Z., Kasper L.H., Lee J.E., Wang C., Brindle P.K., SYR Dent, Ge K. Distinct roles of GCN5/PCAF-mediated H3K9ac and CBP/p300-mediated H3K18/27ac in nuclear receptor transactivation. EMBO J. 2010, 30:249-262.
    • (2010) EMBO J. , vol.30 , pp. 249-262
    • Jin, Q.1    Yu, L.R.2    Wang, L.3    Zhang, Z.4    Kasper, L.H.5    Lee, J.E.6    Wang, C.7    Brindle, P.K.8    SYR, D.9    Ge, K.10
  • 28
    • 81055140401 scopus 로고    scopus 로고
    • Proteomic analysis of early response lymph node proteins in mice treated with titanium dioxide nanoparticles
    • Gao Y., Gopee N.V., Howard P.C., Yu L.R. Proteomic analysis of early response lymph node proteins in mice treated with titanium dioxide nanoparticles. J. Proteom. 2011, 74:2745-2759.
    • (2011) J. Proteom. , vol.74 , pp. 2745-2759
    • Gao, Y.1    Gopee, N.V.2    Howard, P.C.3    Yu, L.R.4
  • 29
    • 33751003258 scopus 로고    scopus 로고
    • Inactivation of oxidized and S-nitrosylated mitochondrial proteins in alcoholic fatty liver of rats
    • Moon K.H., Hood B.L., Kim B.J., Hardwick J.P., Conrads T.P., Veenstra T.D., Song B.J. Inactivation of oxidized and S-nitrosylated mitochondrial proteins in alcoholic fatty liver of rats. Hepatology 2006, 44:1218-1230.
    • (2006) Hepatology , vol.44 , pp. 1218-1230
    • Moon, K.H.1    Hood, B.L.2    Kim, B.J.3    Hardwick, J.P.4    Conrads, T.P.5    Veenstra, T.D.6    Song, B.J.7
  • 31
    • 0019800167 scopus 로고
    • Enzymology and subcellular localization of aldehyde oxidation in rat liver: oxidation of 3,4-dihydroxyphenylacetaldehyde derived from dopamine to 3,4-dihydroxyphenylacetic acid
    • Tank A.W., Weiner H., Thurman J.A. Enzymology and subcellular localization of aldehyde oxidation in rat liver: oxidation of 3,4-dihydroxyphenylacetaldehyde derived from dopamine to 3,4-dihydroxyphenylacetic acid. Biochem. Pharmacol. 1981, 30:3265-3275.
    • (1981) Biochem. Pharmacol. , vol.30 , pp. 3265-3275
    • Tank, A.W.1    Weiner, H.2    Thurman, J.A.3
  • 32
    • 79955544880 scopus 로고    scopus 로고
    • Mitochondrial c-Jun N-terminal kinase (JNK) signaling initiates physiological changes resulting in amplification of reactive oxygen species generation
    • Chambers J.W., LoGrasso P.V. Mitochondrial c-Jun N-terminal kinase (JNK) signaling initiates physiological changes resulting in amplification of reactive oxygen species generation. J. Biol. Chem. 2011, 286:16052-16062.
    • (2011) J. Biol. Chem. , vol.286 , pp. 16052-16062
    • Chambers, J.W.1    LoGrasso, P.V.2
  • 33
    • 0002456587 scopus 로고
    • α-ketoglutarate dehydrogenase from pig heart
    • Sanadi D. α-ketoglutarate dehydrogenase from pig heart. Methods Enzymol. 1969, 13:52-55.
    • (1969) Methods Enzymol. , vol.13 , pp. 52-55
    • Sanadi, D.1
  • 34
    • 4544231105 scopus 로고    scopus 로고
    • Methods to measure membrane potential and permeability transition in mitochondria during apoptosis
    • Zamzami N., Kroemer G. Methods to measure membrane potential and permeability transition in mitochondria during apoptosis. Methods Mol. Biol. 2004, 282:103-116.
    • (2004) Methods Mol. Biol. , vol.282 , pp. 103-116
    • Zamzami, N.1    Kroemer, G.2
  • 36
    • 34347329203 scopus 로고    scopus 로고
    • Activation of mitogen activated protein kinase (MAPK) during carbon tetrachloride intoxication in the rat liver
    • Iida C., Fujii K., Kishioka T., Nagae R., Onishi Y., Ichi I., Kojo S. Activation of mitogen activated protein kinase (MAPK) during carbon tetrachloride intoxication in the rat liver. Arch. Toxicol. 2007, 81:489-493.
    • (2007) Arch. Toxicol. , vol.81 , pp. 489-493
    • Iida, C.1    Fujii, K.2    Kishioka, T.3    Nagae, R.4    Onishi, Y.5    Ichi, I.6    Kojo, S.7
  • 37
    • 0037308871 scopus 로고    scopus 로고
    • Critical role of c-Jun N-terminal protein kinase activation in troglitazone-induced apoptosis of human HepG2 hepatoma cells
    • Bae M.A., Song B.J. Critical role of c-Jun N-terminal protein kinase activation in troglitazone-induced apoptosis of human HepG2 hepatoma cells. Mol. Pharmacol. 2003, 63:401-408.
    • (2003) Mol. Pharmacol. , vol.63 , pp. 401-408
    • Bae, M.A.1    Song, B.J.2
  • 38
    • 33847750361 scopus 로고    scopus 로고
    • Mitochondrial protection by the JNK inhibitor leflunomide rescues mice from acetaminophen-induced liver injury
    • Latchoumycandane C., Goh C.W., Ong M.M.K., Boelsterli U.A. Mitochondrial protection by the JNK inhibitor leflunomide rescues mice from acetaminophen-induced liver injury. Hepatology 2007, 45:412-421.
    • (2007) Hepatology , vol.45 , pp. 412-421
    • Latchoumycandane, C.1    Goh, C.W.2    Ong, M.M.K.3    Boelsterli, U.A.4
  • 39
    • 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., Gaarde W.A., Han D., Kaplowitz N. Role of JNK translocation to mitochondria leading to inhibition of mitochondria bioenergetics in acetaminophen-induced liver injury. J. Biol. Chem. 2008, 283:13565-13577.
    • (2008) J. Biol. Chem. , vol.283 , pp. 13565-13577
    • Hanawa, N.1    Shinohara, M.2    Saberi, B.3    Gaarde, W.A.4    Han, D.5    Kaplowitz, N.6
  • 40
    • 13444273562 scopus 로고    scopus 로고
    • Recognizing drug-induced liver injury: current problems, possible solutions
    • Lee W.M., Senior J.R. Recognizing drug-induced liver injury: current problems, possible solutions. Toxicol. Pathol. 2005, 33:155-164.
    • (2005) Toxicol. Pathol. , vol.33 , pp. 155-164
    • Lee, W.M.1    Senior, J.R.2
  • 42
    • 0026353391 scopus 로고
    • Hepatic biochemical changes as a result of acute cocaine administration in the mouse
    • Boyer C.S., Petersen D.R. Hepatic biochemical changes as a result of acute cocaine administration in the mouse. Hepatology 1991, 14:1209-1216.
    • (1991) Hepatology , vol.14 , pp. 1209-1216
    • Boyer, C.S.1    Petersen, D.R.2
  • 43
    • 0026680529 scopus 로고
    • Toxicity and deaths from 3,4-methylenedioxy methamphetamine
    • Henry J., Jeffreys K., Dawling S. Toxicity and deaths from 3,4-methylenedioxy methamphetamine. Lancet 1992, 340:384-387.
    • (1992) Lancet , vol.340 , pp. 384-387
    • Henry, J.1    Jeffreys, K.2    Dawling, S.3
  • 44
    • 0036303941 scopus 로고    scopus 로고
    • Effects of concurrent use of alcohol and cocaine
    • Pennings E.J.M., Leccese A.P., Wolff F.A. Effects of concurrent use of alcohol and cocaine. Addiction 2002, 97:773-783.
    • (2002) Addiction , vol.97 , pp. 773-783
    • Pennings, E.J.M.1    Leccese, A.P.2    Wolff, F.A.3
  • 46
    • 84868234595 scopus 로고    scopus 로고
    • Damage-associated molecular patterns: their impact on the liver and beyond during acetaminophen overdose
    • Ju C. Damage-associated molecular patterns: their impact on the liver and beyond during acetaminophen overdose. Hepatology 2012, 56:1599-1601.
    • (2012) Hepatology , vol.56 , pp. 1599-1601
    • Ju, C.1
  • 47
    • 84901379933 scopus 로고    scopus 로고
    • Functional roles of protein nitration in acute and chronic liver diseases
    • Abdelmegeed M.A., Song B.J. Functional roles of protein nitration in acute and chronic liver diseases. Oxid. Med. Cell. Longev. 2014, 2014:149627.
    • (2014) Oxid. Med. Cell. Longev. , vol.2014 , pp. 149627
    • Abdelmegeed, M.A.1    Song, B.J.2
  • 48
    • 84918551836 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications
    • Song B.J., Akbar M., Abdelmegeed M.A., Byun K., Lee B., Yoon S.K., Hardwick J.P. Mitochondrial dysfunction and tissue injury by alcohol, high fat, nonalcoholic substances and pathological conditions through post-translational protein modifications. Redox Biol. 2014, 3:109-123.
    • (2014) Redox Biol. , vol.3 , pp. 109-123
    • Song, B.J.1    Akbar, M.2    Abdelmegeed, M.A.3    Byun, K.4    Lee, B.5    Yoon, S.K.6    Hardwick, J.P.7
  • 49
    • 0037392942 scopus 로고    scopus 로고
    • The specificities of protein kinase inhibitors: an update
    • Bain J., McLauchlan H., Elliott M., Cohen P. The specificities of protein kinase inhibitors: an update. Biochem. J. 2003, 371:199-204.
    • (2003) Biochem. J. , vol.371 , pp. 199-204
    • Bain, J.1    McLauchlan, H.2    Elliott, M.3    Cohen, P.4
  • 51
    • 77951082847 scopus 로고    scopus 로고
    • Utility and limitations of SP600125, an inhibitor of stress-responsive c-Jun N-terminal kinase
    • Tanemura S., Yamasaki T., Katada T., Nishina H. Utility and limitations of SP600125, an inhibitor of stress-responsive c-Jun N-terminal kinase. Curr. Enzym. Inhib. 2010, 6:26-33.
    • (2010) Curr. Enzym. Inhib. , vol.6 , pp. 26-33
    • Tanemura, S.1    Yamasaki, T.2    Katada, T.3    Nishina, H.4
  • 52
    • 77949659740 scopus 로고    scopus 로고
    • SP600125 suppresses Cdk1 and induces endoreplication directly from G2 phase, independent of JNK inhibition
    • Kim J., Lee J., Margolis R., Fotedar R. SP600125 suppresses Cdk1 and induces endoreplication directly from G2 phase, independent of JNK inhibition. Oncogene 2010, 29:1702-1716.
    • (2010) Oncogene , vol.29 , pp. 1702-1716
    • Kim, J.1    Lee, J.2    Margolis, R.3    Fotedar, R.4
  • 53
    • 33748707782 scopus 로고    scopus 로고
    • SP600125, a selective JNK inhibitor, aggravates hepatic ischemia-reperfusion injury
    • Lee K.H., Kim S.E., Lee Y.S. SP600125, a selective JNK inhibitor, aggravates hepatic ischemia-reperfusion injury. Exp. Mol. Med. 2006, 38:408-416.
    • (2006) Exp. Mol. Med. , vol.38 , pp. 408-416
    • Lee, K.H.1    Kim, S.E.2    Lee, Y.S.3
  • 54
    • 0034894722 scopus 로고    scopus 로고
    • Vascular and hepatocellular peroxynitrite formation during acetaminophen toxicity: role of mitochondrial oxidant stress
    • Knight T.R., Kurtz A., Bajt M.L., Hinson J.A., Jaeschke H. Vascular and hepatocellular peroxynitrite formation during acetaminophen toxicity: role of mitochondrial oxidant stress. Toxicol. Sci. 2001, 62:212-220.
    • (2001) Toxicol. Sci. , vol.62 , pp. 212-220
    • Knight, T.R.1    Kurtz, A.2    Bajt, M.L.3    Hinson, J.A.4    Jaeschke, H.5
  • 55
    • 84875550946 scopus 로고    scopus 로고
    • Robust protein nitration contributes to acetaminophen-induced mitochondrial dysfunction and acute liver injury
    • Abdelmegeed M.A., Jang S., Banerjee A., Hardwick J.P., Song B.J. Robust protein nitration contributes to acetaminophen-induced mitochondrial dysfunction and acute liver injury. Free Radic. Biol. Med. 2013, 60:211-222.
    • (2013) Free Radic. Biol. Med. , vol.60 , pp. 211-222
    • Abdelmegeed, M.A.1    Jang, S.2    Banerjee, A.3    Hardwick, J.P.4    Song, B.J.5
  • 57
    • 80053425902 scopus 로고    scopus 로고
    • C-Jun N-terminal Kinase (JNK)-dependent acute liver injury from acetaminophen or tumor necrosis factor (TNF) requires mitochondrial Sab protein expression in mice
    • Win S., Than T.A., Han D., Petrovic L.M., Kaplowitz N. c-Jun N-terminal Kinase (JNK)-dependent acute liver injury from acetaminophen or tumor necrosis factor (TNF) requires mitochondrial Sab protein expression in mice. J. Biol. Chem. 2011, 286:35071-35078.
    • (2011) J. Biol. Chem. , vol.286 , pp. 35071-35078
    • Win, S.1    Than, T.A.2    Han, D.3    Petrovic, L.M.4    Kaplowitz, N.5
  • 58
    • 80051999961 scopus 로고    scopus 로고
    • Selective inhibition of mitochondrial JNK signaling achieved using peptide mimicry of the Sab kinase interacting motif-1 (KIM1)
    • Chambers J., Cherry L., Laughlin J., Figuera-Losada M., Lograsso P.V. Selective inhibition of mitochondrial JNK signaling achieved using peptide mimicry of the Sab kinase interacting motif-1 (KIM1). ACS Chem. Biol. 2011, 6:808-818.
    • (2011) ACS Chem. Biol. , vol.6 , pp. 808-818
    • Chambers, J.1    Cherry, L.2    Laughlin, J.3    Figuera-Losada, M.4    Lograsso, P.V.5
  • 59
    • 33845653234 scopus 로고    scopus 로고
    • Uses for JNK: the many and varied substrates of the c- Jun N-terminal kinases
    • Bogoyevitch M.A., Kobe B. Uses for JNK: the many and varied substrates of the c- Jun N-terminal kinases. Microbiol. Mol. Biol. Rev. 2006, 70:1061-1095.
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 1061-1095
    • Bogoyevitch, M.A.1    Kobe, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.