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Volumn 12, Issue 9, 2003, Pages 1511-1519

Challenges and opportunies with glycogen synthase kinase-3 inhibitors for insulin resistance and Type 2 diabetes treatment

Author keywords

GSK 3; Insulin resistance; Protein kinase inhibitors; Type 2 diabetes

Indexed keywords

2 (2,4 DICHLOROPHENYL) 3 (1 METHYL 3 INDOLYL)MALEIMIDE; ALSTERPAULLONE; AMINOPYRIDINE DERIVATIVE; BERYLLIUM; BETA CATENIN; CHIR 98014; CHIR 98023; CHIR 99021; CYCLIN DEPENDENT KINASE INHIBITOR; FLAVOPIRIDOL; GLYCOGEN SYNTHASE KINASE 3; INSULIN; INSULIN RECEPTOR SUBSTRATE 1; LITHIUM DERIVATIVE; MALEIMIDE DERIVATIVE; METAL DERIVATIVE; NNC 57 0545; NNC 57 0588; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE INHIBITOR; PYRAZOLOPYRIMIDINE DERIVATIVE; QUINAZOLINE; SB 41528; SERINE PROTEINASE INHIBITOR; THIAZOLIDINE DERIVATIVE; THREONINE PROTEINASE; TOYOCAMYCIN; UNCLASSIFIED DRUG; UNINDEXED DRUG; VX 608; ZINC DERIVATIVE; ENZYME INHIBITOR;

EID: 0141740215     PISSN: 13543784     EISSN: None     Source Type: Journal    
DOI: 10.1517/13543784.12.9.1511     Document Type: Review
Times cited : (48)

References (83)
  • 1
    • 0042570843 scopus 로고    scopus 로고
    • Protein-protein interaction in insulin signalling and the molecular mechanisms of insulin resistance
    • VIRKAMAKI A, UEKI K, KAHN CR: Protein-protein interaction in insulin signalling and the molecular mechanisms of insulin resistance. J. Clin. Invest. (1999) 103:931-943.
    • (1999) J. Clin. Invest. , vol.103 , pp. 931-943
    • Virkamaki, A.1    Ueki, K.2    Kahn, C.R.3
  • 2
    • 0036470213 scopus 로고    scopus 로고
    • Insulin signalling pathways in time and space
    • SALTIEL AR, PESSIN JE: Insulin signalling pathways in time and space. Trends Cell Biol. (2002) 12:65-71.
    • (2002) Trends Cell Biol. , vol.12 , pp. 65-71
    • Saltiel, A.R.1    Pessin, J.E.2
  • 3
    • 0027978816 scopus 로고
    • The inhibition of glycogen synthase kinase-3 by insulin or insulin-like growth factor-1 in the rat skeletal muscle cell line L6 is blocked by wortmannin but not by rapamycin: Evidence that wortmannin blocks activation of the mitogen-activated protein kinase pathway in L6 cells between Ras and Raf
    • CROSS DA, ALESSI DR, VANDENHEEDE JR, MCDOWELL HE, HUNDAL HS, COHEN P: The inhibition of glycogen synthase kinase-3 by insulin or insulin-like growth factor-1 in the rat skeletal muscle cell line L6 is blocked by wortmannin but not by rapamycin: evidence that wortmannin blocks activation of the mitogen-activated protein kinase pathway in L6 cells between Ras and Raf. Biocbem. J. (1994) 303:21-26.
    • (1994) Biocbem. J. , vol.303 , pp. 21-26
    • Cross, D.A.1    Alessi, D.R.2    Vandenheede, J.R.3    McDowell, H.E.4    Hundal, H.S.5    Cohen, P.6
  • 4
    • 0027430039 scopus 로고
    • Glycogen synthase kinase-3 is rapidly inactivated in response to insulin and phosphorylates eukaryotic initiation factor eIF-2B
    • WELSH GI, PROUD CG: Glycogen synthase kinase-3 is rapidly inactivated in response to insulin and phosphorylates eukaryotic initiation factor eIF-2B. Biochem. J. (1993) 294:625-629.
    • (1993) Biochem. J. , vol.294 , pp. 625-629
    • Welsh, G.I.1    Proud, C.G.2
  • 5
    • 16944366762 scopus 로고    scopus 로고
    • Regulation of protein kinase B and glycogen synthase kinase-3 by insulin and beta-adrenergic agonist in rat epididymal fat cells
    • MOULE SK, WELSH GI, EDGELL NJ, FOULSTONE EJ, PROUD CG, DENTON RM: Regulation of protein kinase B and glycogen synthase kinase-3 by insulin and beta-adrenergic agonist in rat epididymal fat cells. J. Biol. Chem. (1997) 272:7713-7719.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7713-7719
    • Moule, S.K.1    Welsh, G.I.2    Edgell, N.J.3    Foulstone, E.J.4    Proud, C.G.5    Denton, R.M.6
  • 6
    • 0021174730 scopus 로고
    • Multisite phosphorylation of glycogen synthase. Molecular basis for the substrate specificity of glycogen synthase kinase-3 and casein kinase-II (glycogen synthase kinase-5)
    • WOODGETT JR, COHEN P: Multisite phosphorylation of glycogen synthase. Molecular basis for the substrate specificity of glycogen synthase kinase-3 and casein kinase-II (glycogen synthase kinase-5). Biochim. Biophys. Acta (1984) 788:339-347.
    • (1984) Biochim. Biophys. Acta , vol.788 , pp. 339-347
    • Woodgett, J.R.1    Cohen, P.2
  • 7
    • 0027448949 scopus 로고
    • Inactivation of rabbit muscle glycogen synthase by glycogen synthase kinase-3. Dominant role of the phosphorylation of Ser-640 (site-3a)
    • WANG Y, ROACH PJ: Inactivation of rabbit muscle glycogen synthase by glycogen synthase kinase-3. Dominant role of the phosphorylation of Ser-640 (site-3a). J. Biol. Chem. (1993) 268:23876-23880.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23876-23880
    • Wang, Y.1    Roach, P.J.2
  • 8
    • 0033536157 scopus 로고    scopus 로고
    • Cellular mechanisms of insulin resistance in humans
    • SHULMAN GI: Cellular mechanisms of insulin resistance in humans. Am. J. Cardiol. (1999) 84:3J-10J.
    • (1999) Am. J. Cardiol. , vol.84
    • Shulman, G.I.1
  • 9
    • 0030931560 scopus 로고    scopus 로고
    • Phosphorylation of insulin receptor substrate-1 by glycogen synthase kinase-3 impairs insulin action
    • ELDAR-FINKELMAN H, KREBS EG: Phosphorylation of insulin receptor substrate-1 by glycogen synthase kinase-3 impairs insulin action. Proc. Natl. Acad. Sci. USA (1997) 94:9660-9664.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9660-9664
    • Eldar-Finkelman, H.1    Krebs, E.G.2
  • 10
    • 0028023002 scopus 로고
    • Serine/threonine phosphorylation of insulin receptor substrate 1 modulates insulin receptor signalling
    • TANTI JF, GR'EMEAUX T, VAN OBBERGHEN E, LE MARCHAND-BRUSTEL Y: Serine/threonine phosphorylation of insulin receptor substrate 1 modulates insulin receptor signalling. J. Biol. Chem. (1994) 269:6051-6057.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6051-6057
    • Tanti, J.F.1    Gr'Emeaux, T.2    Van Obberghen, E.3    Le Marchand-Brustel, Y.4
  • 11
    • 0030061922 scopus 로고    scopus 로고
    • IRS-1 mediated inhibition of insulin receptor tyrosine kinase activity in TNF-α and obesity induced insulin resistance
    • HOTAMISLIGIL GS, PERALDI P, BUDAVARI A, ELLIS R, WHITE MF, SPIEGELMAN BM: IRS-1 mediated inhibition of insulin receptor tyrosine kinase activity in TNF-α and obesity induced insulin resistance. Science (1996) 271:665-668.
    • (1996) Science , vol.271 , pp. 665-668
    • Hotamisligil, G.S.1    Peraldi, P.2    Budavari, A.3    Ellis, R.4    White, M.F.5    Spiegelman, B.M.6
  • 13
    • 0032802629 scopus 로고    scopus 로고
    • Increased glycogen synthase kinase-3 activity in diabetes and obesity prone C57BL/6J mice
    • ELDAR-FINKELMAN H, SCHREYER SA, SHINOHARA MM, LEBOEUF RC, KREBS EG: Increased glycogen synthase kinase-3 activity in diabetes and obesity prone C57BL/6J mice. Diabetes (1999) 48:1662-1666.
    • (1999) Diabetes , vol.48 , pp. 1662-1666
    • Eldar-Finkelman, H.1    Schreyer, S.A.2    Shinohara, M.M.3    Leboeuf, R.C.4    Krebs, E.G.5
  • 14
    • 0030875687 scopus 로고    scopus 로고
    • Chromosomal mapping and mutational analysis of the coding region of the glycogen synthase kinase-3alpha and beta isoforms in patients with NIDDM
    • HANSEN L, ARDEN K, RASMUSSEN S et al.: Chromosomal mapping and mutational analysis of the coding region of the glycogen synthase kinase-3alpha and beta isoforms in patients with NIDDM. Diabetologia (1997) 40(8):940-946.
    • (1997) Diabetologia , vol.40 , Issue.8 , pp. 940-946
    • Hansen, L.1    Arden, K.2    Rasmussen, S.3
  • 15
    • 0026353474 scopus 로고
    • cDNA, cloning and properties of glycogen synthase kinase-3
    • WOODGETT JR: cDNA cloning and properties of glycogen synthase kinase-3. Methods Enzymol. (1991) 200:564-577.
    • (1991) Methods Enzymol. , vol.200 , pp. 564-577
    • Woodgett, J.R.1
  • 16
    • 0035909112 scopus 로고    scopus 로고
    • Judging a protein more than its name: GSK-3
    • RE12
    • WOODGETT JR: Judging a protein more than its name: GSK-3. Sci. STKE (2001) 100:RE12.
    • (2001) Sci. STKE , vol.100
    • Woodgett, J.R.1
  • 17
    • 0034859101 scopus 로고    scopus 로고
    • The multifaceted roles of glycogen synthase kinase 3beta in cellular signalling
    • GRIMES CA, JOPE RS: The multifaceted roles of glycogen synthase kinase 3beta in cellular signalling. Prog. Neurobiol. (2001) 65:391-426.
    • (2001) Prog. Neurobiol. , vol.65 , pp. 391-426
    • Grimes, C.A.1    Jope, R.S.2
  • 18
    • 0036090823 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3: An emerging therapeutic target
    • ELDAR-FINKELMAN H: Glycogen synthase kinase-3: an emerging therapeutic target. Trends Mol. Med. (2002) 8:126-132.
    • (2002) Trends Mol. Med. , vol.8 , pp. 126-132
    • Eldar-Finkelman, H.1
  • 19
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • CROSS DA, ALJESSI DR. COHEN P, ANDJELKOVICH M, HEMMINGS BA: Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature (1995) 378:785-789.
    • (1995) Nature , vol.378 , pp. 785-789
    • Cross, D.A.1    Aljessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Hemmings, B.A.5
  • 20
    • 0023656594 scopus 로고
    • Formation of protein kinase recognition sites by covalent modification of the substrate. Molecular mechanism for the synergistic action of casein kinase II and glycogen synthase kinase 3
    • FIOL CJ, MAHRENHOLZ AM, WANG Y, ROESKE RW, ROACH PJ: Formation of protein kinase recognition sites by covalent modification of the substrate. Molecular mechanism for the synergistic action of casein kinase II and glycogen synthase kinase 3. J. Biol. Chem (1987) 262:14042-14048.
    • (1987) J. Biol. Chem , vol.262 , pp. 14042-14048
    • Fiol, C.J.1    Mahrenholz, A.M.2    Wang, Y.3    Roeske, R.W.4    Roach, P.J.5
  • 22
    • 0035875098 scopus 로고    scopus 로고
    • Crystal structure of glycogen synthase kinase 3 beta: Structural basis for phosphate-primed substrate specificity and autoinhibition
    • DAJANI R, FRASER E, ROE SM et al.: Crystal structure of glycogen synthase kinase 3 beta: structural basis for phosphate-primed substrate specificity and autoinhibition. Cell (2001) 105:721-732.
    • (2001) Cell , vol.105 , pp. 721-732
    • Dajani, R.1    Fraser, E.2    Roe, S.M.3
  • 23
    • 0032990197 scopus 로고    scopus 로고
    • Phosphorylated seryl and threonyl but not tyrosyl, residues are efficient specificity determinants for GSK-3β and Shaggy
    • WILLIAMS DD, MARIN O, PINNA LA, PROUD CG: Phosphorylated seryl and threonyl but not tyrosyl, residues are efficient specificity determinants for GSK-3β and Shaggy. FEBS Lett. (1999) 448:86-90.
    • (1999) FEBS Lett. , vol.448 , pp. 86-90
    • Williams, D.D.1    Marin, O.2    Pinna, L.A.3    Proud, C.G.4
  • 24
    • 0038811796 scopus 로고    scopus 로고
    • Insulin mimetic action of synthetic phosphorylated peptide inhibitors of glycogen synthase kinase-3
    • PLOTKIN B, KAIDANOVICH O, TALIOR I, ELDAR-FINKELMAN H: Insulin mimetic action of synthetic phosphorylated peptide inhibitors of glycogen synthase kinase-3. J. Pharm. Exp. Ther. (2003) 305:974-980.
    • (2003) J. Pharm. Exp. Ther. , vol.305 , pp. 974-980
    • Plotkin, B.1    Kaidanovich, O.2    Talior, I.3    Eldar-Finkelman, H.4
  • 25
    • 0037127255 scopus 로고    scopus 로고
    • Identification of the Axin and Frat binding region of glycogen synthase kinase-3
    • FRASER E, YOUNG N, DAJANI R et al.: Identification of the Axin and Frat binding region of glycogen synthase kinase-3. J. Biol. Chem. (2002) 277:2176-2185.
    • (2002) J. Biol. Chem. , vol.277 , pp. 2176-2185
    • Fraser, E.1    Young, N.2    Dajani, R.3
  • 26
    • 0029664368 scopus 로고    scopus 로고
    • Binding of GSK-3 beta to the APC-beta-catenin complex and regulation of complex assembly
    • RUBINFELD B, ALBERT I, PORFIRI E, FIOL C, MUNEMITSU S, POLAKIS P: Binding of GSK-3 beta to the APC-beta-catenin complex and regulation of complex assembly. Science (1996) 272:1023-1026.
    • (1996) Science , vol.272 , pp. 1023-1026
    • Rubinfeld, B.1    Albert, I.2    Porfiri, E.3    Fiol, C.4    Munemitsu, S.5    Polakis, P.6
  • 28
    • 0029683606 scopus 로고    scopus 로고
    • The axis-inducing activity, stability and subcellular distribution of beta-catenin is regulated in Xenopus embryos by glycogen synthase kinase 3
    • YOST C, TORRES M, MILLER J, HUANG E, KIMELMAN D, MOON R: The axis-inducing activity, stability and subcellular distribution of beta-catenin is regulated in Xenopus embryos by glycogen synthase kinase 3. Genes Dev. (1996) 10:1443-1454.
    • (1996) Genes Dev. , vol.10 , pp. 1443-1454
    • Yost, C.1    Torres, M.2    Miller, J.3    Huang, E.4    Kimelman, D.5    Moon, R.6
  • 29
    • 0028569010 scopus 로고
    • Phosphorylation of the Drosophila adherens junction protein Armadillo: Roles for wingless signal and zeste-white 3 kinase
    • PEIFER M, PAI LM, CASEY M: Phosphorylation of the Drosophila. adherens junction protein Armadillo: roles for wingless signal and zeste-white 3 kinase. Dev. Biol. (1994) 166:543-556.
    • (1994) Dev. Biol. , vol.166 , pp. 543-556
    • Peifer, M.1    Pai, L.M.2    Casey, M.3
  • 30
    • 0034053069 scopus 로고    scopus 로고
    • Wnt signaling in oncogenesis and embryogenesis - A look outside the nucleus
    • PEIFER M, POLAKIS P: Wnt signaling in oncogenesis and embryogenesis - a look outside the nucleus. Science (2000) 287:1606-1609.
    • (2000) Science , vol.287 , pp. 1606-1609
    • Peifer, M.1    Polakis, P.2
  • 31
    • 0032821768 scopus 로고    scopus 로고
    • A GSK3-binding peptide from FRAT1 selectively inhibits the GSK3-catalysed phosphorylation of Axin and β-catenin
    • THOMAS GM, FRAME S, GOEDERT M, NATHKE I, POLAKIS P, COHEN P: A GSK3-binding peptide from FRAT1 selectively inhibits the GSK3-catalysed phosphorylation of Axin and β-catenin. FEBS Lett. (1999) 458:247-251.
    • (1999) FEBS Lett. , vol.458 , pp. 247-251
    • Thomas, G.M.1    Frame, S.2    Goedert, M.3    Nathke, I.4    Polakis, P.5    Cohen, P.6
  • 33
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: Structural basis for regulation
    • JOHNSON LN, NOBLE ME, OWEN DJ: Active and inactive protein kinases: structural basis for regulation. Cell (1996) 85:149-158.
    • (1996) Cell , vol.85 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.2    Owen, D.J.3
  • 34
    • 0031197185 scopus 로고    scopus 로고
    • Protein kinase inhibition: Natural and synthetic variations on a theme
    • TAYLOR SS, RADZIO-ANDZELM E: Protein kinase inhibition: natural and synthetic variations on a theme. Curr. Opin. Chem. Biol. (1997) 1:219-226.
    • (1997) Curr. Opin. Chem. Biol. , vol.1 , pp. 219-226
    • Taylor, S.S.1    Radzio-Andzelm, E.2
  • 35
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • DAVIES SP, REDDY H, CAIVANO M, COHEN P: Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem. J. (2000) 351:95-105.
    • (2000) Biochem. J. , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 36
    • 0036591874 scopus 로고    scopus 로고
    • Structural biology in drug design: Selective protein kinase inhibitors
    • SCAPIN G: Structural biology in drug design: selective protein kinase inhibitors. Drug Discov. Today (2002) 7:601-611.
    • (2002) Drug Discov. Today , vol.7 , pp. 601-611
    • Scapin, G.1
  • 37
    • 0032854118 scopus 로고    scopus 로고
    • The structure-based design of ATP-site directed protein kinase inhibitors
    • TOLEDO LM, LYDON NB, ELBAUM D: The structure-based design of ATP-site directed protein kinase inhibitors. Curr. Med. Chem. (1999) 6:775-805.
    • (1999) Curr. Med. Chem. , vol.6 , pp. 775-805
    • Toledo, L.M.1    Lydon, N.B.2    Elbaum, D.3
  • 39
    • 0033026444 scopus 로고    scopus 로고
    • Strategies toward the design of novel and selective protein tyrosine kinase inhibitors
    • TRAXLER P, FURET P: Strategies toward the design of novel and selective protein tyrosine kinase inhibitors. Pharmacol. Ther. (1999) 82:195-206.
    • (1999) Pharmacol. Ther. , vol.82 , pp. 195-206
    • Traxler, P.1    Furet, P.2
  • 40
    • 0035990905 scopus 로고    scopus 로고
    • Designing bisubstrate analog inhibitors for protein kinases
    • PARANG K, COLE PA: Designing bisubstrate analog inhibitors for protein kinases. Pharmacol. Ther. (2002) 93:145-157.
    • (2002) Pharmacol. Ther. , vol.93 , pp. 145-157
    • Parang, K.1    Cole, P.A.2
  • 41
    • 0037339766 scopus 로고    scopus 로고
    • Selective glycogen synthase kinase 3 inhibitors potentiate insulin activation of glucose transport and utilization in vitro and in vivo
    • RING DB, JOHNSON KW, HENRIKSEN EJ et al.: Selective glycogen synthase kinase 3 inhibitors potentiate insulin activation of glucose transport and utilization in vitro and in vivo. Diabetes (2003) 52:588-595.
    • (2003) Diabetes , vol.52 , pp. 588-595
    • Ring, D.B.1    Johnson, K.W.2    Henriksen, E.J.3
  • 42
    • 0033776383 scopus 로고    scopus 로고
    • Selective small molecule inhibitors of glycogen synthase kinase-3 modulate glycogen metabolism and gene transcription
    • COGHLAN MP, CULBERT AA, CROSS DA et al.: Selective small molecule inhibitors of glycogen synthase kinase-3 modulate glycogen metabolism and gene transcription. Chem. Biol. (2000) 7:793-803.
    • (2000) Chem. Biol. , vol.7 , pp. 793-803
    • Coghlan, M.P.1    Culbert, A.A.2    Cross, D.A.3
  • 43
    • 0032827466 scopus 로고    scopus 로고
    • Lithium at 50: Have the neuroprotective effects of this unique cation been overlooked?
    • MANJI HM, MOORE GJ, CHEN G: Lithium at 50: have the neuroprotective effects of this unique cation been overlooked? Biol. Psychiatry (1999) 46:929-940.
    • (1999) Biol. Psychiatry , vol.46 , pp. 929-940
    • Manji, H.M.1    Moore, G.J.2    Chen, G.3
  • 44
    • 0032947795 scopus 로고    scopus 로고
    • Antibipolar therapy: Mechanism of action of lithium
    • JOPE RS: Antibipolar therapy: mechanism of action of lithium. Mol. Psych. (1999) 4:117-128.
    • (1999) Mol. Psych. , vol.4 , pp. 117-128
    • Jope, R.S.1
  • 45
    • 0029776032 scopus 로고    scopus 로고
    • A Molecular Mechanism for the Effect of Lithium on Development
    • KLEIN PS, MELTON DA: A Molecular Mechanism for the Effect of Lithium on Development. Proc. Natl. Acad. sci. USA (1996) 93:8455-8459.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8455-8459
    • Klein, P.S.1    Melton, D.A.2
  • 46
    • 0034805180 scopus 로고    scopus 로고
    • Lithium inhibits glycogen synthase kinase-3 by competition for magnesium
    • RYVES WJ, HARWOOD AJ: Lithium inhibits glycogen synthase kinase-3 by competition for magnesium. Biochem. Biophys. Res. Comm. (2001) 280:720-725.
    • (2001) Biochem. Biophys. Res. Comm. , vol.280 , pp. 720-725
    • Ryves, W.J.1    Harwood, A.J.2
  • 47
    • 0021064785 scopus 로고
    • 'Insulin-like' effects of lithium ion on isolated rat adipocytes. II. Specific activation of glycogen synthase
    • CHENG K, CREACY S, LARNER J: 'Insulin-like' effects of lithium ion on isolated rat adipocytes. II. Specific activation of glycogen synthase. Mol. Cell. Biochem. (1983) 56:183-189.
    • (1983) Mol. Cell. Biochem. , vol.56 , pp. 183-189
    • Cheng, K.1    Creacy, S.2    Larner, J.3
  • 48
    • 0018602215 scopus 로고
    • Effect of lithium on glycogen synthesis in bepatocytcs from rat liver
    • NYFELER F, WALTER P: Effect of lithium on glycogen synthesis in bepatocytcs from rat liver. FEBS Lett. (1979) 108:197-199.
    • (1979) FEBS Lett. , vol.108 , pp. 197-199
    • Nyfeler, F.1    Walter, P.2
  • 49
    • 0030449964 scopus 로고    scopus 로고
    • Lithium inhibits glycogen synthase kinase-3 activity and mimics wingless signalling in intact cells
    • STAMBOLIC V, RUEL L, WOODGETT JR: Lithium inhibits glycogen synthase kinase-3 activity and mimics wingless signalling in intact cells. Curr. Biol. (1996) 6:1664-1668.
    • (1996) Curr. Biol. , vol.6 , pp. 1664-1668
    • Stambolic, V.1    Ruel, L.2    Woodgett, J.R.3
  • 50
    • 0021039875 scopus 로고
    • 'Insulin-like' effects of lithium ion on isolated rat adipocytes. I. Stimulation of glycogenesis beyond glucose transport
    • CHENG K, CREACY S, LARNER J: 'Insulin-like' effects of lithium ion on isolated rat adipocytes. I. Stimulation of glycogenesis beyond glucose transport. Mol. Cell. Biochem. (1983) 56:177-182.
    • (1983) Mol. Cell. Biochem. , vol.56 , pp. 177-182
    • Cheng, K.1    Creacy, S.2    Larner, J.3
  • 51
    • 0034717141 scopus 로고    scopus 로고
    • Inhibition of GSK-3 stimulates glycogen synthase and glucose transport by distinct mechanisms in 3T3-L1 adipocytes
    • ORENA SJ, TORCHIA AJ, GAROFALO RS: Inhibition of GSK-3 stimulates glycogen synthase and glucose transport by distinct mechanisms in 3T3-L1 adipocytes. J. Biol. Chem. (2000) 275:15765-15772.
    • (2000) J. Biol. Chem. , vol.275 , pp. 15765-15772
    • Orena, S.J.1    Torchia, A.J.2    Garofalo, R.S.3
  • 52
    • 0036295233 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 inhibition by lithium and beryllium suggests the presence of two magnesium binding sites
    • RYVES WJ, DAJANI R, PEARL L, HARWOOD AJ: Glycogen synthase kinase-3 inhibition by lithium and beryllium suggests the presence of two magnesium binding sites. Biochem. Biophys. Res. Comm. (2002) 290:967-972.
    • (2002) Biochem. Biophys. Res. Comm. , vol.290 , pp. 967-972
    • Ryves, W.J.1    Dajani, R.2    Pearl, L.3    Harwood, A.J.4
  • 53
    • 0036302005 scopus 로고    scopus 로고
    • Inhibition of glycogen synthase kinase-3b by bivalent zinc ions: Insight into the insulin-mimetic action of zinc
    • ILOUZ R, KAIDANOVIDH O, GURWITZ D, ELDAR-FINKELMAN H: Inhibition of glycogen synthase kinase-3b by bivalent zinc ions: insight into the insulin-mimetic action of zinc. Biochem. Biophys. Res. Commun. (2002) 295:102-106.
    • (2002) Biochem. Biophys. Res. Commun. , vol.295 , pp. 102-106
    • Ilouz, R.1    Kaidanovidh, O.2    Gurwitz, D.3    Eldar-Finkelman, H.4
  • 54
    • 0019287147 scopus 로고
    • Insulin-like effect of zinc on adipocytes
    • COULSTON L, DANDONA P: Insulin-like effect of zinc on adipocytes. Diabetes (1980) 29:665-667.
    • (1980) Diabetes , vol.29 , pp. 665-667
    • Coulston, L.1    Dandona, P.2
  • 55
    • 0019941222 scopus 로고
    • The mechanism of the insulin-like effects of ionic zinc
    • MAY JM, CONTOREGGI CS: The mechanism of the insulin-like effects of ionic zinc. J. Biol. Chem. (1982) 257:4362-4368.
    • (1982) J. Biol. Chem. , vol.257 , pp. 4362-4368
    • May, J.M.1    Contoreggi, C.S.2
  • 56
    • 0024441309 scopus 로고
    • IIb group metal ions (Zn2+, Cd2+, Hg2+) stimulate glucose transport activity by postinsulin receptor kinase mechanism in rat adipocyres
    • EZAKI O: IIb group metal ions (Zn2+, Cd2+, Hg2+) stimulate glucose transport activity by postinsulin receptor kinase mechanism in rat adipocyres. J. Biol. Chem. (1989) 264:16118-16222.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16118-16222
    • Ezaki, O.1
  • 57
    • 0035168559 scopus 로고    scopus 로고
    • Dietary zinc supplementation attenuates hyperglycemia in db/db mice
    • SIMON SF, TAYLOR CG: Dietary zinc supplementation attenuates hyperglycemia in db/db mice. Exp. Biol. Med. (2001) 226:43-51.
    • (2001) Exp. Biol. Med. , vol.226 , pp. 43-51
    • Simon, S.F.1    Taylor, C.G.2
  • 58
    • 0035808457 scopus 로고    scopus 로고
    • Indirubins inhibit glycogen synthase kinase-3 beta and CDK5/p25, two protein kinases involved in abnormal tau phosphorylation in Alzheimer's disease. A property common to most cyclin-dependent kinase inhibitors?
    • LECLERC S, GARNIER M, HOESSEL R et al.: Indirubins inhibit glycogen synthase kinase-3 beta and CDK5/p25, two protein kinases involved in abnormal tau phosphorylation in Alzheimer's disease. A property common to most cyclin-dependent kinase inhibitors? J. Biol. Chem. (2001) 276:251-260.
    • (2001) J. Biol. Chem. , vol.276 , pp. 251-260
    • Leclerc, S.1    Garnier, M.2    Hoessel, R.3
  • 59
    • 0033798031 scopus 로고    scopus 로고
    • Paullones are potent inhibitors of glycogen synthase kinase-3beta and cyclin-dependent kinase 5/p25
    • LEOST M, SCHULTZ C, LINK A et al.: Paullones are potent inhibitors of glycogen synthase kinase-3beta and cyclin-dependent kinase 5/p25. Eur. J. Biochem. (2000) 267:5983-5994.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 5983-5994
    • Leost, M.1    Schultz, C.2    Link, A.3
  • 60
    • 0032493729 scopus 로고    scopus 로고
    • Role of glycogen synthase kinase-3 in the phosphatidylinositol 3-Kinase/Akt cell survival pathway
    • PAP M, COOPER G: Role of glycogen synthase kinase-3 in the phosphatidylinositol 3-Kinase/Akt cell survival pathway. J. Biol. Chem. (1998) 273:19929-19932.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19929-19932
    • Pap, M.1    Cooper, G.2
  • 61
    • 0034677804 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 beta facilitates staurosporine- and heat shock-induced apoptosis. Protection by lithium
    • BIJUR GN, DE SARNO P, JOPE RS: Glycogen synthase kinase-3 beta facilitates staurosporine- and heat shock-induced apoptosis. Protection by lithium. J. Biol. Chem. (2000) 275:7583-7590.
    • (2000) J. Biol. Chem. , vol.275 , pp. 7583-7590
    • Bijur, G.N.1    De Sarno, P.2    Jope, R.S.3
  • 63
    • 0035038729 scopus 로고    scopus 로고
    • Inhibition of GSK-3 selectively reduces glucose-6-phosphatase and phosphatase and phosphoenolypyruvate carboxykinase gene expression
    • LOCHHEAD PA, COGHLAN M, RICE SQ, SUTHERLAND C: Inhibition of GSK-3 selectively reduces glucose-6-phosphatase and phosphatase and phosphoenolypyruvate carboxykinase gene expression. Diabetes (2001) 50:937-946.
    • (2001) Diabetes , vol.50 , pp. 937-946
    • Lochhead, P.A.1    Coghlan, M.2    Rice, S.Q.3    Sutherland, C.4
  • 64
    • 0037420819 scopus 로고    scopus 로고
    • 5-Aryl-pyrazolo[3,4-b]pyridazines: Potent inhibitors of glycogen synthase kinase-3 (GSK-3)
    • WITHERINGTON J, BORDAS V, HAIGH D et al.: 5-Aryl-pyrazolo[3,4-b]pyridazines: potent inhibitors of glycogen synthase kinase-3 (GSK-3). Bioorg. Med. Chem. Lett. (2003) 13:1581-1584.
    • (2003) Bioorg. Med. Chem. Lett. , vol.13 , pp. 1581-1584
    • Witherington, J.1    Bordas, V.2    Haigh, D.3
  • 65
    • 0036302960 scopus 로고    scopus 로고
    • Inhibition of glycogen synthase kinase 3 improves insulin action and glucose metabolism in human skeletal muscle
    • NIKOULINA SE, CIARALDI TP, MUDALIAR S, CARTER L, JOHNSON K, HENRY RR: Inhibition of glycogen synthase kinase 3 improves insulin action and glucose metabolism in human skeletal muscle. Diabetes (2002) 51:2190-2198.
    • (2002) Diabetes , vol.51 , pp. 2190-2198
    • Nikoulina, S.E.1    Ciaraldi, T.P.2    Mudaliar, S.3    Carter, L.4    Johnson, K.5    Henry, R.R.6
  • 66
    • 0037405647 scopus 로고    scopus 로고
    • Modulation of muscle insulin resistance by selective inhibition of GSK-3 in Zucker diabetic fatty rats
    • HENRIKSEN EJ, KINNICK TR, TEACHEY MK et al.: Modulation of muscle insulin resistance by selective inhibition of GSK-3 in Zucker diabetic fatty rats. Am. J. Physiol. Endocrinol. Metab. (2003) 284:E892-E900.
    • (2003) Am. J. Physiol. Endocrinol. Metab. , vol.284
    • Henriksen, E.J.1    Kinnick, T.R.2    Teachey, M.K.3
  • 67
    • 0036789185 scopus 로고    scopus 로고
    • Effects of a novel glycogen synthase kinase-3 inhibitor on insulin-stimulated glucose metabolism in Zucker diabetic fatty (fa/fa) rats
    • CLINE GW, JOHNSON K, REGITTNIG W et al.: Effects of a novel glycogen synthase kinase-3 inhibitor on insulin-stimulated glucose metabolism in Zucker diabetic fatty (fa/fa) rats. Diabetes (2002) 51:2903-2910.
    • (2002) Diabetes , vol.51 , pp. 2903-2910
    • Cline, G.W.1    Johnson, K.2    Regittnig, W.3
  • 68
    • 0141712049 scopus 로고    scopus 로고
    • VX-608. IDdb3 Drug Report
    • VX-608. IDdb3 Drug Report (2003).
    • (2003)
  • 69
    • 0141488804 scopus 로고    scopus 로고
    • KINETEK: GSK-3β inhibitors. IDdb3 Drug Report
    • KINETEK: GSK-3β inhibitors. IDdb3 Drug Report (2002).
    • (2002)
  • 70
    • 0037013685 scopus 로고    scopus 로고
    • Scaffold hopping and optimization towards libraries of glycogen synthase kinase-3 inhibitors
    • NAERUM L, NORSKOV-LAURITSEN L, OLESEN PH: Scaffold hopping and optimization towards libraries of glycogen synthase kinase-3 inhibitors. Bioorg. Med. Chem. Lett. (2002) 12:1525-1528.
    • (2002) Bioorg. Med. Chem. Lett. , vol.12 , pp. 1525-1528
    • Naerum, L.1    Norskov-Lauritsen, L.2    Olesen, P.H.3
  • 71
    • 0141823362 scopus 로고    scopus 로고
    • NOVO NORDISK: GSK-3 inhibitors. IDdb3 Drug Report
    • NOVO NORDISK: GSK-3 inhibitors. IDdb3 Drug Report (2002).
    • (2002)
  • 72
    • 0037075791 scopus 로고    scopus 로고
    • First non-ATP competitive glycogen synthase kinase 3 beta (GSK-3beta) inhibitors: Thiadiazolidinones (TDZD) as potential drugs for the treatment of Alzheimer's disease
    • MARTINEZ A, ALONSO M, CASTRO A, PEREZ C, MORENO FJ: First non-ATP competitive glycogen synthase kinase 3 beta (GSK-3beta) inhibitors: thiadiazolidinones (TDZD) as potential drugs for the treatment of Alzheimer's disease. J. Med. Chem. (2002) 45:1292-1299.
    • (2002) J. Med. Chem. , vol.45 , pp. 1292-1299
    • Martinez, A.1    Alonso, M.2    Castro, A.3    Perez, C.4    Moreno, F.J.5
  • 73
    • 0036792527 scopus 로고    scopus 로고
    • Peptide-mediated cell delivery: Application in protein target validation
    • LINDSAY MA: Peptide-mediated cell delivery: application in protein target validation. Curr. Opin. Pahrmacol. (2002) 2:587-594.
    • (2002) Curr. Opin. Pahrmacol. , vol.2 , pp. 587-594
    • Lindsay, M.A.1
  • 74
    • 0033023173 scopus 로고    scopus 로고
    • Noninvasive intracellular delivery of functional peptides and proteins
    • HAWIGER J: Noninvasive intracellular delivery of functional peptides and proteins. Curr. Opin. Chem. Biol. (1999) 3:89-94.
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 89-94
    • Hawiger, J.1
  • 75
    • 0034844734 scopus 로고    scopus 로고
    • Alternative routes of administration as an approach to improve insulin therapy: Update on dermal, oral, nasal and pulmonary delivery
    • HEINEMANN L, PFUTZNER A, HEISE T: Alternative routes of administration as an approach to improve insulin therapy: update on dermal, oral, nasal and pulmonary delivery. Curr. Pharm. Des. (2001) 14:1327-1351.
    • (2001) Curr. Pharm. Des. , vol.14 , pp. 1327-1351
    • Heinemann, L.1    Pfutzner, A.2    Heise, T.3
  • 76
    • 0035019608 scopus 로고    scopus 로고
    • Delivery of bioacrive peptides and proteins across oral (buccal) mucosa
    • SENEL S, KREMER M, NAGY K, SQUIER C: Delivery of bioacrive peptides and proteins across oral (buccal) mucosa. Curr. Pharm. Biotechnol. (2001) 2:175-186.
    • (2001) Curr. Pharm. Biotechnol. , vol.2 , pp. 175-186
    • Senel, S.1    Kremer, M.2    Nagy, K.3    Squier, C.4
  • 77
    • 0037144397 scopus 로고    scopus 로고
    • Albumin binding as a general strategy for improving the pharmacokinetics of proteins
    • DENNIS MS, ZHANG M, MENG YG et al.: Albumin binding as a general strategy for improving the pharmacokinetics of proteins. J. Biol. Chem. (2002) 277:35035-35043.
    • (2002) J. Biol. Chem. , vol.277 , pp. 35035-35043
    • Dennis, M.S.1    Zhang, M.2    Meng, Y.G.3
  • 78
    • 9044226136 scopus 로고    scopus 로고
    • Soluble, fatty acid acylated insulins bind to albumin and show protracted action in pigs
    • MARKUSSEN J, HAVELUND S, KURTZHALS P et al.: Soluble, fatty acid acylated insulins bind to albumin and show protracted action in pigs. Diabetologia (1996) 39:281-288.
    • (1996) Diabetologia , vol.39 , pp. 281-288
    • Markussen, J.1    Havelund, S.2    Kurtzhals, P.3
  • 79
    • 0037442990 scopus 로고    scopus 로고
    • A role for glycogen synthase kinase-3 in mitotic spindle dynamics and chromosome alignment
    • WAKEFIELD JG, STEPHENS DJ, TAVARE JM: A role for glycogen synthase kinase-3 in mitotic spindle dynamics and chromosome alignment. J. Cell Sci. (2003) 116:637-646.
    • (2003) J. Cell Sci. , vol.116 , pp. 637-646
    • Wakefield, J.G.1    Stephens, D.J.2    Tavare, J.M.3
  • 80
    • 0034612636 scopus 로고    scopus 로고
    • Requirement for glycogen synthase kinase-3β in cell survival and NF-κB activation
    • HOEFLICH KP, LUO J, RUBIE EA, TSAO MS, JIN O, WOODGETT JR: Requirement for glycogen synthase kinase-3β in cell survival and NF-κB activation. Nature (2000) 406:86-90.
    • (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
  • 81
    • 0025195547 scopus 로고
    • (+)-binding properties of a recombinant protein-tyrosine kinase derived from the human insulin receptor
    • (+)-binding properties of a recombinant protein-tyrosine kinase derived from the human insulin receptor. Proc. Natl. Acad. Sci. USA (1990) 87:2805-2809.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2805-2809
    • Wente, S.R.1    Villalba, M.2    Schramm, V.L.3    Rosen, O.M.4
  • 82
    • 0027957437 scopus 로고
    • Isoform differences in substrate recognition by glycogen synthase kinases 3 alpha and beta in the phosphorylation of phosphatase inhibitor 2
    • WANG QM, PARK IK, FIOL CJ, ROACH PJ, DEPAOLI-ROACH AA: Isoform differences in substrate recognition by glycogen synthase kinases 3 alpha and beta in the phosphorylation of phosphatase inhibitor 2. Biochemistry (1994) 33:143-147.
    • (1994) Biochemistry , vol.33 , pp. 143-147
    • Wang, Q.M.1    Park, I.K.2    Fiol, C.J.3    Roach, P.J.4    Depaoli-Roach, A.A.5
  • 83
    • 0141488803 scopus 로고    scopus 로고
    • VERTEX: IDdb3 report
    • VERTEX: IDdb3 report (2003).
    • (2003)


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