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Volumn 97, Issue , 2015, Pages 16-26

Glycogen synthase kinase-3 beta (GSK-3β) signaling: Implications for Parkinson's disease

Author keywords

Alpha Synuclein; ER stress; Glycogen synthase kinase 3; Mitochondrial dysfunction; Neuroinflammation; Parkinson's disease; Tauopathy

Indexed keywords

1 (4 METHOXYBENZYL) 3 (5 NITRO 2 THIAZOLYL)UREA; 2 (2,4 DICHLOROPHENYL) 3 (1 METHYL 3 INDOLYL)MALEIMIDE; 2 (3 CHLORO 4 HYDROXYANILINO) 3 (2 NITROPHENYL)MALEIMIDE; ALPHA SYNUCLEIN; BETA CATENIN; BIP 135; DOPAMINE RECEPTOR; GLYCOGEN SYNTHASE KINASE 3 INHIBITOR; GLYCOGEN SYNTHASE KINASE 3BETA; GLYCOGEN SYNTHASE KINASE 3BETA INHIBITOR; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INDIRUBIN 3' MONOXIME; INDIRUBIN 3' OXIME; INTERLEUKIN 10; KENPAULLONE; L 803 MTS; LITHIUM; LITHIUM CHLORIDE; MAMMALIAN TARGET OF RAPAMYCIN; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE B; ROTTLERIN; SC 001; STAT PROTEIN; TACRINE(2) FERULIC ACID; TDZD 8; TRANSFORMING GROWTH FACTOR BETA1; UNCLASSIFIED DRUG; ANTIPARKINSON AGENT; ENZYME INHIBITOR; GLYCOGEN SYNTHASE KINASE 3; GLYCOGEN SYNTHASE KINASE 3 BETA;

EID: 84928608814     PISSN: 10436618     EISSN: 10961186     Source Type: Journal    
DOI: 10.1016/j.phrs.2015.03.010     Document Type: Review
Times cited : (228)

References (179)
  • 1
    • 0019026208 scopus 로고
    • Glycogen synthase kinase-3 from rabbit skeletal muscle. Separation from cyclic-AMP-dependent protein kinase and phosphorylase kinase
    • N. Embi, D.B. Rylatt, and P. Cohen Glycogen synthase kinase-3 from rabbit skeletal muscle. Separation from cyclic-AMP-dependent protein kinase and phosphorylase kinase Eur. J. Biochem. 107 1980 519 527
    • (1980) Eur. J. Biochem. , vol.107 , pp. 519-527
    • Embi, N.1    Rylatt, D.B.2    Cohen, P.3
  • 3
    • 80054702113 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 beta positively regulates Notch signaling in vascular smooth muscle cells: Role in cell proliferation and survival
    • S. Guha, J.P. Cullen, D. Morrow, A. Colombo, C. Lally, D. Walls, E.M. Redmond, and P.A. Cahill Glycogen synthase kinase 3 beta positively regulates Notch signaling in vascular smooth muscle cells: role in cell proliferation and survival Basic Res. Cardiol. 106 2011 773 785
    • (2011) Basic Res. Cardiol. , vol.106 , pp. 773-785
    • Guha, S.1    Cullen, J.P.2    Morrow, D.3    Colombo, A.4    Lally, C.5    Walls, D.6    Redmond, E.M.7    Cahill, P.A.8
  • 4
    • 0032533225 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta regulates cyclin D1 proteolysis and subcellular localization
    • J.A. Diehl, M. Cheng, M.F. Roussel, and C.J. Sherr Glycogen synthase kinase-3beta regulates cyclin D1 proteolysis and subcellular localization Genes Dev. 12 1998 3499 3511
    • (1998) Genes Dev. , vol.12 , pp. 3499-3511
    • Diehl, J.A.1    Cheng, M.2    Roussel, M.F.3    Sherr, C.J.4
  • 5
    • 82755187773 scopus 로고    scopus 로고
    • Glycogen synthase kinase (GSK)-3 promotes p70 ribosomal protein S6 kinase (p70S6K) activity and cell proliferation
    • S. Shin, L. Wolgamott, Y. Yu, J. Blenis, and S.O. Yoon Glycogen synthase kinase (GSK)-3 promotes p70 ribosomal protein S6 kinase (p70S6K) activity and cell proliferation Proc. Natl. Acad. Sci. U. S. A. 108 2011 E1204 E1213
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. E1204-E1213
    • Shin, S.1    Wolgamott, L.2    Yu, Y.3    Blenis, J.4    Yoon, S.O.5
  • 6
    • 65649100104 scopus 로고    scopus 로고
    • Unique and overlapping functions of GSK-3 isoforms in cell differentiation and proliferation and cardiovascular development
    • T. Forceand, and J.R. Woodgett Unique and overlapping functions of GSK-3 isoforms in cell differentiation and proliferation and cardiovascular development J. Biol. Chem. 284 2009 9643 9647
    • (2009) J. Biol. Chem. , vol.284 , pp. 9643-9647
    • Forceand, T.1    Woodgett, J.R.2
  • 7
    • 0442274617 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta (GSK3beta) binds to and promotes the actions of p53
    • P. Watcharasit, G.N. Bijur, L. Song, J. Zhu, X. Chen, and R.S. Jope Glycogen synthase kinase-3beta (GSK3beta) binds to and promotes the actions of p53 J. Biol. Chem. 278 2003 48872 48879
    • (2003) J. Biol. Chem. , vol.278 , pp. 48872-48879
    • Watcharasit, P.1    Bijur, G.N.2    Song, L.3    Zhu, J.4    Chen, X.5    Jope, R.S.6
  • 9
    • 84900436758 scopus 로고    scopus 로고
    • GSK3beta, but not GSK3alpha, inhibits the neuronal differentiation of neural progenitor cells as a downstream target of mammalian target of rapamycin complex1
    • J. Ahn, J. Jang, J. Choi, J. Lee, S.H. Oh, J. Lee, K. Yoon, and S. Kim GSK3beta, but not GSK3alpha, inhibits the neuronal differentiation of neural progenitor cells as a downstream target of mammalian target of rapamycin complex1 Stem Cells Dev. 23 2014 1121 1133
    • (2014) Stem Cells Dev. , vol.23 , pp. 1121-1133
    • Ahn, J.1    Jang, J.2    Choi, J.3    Lee, J.4    Oh, S.H.5    Lee, J.6    Yoon, K.7    Kim, S.8
  • 10
    • 77956198669 scopus 로고    scopus 로고
    • Regulation of AMPA receptor trafficking and function by glycogen synthase kinase 3
    • J. Wei, W. Liu, and Z. Yan Regulation of AMPA receptor trafficking and function by glycogen synthase kinase 3 J. Biol. Chem. 285 2010 26369 26376
    • (2010) J. Biol. Chem. , vol.285 , pp. 26369-26376
    • Wei, J.1    Liu, W.2    Yan, Z.3
  • 11
    • 0025286104 scopus 로고
    • Molecular cloning and expression of glycogen synthase kinase-3/factor A
    • J.R. Woodgett Molecular cloning and expression of glycogen synthase kinase-3/factor A EMBO J. 9 1990 2431 2438
    • (1990) EMBO J. , vol.9 , pp. 2431-2438
    • Woodgett, J.R.1
  • 12
    • 84873671033 scopus 로고    scopus 로고
    • Dual regulation of glycogen synthase kinase 3 (GSK3)alpha/beta by protein kinase C (PKC)alpha and Akt promotes thrombin-mediated integrin alphaIIbbeta3 activation and granule secretion in platelets
    • S.F. Moore, M.T. van den Bosch, R.W. Hunter, K. Sakamoto, A.W. Poole, and I. Hers Dual regulation of glycogen synthase kinase 3 (GSK3)alpha/beta by protein kinase C (PKC)alpha and Akt promotes thrombin-mediated integrin alphaIIbbeta3 activation and granule secretion in platelets J. Biol. Chem. 288 2013 3918 3928
    • (2013) J. Biol. Chem. , vol.288 , pp. 3918-3928
    • Moore, S.F.1    Van Den Bosch, M.T.2    Hunter, R.W.3    Sakamoto, K.4    Poole, A.W.5    Hers, I.6
  • 14
    • 0029811434 scopus 로고    scopus 로고
    • Wingless inactivates glycogen synthase kinase-3 via an intracellular signalling pathway which involves a protein kinase C
    • D. Cook, M.J. Fry, K. Hughes, R. Sumathipala, J.R. Woodgett, and T.C. Dale Wingless inactivates glycogen synthase kinase-3 via an intracellular signalling pathway which involves a protein kinase C EMBO J. 15 1996 4526 4536
    • (1996) EMBO J. , vol.15 , pp. 4526-4536
    • Cook, D.1    Fry, M.J.2    Hughes, K.3    Sumathipala, R.4    Woodgett, J.R.5    Dale, T.C.6
  • 15
    • 0035477020 scopus 로고    scopus 로고
    • GSK3 takes centre stage more than 20 years after its discovery
    • S. Frameand, and P. Cohen GSK3 takes centre stage more than 20 years after its discovery Biochem. J. 359 2001 1 16
    • (2001) Biochem. J. , vol.359 , pp. 1-16
    • Frameand, S.1    Cohen, P.2
  • 17
    • 33947519417 scopus 로고    scopus 로고
    • Regulation and function of glycogen synthase kinase-3 isoforms in neuronal survival
    • M.H. Liangand, and D.M. Chuang Regulation and function of glycogen synthase kinase-3 isoforms in neuronal survival J. Biol. Chem. 282 2007 3904 3917
    • (2007) J. Biol. Chem. , vol.282 , pp. 3904-3917
    • Liangand, M.H.1    Chuang, D.M.2
  • 18
    • 40049099291 scopus 로고    scopus 로고
    • Inhibition of GSK3 differentially modulates NF-κB, CREB, AP-1 and β-catenin signaling in hepatocytes, but fails to promote TNF-α-induced apoptosis
    • F. Götschel, C. Kern, S. Lang, T. Sparna, C. Markmann, J. Schwager, S. McNelly, F. von Weizsäcker, S. Laufer, and A. Hecht Inhibition of GSK3 differentially modulates NF-κB, CREB, AP-1 and β-catenin signaling in hepatocytes, but fails to promote TNF-α-induced apoptosis Exp. Cell Res. 314 2008 1351 1366
    • (2008) Exp. Cell Res. , vol.314 , pp. 1351-1366
    • Götschel, F.1    Kern, C.2    Lang, S.3    Sparna, T.4    Markmann, C.5    Schwager, J.6    McNelly, S.7    Von Weizsäcker, F.8    Laufer, S.9    Hecht, A.10
  • 19
    • 5444269904 scopus 로고    scopus 로고
    • Dual regulation of snail by GSK-3beta-mediated phosphorylation in control of epithelial-mesenchymal transition
    • B.P. Zhou, J. Deng, W. Xia, J. Xu, Y.M. Li, M. Gunduz, and M.C. Hung Dual regulation of snail by GSK-3beta-mediated phosphorylation in control of epithelial-mesenchymal transition Nat. Cell Biol. 6 2004 931 940
    • (2004) Nat. Cell Biol. , vol.6 , pp. 931-940
    • Zhou, B.P.1    Deng, J.2    Xia, W.3    Xu, J.4    Li, Y.M.5    Gunduz, M.6    Hung, M.C.7
  • 20
    • 84881272818 scopus 로고    scopus 로고
    • Role of GSK-3β in isoflurane-induced neuroinflammation and cognitive dysfunction in aged rats
    • S.-y. Li, X. Chen, Y.-l. Chen, L. Tan, Y.-l. Zhao, J.-t. Wang, Q. Xiang, and A.-l. Luo Role of GSK-3β in isoflurane-induced neuroinflammation and cognitive dysfunction in aged rats J. Huazhong Univ. Sci. Technolog. Med. Sci. 33 2013 530 535
    • (2013) J. Huazhong Univ. Sci. Technolog. Med. Sci. , vol.33 , pp. 530-535
    • Chen, X.1    Xiang, Q.2
  • 21
    • 84940602638 scopus 로고    scopus 로고
    • Combined regulation of mTORC1 and lysosomal acidification by GSK-3 suppresses autophagy and contributes to cancer cell growth
    • I. Azoulay-Alfaguter, R. Elya, L. Avrahami, A. Katz, and H. Eldar-Finkelman Combined regulation of mTORC1 and lysosomal acidification by GSK-3 suppresses autophagy and contributes to cancer cell growth Oncogene 2014
    • (2014) Oncogene
    • Azoulay-Alfaguter, I.1    Elya, R.2    Avrahami, L.3    Katz, A.4    Eldar-Finkelman, H.5
  • 22
    • 84860520259 scopus 로고    scopus 로고
    • GSK3: A key target for the development of novel treatments for type 2 diabetes mellitus and Alzheimer disease
    • C. Gao, C. Holscher, Y. Liu, and L. Li GSK3: a key target for the development of novel treatments for type 2 diabetes mellitus and Alzheimer disease Rev. Neurosci. 23 2012 1 11
    • (2012) Rev. Neurosci. , vol.23 , pp. 1-11
    • Gao, C.1    Holscher, C.2    Liu, Y.3    Li, L.4
  • 25
    • 84928631832 scopus 로고    scopus 로고
    • Antipsychotics: Neurobiological bases for a therapeutic approach
    • S. Gumruand, and F. Aricioglu Antipsychotics: neurobiological bases for a therapeutic approach Bull. Clin. Psychopharmacol. 23 2013 91 98
    • (2013) Bull. Clin. Psychopharmacol. , vol.23 , pp. 91-98
    • Gumruand, S.1    Aricioglu, F.2
  • 26
    • 77649184739 scopus 로고    scopus 로고
    • The regulation of IL-10 production by immune cells
    • M. Saraivaand, and A. O'Garra The regulation of IL-10 production by immune cells Nat. Rev. Immunol. 10 2010 170 181
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 170-181
    • Saraivaand, M.1    O'Garra, A.2
  • 28
    • 78649908226 scopus 로고    scopus 로고
    • GSK-3 beta activity and hyperdopamine-dependent behaviors
    • Y.C. Liand, and W.J. Gao GSK-3 beta activity and hyperdopamine-dependent behaviors Neurosci. Biobehav. Rev. 35 2011 645 654
    • (2011) Neurosci. Biobehav. Rev. , vol.35 , pp. 645-654
    • Liand, Y.C.1    Gao, W.J.2
  • 30
    • 23944486750 scopus 로고    scopus 로고
    • Toll-like receptor-mediated cytokine production is differentially regulated by glycogen synthase kinase 3
    • M. Martin, K. Rehani, R.S. Jope, and S.M. Michalek Toll-like receptor-mediated cytokine production is differentially regulated by glycogen synthase kinase 3 Nat. Immunol. 6 2005 777 784
    • (2005) Nat. Immunol. , vol.6 , pp. 777-784
    • Martin, M.1    Rehani, K.2    Jope, R.S.3    Michalek, S.M.4
  • 31
    • 52049094596 scopus 로고    scopus 로고
    • Differential regulation of STAT family members by glycogen synthase kinase-3
    • E. Beureland, and R.S. Jope Differential regulation of STAT family members by glycogen synthase kinase-3 J. Biol. Chem. 283 2008 21934 21944
    • (2008) J. Biol. Chem. , vol.283 , pp. 21934-21944
    • Beureland, E.1    Jope, R.S.2
  • 33
    • 84859336635 scopus 로고    scopus 로고
    • Regulation by glycogen synthase kinase-3 of inflammation and T cells in CNS diseases
    • E. Beurel Regulation by glycogen synthase kinase-3 of inflammation and T cells in CNS diseases Front. Mol. Neurosci. 4 2011
    • (2011) Front. Mol. Neurosci. , vol.4
    • Beurel, E.1
  • 34
    • 0141928780 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 beta regulates NF-kappa B1/p105 stability
    • F. Demarchi, C. Bertoli, P. Sandy, and C. Schneider Glycogen synthase kinase-3 beta regulates NF-kappa B1/p105 stability J. Biol. Chem. 278 2003 39583 39590
    • (2003) J. Biol. Chem. , vol.278 , pp. 39583-39590
    • Demarchi, F.1    Bertoli, C.2    Sandy, P.3    Schneider, C.4
  • 35
    • 84860822029 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 beta inhibitor suppresses Porphyromonas gingivalis lipopolysaccharide-induced CD40 expression by inhibiting nuclear factor-kappa B activation in mouse osteoblasts
    • L. Die, P. Yan, Z. Jun Jiang, T. Min Hua, W. Cai, and L. Xing Glycogen synthase kinase-3 beta inhibitor suppresses Porphyromonas gingivalis lipopolysaccharide-induced CD40 expression by inhibiting nuclear factor-kappa B activation in mouse osteoblasts Mol. Immunol. 52 2012 38 49
    • (2012) Mol. Immunol. , vol.52 , pp. 38-49
    • Die, L.1    Yan, P.2    Jun Jiang, Z.3    Min Hua, T.4    Cai, W.5    Xing, L.6
  • 36
    • 25444530592 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3beta functions to specify gene-specific, NF-kappaB-dependent transcription
    • K.A. Steinbrecher, W. Wilson 3rd, P.C. Cogswell, and A.S. Baldwin Glycogen synthase kinase 3beta functions to specify gene-specific, NF-kappaB-dependent transcription Mol. Cell Biol. 25 2005 8444 8455
    • (2005) Mol. Cell Biol. , vol.25 , pp. 8444-8455
    • Steinbrecher, K.A.1    Wilson, W.2    Cogswell, P.C.3    Baldwin, A.S.4
  • 40
    • 84877583717 scopus 로고    scopus 로고
    • Looking beyond the Wnt pathway for the deep nature of β-catenin
    • F. Fagotto Looking beyond the Wnt pathway for the deep nature of β-catenin EMBO Rep. 14 2013 422 433
    • (2013) EMBO Rep. , vol.14 , pp. 422-433
    • Fagotto, F.1
  • 41
    • 84864958637 scopus 로고    scopus 로고
    • Crossroads of integrins and cadherins in epithelia and stroma remodeling
    • C. Epifanoand, and M. Perez-Moreno Crossroads of integrins and cadherins in epithelia and stroma remodeling Cell Adhes. Migr. 6 2012 261 273
    • (2012) Cell Adhes. Migr. , vol.6 , pp. 261-273
    • Epifanoand, C.1    Perez-Moreno, M.2
  • 43
    • 84860756221 scopus 로고    scopus 로고
    • Maternal Wnt/β-catenin signaling coactivates transcription through NF-κB binding sites during xenopus axis formation
    • N.J. Armstrong, F. Fagotto, C. Prothmann, and R.A. Rupp Maternal Wnt/β-catenin signaling coactivates transcription through NF-κB binding sites during xenopus axis formation PLoS One 7 2012 e36136
    • (2012) PLoS One , vol.7 , pp. e36136
    • Armstrong, N.J.1    Fagotto, F.2    Prothmann, C.3    Rupp, R.A.4
  • 44
    • 84894442075 scopus 로고    scopus 로고
    • Ultraviolet radiation-induced inflammation activates beta-catenin signaling in mouse skin and skin tumors
    • R. Prasadand, and S.K. Katiyar Ultraviolet radiation-induced inflammation activates beta-catenin signaling in mouse skin and skin tumors Int. J. Oncol. 44 2014 1199 1206
    • (2014) Int. J. Oncol. , vol.44 , pp. 1199-1206
    • Prasadand, R.1    Katiyar, S.K.2
  • 45
    • 84896854393 scopus 로고    scopus 로고
    • A Wnt/beta-catenin negative feedback loop represses TLR-triggered inflammatory responses in alveolar epithelial cells
    • Y. Li, J. Shi, J. Yang, Y. Ma, L. Cheng, J. Zeng, X. Hao, C. Ma, Y. Wang, and X. Liu A Wnt/beta-catenin negative feedback loop represses TLR-triggered inflammatory responses in alveolar epithelial cells Mol. Immunol. 59 2014 128 135
    • (2014) Mol. Immunol. , vol.59 , pp. 128-135
    • Li, Y.1    Shi, J.2    Yang, J.3    Ma, Y.4    Cheng, L.5    Zeng, J.6    Hao, X.7    Ma, C.8    Wang, Y.9    Liu, X.10
  • 46
    • 34249034925 scopus 로고    scopus 로고
    • Beta-Catenin activity negatively regulates bacteria-induced inflammation
    • Y. Duan, A.P. Liao, S. Kuppireddi, Z. Ye, M.J. Ciancio, and J. Sun beta-Catenin activity negatively regulates bacteria-induced inflammation Lab. Invest. 87 2007 613 624
    • (2007) Lab. Invest. , vol.87 , pp. 613-624
    • Duan, Y.1    Liao, A.P.2    Kuppireddi, S.3    Ye, Z.4    Ciancio, M.J.5    Sun, J.6
  • 47
    • 79960007964 scopus 로고    scopus 로고
    • GSK-3β: A signaling pathway node modulating neural stem cell and endothelial cell interactions
    • Q. Li, M. Michaud, S. Canosa, A. Kuo, and J.A. Madri GSK-3β: a signaling pathway node modulating neural stem cell and endothelial cell interactions Angiogenesis 14 2011 173 185
    • (2011) Angiogenesis , vol.14 , pp. 173-185
    • Li, Q.1    Michaud, M.2    Canosa, S.3    Kuo, A.4    Madri, J.A.5
  • 48
    • 84857063792 scopus 로고    scopus 로고
    • Oct4 was a novel target of Wnt signaling pathway
    • J. Li, J. Li, and B. Chen Oct4 was a novel target of Wnt signaling pathway Mol. Cell. Biochem. 362 2012 233 240
    • (2012) Mol. Cell. Biochem. , vol.362 , pp. 233-240
    • Li, J.1    Li, J.2    Chen, B.3
  • 49
    • 0033119582 scopus 로고    scopus 로고
    • Beta-catenin mutations are more frequent in small colorectal adenomas than in larger adenomas and invasive carcinomas
    • W.S. Samowitz, M.D. Powers, L.N. Spirio, F. Nollet, F. van Roy, and M.L. Slattery Beta-catenin mutations are more frequent in small colorectal adenomas than in larger adenomas and invasive carcinomas Cancer Res. 59 1999 1442 1444
    • (1999) Cancer Res. , vol.59 , pp. 1442-1444
    • Samowitz, W.S.1    Powers, M.D.2    Spirio, L.N.3    Nollet, F.4    Van Roy, F.5    Slattery, M.L.6
  • 50
    • 0036295950 scopus 로고    scopus 로고
    • Characterisation of the phosphorylation of beta-catenin at the GSK-3 priming site Ser45
    • T. Hagenand, and A. Vidal-Puig Characterisation of the phosphorylation of beta-catenin at the GSK-3 priming site Ser45 Biochem. Biophys. Res. Commun. 294 2002 324 328
    • (2002) Biochem. Biophys. Res. Commun. , vol.294 , pp. 324-328
    • Hagenand, T.1    Vidal-Puig, A.2
  • 52
    • 83155180663 scopus 로고    scopus 로고
    • Dishevelled C-terminus: Prolyl and histidinyl motifs
    • H.Y. Wangand, and C.C. Malbon Dishevelled C-terminus: prolyl and histidinyl motifs Acta Physiol. 204 2012 65 73
    • (2012) Acta Physiol. , vol.204 , pp. 65-73
    • Wangand, H.Y.1    Malbon, C.C.2
  • 53
    • 84887619249 scopus 로고    scopus 로고
    • Toggling a conformational switch in Wnt/β-catenin signaling: Regulation of axin phosphorylation
    • O. Tacchelly-Benites, Z. Wang, E. Yang, E. Lee, and Y. Ahmed Toggling a conformational switch in Wnt/β-catenin signaling: regulation of axin phosphorylation BioEssays 35 2013 1063 1070
    • (2013) BioEssays , vol.35 , pp. 1063-1070
    • Tacchelly-Benites, O.1    Wang, Z.2    Yang, E.3    Lee, E.4    Ahmed, Y.5
  • 57
    • 63549084922 scopus 로고    scopus 로고
    • GSK3β N-terminus binding to p53 promotes its acetylation
    • T.-Y. Eomand, and R. Jope GSK3β N-terminus binding to p53 promotes its acetylation Mol. Cancer 8 2009 14
    • (2009) Mol. Cancer , vol.8 , pp. 14
    • Eomand, T.-Y.1    Jope, R.2
  • 58
    • 84876734646 scopus 로고    scopus 로고
    • MTOR signaling for biological control and cancer
    • A. Alayevand, and M.K. Holz mTOR signaling for biological control and cancer J. Cell. Physiol. 228 2013 1658 1664
    • (2013) J. Cell. Physiol. , vol.228 , pp. 1658-1664
    • Alayevand, A.1    Holz, M.K.2
  • 60
    • 33750040886 scopus 로고    scopus 로고
    • S6K1 regulates GSK3 under conditions of mTOR-dependent feedback inhibition of Akt
    • H.H. Zhang, A.I. Lipovsky, C.C. Dibble, M. Sahin, and B.D. Manning S6K1 regulates GSK3 under conditions of mTOR-dependent feedback inhibition of Akt Mol. Cell 24 2006 185 197
    • (2006) Mol. Cell , vol.24 , pp. 185-197
    • Zhang, H.H.1    Lipovsky, A.I.2    Dibble, C.C.3    Sahin, M.4    Manning, B.D.5
  • 61
    • 79955548609 scopus 로고    scopus 로고
    • Convergence of the mammalian target of rapamycin complex 1- and glycogen synthase kinase 3-beta-signaling pathways regulates the innate inflammatory response
    • H. Wang, J. Brown, Z. Gu, C.A. Garcia, R. Liang, P. Alard, E. Beurel, R.S. Jope, T. Greenway, and M. Martin Convergence of the mammalian target of rapamycin complex 1- and glycogen synthase kinase 3-beta-signaling pathways regulates the innate inflammatory response J. Immunol. (Baltimore, MD: 1950) 186 2011 5217 5226
    • (2011) J. Immunol. (Baltimore, MD: 1950) , vol.186 , pp. 5217-5226
    • Wang, H.1    Brown, J.2    Gu, Z.3    Garcia, C.A.4    Liang, R.5    Alard, P.6    Beurel, E.7    Jope, R.S.8    Greenway, T.9    Martin, M.10
  • 62
  • 63
    • 84887296037 scopus 로고    scopus 로고
    • Potential role of signal transducer and activator of transcription (STAT) 3 signaling pathway in inflammation, survival, proliferation and invasion of hepatocellular carcinoma
    • A. Subramaniam, M.K. Shanmugam, E. Perumal, F. Li, A. Nachiyappan, X. Dai, S.N. Swamy, K.S. Ahn, A.P. Kumar, and B.K. Tan Potential role of signal transducer and activator of transcription (STAT) 3 signaling pathway in inflammation, survival, proliferation and invasion of hepatocellular carcinoma Biochim. Biophy. Acta 2012
    • (2012) Biochim. Biophy. Acta
    • Subramaniam, A.1    Shanmugam, M.K.2    Perumal, E.3    Li, F.4    Nachiyappan, A.5    Dai, X.6    Swamy, S.N.7    Ahn, K.S.8    Kumar, A.P.9    Tan, B.K.10
  • 64
    • 84872178910 scopus 로고    scopus 로고
    • Comprehensive meta-analysis of Signal Transducers and Activators of Transcription (STAT) genomic binding patterns discerns cell-specific cis-regulatory modules
    • K. Kang, G.W. Robinson, and L. Hennighausen Comprehensive meta-analysis of Signal Transducers and Activators of Transcription (STAT) genomic binding patterns discerns cell-specific cis-regulatory modules BMC Genomics 14 2013 4
    • (2013) BMC Genomics , vol.14 , pp. 4
    • Kang, K.1    Robinson, G.W.2    Hennighausen, L.3
  • 66
    • 84866555886 scopus 로고    scopus 로고
    • From IL-2 to IL-37: The expanding spectrum of anti-inflammatory cytokines
    • J. Banchereau, V. Pascual, and A. O'Garra From IL-2 to IL-37: the expanding spectrum of anti-inflammatory cytokines Nat. Immunol. 13 2012 925 931
    • (2012) Nat. Immunol. , vol.13 , pp. 925-931
    • Banchereau, J.1    Pascual, V.2    O'Garra, A.3
  • 68
    • 84866334922 scopus 로고    scopus 로고
    • TGF-β-induced epithelial-mesenchymal transition: A link between cancer and inflammation
    • J. Fuxeand, and M.C. Karlsson TGF-β-induced epithelial-mesenchymal transition: a link between cancer and inflammation Semin. Cancer Biol. 22 2012 455 461
    • (2012) Semin. Cancer Biol. , vol.22 , pp. 455-461
    • Fuxeand, J.1    Karlsson, M.C.2
  • 69
    • 84867591701 scopus 로고    scopus 로고
    • Interventions in Wnt signaling as a novel therapeutic approach to improve myocardial infarct healing
    • K. Hermans, E.P. Daskalopoulos, and W.M. Blankesteijn Interventions in Wnt signaling as a novel therapeutic approach to improve myocardial infarct healing Fibrogenesis Tissue Repair 5 2012 16
    • (2012) Fibrogenesis Tissue Repair , vol.5 , pp. 16
    • Hermans, K.1    Daskalopoulos, E.P.2    Blankesteijn, W.M.3
  • 71
    • 84878071516 scopus 로고    scopus 로고
    • Regulation of the expression of GARP/latent TGF-β1 complexes on mouse T cells and their role in regulatory T cell and Th17 differentiation
    • J.P. Edwards, H. Fujii, A.X. Zhou, J. Creemers, D. Unutmaz, and E.M. Shevach Regulation of the expression of GARP/latent TGF-β1 complexes on mouse T cells and their role in regulatory T cell and Th17 differentiation J. Immunol. 190 2013 5506 5515
    • (2013) J. Immunol. , vol.190 , pp. 5506-5515
    • Edwards, J.P.1    Fujii, H.2    Zhou, A.X.3    Creemers, J.4    Unutmaz, D.5    Shevach, E.M.6
  • 72
    • 84879546865 scopus 로고    scopus 로고
    • Role of interleukin-10 in the regulation of tumorigenicity of a T cell lymphoma
    • M.R. Hassuneh, M. Nagarkatti, and P.S. Nagarkatti Role of interleukin-10 in the regulation of tumorigenicity of a T cell lymphoma Leuk. Lymphoma 54 2013 827 834
    • (2013) Leuk. Lymphoma , vol.54 , pp. 827-834
    • Hassuneh, M.R.1    Nagarkatti, M.2    Nagarkatti, P.S.3
  • 73
    • 84866528957 scopus 로고    scopus 로고
    • Restraint of inflammatory signaling by interdependent strata of negative regulatory pathways
    • P.J. Murrayand, and S.T. Smale Restraint of inflammatory signaling by interdependent strata of negative regulatory pathways Nat. Immunol. 13 2012 916 924
    • (2012) Nat. Immunol. , vol.13 , pp. 916-924
    • Murrayand, P.J.1    Smale, S.T.2
  • 77
    • 84884154793 scopus 로고    scopus 로고
    • Dendritic cells from the elderly display an intrinsic defect in the production of IL-10 in response to lithium chloride
    • S. Agrawal, S. Gollapudi, S. Gupta, and A. Agrawal Dendritic cells from the elderly display an intrinsic defect in the production of IL-10 in response to lithium chloride Exp. Gerontol. 48 2013 1285 1292
    • (2013) Exp. Gerontol. , vol.48 , pp. 1285-1292
    • Agrawal, S.1    Gollapudi, S.2    Gupta, S.3    Agrawal, A.4
  • 78
    • 84860165740 scopus 로고    scopus 로고
    • Mammalian MAPK signal transduction pathways activated by stress and inflammation: A 10-year update
    • J.M. Kyriakisand, and J. Avruch Mammalian MAPK signal transduction pathways activated by stress and inflammation: a 10-year update Physiol. Rev. 92 2012 689 737
    • (2012) Physiol. Rev. , vol.92 , pp. 689-737
    • Kyriakisand, J.M.1    Avruch, J.2
  • 79
    • 80052712201 scopus 로고    scopus 로고
    • The ins and outs of the epithelial to mesenchymal transition in health and disease
    • M.A. Nieto The ins and outs of the epithelial to mesenchymal transition in health and disease Annu. Rev. Cell Dev. Biol. 27 2011 347 376
    • (2011) Annu. Rev. Cell Dev. Biol. , vol.27 , pp. 347-376
    • Nieto, M.A.1
  • 81
    • 84884734979 scopus 로고    scopus 로고
    • Rasagiline in Parkinson's disease: A review based on meta-analysis of clinical data
    • S. Minguez-Minguez, J. Solis-Garcia Del Pozo, and J. Jordan Rasagiline in Parkinson's disease: a review based on meta-analysis of clinical data Pharmacol. Res. 74 2013 78-86
    • (2013) Pharmacol. Res. , vol.74 , pp. 78-86
    • Minguez-Minguez, S.1    Solis-Garcia Del Pozo, J.2    Jordan, J.3
  • 82
    • 55249089986 scopus 로고    scopus 로고
    • Medical management of Parkinson's disease
    • M.M. Goldenberg Medical management of Parkinson's disease P & T 33 2008 590 606
    • (2008) P & T , vol.33 , pp. 590-606
    • Goldenberg, M.M.1
  • 83
    • 84884879594 scopus 로고    scopus 로고
    • Mitochondrial defects and oxidative stress in Alzheimer disease and Parkinson disease
    • M.H. Yan, X. Wang, and X. Zhu Mitochondrial defects and oxidative stress in Alzheimer disease and Parkinson disease Free Radic. Biol. Med. 62 2013 90 101
    • (2013) Free Radic. Biol. Med. , vol.62 , pp. 90-101
    • Yan, M.H.1    Wang, X.2    Zhu, X.3
  • 85
    • 9444257518 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 beta (GSK3 beta) mediates 6-hydroxydopamine-induced neuronal death
    • G. Chen, K.A. Bower, C.L. Ma, S.Y. Fang, C.J. Thiele, and J. Luo Glycogen synthase kinase 3 beta (GSK3 beta) mediates 6-hydroxydopamine-induced neuronal death FASEB J. 18 2004 1162 1164
    • (2004) FASEB J. , vol.18 , pp. 1162-1164
    • Chen, G.1    Bower, K.A.2    Ma, C.L.3    Fang, S.Y.4    Thiele, C.J.5    Luo, J.6
  • 87
    • 77952960864 scopus 로고    scopus 로고
    • GSK-3 beta: A central kinase for neurodegenerative diseases?
    • A. Petit-Paitel GSK-3 beta: a central kinase for neurodegenerative diseases? Med. Sci. 26 2010 516 521
    • (2010) Med. Sci. , vol.26 , pp. 516-521
    • Petit-Paitel, A.1
  • 88
    • 56949087160 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta is associated with Parkinson's disease
    • M. Nagaoand, and H. Hayashi Glycogen synthase kinase-3beta is associated with Parkinson's disease Neurosci. Lett. 449 2009 103 107
    • (2009) Neurosci. Lett. , vol.449 , pp. 103-107
    • Nagaoand, M.1    Hayashi, H.2
  • 89
    • 77955664249 scopus 로고    scopus 로고
    • Elevated tauopathy and alpha-synuclein pathology in postmortem Parkinson's disease brains with and without dementia
    • J. Wills, J. Jones, T. Haggerty, V. Duka, J.N. Joyce, and A. Sidhu Elevated tauopathy and alpha-synuclein pathology in postmortem Parkinson's disease brains with and without dementia Exp. Neurol. 225 2010 210 218
    • (2010) Exp. Neurol. , vol.225 , pp. 210-218
    • Wills, J.1    Jones, J.2    Haggerty, T.3    Duka, V.4    Joyce, J.N.5    Sidhu, A.6
  • 90
    • 70349331692 scopus 로고    scopus 로고
    • Alpha-Synuclein contributes to GSK-3 beta-catalyzed Tau phosphorylation in Parkinson's disease models
    • T. Duka, V. Duka, J.N. Joyce, and A. Sidhu alpha-Synuclein contributes to GSK-3 beta-catalyzed Tau phosphorylation in Parkinson's disease models FASEB J. 23 2009 2820 2830
    • (2009) FASEB J. , vol.23 , pp. 2820-2830
    • Duka, T.1    Duka, V.2    Joyce, J.N.3    Sidhu, A.4
  • 92
    • 84861195059 scopus 로고    scopus 로고
    • Role of tau kinases (CDK5R1 and GSK3B) in Parkinson's disease: A study from India
    • e9-e15
    • G. Das, A.K. Misra, S.K. Das, K. Ray, and J. Ray Role of tau kinases (CDK5R1 and GSK3B) in Parkinson's disease: a study from India Neurobiol. Aging 33 2012 1485 e9-e15
    • (2012) Neurobiol. Aging , vol.33 , pp. 1485
    • Das, G.1    Misra, A.K.2    Das, S.K.3    Ray, K.4    Ray, J.5
  • 99
    • 84881098355 scopus 로고    scopus 로고
    • Activation of GSK-3beta and caspase-3 occurs in Nigral dopamine neurons during the development of apoptosis activated by a striatal injection of 6-hydroxydopamine
    • D. Hernandez-Baltazar, M.E. Mendoza-Garrido, and D. Martinez-Fong Activation of GSK-3beta and caspase-3 occurs in Nigral dopamine neurons during the development of apoptosis activated by a striatal injection of 6-hydroxydopamine PLoS One 8 2013 e70951
    • (2013) PLoS One , vol.8 , pp. e70951
    • Hernandez-Baltazar, D.1    Mendoza-Garrido, M.E.2    Martinez-Fong, D.3
  • 100
    • 78650183178 scopus 로고    scopus 로고
    • Knockdown of glycogen synthase kinase 3 beta attenuates 6-hydroxydopamine-induced apoptosis in SH-SY5Y cells
    • Y. Li, F. Luo, L. Wei, Z. Liu, and P. Xu Knockdown of glycogen synthase kinase 3 beta attenuates 6-hydroxydopamine-induced apoptosis in SH-SY5Y cells Neurosci. Lett. 487 2011 41 46
    • (2011) Neurosci. Lett. , vol.487 , pp. 41-46
    • Li, Y.1    Luo, F.2    Wei, L.3    Liu, Z.4    Xu, P.5
  • 101
    • 65549123313 scopus 로고    scopus 로고
    • Involvment of cytosolic and mitochondrial GSK-3beta in mitochondrial dysfunction and neuronal cell death of MPTP/MPP-treated neurons
    • A. Petit-Paitel, F. Brau, J. Cazareth, and J. Chabry Involvment of cytosolic and mitochondrial GSK-3beta in mitochondrial dysfunction and neuronal cell death of MPTP/MPP-treated neurons PLoS One 4 2009 e5491
    • (2009) PLoS One , vol.4 , pp. e5491
    • Petit-Paitel, A.1    Brau, F.2    Cazareth, J.3    Chabry, J.4
  • 102
    • 80054976654 scopus 로고    scopus 로고
    • Tacrine(2)-ferulic acid, a novel multifunctional dimer, attenuates 6-hydroxydopamine-induced apoptosis in PC12 cells by activating Akt pathway
    • H. Zhang, S.H. Mak, W. Cui, W.M. Li, R.W. Han, S.Q. Hu, M.Z. Ye, R.B. Pi, and Y.F. Han Tacrine(2)-ferulic acid, a novel multifunctional dimer, attenuates 6-hydroxydopamine-induced apoptosis in PC12 cells by activating Akt pathway Neurochem. Int. 59 2011 981 988
    • (2011) Neurochem. Int. , vol.59 , pp. 981-988
    • Zhang, H.1    Mak, S.H.2    Cui, W.3    Li, W.M.4    Han, R.W.5    Hu, S.Q.6    Ye, M.Z.7    Pi, R.B.8    Han, Y.F.9
  • 104
    • 58149395816 scopus 로고    scopus 로고
    • RTP801 is induced in Parkinson's disease and mediates neuron death by inhibiting Akt phosphorylation/activation
    • C. Malagelada, Z.H. Jin, and L.A. Greene RTP801 is induced in Parkinson's disease and mediates neuron death by inhibiting Akt phosphorylation/activation J. Neurosci. 28 2008 14363 14371
    • (2008) J. Neurosci. , vol.28 , pp. 14363-14371
    • Malagelada, C.1    Jin, Z.H.2    Greene, L.A.3
  • 105
    • 22344431879 scopus 로고    scopus 로고
    • Akt is essential for insulin modulation of amphetamine-induced human dopamine transporter cell-surface redistribution
    • B.G. Garcia, Y. Wei, J.A. Moron, R.Z. Lin, J.A. Javitch, and A. Galli Akt is essential for insulin modulation of amphetamine-induced human dopamine transporter cell-surface redistribution Mol. Pharmacol. 68 2005 102 109
    • (2005) Mol. Pharmacol. , vol.68 , pp. 102-109
    • Garcia, B.G.1    Wei, Y.2    Moron, J.A.3    Lin, R.Z.4    Javitch, J.A.5    Galli, A.6
  • 107
    • 44549085003 scopus 로고    scopus 로고
    • Bromocriptine activates NQO1 via Nrf2-PI3K/Akt signaling: Novel cytoprotective mechanism against oxidative damage
    • J.H. Lim, K.M. Kim, S.W. Kim, O. Hwang, and H.J. Choi Bromocriptine activates NQO1 via Nrf2-PI3K/Akt signaling: novel cytoprotective mechanism against oxidative damage Pharmacol. Res. 57 2008 325 331
    • (2008) Pharmacol. Res. , vol.57 , pp. 325-331
    • Lim, J.H.1    Kim, K.M.2    Kim, S.W.3    Hwang, O.4    Choi, H.J.5
  • 108
    • 33750358311 scopus 로고    scopus 로고
    • Involvement of multiple survival signal transduction pathways in the neuroprotective, neurorescue and APP processing activity of rasagiline and its propargyl moiety
    • O. Weinreb, T. Amit, O. Bar-Am, Y. Sagi, S. Mandel, and M.B. Youdim Involvement of multiple survival signal transduction pathways in the neuroprotective, neurorescue and APP processing activity of rasagiline and its propargyl moiety J. Neural Transm. Suppl. 2006 457 465
    • (2006) J. Neural Transm. Suppl. , pp. 457-465
    • Weinreb, O.1    Amit, T.2    Bar-Am, O.3    Sagi, Y.4    Mandel, S.5    Youdim, M.B.6
  • 109
    • 33645231485 scopus 로고    scopus 로고
    • An analog of a dipeptide-like structure of FK506 increases glial cell line-derived neurotrophic factor expression through cAMP response element-binding protein activated by heat shock protein 90/Akt signaling pathway
    • X. Cen, A. Nitta, S. Ohya, Y. Zhao, N. Ozawa, A. Mouri, D. Ibi, L. Wang, M. Suzuki, K. Saito, Y. Ito, T. Kawagoe, Y. Noda, Y. Ito, S. Furukawa, and T. Nabeshima An analog of a dipeptide-like structure of FK506 increases glial cell line-derived neurotrophic factor expression through cAMP response element-binding protein activated by heat shock protein 90/Akt signaling pathway J. Neurosci. 26 2006 3335 3344
    • (2006) J. Neurosci. , vol.26 , pp. 3335-3344
    • Cen, X.1    Nitta, A.2    Ohya, S.3    Zhao, Y.4    Ozawa, N.5    Mouri, A.6    Ibi, D.7    Wang, L.8    Suzuki, M.9    Saito, K.10    Ito, Y.11    Kawagoe, T.12    Noda, Y.13    Ito, Y.14    Furukawa, S.15    Nabeshima, T.16
  • 110
    • 24044489242 scopus 로고    scopus 로고
    • Brain-derived growth factor and glial cell line-derived growth factor use distinct intracellular signaling pathways to protect PD cybrids from H2O2-induced neuronal death
    • I.G. Onyango, J.B. Tuttle, and J.P. Bennett Jr. Brain-derived growth factor and glial cell line-derived growth factor use distinct intracellular signaling pathways to protect PD cybrids from H2O2-induced neuronal death Neurobiol. Dis. 20 2005 141 154
    • (2005) Neurobiol. Dis. , vol.20 , pp. 141-154
    • Onyango, I.G.1    Tuttle, J.B.2    Bennett, Jr.J.P.3
  • 111
    • 84907597785 scopus 로고    scopus 로고
    • Reduced striatal dopamine da D2 receptor function in dominant-negative GSK-3 transgenic mice
    • R. Gomez-Sintes, A. Bortolozzi, F. Artigas, and J.J. Lucas Reduced striatal dopamine DA D2 receptor function in dominant-negative GSK-3 transgenic mice Eur. Neuropsychopharmacol. 24 2014 1524 1533
    • (2014) Eur. Neuropsychopharmacol. , vol.24 , pp. 1524-1533
    • Gomez-Sintes, R.1    Bortolozzi, A.2    Artigas, F.3    Lucas, J.J.4
  • 112
    • 84874407555 scopus 로고    scopus 로고
    • Deletion of GSK3β in D2R-expressing neurons reveals distinct roles for β-arrestin signaling in antipsychotic and lithium action
    • N.M. Urs, J.C. Snyder, J.P. Jacobsen, S.M. Peterson, and M.G. Caron Deletion of GSK3β in D2R-expressing neurons reveals distinct roles for β-arrestin signaling in antipsychotic and lithium action Proc. Natl. Acad. Sci. 109 2012 20732 20737
    • (2012) Proc. Natl. Acad. Sci. , vol.109 , pp. 20732-20737
    • Urs, N.M.1    Snyder, J.C.2    Jacobsen, J.P.3    Peterson, S.M.4    Caron, M.G.5
  • 113
    • 22744449073 scopus 로고    scopus 로고
    • An Akt/beta-arrestin 2/PP2A signaling complex mediates dopaminergic neurotransmission and behavior
    • J.M. Beaulieu, T.D. Sotnikova, S. Marion, R.J. Lefkowitz, R.R. Gainetdinov, and M.G. Caron An Akt/beta-arrestin 2/PP2A signaling complex mediates dopaminergic neurotransmission and behavior Cell 122 2005 261 273
    • (2005) Cell , vol.122 , pp. 261-273
    • Beaulieu, J.M.1    Sotnikova, T.D.2    Marion, S.3    Lefkowitz, R.J.4    Gainetdinov, R.R.5    Caron, M.G.6
  • 116
    • 0842310838 scopus 로고    scopus 로고
    • Convergent evidence for impaired AKT1-GSK3beta signaling in schizophrenia
    • E.S. Emamian, D. Hall, M.J. Birnbaum, M. Karayiorgou, and J.A. Gogos Convergent evidence for impaired AKT1-GSK3beta signaling in schizophrenia Nat. Genet. 36 2004 131 137
    • (2004) Nat. Genet. , vol.36 , pp. 131-137
    • Emamian, E.S.1    Hall, D.2    Birnbaum, M.J.3    Karayiorgou, M.4    Gogos, J.A.5
  • 117
    • 84885105668 scopus 로고    scopus 로고
    • Altered GSK3 beta signaling in an infection-based mouse model of developmental neuropsychiatric disease
    • R. Willi, A. Harmeier, S. Giovanoli, and U. Meyer Altered GSK3 beta signaling in an infection-based mouse model of developmental neuropsychiatric disease Neuropharmacology 73 2013 56 65
    • (2013) Neuropharmacology , vol.73 , pp. 56-65
    • Willi, R.1    Harmeier, A.2    Giovanoli, S.3    Meyer, U.4
  • 118
    • 34447295080 scopus 로고    scopus 로고
    • Dopamine depletion and subsequent treatment with L-DOPA, but not the long-lived dopamine agonist pergolide, enhances activity of the Akt pathway in the rat striatum
    • E. Bychkov, M.R. Ahmed, K.N. Dalby, and E.V. Gurevich Dopamine depletion and subsequent treatment with L-DOPA, but not the long-lived dopamine agonist pergolide, enhances activity of the Akt pathway in the rat striatum J. Neurochem. 102 2007 699 711
    • (2007) J. Neurochem. , vol.102 , pp. 699-711
    • Bychkov, E.1    Ahmed, M.R.2    Dalby, K.N.3    Gurevich, E.V.4
  • 120
    • 0034531475 scopus 로고    scopus 로고
    • The alpha-synucleinopathies: Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy
    • M.G. Spillantiniand, and M. Goedert The alpha-synucleinopathies: Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy Ann. N. Y. Acad. Sci. 920 2000 16 27
    • (2000) Ann. N. Y. Acad. Sci. , vol.920 , pp. 16-27
    • Spillantiniand, M.G.1    Goedert, M.2
  • 122
    • 84928597963 scopus 로고    scopus 로고
    • The molecular mechanism of rotenone-induced alpha-synuclein aggregation: Emphasizing the role of the calcium/GSK3beta pathway
    • Y.H. Yuan, W.F. Yan, J.D. Sun, J.Y. Huang, Z. Mu, and N.H. Chen The molecular mechanism of rotenone-induced alpha-synuclein aggregation: emphasizing the role of the calcium/GSK3beta pathway Toxicol. Lett. 2014
    • (2014) Toxicol. Lett.
    • Yuan, Y.H.1    Yan, W.F.2    Sun, J.D.3    Huang, J.Y.4    Mu, Z.5    Chen, N.H.6
  • 123
    • 84899547628 scopus 로고    scopus 로고
    • Extracellular alpha-synuclein leads to microtubule destabilization via GSK-3beta-dependent Tau phosphorylation in PC12 cells
    • M. Gassowska, G.A. Czapski, B. Pajak, M. Cieslik, A.M. Lenkiewicz, and A. Adamczyk Extracellular alpha-synuclein leads to microtubule destabilization via GSK-3beta-dependent Tau phosphorylation in PC12 cells PLoS One 9 2014 e94259
    • (2014) PLoS One , vol.9 , pp. e94259
    • Gassowska, M.1    Czapski, G.A.2    Pajak, B.3    Cieslik, M.4    Lenkiewicz, A.M.5    Adamczyk, A.6
  • 124
    • 30044440010 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3beta modulates synphilin-1 ubiquitylation and cellular inclusion formation by SIAH: Implications for proteasomal function and Lewy body formation
    • E. Avraham, R. Szargel, A. Eyal, R. Rott, and S. Engelender Glycogen synthase kinase 3beta modulates synphilin-1 ubiquitylation and cellular inclusion formation by SIAH: implications for proteasomal function and Lewy body formation J. Biol. Chem. 280 2005 42877 42886
    • (2005) J. Biol. Chem. , vol.280 , pp. 42877-42886
    • Avraham, E.1    Szargel, R.2    Eyal, A.3    Rott, R.4    Engelender, S.5
  • 125
    • 34447527676 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress: Signaling the unfolded protein response
    • E. Lai, T. Teodoro, and A. Volchuk Endoplasmic reticulum stress: signaling the unfolded protein response Physiology (Bethesda, MD) 22 2007 193 201
    • (2007) Physiology (Bethesda, MD) , vol.22 , pp. 193-201
    • Lai, E.1    Teodoro, T.2    Volchuk, A.3
  • 126
    • 84953347508 scopus 로고    scopus 로고
    • Crosstalk between endoplasmic reticulum stress, oxidative stress, and autophagy: Potential therapeutic targets for acute CNS injuries
    • V.P. Nakka, P. Prakash-Babu, and R. Vemuganti Crosstalk between endoplasmic reticulum stress, oxidative stress, and autophagy: potential therapeutic targets for acute CNS injuries Mol. Neurobiol. 2014
    • (2014) Mol. Neurobiol.
    • Nakka, V.P.1    Prakash-Babu, P.2    Vemuganti, R.3
  • 128
    • 0037114971 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson's disease
    • E.J. Ryu, H.P. Harding, J.M. Angelastro, O.V. Vitolo, D. Ron, and L.A. Greene Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson's disease J. Neurosci. 22 2002 10690 10698
    • (2002) J. Neurosci. , vol.22 , pp. 10690-10698
    • Ryu, E.J.1    Harding, H.P.2    Angelastro, J.M.3    Vitolo, O.V.4    Ron, D.5    Greene, L.A.6
  • 129
    • 0037160134 scopus 로고    scopus 로고
    • Central role of glycogen synthase kinase-3beta in endoplasmic reticulum stress-induced caspase-3 activation
    • L. Song, P. De Sarno, and R.S. Jope Central role of glycogen synthase kinase-3beta in endoplasmic reticulum stress-induced caspase-3 activation J. Biol. Chem. 277 2002 44701 44708
    • (2002) J. Biol. Chem. , vol.277 , pp. 44701-44708
    • Song, L.1    De Sarno, P.2    Jope, R.S.3
  • 130
    • 14044261099 scopus 로고    scopus 로고
    • Valproate protects cells from ER stress-induced lipid accumulation and apoptosis by inhibiting glycogen synthase kinase-3
    • A.J. Kim, Y. Shi, R.C. Austin, and G.H. Werstuck Valproate protects cells from ER stress-induced lipid accumulation and apoptosis by inhibiting glycogen synthase kinase-3 J. Cell Sci. 118 2005 89 99
    • (2005) J. Cell Sci. , vol.118 , pp. 89-99
    • Kim, A.J.1    Shi, Y.2    Austin, R.C.3    Werstuck, G.H.4
  • 131
    • 84908105412 scopus 로고    scopus 로고
    • The mitochondrial complex i inhibitor rotenone induces endoplasmic reticulum stress and activation of GSK-3beta in cultured rat retinal cells
    • G. Han, R.J. Casson, G. Chidlow, and J.P. Wood The mitochondrial complex I inhibitor rotenone induces endoplasmic reticulum stress and activation of GSK-3beta in cultured rat retinal cells Invest. Ophthalmol. Vis. Sci. 55 2014 5616 5628
    • (2014) Invest. Ophthalmol. Vis. Sci. , vol.55 , pp. 5616-5628
    • Han, G.1    Casson, R.J.2    Chidlow, G.3    Wood, J.P.4
  • 132
    • 33845989064 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3β activity plays very important roles in determining the fate of oxidative stress-inflicted neuronal cells
    • K.-Y. Lee, S.-H. Koh, M.Y. Noh, K.-W. Park, Y.J. Lee, and S.H. Kim Glycogen synthase kinase-3β activity plays very important roles in determining the fate of oxidative stress-inflicted neuronal cells Brain Res. 1129 2007 89 99
    • (2007) Brain Res. , vol.1129 , pp. 89-99
    • Lee, K.-Y.1    Koh, S.-H.2    Noh, M.Y.3    Park, K.-W.4    Lee, Y.J.5    Kim, S.H.6
  • 133
    • 41149134840 scopus 로고    scopus 로고
    • GSK-3β down-regulates the transcription factor Nrf2 after oxidant damage: Relevance to exposure of neuronal cells to oxidative stress
    • A.I. Rojo, M.R.d. Sagarra, and A. Cuadrado GSK-3β down-regulates the transcription factor Nrf2 after oxidant damage: relevance to exposure of neuronal cells to oxidative stress J. Neurochem. 105 2008 192 202
    • (2008) J. Neurochem. , vol.105 , pp. 192-202
    • Rojo, A.I.1    Sagarra, M.R.D.2    Cuadrado, A.3
  • 134
    • 84867516589 scopus 로고    scopus 로고
    • Mitochondrial biogenesis contributes to ischemic neuroprotection afforded by LPS preconditioning
    • R. Anne Stetler, R.K. Leak, W. Yin, L. Zhang, S. Wang, Y. Gao, and J. Chen Mitochondrial biogenesis contributes to ischemic neuroprotection afforded by LPS preconditioning J. Neurochem. 123 2012 125 137
    • (2012) J. Neurochem. , vol.123 , pp. 125-137
    • Anne Stetler, R.1    Leak, R.K.2    Yin, W.3    Zhang, L.4    Wang, S.5    Gao, Y.6    Chen, J.7
  • 135
    • 14744289621 scopus 로고    scopus 로고
    • Expression time course and spatial distribution of activated caspase-3 after experimental status epilepticus: Contribution of delayed neuronal cell death to seizure-induced neuronal injury
    • J. Weise, T. Engelhorn, A. Dörfler, S. Aker, M. Bähr, and A. Hufnagel Expression time course and spatial distribution of activated caspase-3 after experimental status epilepticus: contribution of delayed neuronal cell death to seizure-induced neuronal injury Neurobiol. Dis. 18 2005 582 590
    • (2005) Neurobiol. Dis. , vol.18 , pp. 582-590
    • Weise, J.1    Engelhorn, T.2    Dörfler, A.3    Aker, S.4    Bähr, M.5    Hufnagel, A.6
  • 136
    • 72649106290 scopus 로고    scopus 로고
    • Phosphorus and proton magnetic resonance spectroscopy demonstrates mitochondrial dysfunction in early and advanced Parkinson's disease
    • E. Hattingen, J. Magerkurth, U. Pilatus, A. Mozer, C. Seifried, H. Steinmetz, F. Zanella, and R. Hilker Phosphorus and proton magnetic resonance spectroscopy demonstrates mitochondrial dysfunction in early and advanced Parkinson's disease Brain 132 2009 3285 3297
    • (2009) Brain , vol.132 , pp. 3285-3297
    • Hattingen, E.1    Magerkurth, J.2    Pilatus, U.3    Mozer, A.4    Seifried, C.5    Steinmetz, H.6    Zanella, F.7    Hilker, R.8
  • 137
    • 0442290275 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 beta is highly activated in nuclei and mitochondria
    • G.N. Bijurand, and R.S. Jope Glycogen synthase kinase-3 beta is highly activated in nuclei and mitochondria Neuroreport 14 2003 2415 2419
    • (2003) Neuroreport , vol.14 , pp. 2415-2419
    • Bijurand, G.N.1    Jope, R.S.2
  • 138
    • 62749123028 scopus 로고    scopus 로고
    • Unregulated mitochondrial GSK3β activity results in NADH: Ubiquinone oxidoreductase deficiency
    • T.D. King, B. Clodfelder-Miller, K.A. Barksdale, and G.N. Bijur Unregulated mitochondrial GSK3β activity results in NADH: ubiquinone oxidoreductase deficiency Neurotox. Res. 14 2008 367 382
    • (2008) Neurotox. Res. , vol.14 , pp. 367-382
    • King, T.D.1    Clodfelder-Miller, B.2    Barksdale, K.A.3    Bijur, G.N.4
  • 140
    • 0035469857 scopus 로고    scopus 로고
    • Growth factor withdrawal from primary human erythroid progenitors induces apoptosis through a pathway involving glycogen synthase kinase-3 and Bax
    • T.C. Somervaille, D.C. Linch, and A. Khwaja Growth factor withdrawal from primary human erythroid progenitors induces apoptosis through a pathway involving glycogen synthase kinase-3 and Bax Blood 98 2001 1374 1381
    • (2001) Blood , vol.98 , pp. 1374-1381
    • Somervaille, T.C.1    Linch, D.C.2    Khwaja, A.3
  • 141
    • 84873568965 scopus 로고    scopus 로고
    • Downregulation of Mcl-1 through GSK-3beta activation contributes to arsenic trioxide-induced apoptosis in acute myeloid leukemia cells
    • R. Wang, L. Xia, J. Gabrilove, S. Waxman, and Y. Jing Downregulation of Mcl-1 through GSK-3beta activation contributes to arsenic trioxide-induced apoptosis in acute myeloid leukemia cells Leukemia 27 2013 315 324
    • (2013) Leukemia , vol.27 , pp. 315-324
    • Wang, R.1    Xia, L.2    Gabrilove, J.3    Waxman, S.4    Jing, Y.5
  • 143
    • 33845643466 scopus 로고    scopus 로고
    • Alpha-synuclein induces hyperphosphorylation of tau in the MPTP model of parkinsonism
    • T. Duka, M. Rusnak, R.E. Drolet, V. Duka, C. Wersinger, J.L. Goudreau, and A. Sidhu Alpha-synuclein induces hyperphosphorylation of tau in the MPTP model of parkinsonism FASEB J. 20 2006 2302 2312
    • (2006) FASEB J. , vol.20 , pp. 2302-2312
    • Duka, T.1    Rusnak, M.2    Drolet, R.E.3    Duka, V.4    Wersinger, C.5    Goudreau, J.L.6    Sidhu, A.7
  • 144
    • 33750605793 scopus 로고    scopus 로고
    • The neurotoxin, MPP+, induces hyperphosphorylation of tau, in the presence of alpha-Synuclein, in SH-SY5Y neuroblastoma cells
    • T. Dukaand, and A. Sidhu The neurotoxin, MPP+, induces hyperphosphorylation of tau, in the presence of alpha-Synuclein, in SH-SY5Y neuroblastoma cells Neurotox. Res. 10 2006 1 10
    • (2006) Neurotox. Res. , vol.10 , pp. 1-10
    • Dukaand, T.1    Sidhu, A.2
  • 145
    • 67349186239 scopus 로고    scopus 로고
    • Microtubule-associated protein tau (MAPT) influences the risk of Parkinson's disease among Indians
    • G. Das, A.K. Misra, S.K. Das, K. Ray, and J. Ray Microtubule-associated protein tau (MAPT) influences the risk of Parkinson's disease among Indians Neurosci. Lett. 460 2009 16 20
    • (2009) Neurosci. Lett. , vol.460 , pp. 16-20
    • Das, G.1    Misra, A.K.2    Das, S.K.3    Ray, K.4    Ray, J.5
  • 153
    • 68649126582 scopus 로고    scopus 로고
    • Targets for neuroprotection in Parkinson's disease
    • T.A. Yacoubianand, and D.G. Standaert Targets for neuroprotection in Parkinson's disease Biochim. Biophys. Acta 1792 2009 676 687
    • (2009) Biochim. Biophys. Acta , vol.1792 , pp. 676-687
    • Yacoubianand, T.A.1    Standaert, D.G.2
  • 154
    • 63849147445 scopus 로고    scopus 로고
    • GSK-3 inhibitors and insulin receptor signaling in health, disease, and therapeutics
    • A. Wada GSK-3 inhibitors and insulin receptor signaling in health, disease, and therapeutics Front. Biosci. 14 2009 1558 1570
    • (2009) Front. Biosci. , vol.14 , pp. 1558-1570
    • Wada, A.1
  • 155
    • 77955682056 scopus 로고    scopus 로고
    • Using small molecule GSK3 inhibitors to treat inflammation
    • G. Klamer, E. Song, K. Ko, T. OBrien, and A. Dolnikov Using small molecule GSK3 inhibitors to treat inflammation Curr. Med. Chem. 17 2010 2873 2881
    • (2010) Curr. Med. Chem. , vol.17 , pp. 2873-2881
    • Klamer, G.1    Song, E.2    Ko, K.3    Obrien, T.4    Dolnikov, A.5
  • 158
    • 67349222563 scopus 로고    scopus 로고
    • Anti-hypertrophic effect of NHE-1 inhibition involves GSK-3beta-dependent attenuation of mitochondrial dysfunction
    • S. Javadov, V. Rajapurohitam, A. Kilic, A. Zeidan, A. Choi, and M. Karmazyn Anti-hypertrophic effect of NHE-1 inhibition involves GSK-3beta-dependent attenuation of mitochondrial dysfunction J. Mol. Cell. Cardiol. 46 2009 998 1007
    • (2009) J. Mol. Cell. Cardiol. , vol.46 , pp. 998-1007
    • Javadov, S.1    Rajapurohitam, V.2    Kilic, A.3    Zeidan, A.4    Choi, A.5    Karmazyn, M.6
  • 159
    • 84893769413 scopus 로고    scopus 로고
    • Mitochondrial permeability transition pore regulates Parkinson's disease development in mutant alpha-synuclein transgenic mice
    • L.J. Martin, S. Semenkow, A. Hanaford, and M. Wong Mitochondrial permeability transition pore regulates Parkinson's disease development in mutant alpha-synuclein transgenic mice Neurobiol. Aging 35 2014 1132 1152
    • (2014) Neurobiol. Aging , vol.35 , pp. 1132-1152
    • Martin, L.J.1    Semenkow, S.2    Hanaford, A.3    Wong, M.4
  • 160
    • 84981484055 scopus 로고    scopus 로고
    • The mood stabilizer lithium potentiates the antidepressant-like effects and ameliorates oxidative stress induced by acute ketamine in a mouse model of stress
    • C.T. Chiu, L. Scheuing, G. Liu, H.M. Liao, G.R. Linares, D. Lin, and M. Chuang The mood stabilizer lithium potentiates the antidepressant-like effects and ameliorates oxidative stress induced by acute ketamine in a mouse model of stress Int. J. Neuropsychopharmacol. 2014
    • (2014) Int. J. Neuropsychopharmacol.
    • Chiu, C.T.1    Scheuing, L.2    Liu, G.3    Liao, H.M.4    Linares, G.R.5    Lin, D.6    Chuang, M.7
  • 161
    • 84863400602 scopus 로고    scopus 로고
    • Identification of a maleimide-based glycogen synthase kinase-3 (GSK-3) inhibitor, BIP-135, that prolongs the median survival time of delta7 SMA KO mouse model of spinal muscular atrophy
    • P.C. Chen, I.N. Gaisina, B.F. El-Khodor, S. Ramboz, N.R. Makhortova, L.L. Rubin, and A.P. Kozikowski Identification of a maleimide-based glycogen synthase kinase-3 (GSK-3) inhibitor, BIP-135, that prolongs the median survival time of delta7 SMA KO mouse model of spinal muscular atrophy ACS Chem. Neurosci. 3 2012 5 11
    • (2012) ACS Chem. Neurosci. , vol.3 , pp. 5-11
    • Chen, P.C.1    Gaisina, I.N.2    El-Khodor, B.F.3    Ramboz, S.4    Makhortova, N.R.5    Rubin, L.L.6    Kozikowski, A.P.7
  • 162
    • 79956298780 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 regulates endoplasmic reticulum (ER) stress-induced CHOP expression in neuronal cells
    • G.P. Meares, M.A. Mines, E. Beurel, T.Y. Eom, L. Song, A.A. Zmijewska, and R.S. Jope Glycogen synthase kinase-3 regulates endoplasmic reticulum (ER) stress-induced CHOP expression in neuronal cells Exp. Cell Res. 317 2011 1621 1628
    • (2011) Exp. Cell Res. , vol.317 , pp. 1621-1628
    • Meares, G.P.1    Mines, M.A.2    Beurel, E.3    Eom, T.Y.4    Song, L.5    Zmijewska, A.A.6    Jope, R.S.7
  • 163
    • 68049121855 scopus 로고    scopus 로고
    • Blocked inhibitory serine-phosphorylation of glycogen synthase kinase-3 alpha/beta impairs in vivo neural precursor cell proliferation
    • T.Y. Eomand, and R.S. Jope Blocked inhibitory serine-phosphorylation of glycogen synthase kinase-3 alpha/beta impairs in vivo neural precursor cell proliferation Biol. Psychiatry 66 2009 494 502
    • (2009) Biol. Psychiatry , vol.66 , pp. 494-502
    • Eomand, T.Y.1    Jope, R.S.2
  • 165
    • 1942468747 scopus 로고    scopus 로고
    • Prevention of MPTP (N-methyl-4-phenyl-1,2,3,6-tetrahydropyridine) dopaminergic neurotoxicity in mice by chronic lithium: Involvements of Bcl-2 and Bax
    • M.B. Youdimand, and Z. Arraf Prevention of MPTP (N-methyl-4-phenyl-1,2,3,6-tetrahydropyridine) dopaminergic neurotoxicity in mice by chronic lithium: involvements of Bcl-2 and Bax Neuropharmacology 46 2004 1130 1140
    • (2004) Neuropharmacology , vol.46 , pp. 1130-1140
    • Youdimand, M.B.1    Arraf, Z.2
  • 167
    • 79954421190 scopus 로고    scopus 로고
    • Lithium fails to protect dopaminergic neurons in the 6-OHDA model of Parkinson's disease
    • Y. Yong, H.Q. Ding, Z.Q. Fan, J. Luo, and Z.J. Ke Lithium fails to protect dopaminergic neurons in the 6-OHDA model of Parkinson's disease Neurochem. Res. 36 2011 367 374
    • (2011) Neurochem. Res. , vol.36 , pp. 367-374
    • Yong, Y.1    Ding, H.Q.2    Fan, Z.Q.3    Luo, J.4    Ke, Z.J.5
  • 169
    • 84904187600 scopus 로고    scopus 로고
    • Parkinsonism and severe hypothyroidism in an elderly patient: A case of lithium toxicity due to pharmacological interactions
    • G. Basile, A. Epifanio, R. Mandraffino, and G. Trifiro Parkinsonism and severe hypothyroidism in an elderly patient: a case of lithium toxicity due to pharmacological interactions J. Clin. Pharm. Ther. 39 2014 452 454
    • (2014) J. Clin. Pharm. Ther. , vol.39 , pp. 452-454
    • Basile, G.1    Epifanio, A.2    Mandraffino, R.3    Trifiro, G.4
  • 170
    • 77954966128 scopus 로고    scopus 로고
    • NFAT/Fas signaling mediates the neuronal apoptosis and motor side effects of GSK-3 inhibition in a mouse model of lithium therapy
    • R. Gomez-Sintesand, and J.J. Lucas NFAT/Fas signaling mediates the neuronal apoptosis and motor side effects of GSK-3 inhibition in a mouse model of lithium therapy J. Clin. Invest. 120 2010 2432 2445
    • (2010) J. Clin. Invest. , vol.120 , pp. 2432-2445
    • Gomez-Sintesand, R.1    Lucas, J.J.2
  • 172
    • 2642523803 scopus 로고    scopus 로고
    • Lithium facilitates apoptotic signaling induced by activation of the Fas death domain-containing receptor
    • L. Song, T. Zhou, and R.S. Jope Lithium facilitates apoptotic signaling induced by activation of the Fas death domain-containing receptor BMC Neurosci. 5 2004 20
    • (2004) BMC Neurosci. , vol.5 , pp. 20
    • Song, L.1    Zhou, T.2    Jope, R.S.3
  • 173
    • 84855719836 scopus 로고    scopus 로고
    • Lithium regulates keratinocyte proliferation via glycogen synthase kinase 3 and NFAT2 (nuclear factor of activated T cells 2)
    • P.J. Hampton, R. Jans, R.J. Flockhart, G. Parker, and N.J. Reynolds Lithium regulates keratinocyte proliferation via glycogen synthase kinase 3 and NFAT2 (nuclear factor of activated T cells 2) J. Cell Physiol. 227 2012 1529 1537
    • (2012) J. Cell Physiol. , vol.227 , pp. 1529-1537
    • Hampton, P.J.1    Jans, R.2    Flockhart, R.J.3    Parker, G.4    Reynolds, N.J.5
  • 174
    • 0034600901 scopus 로고    scopus 로고
    • Negative regulation of T cell proliferation and interleukin 2 production by the serine threonine kinase GSK-3
    • T. Ohteki, M. Parsons, A. Zakarian, R.G. Jones, L.T. Nguyen, J.R. Woodgett, and P.S. Ohashi Negative regulation of T cell proliferation and interleukin 2 production by the serine threonine kinase GSK-3 J. Exp. Med. 192 2000 99 104
    • (2000) J. Exp. Med. , vol.192 , pp. 99-104
    • Ohteki, T.1    Parsons, M.2    Zakarian, A.3    Jones, R.G.4    Nguyen, L.T.5    Woodgett, J.R.6    Ohashi, P.S.7
  • 175
    • 84863057878 scopus 로고    scopus 로고
    • Lithium treatment of APPSwDI/NOS2-/- mice leads to reduced hyperphosphorylated tau, increased amyloid deposition and altered inflammatory phenotype
    • T.L. Sudduth, J.G. Wilson, A. Everhart, C.A. Colton, and D.M. Wilcock Lithium treatment of APPSwDI/NOS2-/- mice leads to reduced hyperphosphorylated tau, increased amyloid deposition and altered inflammatory phenotype PLoS One 7 2012 e31993
    • (2012) PLoS One , vol.7 , pp. e31993
    • Sudduth, T.L.1    Wilson, J.G.2    Everhart, A.3    Colton, C.A.4    Wilcock, D.M.5
  • 176
    • 77049116286 scopus 로고    scopus 로고
    • Lithium treatment arrests the development of neurofibrillary tangles in mutant tau transgenic mice with advanced neurofibrillary pathology
    • K. Leroy, K. Ando, C. Heraud, Z. Yilmaz, M. Authelet, J.M. Boeynaems, L. Buee, R. De Decker, and J.P. Brion Lithium treatment arrests the development of neurofibrillary tangles in mutant tau transgenic mice with advanced neurofibrillary pathology J. Alzheimer's Dis. 19 2010 705 719
    • (2010) J. Alzheimer's Dis. , vol.19 , pp. 705-719
    • Leroy, K.1    Ando, K.2    Heraud, C.3    Yilmaz, Z.4    Authelet, M.5    Boeynaems, J.M.6    Buee, L.7    De Decker, R.8    Brion, J.P.9
  • 177
    • 8744271562 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 in insulin and Wnt signalling: A double-edged sword?
    • S. Patel, B. Doble, and J.R. Woodgett Glycogen synthase kinase-3 in insulin and Wnt signalling: a double-edged sword? Biochem. Soc. Trans. 32 2004 803 808
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 803-808
    • Patel, S.1    Doble, B.2    Woodgett, J.R.3
  • 178
    • 0036081578 scopus 로고    scopus 로고
    • Role of glycogen synthase kinase-3 in TNF-alpha-induced NF-kappaB activation and apoptosis in hepatocytes
    • R.F. Schwabeand, and D.A. Brenner Role of glycogen synthase kinase-3 in TNF-alpha-induced NF-kappaB activation and apoptosis in hepatocytes Am. J. Physiol. Gastrointest. Liver Physiol. 283 2002 G204 G211
    • (2002) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.283 , pp. G204-G211
    • Schwabeand, R.F.1    Brenner, D.A.2
  • 179
    • 0034612636 scopus 로고    scopus 로고
    • Requirement for glycogen synthase kinase-3beta in cell survival and NF-kappaB activation
    • K.P. Hoeflich, J. Luo, E.A. Rubie, M.S. Tsao, O. Jin, and J.R. Woodgett Requirement for glycogen synthase kinase-3beta in cell survival and NF-kappaB activation Nature 406 2000 86 90
    • (2000) Nature , vol.406 , pp. 86-90
    • Hoeflich, K.P.1    Luo, J.2    Rubie, E.A.3    Tsao, M.S.4    Jin, O.5    Woodgett, J.R.6


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