메뉴 건너뛰기




Volumn 8, Issue 7, 2013, Pages

Glycogen Phosphorylase Inhibitor N-(3,5-Dimethyl-Benzoyl)-N'-(β-D-Glucopyranosyl)Urea Improves Glucose Tolerance under Normoglycemic and Diabetic Conditions and Rearranges Hepatic Metabolism

Author keywords

[No Author keywords available]

Indexed keywords

GLUCOSE; GLYCOGEN PHOSPHORYLASE; GLYCOSYLTRANSFERASE INHIBITOR; KB 228; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 2; N (3,5 DIMETHYL BENZOYL) N' (BETA DEXTRO GLUCOPYRANOSYL)UREA; UNCLASSIFIED DRUG; UNCOUPLING PROTEIN 2;

EID: 84880807739     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0069420     Document Type: Article
Times cited : (46)

References (49)
  • 1
    • 33244464562 scopus 로고    scopus 로고
    • Critical nodes in signalling pathways: insights into insulin action
    • Taniguchi CM, Emanuelli B, Kahn CR, (2006) Critical nodes in signalling pathways: insights into insulin action. Nat Rev Mol Cell Biol 7: 85-96.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 85-96
    • Taniguchi, C.M.1    Emanuelli, B.2    Kahn, C.R.3
  • 2
    • 0023138702 scopus 로고
    • Control of glycogen synthesis in health and disease
    • Stalmans W, Bollen M, Mvumbi L, (1987) Control of glycogen synthesis in health and disease. Diabetes Metab Rev 3: 127-161.
    • (1987) Diabetes Metab Rev , vol.3 , pp. 127-161
    • Stalmans, W.1    Bollen, M.2    Mvumbi, L.3
  • 3
    • 0025069757 scopus 로고
    • Short-term hormonal control of protein phosphatases involved in hepatic glycogen metabolism
    • Stalmans W, Bollen M, Toth B, Gergely P, (1990) Short-term hormonal control of protein phosphatases involved in hepatic glycogen metabolism. Adv Enzyme Regul 30: 305-327.
    • (1990) Adv Enzyme Regul , vol.30 , pp. 305-327
    • Stalmans, W.1    Bollen, M.2    Toth, B.3    Gergely, P.4
  • 4
    • 84855449701 scopus 로고    scopus 로고
    • Acetylation negatively regulates glycogen phosphorylase by recruiting protein phosphatase 1
    • Zhang T, Wang S, Lin Y, Xu W, Ye D, et al. (2012) Acetylation negatively regulates glycogen phosphorylase by recruiting protein phosphatase 1. Cell Metab 15: 75-87.
    • (2012) Cell Metab , vol.15 , pp. 75-87
    • Zhang, T.1    Wang, S.2    Lin, Y.3    Xu, W.4    Ye, D.5
  • 5
    • 0035968302 scopus 로고    scopus 로고
    • Hepatic glycogen synthesis is highly sensitive to phosphorylase activity: evidence from metabolic control analysis
    • Aiston S, Hampson L, Gomez-Foix AM, Guinovart JJ, Agius L, (2001) Hepatic glycogen synthesis is highly sensitive to phosphorylase activity: evidence from metabolic control analysis. J Biol Chem 276: 23858-23866.
    • (2001) J Biol Chem , vol.276 , pp. 23858-23866
    • Aiston, S.1    Hampson, L.2    Gomez-Foix, A.M.3    Guinovart, J.J.4    Agius, L.5
  • 6
    • 0034027521 scopus 로고    scopus 로고
    • Impaired glycogen synthesis in hepatocytes from Zucker fatty fa/fa rats: the role of increased phosphorylase activity
    • Aiston S, Peak M, Agius L, (2000) Impaired glycogen synthesis in hepatocytes from Zucker fatty fa/fa rats: the role of increased phosphorylase activity. Diabetologia 43: 589-597.
    • (2000) Diabetologia , vol.43 , pp. 589-597
    • Aiston, S.1    Peak, M.2    Agius, L.3
  • 7
    • 78549257789 scopus 로고    scopus 로고
    • Physiological control of liver glycogen metabolism: lessons from novel glycogen phosphorylase inhibitors
    • Agius L, (2010) Physiological control of liver glycogen metabolism: lessons from novel glycogen phosphorylase inhibitors. Mini Rev Med Chem 10: 1175-1187.
    • (2010) Mini Rev Med Chem , vol.10 , pp. 1175-1187
    • Agius, L.1
  • 8
    • 33748311966 scopus 로고    scopus 로고
    • The experimental type 2 diabetes therapy glycogen phosphorylase inhibition can impair aerobic muscle function during prolonged contraction
    • Baker DJ, Greenhaff PL, MacInnes A, Timmons JA, (2006) The experimental type 2 diabetes therapy glycogen phosphorylase inhibition can impair aerobic muscle function during prolonged contraction. Diabetes 55: 1855-1861.
    • (2006) Diabetes , vol.55 , pp. 1855-1861
    • Baker, D.J.1    Greenhaff, P.L.2    MacInnes, A.3    Timmons, J.A.4
  • 9
    • 79953782814 scopus 로고    scopus 로고
    • Effect of glucopyranosylidene-spiro-thiohydantoin on glycogen metabolism in liver tissues of streptozotocin-induced and obese diabetic rats
    • Docsa T, Czifrak K, Huse C, Somsak L, Gergely P, (2011) Effect of glucopyranosylidene-spiro-thiohydantoin on glycogen metabolism in liver tissues of streptozotocin-induced and obese diabetic rats. Mol Med Report 4: 477-481.
    • (2011) Mol Med Report , vol.4 , pp. 477-481
    • Docsa, T.1    Czifrak, K.2    Huse, C.3    Somsak, L.4    Gergely, P.5
  • 11
    • 36549069114 scopus 로고    scopus 로고
    • New hepatic targets for glycaemic control in diabetes
    • Agius L, (2007) New hepatic targets for glycaemic control in diabetes. Best Pract Res Clin Endocrinol Metab 21: 587-605.
    • (2007) Best Pract Res Clin Endocrinol Metab , vol.21 , pp. 587-605
    • Agius, L.1
  • 12
    • 0032533162 scopus 로고    scopus 로고
    • Specific features of glycogen metabolism in the liver
    • Bollen M, Keppens S, Stalmans W, (1998) Specific features of glycogen metabolism in the liver. Biochem J 336 (Pt 1): 19-31.
    • (1998) Biochem J , vol.336 , Issue.Pt 1 , pp. 19-31
    • Bollen, M.1    Keppens, S.2    Stalmans, W.3
  • 13
    • 1642452990 scopus 로고    scopus 로고
    • Glucose 6-phosphate causes translocation of phosphorylase in hepatocytes and inactivates the enzyme synergistically with glucose
    • Aiston S, Green A, Mukhtar M, Agius L, (2004) Glucose 6-phosphate causes translocation of phosphorylase in hepatocytes and inactivates the enzyme synergistically with glucose. Biochem J 377: 195-204.
    • (2004) Biochem J , vol.377 , pp. 195-204
    • Aiston, S.1    Green, A.2    Mukhtar, M.3    Agius, L.4
  • 14
    • 58149402805 scopus 로고    scopus 로고
    • New inhibitors of glycogen phosphorylase as potential antidiabetic agents
    • Somsak L, Czifrak K, Toth M, Bokor E, Chrysina ED, et al. (2008) New inhibitors of glycogen phosphorylase as potential antidiabetic agents. Curr Med Chem 15: 2933-2983.
    • (2008) Curr Med Chem , vol.15 , pp. 2933-2983
    • Somsak, L.1    Czifrak, K.2    Toth, M.3    Bokor, E.4    Chrysina, E.D.5
  • 15
    • 64849099553 scopus 로고    scopus 로고
    • Disruption of the allosteric phosphorylase a regulation of the hepatic glycogen-targeted protein phosphatase 1 improves glucose tolerance in vivo
    • Kelsall IR, Rosenzweig D, Cohen PT, (2009) Disruption of the allosteric phosphorylase a regulation of the hepatic glycogen-targeted protein phosphatase 1 improves glucose tolerance in vivo. Cell Signal 21: 1123-1134.
    • (2009) Cell Signal , vol.21 , pp. 1123-1134
    • Kelsall, I.R.1    Rosenzweig, D.2    Cohen, P.T.3
  • 16
  • 17
    • 25144503390 scopus 로고    scopus 로고
    • FR258900, a novel glycogen phosphorylase inhibitor isolated from Fungus No. 138354. II. Anti-hyperglycemic effects in diabetic animal models
    • Furukawa S, Murakami K, Nishikawa M, Nakayama O, Hino M, (2005) FR258900, a novel glycogen phosphorylase inhibitor isolated from Fungus No. 138354. II. Anti-hyperglycemic effects in diabetic animal models. J Antibiot (Tokyo) 58: 503-506.
    • (2005) J Antibiot (Tokyo) , vol.58 , pp. 503-506
    • Furukawa, S.1    Murakami, K.2    Nishikawa, M.3    Nakayama, O.4    Hino, M.5
  • 18
    • 1642463950 scopus 로고    scopus 로고
    • Regulation of glycogen metabolism in cultured human muscles by the glycogen phosphorylase inhibitor CP-91149
    • Lerin C, Montell E, Nolasco T, Garcia-Rocha M, Guinovart JJ, et al. (2004) Regulation of glycogen metabolism in cultured human muscles by the glycogen phosphorylase inhibitor CP-91149. Biochem J 378: 1073-1077.
    • (2004) Biochem J , vol.378 , pp. 1073-1077
    • Lerin, C.1    Montell, E.2    Nolasco, T.3    Garcia-Rocha, M.4    Guinovart, J.J.5
  • 19
    • 84880799482 scopus 로고    scopus 로고
    • Synthesis of tartaric acid analogues of FR258900 and their evaluation as glycogen phosphorylase inhibitors
    • doi: 10.1016/j.bmcl.2013.1001.1042
    • Varga G, Docsa T, Gergely P, Juhasz L, Somsak L (2012) Synthesis of tartaric acid analogues of FR258900 and their evaluation as glycogen phosphorylase inhibitors. Bioorg Med Chem Lett: doi: 10.1016/j.bmcl.2013.1001.1042.
    • (2012) Bioorg Med Chem Lett
    • Varga, G.1    Docsa, T.2    Gergely, P.3    Juhasz, L.4    Somsak, L.5
  • 20
    • 79951956130 scopus 로고    scopus 로고
    • Glucose derived inhibitors of glycogen phosphorylase
    • Somsak L, (2011) Glucose derived inhibitors of glycogen phosphorylase. Compt Rend Chimie 14: 211-223.
    • (2011) Compt Rend Chimie , vol.14 , pp. 211-223
    • Somsak, L.1
  • 21
    • 84857362748 scopus 로고    scopus 로고
    • N-(4-Substituted-benzoyl)-N'-(beta-d-glucopyranosyl)ureas as inhibitors of glycogen phosphorylase: Synthesis and evaluation by kinetic, crystallographic, and molecular modelling methods
    • Nagy V, Felfoldi N, Konya B, Praly JP, Docsa T, et al. (2012) N-(4-Substituted-benzoyl)-N'-(beta-d-glucopyranosyl)ureas as inhibitors of glycogen phosphorylase: Synthesis and evaluation by kinetic, crystallographic, and molecular modelling methods. Bioorg Med Chem 20: 1801-1816.
    • (2012) Bioorg Med Chem , vol.20 , pp. 1801-1816
    • Nagy, V.1    Felfoldi, N.2    Konya, B.3    Praly, J.P.4    Docsa, T.5
  • 22
    • 41949086319 scopus 로고    scopus 로고
    • Advances in glycogen phosphorylase inhibitor design
    • Oikonomakos NG, Somsak L, (2008) Advances in glycogen phosphorylase inhibitor design. Curr Opin Investig Drugs 9: 379-395.
    • (2008) Curr Opin Investig Drugs , vol.9 , pp. 379-395
    • Oikonomakos, N.G.1    Somsak, L.2
  • 23
    • 0013201627 scopus 로고
    • The Reaction of Oxalyl Chloride with Amides. IV. Synthesis of Acyl Isocyanates
    • Speziale AJ, Smith LR, Fedder J, (1965) The Reaction of Oxalyl Chloride with Amides. IV. Synthesis of Acyl Isocyanates. J Org Chem 30: 4306-4307.
    • (1965) J Org Chem , vol.30 , pp. 4306-4307
    • Speziale, A.J.1    Smith, L.R.2    Fedder, J.3
  • 24
    • 84985181061 scopus 로고
    • Synthesis and reactivity of N-[α-acetoxy)-4-pyridylmethyl]-3,5-dimethylbenzamide
    • Braña MF, López Rodriguez ML, (1981) Synthesis and reactivity of N-[α-acetoxy)-4-pyridylmethyl]-3,5-dimethylbenzamide. J Het Chem 18: 869-871.
    • (1981) J Het Chem , vol.18 , pp. 869-871
    • Braña, M.F.1    López Rodriguez, M.L.2
  • 25
    • 0036261973 scopus 로고    scopus 로고
    • New efficient synthesis of beta-glucosylamines of mono- and disaccharides with the use of ammonium carbamate
    • Likhosherstov LM, Novikova OS, Shibaev VN, (2002) New efficient synthesis of beta-glucosylamines of mono- and disaccharides with the use of ammonium carbamate. Dokl Chem 383: 89-92.
    • (2002) Dokl Chem , vol.383 , pp. 89-92
    • Likhosherstov, L.M.1    Novikova, O.S.2    Shibaev, V.N.3
  • 26
    • 0033577776 scopus 로고    scopus 로고
    • Efficient inhibition of muscle and liver glycogen phosphorylases by a new glucopyranosylidene-spiro-thiohydantoin
    • Osz E, Somsak L, Szilagyi L, Kovacs L, Docsa T, et al. (1999) Efficient inhibition of muscle and liver glycogen phosphorylases by a new glucopyranosylidene-spiro-thiohydantoin. Bioorg Med Chem Lett 9: 1385-1390.
    • (1999) Bioorg Med Chem Lett , vol.9 , pp. 1385-1390
    • Osz, E.1    Somsak, L.2    Szilagyi, L.3    Kovacs, L.4    Docsa, T.5
  • 27
    • 79953761260 scopus 로고    scopus 로고
    • PARP-2 Regulates SIRT1 Expression and Whole-Body Energy Expenditure
    • Bai P, Canto C, Brunyanszki A, Huber A, Szanto M, et al. (2011) PARP-2 Regulates SIRT1 Expression and Whole-Body Energy Expenditure. Cell Metab 13: 450-460.
    • (2011) Cell Metab , vol.13 , pp. 450-460
    • Bai, P.1    Canto, C.2    Brunyanszki, A.3    Huber, A.4    Szanto, M.5
  • 28
    • 79953752384 scopus 로고    scopus 로고
    • PARP-1 Inhibition Increases Mitochondrial Metabolism through SIRT1 Activation
    • Bai P, Canto C, Oudart H, Brunyanszki A, Cen Y, et al. (2011) PARP-1 Inhibition Increases Mitochondrial Metabolism through SIRT1 Activation. Cell Metab 13: 461-468.
    • (2011) Cell Metab , vol.13 , pp. 461-468
    • Bai, P.1    Canto, C.2    Oudart, H.3    Brunyanszki, A.4    Cen, Y.5
  • 29
    • 81055125040 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-2 depletion reduces doxorubicin-induced damage through SIRT1 induction
    • Szanto M, Rutkai I, Hegedus C, Czikora A, Rozsahegyi M, et al. (2011) Poly(ADP-ribose) polymerase-2 depletion reduces doxorubicin-induced damage through SIRT1 induction. Cardiovasc Res 92: 430-438.
    • (2011) Cardiovasc Res , vol.92 , pp. 430-438
    • Szanto, M.1    Rutkai, I.2    Hegedus, C.3    Czikora, A.4    Rozsahegyi, M.5
  • 30
    • 77957931901 scopus 로고    scopus 로고
    • Genetic Ablation of PARP-1 Protects Against Oxazolone-Induced Contact Hypersensitivity by Modulating Oxidative Stress
    • Brunyanszki A, Hegedus C, Szanto M, Erdelyi K, Kovacs K, et al. (2010) Genetic Ablation of PARP-1 Protects Against Oxazolone-Induced Contact Hypersensitivity by Modulating Oxidative Stress. J Invest Dermatol 130: 2629-2637.
    • (2010) J Invest Dermatol , vol.130 , pp. 2629-2637
    • Brunyanszki, A.1    Hegedus, C.2    Szanto, M.3    Erdelyi, K.4    Kovacs, K.5
  • 31
    • 45049086023 scopus 로고    scopus 로고
    • Assessment of synthetic methods for the preparation of N-β-D-glucopyranosyl-N'-substituted ureas, -thioureas and related compounds
    • Somsák L, Felföldi N, Kónya B, Hüse C, Telepó K, et al. (2008) Assessment of synthetic methods for the preparation of N-β-D-glucopyranosyl-N'-substituted ureas,-thioureas and related compounds. Carbohydr Res 343: 2083-2093.
    • (2008) Carbohydr Res , vol.343 , pp. 2083-2093
    • Somsák, L.1    Felföldi, N.2    Kónya, B.3    Hüse, C.4    Telepó, K.5
  • 32
    • 23644444478 scopus 로고    scopus 로고
    • Glycogen phosphorylase inhibition in type 2 diabetes therapy: a systematic evaluation of metabolic and functional effects in rat skeletal muscle
    • Baker DJ, Timmons JA, Greenhaff PL, (2005) Glycogen phosphorylase inhibition in type 2 diabetes therapy: a systematic evaluation of metabolic and functional effects in rat skeletal muscle. Diabetes 54: 2453-2459.
    • (2005) Diabetes , vol.54 , pp. 2453-2459
    • Baker, D.J.1    Timmons, J.A.2    Greenhaff, P.L.3
  • 33
    • 78549274015 scopus 로고    scopus 로고
    • The prototype of glycogen phosphorylase
    • Chrysina ED, (2010) The prototype of glycogen phosphorylase. Mini Rev Med Chem 10: 1093-1101.
    • (2010) Mini Rev Med Chem , vol.10 , pp. 1093-1101
    • Chrysina, E.D.1
  • 34
    • 20144373860 scopus 로고    scopus 로고
    • Kinetic and crystallographic studies on 2-(beta-D-glucopyranosyl)-5-methyl-1, 3, 4-oxadiazole, -benzothiazole, and -benzimidazole, inhibitors of muscle glycogen phosphorylase b. Evidence for a new binding site
    • Chrysina ED, Kosmopoulou MN, Tiraidis C, Kardakaris R, Bischler N, et al. (2005) Kinetic and crystallographic studies on 2-(beta-D-glucopyranosyl)-5-methyl-1, 3, 4-oxadiazole,-benzothiazole, and-benzimidazole, inhibitors of muscle glycogen phosphorylase b. Evidence for a new binding site. Protein Sci 14: 873-888.
    • (2005) Protein Sci , vol.14 , pp. 873-888
    • Chrysina, E.D.1    Kosmopoulou, M.N.2    Tiraidis, C.3    Kardakaris, R.4    Bischler, N.5
  • 35
    • 0036207189 scopus 로고    scopus 로고
    • Obesity-related fatty liver is unchanged in mice deficient for mitochondrial uncoupling protein 2
    • Baffy G, Zhang CY, Glickman JN, Lowell BB, (2002) Obesity-related fatty liver is unchanged in mice deficient for mitochondrial uncoupling protein 2. Hepatology 35: 753-761.
    • (2002) Hepatology , vol.35 , pp. 753-761
    • Baffy, G.1    Zhang, C.Y.2    Glickman, J.N.3    Lowell, B.B.4
  • 36
    • 82355161907 scopus 로고    scopus 로고
    • High-resolution respirometry: OXPHOS protocols for human cells and permeabilized fibers from small biopsies of human muscle
    • Pesta D, Gnaiger E, (2012) High-resolution respirometry: OXPHOS protocols for human cells and permeabilized fibers from small biopsies of human muscle. Methods Mol Biol 810: 25-58.
    • (2012) Methods Mol Biol , vol.810 , pp. 25-58
    • Pesta, D.1    Gnaiger, E.2
  • 37
    • 0034643340 scopus 로고    scopus 로고
    • Normalizing mitochondrial superoxide production blocks three pathways of hyperglycaemic damage
    • Nishikawa T, Edelstein D, Du XL, Yamagishi S, Matsumura T, et al. (2000) Normalizing mitochondrial superoxide production blocks three pathways of hyperglycaemic damage. Nature 404: 787-790.
    • (2000) Nature , vol.404 , pp. 787-790
    • Nishikawa, T.1    Edelstein, D.2    Du, X.L.3    Yamagishi, S.4    Matsumura, T.5
  • 38
    • 0033667705 scopus 로고    scopus 로고
    • Disruption of the uncoupling protein-2 gene in mice reveals a role in immunity and reactive oxygen species production
    • Arsenijevic D, Onuma H, Pecqueur C, Raimbault S, Manning BS, et al. (2000) Disruption of the uncoupling protein-2 gene in mice reveals a role in immunity and reactive oxygen species production. Nat Genet 26: 435-439.
    • (2000) Nat Genet , vol.26 , pp. 435-439
    • Arsenijevic, D.1    Onuma, H.2    Pecqueur, C.3    Raimbault, S.4    Manning, B.S.5
  • 39
    • 33751072935 scopus 로고    scopus 로고
    • Bioenergetics and the formation of mitochondrial reactive oxygen species
    • Adam-Vizi V, Chinopoulos C, (2006) Bioenergetics and the formation of mitochondrial reactive oxygen species. Trends Pharmacol Sci 27: 639-645.
    • (2006) Trends Pharmacol Sci , vol.27 , pp. 639-645
    • Adam-Vizi, V.1    Chinopoulos, C.2
  • 40
    • 1242336976 scopus 로고    scopus 로고
    • Uncoupling protein-2 deficiency promotes oxidant stress and delays liver regeneration in mice
    • Horimoto M, Fulop P, Derdak Z, Wands JR, Baffy G, (2004) Uncoupling protein-2 deficiency promotes oxidant stress and delays liver regeneration in mice. Hepatology 39: 386-392.
    • (2004) Hepatology , vol.39 , pp. 386-392
    • Horimoto, M.1    Fulop, P.2    Derdak, Z.3    Wands, J.R.4    Baffy, G.5
  • 41
    • 33748918693 scopus 로고    scopus 로고
    • Lack of UCP2 reduces Fas-mediated liver injury in ob/ob mice and reveals importance of cell-specific UCP2 expression
    • Fulop P, Derdak Z, Sheets A, Sabo E, Berthiaume EP, et al. (2006) Lack of UCP2 reduces Fas-mediated liver injury in ob/ob mice and reveals importance of cell-specific UCP2 expression. Hepatology 44: 592-601.
    • (2006) Hepatology , vol.44 , pp. 592-601
    • Fulop, P.1    Derdak, Z.2    Sheets, A.3    Sabo, E.4    Berthiaume, E.P.5
  • 42
    • 77952524998 scopus 로고    scopus 로고
    • Prolonged inhibition of glycogen phosphorylase in livers of Zucker Diabetic Fatty rats models human glycogen storage diseases
    • Floettmann E, Gregory L, Teague J, Myatt J, Hammond C, et al. (2010) Prolonged inhibition of glycogen phosphorylase in livers of Zucker Diabetic Fatty rats models human glycogen storage diseases. Toxicol Pathol 38: 393-401.
    • (2010) Toxicol Pathol , vol.38 , pp. 393-401
    • Floettmann, E.1    Gregory, L.2    Teague, J.3    Myatt, J.4    Hammond, C.5
  • 43
    • 34347220473 scopus 로고    scopus 로고
    • Defining the role of mTOR in cancer
    • Guertin DA, Sabatini DM, (2007) Defining the role of mTOR in cancer. Cancer Cell 12: 9-22.
    • (2007) Cancer Cell , vol.12 , pp. 9-22
    • Guertin, D.A.1    Sabatini, D.M.2
  • 44
    • 84859778293 scopus 로고    scopus 로고
    • mTOR signaling in growth control and disease
    • Laplante M, Sabatini DM, (2012) mTOR signaling in growth control and disease. Cell 149: 274-293.
    • (2012) Cell , vol.149 , pp. 274-293
    • Laplante, M.1    Sabatini, D.M.2
  • 45
    • 33751348056 scopus 로고    scopus 로고
    • Ablation in mice of the mTORC components raptor, rictor, or mLST8 reveals that mTORC2 is required for signaling to Akt-FOXO and PKCalpha, but not S6K1
    • Guertin DA, Stevens DM, Thoreen CC, Burds AA, Kalaany NY, et al. (2006) Ablation in mice of the mTORC components raptor, rictor, or mLST8 reveals that mTORC2 is required for signaling to Akt-FOXO and PKCalpha, but not S6K1. Dev Cell 11: 859-871.
    • (2006) Dev Cell , vol.11 , pp. 859-871
    • Guertin, D.A.1    Stevens, D.M.2    Thoreen, C.C.3    Burds, A.A.4    Kalaany, N.Y.5
  • 46
    • 78650510609 scopus 로고    scopus 로고
    • mTOR: from growth signal integration to cancer, diabetes and ageing
    • Zoncu R, Efeyan A, Sabatini DM, (2011) mTOR: from growth signal integration to cancer, diabetes and ageing. Nat Rev Mol Cell Biol 12: 21-35.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 21-35
    • Zoncu, R.1    Efeyan, A.2    Sabatini, D.M.3
  • 47
    • 84860454425 scopus 로고    scopus 로고
    • Hepatic mTORC2 activates glycolysis and lipogenesis through Akt, glucokinase, and SREBP1c
    • Hagiwara A, Cornu M, Cybulski N, Polak P, Betz C, et al. (2012) Hepatic mTORC2 activates glycolysis and lipogenesis through Akt, glucokinase, and SREBP1c. Cell Metab 15: 725-738.
    • (2012) Cell Metab , vol.15 , pp. 725-738
    • Hagiwara, A.1    Cornu, M.2    Cybulski, N.3    Polak, P.4    Betz, C.5
  • 48
    • 84855476912 scopus 로고    scopus 로고
    • Molecular basis for the differential use of glucose and glutamine in cell proliferation as revealed by synchronized HeLa cells
    • Colombo SL, Palacios-Callender M, Frakich N, Carcamo S, Kovacs I, et al. (2011) Molecular basis for the differential use of glucose and glutamine in cell proliferation as revealed by synchronized HeLa cells. Proc Natl Acad Sci U S A 108: 21069-21074.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 21069-21074
    • Colombo, S.L.1    Palacios-Callender, M.2    Frakich, N.3    Carcamo, S.4    Kovacs, I.5
  • 49
    • 84870507227 scopus 로고    scopus 로고
    • Glucose Utilization via Glycogen Phosphorylase Sustains Proliferation and Prevents Premature Senescence in Cancer Cells
    • Favaro E, Bensaad K, Chong MG, Tennant DA, Ferguson DJ, et al. (2012) Glucose Utilization via Glycogen Phosphorylase Sustains Proliferation and Prevents Premature Senescence in Cancer Cells. Cell Metab 16: 751-764.
    • (2012) Cell Metab , vol.16 , pp. 751-764
    • Favaro, E.1    Bensaad, K.2    Chong, M.G.3    Tennant, D.A.4    Ferguson, D.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.