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Volumn 15, Issue 2, 2013, Pages 316-324

Taraxerol inhibits LPS-induced inflammatory responses through suppression of TAK1 and Akt activation

Author keywords

Akt; MAPK; NF B; RAW264.7 cells; TAK1; Taraxerol

Indexed keywords

CYCLOOXYGENASE 2; I KAPPA B ALPHA; INTERLEUKIN 1BETA; INTERLEUKIN 6; MITOGEN ACTIVATED PROTEIN KINASE; NITRIC OXIDE; PROSTAGLANDIN E2; PROTEIN KINASE B; TARAXEROL; TRANSFORMING GROWTH FACTOR BETA ACTIVATED KINASE 1; TRITERPENOID; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 84872930365     PISSN: 15675769     EISSN: 18781705     Source Type: Journal    
DOI: 10.1016/j.intimp.2012.12.032     Document Type: Article
Times cited : (44)

References (46)
  • 1
    • 3142724031 scopus 로고    scopus 로고
    • Toll-like receptor signalling
    • S. Akira, and K. Takeda Toll-like receptor signalling Nat Rev Immunol 4 2004 499 511
    • (2004) Nat Rev Immunol , vol.4 , pp. 499-511
    • Akira, S.1    Takeda, K.2
  • 2
    • 84866731086 scopus 로고    scopus 로고
    • Targeting of TAK1 in inflammatory disorders and cancer
    • H. Sakurai Targeting of TAK1 in inflammatory disorders and cancer Trends Pharmacol Sci 33 2012 522 530
    • (2012) Trends Pharmacol Sci , vol.33 , pp. 522-530
    • Sakurai, H.1
  • 3
    • 27744577296 scopus 로고    scopus 로고
    • TAK1, but not TAB1 or TAB2, plays an essential role in multiple signaling pathways in vivo
    • J.H. Shim, C. Xiao, A.E. Paschal, S.T. Bailey, P. Rao, and M.S. Hayden TAK1, but not TAB1 or TAB2, plays an essential role in multiple signaling pathways in vivo Genes Dev 19 2005 2668 2681
    • (2005) Genes Dev , vol.19 , pp. 2668-2681
    • Shim, J.H.1    Xiao, C.2    Paschal, A.E.3    Bailey, S.T.4    Rao, P.5    Hayden, M.S.6
  • 4
    • 77649178841 scopus 로고    scopus 로고
    • The TAK1-TRAF6 signalling pathway
    • M. Landstrom The TAK1-TRAF6 signalling pathway Int J Biochem Cell Biol 42 2010 585 589
    • (2010) Int J Biochem Cell Biol , vol.42 , pp. 585-589
    • Landstrom, M.1
  • 5
    • 67650744586 scopus 로고    scopus 로고
    • The role of ubiquitin in NF-κB regulatory pathways
    • B. Skaug, X. Jiang, and Z.J. Chen The role of ubiquitin in NF-κB regulatory pathways Annu Rev Biochem 78 2009 769 796
    • (2009) Annu Rev Biochem , vol.78 , pp. 769-796
    • Skaug, B.1    Jiang, X.2    Chen, Z.J.3
  • 6
    • 38649124609 scopus 로고    scopus 로고
    • Inhibition of inducible nitric oxide synthase and cyclooxygenase-2 in lipopolysaccharide-stimulated RAW264.7 cells by carboxybutyrylated glucosamine takes place via down-regulation of mitogen-activated protein kinase-mediated nuclear factor-κB signaling
    • N. Rajapakse, M.-M. Kim, E. Mendis, and S.-K. Kim Inhibition of inducible nitric oxide synthase and cyclooxygenase-2 in lipopolysaccharide-stimulated RAW264.7 cells by carboxybutyrylated glucosamine takes place via down-regulation of mitogen-activated protein kinase-mediated nuclear factor-κB signaling Immunology 123 2008 348 357
    • (2008) Immunology , vol.123 , pp. 348-357
    • Rajapakse, N.1    Kim, M.-M.2    Mendis, E.3    Kim, S.-K.4
  • 7
    • 0035282334 scopus 로고    scopus 로고
    • Mammalian MAP kinase signalling cascades
    • L. Chang, and M. Karin Mammalian MAP kinase signalling cascades Nature 410 2001 37 40
    • (2001) Nature , vol.410 , pp. 37-40
    • Chang, L.1    Karin, M.2
  • 8
    • 0036098552 scopus 로고    scopus 로고
    • AP-1 as a regulator of cell life and death
    • E. Shaulian, and M. Karin AP-1 as a regulator of cell life and death Nat Cell Biol 4 2002 E131 E136
    • (2002) Nat Cell Biol , vol.4
    • Shaulian, E.1    Karin, M.2
  • 9
    • 0037352702 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase is involved in Toll-like receptor 4-mediated cytokine expression in mouse macrophages
    • M. Ojaniemi, V. Glumoff, K. Harju, M. Liljeroos, K. Vuori, and M. Hallman Phosphatidylinositol 3-kinase is involved in Toll-like receptor 4-mediated cytokine expression in mouse macrophages Eur J Immunol 33 2003 597 605
    • (2003) Eur J Immunol , vol.33 , pp. 597-605
    • Ojaniemi, M.1    Glumoff, V.2    Harju, K.3    Liljeroos, M.4    Vuori, K.5    Hallman, M.6
  • 10
    • 0036013435 scopus 로고    scopus 로고
    • Degradation of IκBα in activated RAW264.7 cells is blocked by the phosphatidylinositol 3-kinase inhibitor LY294002
    • S.J. Park, S.C. Lee, S.H. Hong, and H.M. Kim Degradation of IκBα in activated RAW264.7 cells is blocked by the phosphatidylinositol 3-kinase inhibitor LY294002 Cell Biol Toxicol 18 2002 121 130
    • (2002) Cell Biol Toxicol , vol.18 , pp. 121-130
    • Park, S.J.1    Lee, S.C.2    Hong, S.H.3    Kim, H.M.4
  • 11
    • 19344365340 scopus 로고    scopus 로고
    • LY294002 inhibits LPS-induced NO production through a inhibition of NF-κB activation: Independent mechanism of phosphatidylinositol 3-kinase
    • Y.H. Kim, K.-H. Choi, J.-W. Park, and T.K. Kwon LY294002 inhibits LPS-induced NO production through a inhibition of NF-κB activation: independent mechanism of phosphatidylinositol 3-kinase Immunol Lett 99 2005 45 50
    • (2005) Immunol Lett , vol.99 , pp. 45-50
    • Kim, Y.H.1    Choi, K.-H.2    Park, J.-W.3    Kwon, T.K.4
  • 12
    • 33646473522 scopus 로고    scopus 로고
    • Class i and III phosphatidylinositol 3′-kinase play distinct roles in TLR signaling pathway
    • C.-C. Kuo, W.-T. Lin, C.-M. Liang, and S.-M. Liang Class I and III phosphatidylinositol 3′-kinase play distinct roles in TLR signaling pathway J Immunol 176 2006 5943 5949
    • (2006) J Immunol , vol.176 , pp. 5943-5949
    • Kuo, C.-C.1    Lin, W.-T.2    Liang, C.-M.3    Liang, S.-M.4
  • 13
    • 33646896934 scopus 로고    scopus 로고
    • New players in TLR-mediated innate immunity
    • M. Ruse, and U. Knaus New players in TLR-mediated innate immunity Immunol Res 34 2006 33 48
    • (2006) Immunol Res , vol.34 , pp. 33-48
    • Ruse, M.1    Knaus, U.2
  • 14
    • 0037629646 scopus 로고    scopus 로고
    • PI3K and negative regulation of TLR signaling
    • T. Fukao, and S. Koyasu PI3K and negative regulation of TLR signaling Trends Immunol 24 2003 358 363
    • (2003) Trends Immunol , vol.24 , pp. 358-363
    • Fukao, T.1    Koyasu, S.2
  • 15
    • 76749166241 scopus 로고    scopus 로고
    • 3beta-Taraxerol of Mangifera indica, a PI3K dependent dual activator of glucose transport and glycogen synthesis in 3T3-L1 adipocytes
    • K.N. Sangeetha, S. Sujatha, V.S. Muthusamy, S. Anand, N. Nithya, and D. Velmurugan 3beta-Taraxerol of Mangifera indica, a PI3K dependent dual activator of glucose transport and glycogen synthesis in 3T3-L1 adipocytes Biochim Biophys Acta 1800 2010 359 366
    • (2010) Biochim Biophys Acta , vol.1800 , pp. 359-366
    • Sangeetha, K.N.1    Sujatha, S.2    Muthusamy, V.S.3    Anand, S.4    Nithya, N.5    Velmurugan, D.6
  • 17
    • 25844459154 scopus 로고    scopus 로고
    • NF-kappaB: Linking inflammation and immunity to cancer development and progression
    • M. Karin, and F.R. Greten NF-kappaB: linking inflammation and immunity to cancer development and progression Nat Rev Immunol 5 2005 749 759
    • (2005) Nat Rev Immunol , vol.5 , pp. 749-759
    • Karin, M.1    Greten, F.R.2
  • 18
    • 67649400356 scopus 로고    scopus 로고
    • Chlorogenic acid inhibits lipopolysaccharide-induced cyclooxygenase-2 expression in RAW264.7 cells through suppressing NF-[kappa]B and JNK/AP-1 activation
    • J. Shan, J. Fu, Z. Zhao, X. Kong, H. Huang, and L. Luo Chlorogenic acid inhibits lipopolysaccharide-induced cyclooxygenase-2 expression in RAW264.7 cells through suppressing NF-[kappa]B and JNK/AP-1 activation Int Immunopharmacol 9 2009 1042 1048
    • (2009) Int Immunopharmacol , vol.9 , pp. 1042-1048
    • Shan, J.1    Fu, J.2    Zhao, Z.3    Kong, X.4    Huang, H.5    Luo, L.6
  • 20
    • 84859973888 scopus 로고    scopus 로고
    • Lys(48)-linked TAK1 polyubiquitination at lysine-72 downregulates TNFalpha-induced NF-kappaB activation via mediating TAK1 degradation
    • Y. Fan, Y. Shi, S. Liu, R. Mao, L. An, and Y. Zhao Lys(48)-linked TAK1 polyubiquitination at lysine-72 downregulates TNFalpha-induced NF-kappaB activation via mediating TAK1 degradation Cell Signal 24 2012 1381 1389
    • (2012) Cell Signal , vol.24 , pp. 1381-1389
    • Fan, Y.1    Shi, Y.2    Liu, S.3    Mao, R.4    An, L.5    Zhao, Y.6
  • 21
    • 77949316183 scopus 로고    scopus 로고
    • Lysine 63-linked polyubiquitination of TAK1 at lysine 158 is required for tumor necrosis factor alpha- and interleukin-1beta-induced IKK/NF-kappaB and JNK/AP-1 activation
    • Y. Fan, Y. Yu, Y. Shi, W. Sun, M. Xie, and N. Ge Lysine 63-linked polyubiquitination of TAK1 at lysine 158 is required for tumor necrosis factor alpha- and interleukin-1beta-induced IKK/NF-kappaB and JNK/AP-1 activation J Biol Chem 285 2010 5347 5360
    • (2010) J Biol Chem , vol.285 , pp. 5347-5360
    • Fan, Y.1    Yu, Y.2    Shi, Y.3    Sun, W.4    Xie, M.5    Ge, N.6
  • 22
    • 84863178651 scopus 로고    scopus 로고
    • Potent anti-inflammatory effect of a novel furan-2,5-dione derivative, BPD, mediated by dual suppression of COX-2 activity and LPS-induced inflammatory gene expression via NF-kappaB inactivation
    • J.S. Shin, S.J. Park, S. Ryu, H.B. Kang, T.W. Kim, and J.H. Choi Potent anti-inflammatory effect of a novel furan-2,5-dione derivative, BPD, mediated by dual suppression of COX-2 activity and LPS-induced inflammatory gene expression via NF-kappaB inactivation Br J Pharmacol 165 2012 1926 1940
    • (2012) Br J Pharmacol , vol.165 , pp. 1926-1940
    • Shin, J.S.1    Park, S.J.2    Ryu, S.3    Kang, H.B.4    Kim, T.W.5    Choi, J.H.6
  • 23
    • 79251646629 scopus 로고    scopus 로고
    • Stercurensin inhibits nuclear factor-kappaB-dependent inflammatory signals through attenuation of TAK1-TAB1 complex formation
    • Y.J. Kim, H.C. Kim, H. Ko, E.C. Amor, J.W. Lee, and H.O. Yang Stercurensin inhibits nuclear factor-kappaB-dependent inflammatory signals through attenuation of TAK1-TAB1 complex formation J Cell Biochem 112 2011 548 558
    • (2011) J Cell Biochem , vol.112 , pp. 548-558
    • Kim, Y.J.1    Kim, H.C.2    Ko, H.3    Amor, E.C.4    Lee, J.W.5    Yang, H.O.6
  • 24
    • 77955497476 scopus 로고    scopus 로고
    • Autoactivation of transforming growth factor beta-activated kinase 1 is a sequential bimolecular process
    • R. Scholz, C.L. Sidler, R.F. Thali, N. Winssinger, P.C. Cheung, and D. Neumann Autoactivation of transforming growth factor beta-activated kinase 1 is a sequential bimolecular process J Biol Chem 285 2010 25753 25766
    • (2010) J Biol Chem , vol.285 , pp. 25753-25766
    • Scholz, R.1    Sidler, C.L.2    Thali, R.F.3    Winssinger, N.4    Cheung, P.C.5    Neumann, D.6
  • 25
    • 0034629146 scopus 로고    scopus 로고
    • TAK1 mitogen-activated protein kinase kinase kinase is activated by autophosphorylation within its activation loop
    • K. Kishimoto, K. Matsumoto, and J. Ninomiya-Tsuji TAK1 mitogen-activated protein kinase kinase kinase is activated by autophosphorylation within its activation loop J Biol Chem 275 2000 7359 7364
    • (2000) J Biol Chem , vol.275 , pp. 7359-7364
    • Kishimoto, K.1    Matsumoto, K.2    Ninomiya-Tsuji, J.3
  • 26
    • 34248570795 scopus 로고    scopus 로고
    • Ubiquitin-mediated activation of TAK1 and IKK
    • A. Adhikari, M. Xu, and Z.J. Chen Ubiquitin-mediated activation of TAK1 and IKK Oncogene 26 2007 3214 3226
    • (2007) Oncogene , vol.26 , pp. 3214-3226
    • Adhikari, A.1    Xu, M.2    Chen, Z.J.3
  • 27
    • 63649116570 scopus 로고    scopus 로고
    • Ubiquitylation in innate and adaptive immunity
    • V.G. Bhoj, and Z.J. Chen Ubiquitylation in innate and adaptive immunity Nature 458 2009 430 437
    • (2009) Nature , vol.458 , pp. 430-437
    • Bhoj, V.G.1    Chen, Z.J.2
  • 28
    • 84867585902 scopus 로고    scopus 로고
    • TAK1 ubiquitination regulates doxorubicin-induced NF-κB activation
    • L. Liang, Y. Fan, J. Cheng, D. Cheng, Y. Zhao, and B. Cao TAK1 ubiquitination regulates doxorubicin-induced NF-κB activation Cell Signal 25 2013 247 254
    • (2013) Cell Signal , vol.25 , pp. 247-254
    • Liang, L.1    Fan, Y.2    Cheng, J.3    Cheng, D.4    Zhao, Y.5    Cao, B.6
  • 29
    • 81255177676 scopus 로고    scopus 로고
    • The E3 ligase Itch and deubiquitinase Cyld act together to regulate Tak1 and inflammation
    • N. Ahmed, M. Zeng, I. Sinha, L. Polin, W.Z. Wei, and C. Rathinam The E3 ligase Itch and deubiquitinase Cyld act together to regulate Tak1 and inflammation Nat Immunol 12 2011 1176 1183
    • (2011) Nat Immunol , vol.12 , pp. 1176-1183
    • Ahmed, N.1    Zeng, M.2    Sinha, I.3    Polin, L.4    Wei, W.Z.5    Rathinam, C.6
  • 30
    • 49549117842 scopus 로고    scopus 로고
    • Ubiquitin chain editing revealed by polyubiquitin linkage-specific antibodies
    • K. Newton, M.L. Matsumoto, I.E. Wertz, D.S. Kirkpatrick, J.R. Lill, and J. Tan Ubiquitin chain editing revealed by polyubiquitin linkage-specific antibodies Cell 134 2008 668 678
    • (2008) Cell , vol.134 , pp. 668-678
    • Newton, K.1    Matsumoto, M.L.2    Wertz, I.E.3    Kirkpatrick, D.S.4    Lill, J.R.5    Tan, J.6
  • 31
    • 78650915537 scopus 로고    scopus 로고
    • Deubiquitinases in the regulation of NF-[kappa]B signaling
    • E.W. Harhaj, and V.M. Dixit Deubiquitinases in the regulation of NF-[kappa]B signaling Cell Res 21 2011 22 39
    • (2011) Cell Res , vol.21 , pp. 22-39
    • Harhaj, E.W.1    Dixit, V.M.2
  • 32
    • 84862761186 scopus 로고    scopus 로고
    • Diverse ubiquitin signaling in NF-κB activation
    • K. Iwai Diverse ubiquitin signaling in NF-κB activation Trends Cell Biol 22 2012 355 364
    • (2012) Trends Cell Biol , vol.22 , pp. 355-364
    • Iwai, K.1
  • 34
    • 33845994781 scopus 로고    scopus 로고
    • Protein phosphatase 6 down-regulates TAK1 kinase activation in the IL-1 signaling pathway
    • T. Kajino, H. Ren, S. Iemura, T. Natsume, B. Stefansson, and D.L. Brautigan Protein phosphatase 6 down-regulates TAK1 kinase activation in the IL-1 signaling pathway J Biol Chem 281 2006 39891 39896
    • (2006) J Biol Chem , vol.281 , pp. 39891-39896
    • Kajino, T.1    Ren, H.2    Iemura, S.3    Natsume, T.4    Stefansson, B.5    Brautigan, D.L.6
  • 35
    • 44849108079 scopus 로고    scopus 로고
    • Protein phosphatase 2A is a negative regulator of transforming growth factor-beta1-induced TAK1 activation in mesangial cells
    • S.I. Kim, J.H. Kwak, L. Wang, and M.E. Choi Protein phosphatase 2A is a negative regulator of transforming growth factor-beta1-induced TAK1 activation in mesangial cells J Biol Chem 283 2008 10753 10763
    • (2008) J Biol Chem , vol.283 , pp. 10753-10763
    • Kim, S.I.1    Kwak, J.H.2    Wang, L.3    Choi, M.E.4
  • 36
    • 42149110310 scopus 로고    scopus 로고
    • Critical roles of the p110β subtype of phosphoinositide 3-kinase in lipopolysaccharide-induced Akt activation and negative regulation of nitrite production in RAW 264.7 cells
    • K. Tsukamoto, K. Hazeki, M. Hoshi, K. Nigorikawa, N. Inoue, and T. Sasaki Critical roles of the p110β subtype of phosphoinositide 3-kinase in lipopolysaccharide-induced Akt activation and negative regulation of nitrite production in RAW 264.7 cells J Immunol 180 2008 2054 2061
    • (2008) J Immunol , vol.180 , pp. 2054-2061
    • Tsukamoto, K.1    Hazeki, K.2    Hoshi, M.3    Nigorikawa, K.4    Inoue, N.5    Sasaki, T.6
  • 38
    • 44849113635 scopus 로고    scopus 로고
    • Genetic analysis of the role of the PI3K-Akt pathway in lipopolysaccharide-induced cytokine and tissue factor gene expression in monocytes/macrophages
    • J.P. Luyendyk, G.A. Schabbauer, M. Tencati, T. Holscher, R. Pawlinski, and N. Mackman Genetic analysis of the role of the PI3K-Akt pathway in lipopolysaccharide-induced cytokine and tissue factor gene expression in monocytes/macrophages J Immunol 180 2008 4218 4226
    • (2008) J Immunol , vol.180 , pp. 4218-4226
    • Luyendyk, J.P.1    Schabbauer, G.A.2    Tencati, M.3    Holscher, T.4    Pawlinski, R.5    Mackman, N.6
  • 39
    • 84857869690 scopus 로고    scopus 로고
    • TLR4-mediated AKT activation is MyD88/TRIF dependent and critical for induction of oxidative phosphorylation and mitochondrial transcription factor A in murine macrophages
    • C.P. Bauerfeld, R. Rastogi, G. Pirockinaite, I. Lee, M. Huttemann, and B. Monks TLR4-mediated AKT activation is MyD88/TRIF dependent and critical for induction of oxidative phosphorylation and mitochondrial transcription factor A in murine macrophages J Immunol 188 2012 2847 2857
    • (2012) J Immunol , vol.188 , pp. 2847-2857
    • Bauerfeld, C.P.1    Rastogi, R.2    Pirockinaite, G.3    Lee, I.4    Huttemann, M.5    Monks, B.6
  • 40
    • 78649736194 scopus 로고    scopus 로고
    • Psoralidin inhibits LPS-induced iNOS expression via repressing Syk-mediated activation of PI3K-IKK-IkappaB signaling pathways
    • W.F. Chiou, M.J. Don, J.F. Liao, and B.L. Wei Psoralidin inhibits LPS-induced iNOS expression via repressing Syk-mediated activation of PI3K-IKK-IkappaB signaling pathways Eur J Pharmacol 650 2011 102 109
    • (2011) Eur J Pharmacol , vol.650 , pp. 102-109
    • Chiou, W.F.1    Don, M.J.2    Liao, J.F.3    Wei, B.L.4
  • 41
    • 77954624419 scopus 로고    scopus 로고
    • Icariin attenuates LPS-induced acute inflammatory responses: Involvement of PI3K/Akt and NF-kappaB signaling pathway
    • C.Q. Xu, B.J. Liu, J.F. Wu, Y.C. Xu, X.H. Duan, and Y.X. Cao Icariin attenuates LPS-induced acute inflammatory responses: involvement of PI3K/Akt and NF-kappaB signaling pathway Eur J Pharmacol 642 2010 146 153
    • (2010) Eur J Pharmacol , vol.642 , pp. 146-153
    • Xu, C.Q.1    Liu, B.J.2    Wu, J.F.3    Xu, Y.C.4    Duan, X.H.5    Cao, Y.X.6
  • 42
    • 84866166696 scopus 로고    scopus 로고
    • Proinflammatory activation of macrophages by bisphenol A-glycidyl-methacrylate involved NFkappaB activation via PI3K/Akt pathway
    • Y.H. Kuan, F.M. Huang, Y.C. Li, and Y.C. Chang Proinflammatory activation of macrophages by bisphenol A-glycidyl-methacrylate involved NFkappaB activation via PI3K/Akt pathway Food Chem Toxicol 50 2012 4003 4009
    • (2012) Food Chem Toxicol , vol.50 , pp. 4003-4009
    • Kuan, Y.H.1    Huang, F.M.2    Li, Y.C.3    Chang, Y.C.4
  • 43
    • 84856091690 scopus 로고    scopus 로고
    • Ampelopsin reduces endotoxic inflammation via repressing ROS-mediated activation of PI3K/Akt/NF-κB signaling pathways
    • S. Qi, Y. Xin, Y. Guo, Y. Diao, X. Kou, and L. Luo Ampelopsin reduces endotoxic inflammation via repressing ROS-mediated activation of PI3K/Akt/NF-κB signaling pathways Int Immunopharmacol 12 2012 278 287
    • (2012) Int Immunopharmacol , vol.12 , pp. 278-287
    • Qi, S.1    Xin, Y.2    Guo, Y.3    Diao, Y.4    Kou, X.5    Luo, L.6
  • 44
    • 79952084572 scopus 로고    scopus 로고
    • Targeting inflammatory pathways by triterpenoids for prevention and treatment of cancer
    • V.R. Yadav, S. Prasad, B. Sung, R. Kannappan, and B.B. Aggarwal Targeting inflammatory pathways by triterpenoids for prevention and treatment of cancer Toxins 2 2010 2428 2466
    • (2010) Toxins , vol.2 , pp. 2428-2466
    • Yadav, V.R.1    Prasad, S.2    Sung, B.3    Kannappan, R.4    Aggarwal, B.B.5
  • 45
    • 76749137504 scopus 로고    scopus 로고
    • Effects of triterpenes on the immune system
    • J.-L. Ríos Effects of triterpenes on the immune system J Ethnopharmacol 128 2010 1 14
    • (2010) J Ethnopharmacol , vol.128 , pp. 1-14
    • Ríos, J.-L.1
  • 46
    • 84355162283 scopus 로고    scopus 로고
    • Canonical and non-canonical autophagy: Variations on a common theme of self-eating?
    • P. Codogno, M. Mehrpour, and T. Proikas-Cezanne Canonical and non-canonical autophagy: variations on a common theme of self-eating? Nat Rev Mol Cell Biol 13 2012 7 12
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 7-12
    • Codogno, P.1    Mehrpour, M.2    Proikas-Cezanne, T.3


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