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Volumn 43, Issue 16, 2015, Pages 7688-7701

Agonistic aptamer to the insulin receptor leads to biased signaling and functional selectivity through allosteric modulation

Author keywords

[No Author keywords available]

Indexed keywords

APTAMER; GLUCOSE; INSULIN; INSULIN RECEPTOR; INSULIN RECEPTOR KINASE; IR A48 APTAMER; OLIGONUCLEOTIDE; PHOSPHATIDYLINOSITOL 3 KINASE; SOMATOMEDIN; UNCLASSIFIED DRUG; GLUCOSE BLOOD LEVEL;

EID: 84942274883     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkv767     Document Type: Article
Times cited : (50)

References (57)
  • 1
    • 0025194307 scopus 로고
    • Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase
    • Tuerk, C. And Gold, L. (1990) Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase. Science, 249, 505-510.
    • (1990) Science , vol.249 , pp. 505-510
    • Tuerk, C.1    Gold, L.2
  • 2
    • 0025074907 scopus 로고
    • In vitro selection of RNA molecules that bind specific ligands
    • Ellington, A. D. And Szostak, J. W. (1990) In vitro selection of RNA molecules that bind specific ligands. Nature, 346, 818-822.
    • (1990) Nature , vol.346 , pp. 818-822
    • Ellington, A.D.1    Szostak, J.W.2
  • 3
    • 67349167635 scopus 로고    scopus 로고
    • Discovery and development of the G-rich oligonucleotide AS1411 as a novel treatment for cancer
    • Bates, P. J., Laber, D. A., Miller, D. M., Thomas, S. D. And Trent, J. O. (2009) Discovery and development of the G-rich oligonucleotide AS1411 as a novel treatment for cancer. Exp. Mol. Pathol., 86, 151-164.
    • (2009) Exp. Mol. Pathol. , vol.86 , pp. 151-164
    • Bates, P.J.1    Laber, D.A.2    Miller, D.M.3    Thomas, S.D.4    Trent, J.O.5
  • 6
    • 0003008343 scopus 로고    scopus 로고
    • Synthetic DNA delivery systems
    • Luo, D. And Saltzman, W. M. (2000) Synthetic DNA delivery systems. Nat. Biotechnol., 18, 33-37.
    • (2000) Nat. Biotechnol. , vol.18 , pp. 33-37
    • Luo, D.1    Saltzman, W.M.2
  • 9
    • 34247140171 scopus 로고    scopus 로고
    • Regulation of insulin receptor function
    • Youngren, J. F. (2007) Regulation of insulin receptor function. Cell. Mol. Life Sci., 64, 873-891.
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 873-891
    • Youngren, J.F.1
  • 10
    • 84861444859 scopus 로고    scopus 로고
    • Regulation of glucose transport by insulin: Traffic control of GLUT4
    • Leto, D. And Saltiel, A. R. (2012) Regulation of glucose transport by insulin: Traffic control of GLUT4. Nat. Rev. Mol. Cell Biol., 13, 383-396.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 383-396
    • Leto, D.1    Saltiel, A.R.2
  • 11
    • 75149130955 scopus 로고    scopus 로고
    • Diagnosis and classification of diabetes mellitus
    • American Diabetes Association.
    • American Diabetes Association. (2010) Diagnosis and classification of diabetes mellitus. Diabetes Care, 33, S62-S69.
    • (2010) Diabetes Care , vol.33 , pp. S62-S69
  • 13
    • 84895743899 scopus 로고    scopus 로고
    • Beyond antibodies: New affinity reagents to unlock the proteome
    • Lollo, B., Steele, F. And Gold, L. (2014) Beyond antibodies: new affinity reagents to unlock the proteome. Proteomics, 14, 638-644.
    • (2014) Proteomics , vol.14 , pp. 638-644
    • Lollo, B.1    Steele, F.2    Gold, L.3
  • 14
    • 36549015742 scopus 로고    scopus 로고
    • Insulin receptor structure and its implications for the IGF-1 receptor
    • Lawrence, M. C., McKern, N. M. And Ward, C. W. (2007) Insulin receptor structure and its implications for the IGF-1 receptor. Curr. Opin. Struct. Biol., 17, 699-705.
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 699-705
    • Lawrence, M.C.1    McKern, N.M.2    Ward, C.W.3
  • 15
    • 0035960597 scopus 로고    scopus 로고
    • Dimerization-induced activation of soluble insulin/IGF-1 receptor kinases: An alternative mechanism of activation
    • Baer, K., Al-Hasani, H., Parvaresch, S., Corona, T., Rufer, A., Nolle, V., Bergschneider, E. And Klein, H. W. (2001) Dimerization-induced activation of soluble insulin/IGF-1 receptor kinases: An alternative mechanism of activation. Biochemistry, 40, 14268-14278.
    • (2001) Biochemistry , vol.40 , pp. 14268-14278
    • Baer, K.1    Al-Hasani, H.2    Parvaresch, S.3    Corona, T.4    Rufer, A.5    Nolle, V.6    Bergschneider, E.7    Klein, H.W.8
  • 16
    • 0026742983 scopus 로고
    • Insulin receptor kinase domain autophosphorylation regulates receptor enzymatic function
    • Wilden, P. A., Kahn, C. R., Siddle, K. And White, M. F. (1992) Insulin receptor kinase domain autophosphorylation regulates receptor enzymatic function. J. Biol. Chem., 267, 16660-16668.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16660-16668
    • Wilden, P.A.1    Kahn, C.R.2    Siddle, K.3    White, M.F.4
  • 17
    • 0028912999 scopus 로고
    • Phosphotyrosine-dependent interaction of SHC and insulin receptor substrate 1 with the NPEY motif of the insulin receptor via a novel non-SH2 domain
    • Gustafson, T. A., He, W., Craparo, A., Schaub, C. D. And O'Neill, T. J. (1995) Phosphotyrosine-dependent interaction of SHC and insulin receptor substrate 1 with the NPEY motif of the insulin receptor via a novel non-SH2 domain. Mol. Cell. Biol., 15, 2500-2508.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2500-2508
    • Gustafson, T.A.1    He, W.2    Craparo, A.3    Schaub, C.D.4    O'Neill, T.J.5
  • 18
    • 0029898718 scopus 로고    scopus 로고
    • Interaction of insulin receptor substrate-2 (IRS-2) with the insulin and insulin-like growth factor i receptors. Evidence for two distinct phosphotyrosine-dependent interaction domains within IRS-2
    • He, W., Craparo, A., Zhu, Y., O'Neill, T. J., Wang, L. M., Pierce, J. H. And Gustafson, T. A. (1996) Interaction of insulin receptor substrate-2 (IRS-2) with the insulin and insulin-like growth factor I receptors. Evidence for two distinct phosphotyrosine-dependent interaction domains within IRS-2. J. Biol. Chem., 271, 11641-11645.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11641-11645
    • He, W.1    Craparo, A.2    Zhu, Y.3    O'Neill, T.J.4    Wang, L.M.5    Pierce, J.H.6    Gustafson, T.A.7
  • 19
    • 0030060965 scopus 로고    scopus 로고
    • Interaction of the molecular weight 85K regulatory subunit of the phosphatidylinositol 3-kinase with the insulin receptor and the insulin-like growth factor-1 (IGF-I) receptor: Comparative study using the yeast two-hybrid system
    • Tartare-Deckert, S., Murdaca, J., Sawka-Verhelle, D., Holt, K. H., Pessin, J. E. And Van Obberghen, E. (1996) Interaction of the molecular weight 85K regulatory subunit of the phosphatidylinositol 3-kinase with the insulin receptor and the insulin-like growth factor-1 (IGF-I) receptor: Comparative study using the yeast two-hybrid system. Endocrinology, 137, 1019-1024.
    • (1996) Endocrinology , vol.137 , pp. 1019-1024
    • Tartare-Deckert, S.1    Murdaca, J.2    Sawka-Verhelle, D.3    Holt, K.H.4    Pessin, J.E.5    Van Obberghen, E.6
  • 20
    • 0028012445 scopus 로고
    • Direct activation of the phosphatidylinositol 3-kinase by the insulin receptor
    • Van Horn, D. J., Myers, M. G. Jr and Backer, J. M. (1994) Direct activation of the phosphatidylinositol 3-kinase by the insulin receptor. J. Biol. Chem., 269, 29-32.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29-32
    • Van Horn, D.J.1    Myers, M.G.2    Backer, J.M.3
  • 21
    • 0032541671 scopus 로고    scopus 로고
    • Cell cycle targets of Ras/Raf signalling
    • Kerkhoff, E. And Rapp, U. R. (1998) Cell cycle targets of Ras/Raf signalling. Oncogene, 17, 1457-1462.
    • (1998) Oncogene , vol.17 , pp. 1457-1462
    • Kerkhoff, E.1    Rapp, U.R.2
  • 23
    • 84929688455 scopus 로고    scopus 로고
    • Surface-expressed insulin receptors as well as IGF-I receptors both contribute to the mitogenic effects of human insulin and its analogues
    • Lundby, A., Bolvig, P., Hegelund, A. C., Hansen, B. F., Worm, J., Lutzen, A., Billestrup, N., Bonnesen, C. And Oleksiewicz, M. B. (2015) Surface-expressed insulin receptors as well as IGF-I receptors both contribute to the mitogenic effects of human insulin and its analogues. J. Appl. Toxicol., 35, 842-850.
    • (2015) J. Appl. Toxicol. , vol.35 , pp. 842-850
    • Lundby, A.1    Bolvig, P.2    Hegelund, A.C.3    Hansen, B.F.4    Worm, J.5    Lutzen, A.6    Billestrup, N.7    Bonnesen, C.8    Oleksiewicz, M.B.9
  • 24
    • 67650504265 scopus 로고    scopus 로고
    • Analysis of signaling pathways related to cell proliferation stimulated by insulin analogs in human mammary epithelial cell lines
    • Shukla, A., Grisouard, J., Ehemann, V., Hermani, A., Enzmann, H. And Mayer, D. (2009) Analysis of signaling pathways related to cell proliferation stimulated by insulin analogs in human mammary epithelial cell lines. Endocr. Relat. Cancer, 16, 429-441.
    • (2009) Endocr. Relat. Cancer , vol.16 , pp. 429-441
    • Shukla, A.1    Grisouard, J.2    Ehemann, V.3    Hermani, A.4    Enzmann, H.5    Mayer, D.6
  • 25
    • 33244464562 scopus 로고    scopus 로고
    • Critical nodes in signalling pathways: Insights into insulin action
    • Taniguchi, C. M., Emanuelli, B. And Kahn, C. R. (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
  • 26
    • 0029079275 scopus 로고
    • The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase
    • Franke, T. F., Yang, S. I., Chan, T. O., Datta, K., Kazlauskas, A., Morrison, D. K., Kaplan, D. R. And Tsichlis, P. N. (1995) The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase. Cell, 81, 727-736.
    • (1995) Cell , vol.81 , pp. 727-736
    • Franke, T.F.1    Yang, S.I.2    Chan, T.O.3    Datta, K.4    Kazlauskas, A.5    Morrison, D.K.6    Kaplan, D.R.7    Tsichlis, P.N.8
  • 27
    • 0029160069 scopus 로고
    • Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction
    • Burgering, B. M. And Coffer, P. J. (1995) Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction. Nature, 376, 599-602.
    • (1995) Nature , vol.376 , pp. 599-602
    • Burgering, B.M.1    Coffer, P.J.2
  • 28
    • 0027939430 scopus 로고
    • Role of phosphatidylinositol-3-kinase in insulin receptor signaling: Studies with inhibitor, LY294002
    • Sanchez-Margalet, V., Goldfine, I. D., Vlahos, C. J. And Sung, C. K. (1994) Role of phosphatidylinositol-3-kinase in insulin receptor signaling: Studies with inhibitor, LY294002. Biochem. Biophys. Res. Commun., 204, 446-452.
    • (1994) Biochem. Biophys. Res. Commun. , vol.204 , pp. 446-452
    • Sanchez-Margalet, V.1    Goldfine, I.D.2    Vlahos, C.J.3    Sung, C.K.4
  • 29
    • 84873978552 scopus 로고    scopus 로고
    • Identification and characterization of an agonistic aptamer against the T cell costimulatory receptor, OX40
    • Pratico, E. D., Sullenger, B. A. And Nair, S. K. (2013) Identification and characterization of an agonistic aptamer against the T cell costimulatory receptor, OX40. Nucleic Acid Ther., 23, 35-43.
    • (2013) Nucleic Acid Ther. , vol.23 , pp. 35-43
    • Pratico, E.D.1    Sullenger, B.A.2    Nair, S.K.3
  • 31
  • 33
    • 78751498756 scopus 로고    scopus 로고
    • Functional selectivity and biased receptor signaling
    • Kenakin, T. (2011) Functional selectivity and biased receptor signaling. J. Pharmacol. Exp. Ther., 336, 296-302.
    • (2011) J. Pharmacol. Exp. Ther. , vol.336 , pp. 296-302
    • Kenakin, T.1
  • 34
    • 84903387265 scopus 로고    scopus 로고
    • Biased ligands at G-protein-coupled receptors: Promise and progress
    • Violin, J. D., Crombie, A. L., Soergel, D. G. And Lark, M. W. (2014) Biased ligands at G-protein-coupled receptors: promise and progress. Trends Pharmacol. Sci., 35, 308-316.
    • (2014) Trends Pharmacol. Sci. , vol.35 , pp. 308-316
    • Violin, J.D.1    Crombie, A.L.2    Soergel, D.G.3    Lark, M.W.4
  • 35
    • 84873348390 scopus 로고    scopus 로고
    • The metabolic and mitogenic properties of basal insulin analogues
    • Tennagels, N. And Werner, U. (2013) The metabolic and mitogenic properties of basal insulin analogues. Arch. Physiol. Biochem., 119, 1-14.
    • (2013) Arch. Physiol. Biochem. , vol.119 , pp. 1-14
    • Tennagels, N.1    Werner, U.2
  • 37
    • 84879946082 scopus 로고    scopus 로고
    • Insulin therapy and cancer in type 2 diabetes
    • Mannucci, E. (2012) Insulin therapy and cancer in type 2 diabetes. ISRN Endocrinol., 2012, 240634.
    • (2012) ISRN Endocrinol. , vol.2012 , pp. 240634
    • Mannucci, E.1
  • 39
    • 68449104156 scopus 로고    scopus 로고
    • Risk of malignancies in patients with diabetes treated with human insulin or insulin analogues: A cohort study
    • Hemkens, L. G., Grouven, U., Bender, R., Gunster, C., Gutschmidt, S., Selke, G. W. And Sawicki, P. T. (2009) Risk of malignancies in patients with diabetes treated with human insulin or insulin analogues: A cohort study. Diabetologia, 52, 1732-1744.
    • (2009) Diabetologia , vol.52 , pp. 1732-1744
    • Hemkens, L.G.1    Grouven, U.2    Bender, R.3    Gunster, C.4    Gutschmidt, S.5    Selke, G.W.6    Sawicki, P.T.7
  • 40
    • 33645766204 scopus 로고    scopus 로고
    • Increased cancer-related mortality for patients with type 2 diabetes who use sulfonylureas or insulin
    • Bowker, S. L., Majumdar, S. R., Veugelers, P. And Johnson, J. A. (2006) Increased cancer-related mortality for patients with type 2 diabetes who use sulfonylureas or insulin. Diabetes Care, 29, 254-258.
    • (2006) Diabetes Care , vol.29 , pp. 254-258
    • Bowker, S.L.1    Majumdar, S.R.2    Veugelers, P.3    Johnson, J.A.4
  • 41
    • 5144234027 scopus 로고    scopus 로고
    • Insulin therapy and colorectal cancer risk among type 2 diabetes mellitus patients
    • Yang, Y. X., Hennessy, S. And Lewis, J. D. (2004) Insulin therapy and colorectal cancer risk among type 2 diabetes mellitus patients. Gastroenterology, 127, 1044-1050.
    • (2004) Gastroenterology , vol.127 , pp. 1044-1050
    • Yang, Y.X.1    Hennessy, S.2    Lewis, J.D.3
  • 42
    • 84863189303 scopus 로고    scopus 로고
    • Systematic review and meta-analysis of insulin therapy and risk of cancer
    • Janghorbani, M., Dehghani, M. And Salehi-Marzijarani, M. (2012) Systematic review and meta-analysis of insulin therapy and risk of cancer. Horm. Cancer, 3, 137-146.
    • (2012) Horm. Cancer , vol.3 , pp. 137-146
    • Janghorbani, M.1    Dehghani, M.2    Salehi-Marzijarani, M.3
  • 43
    • 84860592215 scopus 로고    scopus 로고
    • Selective insulin receptor modulators (SIRM): A new class of antidiabetes drugs
    • Vigneri, R., Squatrito, S. And Frittitta, L. (2012) Selective insulin receptor modulators (SIRM): A new class of antidiabetes drugs? Diabetes, 61, 984-985.
    • (2012) Diabetes , vol.61 , pp. 984-985
    • Vigneri, R.1    Squatrito, S.2    Frittitta, L.3
  • 44
    • 0034633993 scopus 로고    scopus 로고
    • Mechanism of transmembrane signaling: Insulin binding and the insulin receptor
    • Ottensmeyer, F. P., Beniac, D. R., Luo, R. Z. And Yip, C. C. (2000) Mechanism of transmembrane signaling: insulin binding and the insulin receptor. Biochemistry, 39, 12103-12112.
    • (2000) Biochemistry , vol.39 , pp. 12103-12112
    • Ottensmeyer, F.P.1    Beniac, D.R.2    Luo, R.Z.3    Yip, C.C.4
  • 45
    • 0032524350 scopus 로고    scopus 로고
    • Autoregulatory mechanisms in protein-tyrosine kinases
    • Hubbard, S. R., Mohammadi, M. And Schlessinger, J. (1998) Autoregulatory mechanisms in protein-tyrosine kinases. J. Biol. Chem., 273, 11987-11990.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11987-11990
    • Hubbard, S.R.1    Mohammadi, M.2    Schlessinger, J.3
  • 46
    • 0028582185 scopus 로고
    • Crystal structure of the tyrosine kinase domain of the human insulin receptor
    • Hubbard, S. R., Wei, L., Ellis, L. And Hendrickson, W. A. (1994) Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature, 372, 746-754.
    • (1994) Nature , vol.372 , pp. 746-754
    • Hubbard, S.R.1    Wei, L.2    Ellis, L.3    Hendrickson, W.A.4
  • 48
    • 36849015259 scopus 로고    scopus 로고
    • Activation of the insulin receptor by insulin and a synthetic peptide leads to divergent metabolic and mitogenic signaling and responses
    • Jensen, M., Hansen, B., De Meyts, P., Schaffer, L. And Urso, B. (2007) Activation of the insulin receptor by insulin and a synthetic peptide leads to divergent metabolic and mitogenic signaling and responses. J. Biol. Chem., 282, 35179-35186.
    • (2007) J. Biol. Chem. , vol.282 , pp. 35179-35186
    • Jensen, M.1    Hansen, B.2    De Meyts, P.3    Schaffer, L.4    Urso, B.5
  • 50
    • 0031782480 scopus 로고    scopus 로고
    • Constitutive activation of protein kinase B alpha by membrane targeting promotes glucose and system A amino acid transport, protein synthesis, and inactivation of glycogen synthase kinase 3 in L6 muscle cells
    • Hajduch, E., Alessi, D. R., Hemmings, B. A. And Hundal, H. S. (1998) Constitutive activation of protein kinase B alpha by membrane targeting promotes glucose and system A amino acid transport, protein synthesis, and inactivation of glycogen synthase kinase 3 in L6 muscle cells. Diabetes, 47, 1006-1013.
    • (1998) Diabetes , vol.47 , pp. 1006-1013
    • Hajduch, E.1    Alessi, D.R.2    Hemmings, B.A.3    Hundal, H.S.4
  • 51
    • 0030734345 scopus 로고    scopus 로고
    • Physiological role of Akt in insulin-stimulated translocation of GLUT4 in transfected rat adipose cells
    • Cong, L. N., Chen, H., Li, Y., Zhou, L., McGibbon, M. A., Taylor, S. I. And Quon, M. J. (1997) Physiological role of Akt in insulin-stimulated translocation of GLUT4 in transfected rat adipose cells. Mol. Endocrinol., 11, 1881-1890.
    • (1997) Mol. Endocrinol. , vol.11 , pp. 1881-1890
    • Cong, L.N.1    Chen, H.2    Li, Y.3    Zhou, L.4    McGibbon, M.A.5    Taylor, S.I.6    Quon, M.J.7
  • 52
    • 0029908016 scopus 로고    scopus 로고
    • Expression of a constitutively active Akt Ser/Thr kinase in 3T3-L1 adipocytes stimulates glucose uptake and glucose transporter 4 translocation
    • Kohn, A. D., Summers, S. A., Birnbaum, M. J. And Roth, R. A. (1996) Expression of a constitutively active Akt Ser/Thr kinase in 3T3-L1 adipocytes stimulates glucose uptake and glucose transporter 4 translocation. J. Biol. Chem., 271, 31372-31378.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31372-31378
    • Kohn, A.D.1    Summers, S.A.2    Birnbaum, M.J.3    Roth, R.A.4
  • 53
    • 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, D. A., Stevens, D. M., Thoreen, C. C., Burds, A. A., Kalaany, N. Y., Moffat, J., Brown, M., Fitzgerald, K. J. And Sabatini, D. M. (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    Moffat, J.6    Brown, M.7    Fitzgerald, K.J.8    Sabatini, D.M.9
  • 54
    • 33749076673 scopus 로고    scopus 로고
    • SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt phosphorylation and substrate specificity
    • Jacinto, E., Facchinetti, V., Liu, D., Soto, N., Wei, S., Jung, S. Y., Huang, Q., Qin, J. And Su, B. (2006) SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt phosphorylation and substrate specificity. Cell, 127, 125-137.
    • (2006) Cell , vol.127 , pp. 125-137
    • Jacinto, E.1    Facchinetti, V.2    Liu, D.3    Soto, N.4    Wei, S.5    Jung, S.Y.6    Huang, Q.7    Qin, J.8    Su, B.9
  • 55
    • 67349180268 scopus 로고    scopus 로고
    • The level of AKT phosphorylation on threonine 308 but not on serine 473 is associated with high-risk cytogenetics and predicts poor overall survival in acute myeloid leukaemia
    • Gallay, N., Dos Santos, C., Cuzin, L., Bousquet, M., Simmonet Gouy, V., Chaussade, C., Attal, M., Payrastre, B., Demur, C. And Recher, C. (2009) The level of AKT phosphorylation on threonine 308 but not on serine 473 is associated with high-risk cytogenetics and predicts poor overall survival in acute myeloid leukaemia. Leukemia, 23, 1029-1038.
    • (2009) Leukemia , vol.23 , pp. 1029-1038
    • Gallay, N.1    Dos Santos, C.2    Cuzin, L.3    Bousquet, M.4    Simmonet Gouy, V.5    Chaussade, C.6    Attal, M.7    Payrastre, B.8    Demur, C.9    Recher, C.10
  • 57
    • 77953200528 scopus 로고    scopus 로고
    • Fat cell-specific ablation of rictor in mice impairs insulin-regulated fat cell and whole-body glucose and lipid metabolism
    • Kumar, A., Lawrence, J. C. Jr, Jung, D. Y., Ko, H. J., Keller, S. R., Kim, J. K., Magnuson, M. A. And Harris, T. E. (2010) Fat cell-specific ablation of rictor in mice impairs insulin-regulated fat cell and whole-body glucose and lipid metabolism. Diabetes, 59, 1397-1406.
    • (2010) Diabetes , vol.59 , pp. 1397-1406
    • Kumar, A.1    Lawrence, J.C.2    Jung, D.Y.3    Ko, H.J.4    Keller, S.R.5    Kim, J.K.6    Magnuson, M.A.7    Harris, T.E.8


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