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Volumn 112, Issue 2, 2006, Pages 89-104

PTEN and SHIP2 phosphoinositide phosphatases as negative regulators of insulin signalling

Author keywords

Diabetes; Insulin resistance; Insulin signalling; Phosphoinositide phosphatases; PTEN; SHIP2

Indexed keywords

INSULIN; MITOGEN ACTIVATED PROTEIN KINASE 1; PHOSPHATASE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PROTEIN KINASE B; PROTEIN SUBUNIT; PROTEIN TYROSINE PHOSPHATASE; SH2 CONTAINING INOSITOL 5' PHOSPHATASE; UNCLASSIFIED DRUG;

EID: 33748657133     PISSN: 13813455     EISSN: 17444160     Source Type: Journal    
DOI: 10.1080/13813450600711359     Document Type: Conference Paper
Times cited : (77)

References (164)
  • 1
    • 24044536090 scopus 로고    scopus 로고
    • Recent concepts in non-alcoholic fatty liver diseazse
    • Adams LA, Angulo P. 2005. Recent concepts in non-alcoholic fatty liver diseazse. Diabet Med 22(9):1129-33.
    • (2005) Diabet Med , vol.22 , Issue.9 , pp. 1129-1133
    • Adams, L.A.1    Angulo, P.2
  • 2
    • 0032545343 scopus 로고    scopus 로고
    • The inositol phosphatase SHIP inhibits Akt/PKB activation in B cells
    • Aman MJ, Lamkin TD, Okada H, Kurosaki T, Ravichandran KS. 1998. The inositol phosphatase SHIP inhibits Akt/PKB activation in B cells. J Biol Chem 273(51):33922-8.
    • (1998) J Biol Chem , vol.273 , Issue.51 , pp. 33922-33928
    • Aman, M.J.1    Lamkin, T.D.2    Okada, H.3    Kurosaki, T.4    Ravichandran, K.S.5
  • 3
    • 0031919552 scopus 로고    scopus 로고
    • Insulin signal transduction through protein kinase cascades
    • Avruch, J. 1998. Insulin signal transduction through protein kinase cascades. Mol Cell Biochem 182(1-2):31-48.
    • (1998) Mol Cell Biochem , vol.182 , Issue.1-2 , pp. 31-48
    • Avruch, J.1
  • 4
    • 0035794195 scopus 로고    scopus 로고
    • Activation of glycogen synthase by insulin in 3T3-L1 adipocytes involves c-Cbl-associating protein (CAP)-dependent and CAP-independent signaling pathways
    • Baumann CA, Brady MJ, Saltiel AR. 2001. Activation of glycogen synthase by insulin in 3T3-L1 adipocytes involves c-Cbl-associating protein (CAP)-dependent and CAP-independent signaling pathways. J Biol Chem 276(9):6065-8.
    • (2001) J Biol Chem , vol.276 , Issue.9 , pp. 6065-6068
    • Baumann, C.A.1    Brady, M.J.2    Saltiel, A.R.3
  • 6
    • 0029931974 scopus 로고    scopus 로고
    • The proto-oncogene product c-Crk associates with insulin receptor substrate-1 and 4PS. Modulation by insulin growth factor-I (IGF) and enhanced IGF-I signaling
    • Beitner-Johnson D, Blakesley VA, Shen-Orr Z, Jimenez M, Stannard B, Wang LM, Pierce J, LeRoith D. 1996. The proto-oncogene product c-Crk associates with insulin receptor substrate-1 and 4PS. Modulation by insulin growth factor-I (IGF) and enhanced IGF-I signaling. J Biol Chem 271(16):9287-90.
    • (1996) J Biol Chem , vol.271 , Issue.16 , pp. 9287-9290
    • Beitner-Johnson, D.1    Blakesley, V.A.2    Shen-Orr, Z.3    Jimenez, M.4    Stannard, B.5    Wang, L.M.6    Pierce, J.7    LeRoith, D.8
  • 7
    • 0034805868 scopus 로고    scopus 로고
    • The SH2 domain containing inositol 5-phosphatase SHIP2 controls phosphatidylinositol 3,4,5-trisphosphate levels in CHO-IR cells stimulated by insulin
    • Blero D, De Smedt F, Pesesse X, Paternotte N, Moreau C, Payrastre B, Erneux C. 2001. The SH2 domain containing inositol 5-phosphatase SHIP2 controls phosphatidylinositol 3,4,5-trisphosphate levels in CHO-IR cells stimulated by insulin. Biochem Biophys Res Commun 282(3):839-43.
    • (2001) Biochem Biophys Res Commun , vol.282 , Issue.3 , pp. 839-843
    • Blero, D.1    De Smedt, F.2    Pesesse, X.3    Paternotte, N.4    Moreau, C.5    Payrastre, B.6    Erneux, C.7
  • 8
    • 0141434860 scopus 로고
    • Protein kinase C directly phosphorylates the insulin receptor in vitro and reduces its protein-tyrosine kinase activity
    • Bollag GE, Roth RA, Beaudoin J, Mochly-Rosen D, Koshland Jr DE. 1986. Protein kinase C directly phosphorylates the insulin receptor in vitro and reduces its protein-tyrosine kinase activity. Proc Natl Acad Sci USA 83(16):5822-4.
    • (1986) Proc Natl Acad Sci USA , vol.83 , Issue.16 , pp. 5822-5824
    • Bollag, G.E.1    Roth, R.A.2    Beaudoin, J.3    Mochly-Rosen, D.4    Koshland Jr., D.E.5
  • 9
    • 0030792250 scopus 로고    scopus 로고
    • Protein kinase C isoforms beta 1 and beta 2 inhibit the tyrosine kinase activity of the insulin receptor
    • Bossenmaier B, Mosthaf L, Mischak H, Ullrich A, Haring HU. 1997. Protein kinase C isoforms beta 1 and beta 2 inhibit the tyrosine kinase activity of the insulin receptor. Diabetologia 40(7):863-6.
    • (1997) Diabetologia , vol.40 , Issue.7 , pp. 863-866
    • Bossenmaier, B.1    Mosthaf, L.2    Mischak, H.3    Ullrich, A.4    Haring, H.U.5
  • 10
    • 0035787093 scopus 로고    scopus 로고
    • The role of protein phosphatase-1 in insulin action
    • Brady MJ, Saltiel AR. 2001. The role of protein phosphatase-1 in insulin action. Recent Prog Horm Res 56:157-73.
    • (2001) Recent Prog Horm Res , vol.56 , pp. 157-173
    • Brady, M.J.1    Saltiel, A.R.2
  • 11
    • 0033007901 scopus 로고    scopus 로고
    • Membrane-targeting of signalling molecules by SH2/SH3 domain-containing adaptor proteins
    • Buday L. 1999. Membrane-targeting of signalling molecules by SH2/SH3 domain-containing adaptor proteins. Biochim Biophys Acta 1422(2):187-204.
    • (1999) Biochim Biophys Acta , vol.1422 , Issue.2 , pp. 187-204
    • Buday, L.1
  • 12
    • 30944455145 scopus 로고    scopus 로고
    • Insulin resistance: A metabolic pathway to chronic liver disease
    • Bugianesi E, McCullough AJ, Marchesini G. 2005. Insulin resistance: a metabolic pathway to chronic liver disease. Hepatology 42(5):987-1000.
    • (2005) Hepatology , vol.42 , Issue.5 , pp. 987-1000
    • Bugianesi, E.1    McCullough, A.J.2    Marchesini, G.3
  • 13
    • 2442435521 scopus 로고    scopus 로고
    • Non-alcoholic fatty liver and insulin resistance: A cause-effect relationship?
    • Bugianesi E, Zannoni C, Vanni E, Marzocchi R, Marchesini G. 2004. Non-alcoholic fatty liver and insulin resistance: a cause-effect relationship? Dig Liver Dis 36(3):165-73.
    • (2004) Dig Liver Dis , vol.36 , Issue.3 , pp. 165-173
    • Bugianesi, E.1    Zannoni, C.2    Vanni, E.3    Marzocchi, R.4    Marchesini, G.5
  • 15
    • 0031941815 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase-1B acts as a negative regulator of insulin signal transduction
    • Byon JC, Kusari AB, Kusari J. 1998. Protein-tyrosine phosphatase-1B acts as a negative regulator of insulin signal transduction.Mol Cell Biochem 182(1-2):101-8.
    • (1998) Mol Cell Biochem , vol.182 , Issue.1-2 , pp. 101-108
    • Byon, J.C.1    Kusari, A.B.2    Kusari, J.3
  • 16
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • Cantley LC. 2002. The phosphoinositide 3-kinase pathway. Science 296(5573):1655-7.
    • (2002) Science , vol.296 , Issue.5573 , pp. 1655-1657
    • Cantley, L.C.1
  • 17
    • 0032881288 scopus 로고    scopus 로고
    • AKT/PKB and other D3 phosphoinositide-regulated kinases: Kinase activation by phosphoinositide-dependent phosphorylation
    • Chan TO, Rittenhouse SE, Tsichlis PN. 1999. AKT/PKB and other D3 phosphoinositide-regulated kinases: kinase activation by phosphoinositide- dependent phosphorylation. Annu Rev Biochem 68:965-1014.
    • (1999) Annu Rev Biochem , vol.68 , pp. 965-1014
    • Chan, T.O.1    Rittenhouse, S.E.2    Tsichlis, P.N.3
  • 18
    • 0347480266 scopus 로고    scopus 로고
    • Expression of myotubularin by an adenoviral vector demonstrates its function as a phosphatidy-linositol 3-phosphate [PtdIns(3)P] phosphatase in muscle cell lines: Involvement of PtdIns(3)P in insulin-stimulated glucose transport
    • Chaussade C, Pirola L, Bonnafous S, Blondeau F, Brenz-Verca S, Tronchere H, Portis F, Rusconi S, Payrastre B, Laporte J, Van Obberghen E. 2003. Expression of myotubularin by an adenoviral vector demonstrates its function as a phosphatidy-linositol 3-phosphate [PtdIns(3)P] phosphatase in muscle cell lines: involvement of PtdIns(3)P in insulin-stimulated glucose transport. Mol Endocrinol 17(12):2448-60.
    • (2003) Mol Endocrinol , vol.17 , Issue.12 , pp. 2448-2460
    • Chaussade, C.1    Pirola, L.2    Bonnafous, S.3    Blondeau, F.4    Brenz-Verca, S.5    Tronchere, H.6    Portis, F.7    Rusconi, S.8    Payrastre, B.9    Laporte, J.10    Van Obberghen, E.11
  • 19
    • 0036183603 scopus 로고    scopus 로고
    • Coordinated action of protein tyrosine phosphatases in insulin signal transduction
    • Cheng A, Dube N, Gu F, Tremblay ML. 2002. Coordinated action of protein tyrosine phosphatases in insulin signal transduction. Eur J Biochem 269(4):1050-9.
    • (2002) Eur J Biochem , vol.269 , Issue.4 , pp. 1050-1059
    • Cheng, A.1    Dube, N.2    Gu, F.3    Tremblay, M.L.4
  • 21
    • 1342308079 scopus 로고    scopus 로고
    • Redox regulation of PTEN and protein tyrosine phosphatases in H(2)O(2) mediated cell signaling
    • Cho SH, Lee CH, Ahn Y, Kim H, Ahn CY, Yang KS, Lee SR. 2004. Redox regulation of PTEN and protein tyrosine phosphatases in H(2)O(2) mediated cell signaling. FEBS Lett 560(1-3):7-13.
    • (2004) FEBS Lett , vol.560 , Issue.1-3 , pp. 7-13
    • Cho, S.H.1    Lee, C.H.2    Ahn, Y.3    Kim, H.4    Ahn, C.Y.5    Yang, K.S.6    Lee, S.R.7
  • 24
    • 27144504547 scopus 로고    scopus 로고
    • Attenuation of insulin-stimulated insulin receptor substrate-1 serine 307 phosphorylation in insulin resistance of type 2 diabetes
    • Danielsson A, Ost A, Nystrom FH, Stralfors P. 2005. Attenuation of insulin-stimulated insulin receptor substrate-1 serine 307 phosphorylation in insulin resistance of type 2 diabetes. J Biol Chem 280(41):34389-92.
    • (2005) J Biol Chem , vol.280 , Issue.41 , pp. 34389-34392
    • Danielsson, A.1    Ost, A.2    Nystrom, F.H.3    Stralfors, P.4
  • 25
    • 0031465447 scopus 로고    scopus 로고
    • Modulation of insulin receptor substrate-1 tyrosine phosphorylation and function by mitogen-activated protein kinase
    • De Fea K, Roth RA. 1997. Modulation of insulin receptor substrate-1 tyrosine phosphorylation and function by mitogen-activated protein kinase. J Biol Chem 272(50):31400-6.
    • (1997) J Biol Chem , vol.272 , Issue.50 , pp. 31400-31406
    • De Fea, K.1    Roth, R.A.2
  • 27
    • 0034681264 scopus 로고    scopus 로고
    • The multiple roles of PTEN in tumor suppression
    • Di Cristofano A, Pandolfi PP. 2000. The multiple roles of PTEN in tumor suppression. Cell 100(4):387-90.
    • (2000) Cell , vol.100 , Issue.4 , pp. 387-390
    • Di Cristofano, A.1    Pandolfi, P.P.2
  • 28
    • 0031870959 scopus 로고    scopus 로고
    • PTEN is essential for embryonic development and tumour suppression
    • Di Cristofano A, Pesce B, Cordon-Cardo C, Pandolfi PP. 1998. PTEN is essential for embryonic development and tumour suppression. Nat Genet 19(4):348-55.
    • (1998) Nat Genet , vol.19 , Issue.4 , pp. 348-355
    • Di Cristofano, A.1    Pesce, B.2    Cordon-Cardo, C.3    Pandolfi, P.P.4
  • 33
    • 0036094599 scopus 로고    scopus 로고
    • A P387L variant in protein tyrosine phosphatase-1B (PTP-1B) is associated with type 2 diabetes and impaired serine phosphorylation of PTP-1B in vitro
    • Echwald SM, Bach H, Vestergaard H, Richelsen B, Kristensen K, Drivsholm T, Borch-Johnsen K, Hansen T, Pedersen O. 2002. A P387L variant in protein tyrosine phosphatase-1B (PTP-1B) is associated with type 2 diabetes and impaired serine phosphorylation of PTP-1B in vitro. Diabetes 51(1):1-6.
    • (2002) Diabetes , vol.51 , Issue.1 , pp. 1-6
    • Echwald, S.M.1    Bach, H.2    Vestergaard, H.3    Richelsen, B.4    Kristensen, K.5    Drivsholm, T.6    Borch-Johnsen, K.7    Hansen, T.8    Pedersen, O.9
  • 35
    • 0030931560 scopus 로고    scopus 로고
    • Phosphorylation of insulin receptor substrate 1 by glycogen synthase kinase 3 impairs insulin action
    • Eldar-Finkelman H, Krebs EG. 1997. Phosphorylation of insulin receptor substrate 1 by glycogen synthase kinase 3 impairs insulin action. Proc Natl Acad Sci USA 94(18):9660-4.
    • (1997) Proc Natl Acad Sci USA , vol.94 , Issue.18 , pp. 9660-9664
    • Eldar-Finkelman, H.1    Krebs, E.G.2
  • 36
    • 20444371324 scopus 로고    scopus 로고
    • Signalling links in the liver: Knitting SOCS with fat and inflammation
    • Farrell GC. 2005. Signalling links in the liver: knitting SOCS with fat and inflammation. J Hepatol 43(1):193-6.
    • (2005) J Hepatol , vol.43 , Issue.1 , pp. 193-196
    • Farrell, G.C.1
  • 37
    • 1642499409 scopus 로고    scopus 로고
    • Regulation of phosphoinositide 3-kinase by its intrinsic serine kinase activity in vivo
    • Foukas LC, Beeton CA, Jensen J, Phillips WA, Shepherd PR. 2004. Regulation of phosphoinositide 3-kinase by its intrinsic serine kinase activity in vivo. Mol Cell Biol 24(3):966-75.
    • (2004) Mol Cell Biol , vol.24 , Issue.3 , pp. 966-975
    • Foukas, L.C.1    Beeton, C.A.2    Jensen, J.3    Phillips, W.A.4    Shepherd, P.R.5
  • 38
    • 0031039024 scopus 로고    scopus 로고
    • Direct regulation of the Akt proto-oncogene product by phosphatidy-linositol-3,4-bisphosphate
    • Franke TF, Kaplan DR, Cantley LC, Toker A. 1997. Direct regulation of the Akt proto-oncogene product by phosphatidy-linositol-3,4-bisphosphate. Science 275(5300):665-8.
    • (1997) Science , vol.275 , Issue.5300 , pp. 665-668
    • Franke, T.F.1    Kaplan, D.R.2    Cantley, L.C.3    Toker, A.4
  • 39
    • 21344475048 scopus 로고    scopus 로고
    • Impact of the liver-specific expression of SHIP2 (SH2-containing inositol 5′-phosphatase 2) on insulin signaling and glucose metabolism in mice
    • Fukui K, Wada T, Kagawa S, Nagira K, Ikubo M, Ishihara H, Kobayashi M, Sasaoka T. 2005. Impact of the liver-specific expression of SHIP2 (SH2-containing inositol 5′-phosphatase 2) on insulin signaling and glucose metabolism in mice. Diabetes 54(7):1958-7.
    • (2005) Diabetes , vol.54 , Issue.7 , pp. 1958-1967
    • Fukui, K.1    Wada, T.2    Kagawa, S.3    Nagira, K.4    Ikubo, M.5    Ishihara, H.6    Kobayashi, M.7    Sasaoka, T.8
  • 40
    • 0030660615 scopus 로고    scopus 로고
    • 14-3-3 Proteins interact with the insulin-like growth factor receptor but not the insulin receptor
    • Furlanetto RW, Dey BR, Lopaczynski W, Nissley SP. 1997. 14-3-3 proteins interact with the insulin-like growth factor receptor but not the insulin receptor. Biochem J 327(Pt 3):765-71.
    • (1997) Biochem J , vol.327 , Issue.PART 3 , pp. 765-771
    • Furlanetto, R.W.1    Dey, B.R.2    Lopaczynski, W.3    Nissley, S.P.4
  • 41
    • 0037073679 scopus 로고    scopus 로고
    • Serine phosphorylation of insulin receptor substrate 1 by inhibitor kappa B kinase complex
    • Gao Z, Hwang D, Bataille F, Lefevre M, York D, Quon MJ, Ye J. 2002. Serine phosphorylation of insulin receptor substrate 1 by inhibitor kappa B kinase complex. J Biol Chem 277(50):48115-21.
    • (2002) J Biol Chem , vol.277 , Issue.50 , pp. 48115-48121
    • Gao, Z.1    Hwang, D.2    Bataille, F.3    Lefevre, M.4    York, D.5    Quon, M.J.6    Ye, J.7
  • 42
    • 15944406764 scopus 로고    scopus 로고
    • PHLPP: A phosphatase that directly dephosphorylates Akt, promotes apoptosis, and suppresses tumor growth
    • Gao T, Furnari F, Newton AC. 2005. PHLPP: a phosphatase that directly dephosphorylates Akt, promotes apoptosis, and suppresses tumor growth. Mol Cell 18(1):13-24.
    • (2005) Mol Cell , vol.18 , Issue.1 , pp. 13-24
    • Gao, T.1    Furnari, F.2    Newton, A.C.3
  • 43
    • 0942276379 scopus 로고    scopus 로고
    • Nutrient-dependent and insulin-stimulated phosphorylation of insulin receptor substrate-1 on serine 302 correlates with increased insulin signaling
    • Giraud J, Leshan R, Lee YH, White MF. 2004. Nutrient-dependent and insulin-stimulated phosphorylation of insulin receptor substrate-1 on serine 302 correlates with increased insulin signaling. J Biol Chem 279(5):3447-54.
    • (2004) J Biol Chem , vol.279 , Issue.5 , pp. 3447-3454
    • Giraud, J.1    Leshan, R.2    Lee, Y.H.3    White, M.F.4
  • 44
    • 0029618690 scopus 로고
    • In vivo and in vitro studies of vanadate in human and rodent diabetes mellitus
    • Goldfine AB, Simonson DC, Folli F, Patti ME, Kahn CR. 1995. In vivo and in vitro studies of vanadate in human and rodent diabetes mellitus. Mol Cell Biochem 153(1-2):217-31.
    • (1995) Mol Cell Biochem , vol.153 , Issue.1-2 , pp. 217-231
    • Goldfine, A.B.1    Simonson, D.C.2    Folli, F.3    Patti, M.E.4    Kahn, C.R.5
  • 45
    • 0023392635 scopus 로고
    • The insulin receptor: Molecular biology and transmembrane signaling
    • Goldfine ID. 1987. The insulin receptor: molecular biology and transmembrane signaling. Endocr Rev 8(3):235-55.
    • (1987) Endocr Rev , vol.8 , Issue.3 , pp. 235-255
    • Goldfine, I.D.1
  • 46
    • 0031943479 scopus 로고    scopus 로고
    • Regulation of the insulin signalling pathway by cellular protein-tyrosine phosphatases
    • Goldstein BJ, Ahmad F, Ding W, Li PM, Zhang WR. 1998. Regulation of the insulin signalling pathway by cellular protein-tyrosine phosphatases. Mol Cell Biochem 182(1-2):91-9.
    • (1998) Mol Cell Biochem , vol.182 , Issue.1-2 , pp. 91-99
    • Goldstein, B.J.1    Ahmad, F.2    Ding, W.3    Li, P.M.4    Zhang, W.R.5
  • 47
    • 0034635374 scopus 로고    scopus 로고
    • Tyrosine dephosphorylation and deactivation of insulin receptor substrate-1 by protein-tyrosine phosphatase 1B. Possible facilitation by the formation of a ternary complex with the Grb2 adaptor protein
    • Goldstein BJ, Bittner-Kowalczyk A, White MF, Harbeck M. 2000. Tyrosine dephosphorylation and deactivation of insulin receptor substrate-1 by protein-tyrosine phosphatase 1B. Possible facilitation by the formation of a ternary complex with the Grb2 adaptor protein. J Biol Chem 275(6):4283-9.
    • (2000) J Biol Chem , vol.275 , Issue.6 , pp. 4283-4289
    • Goldstein, B.J.1    Bittner-Kowalczyk, A.2    White, M.F.3    Harbeck, M.4
  • 48
    • 12744279326 scopus 로고    scopus 로고
    • Redox paradox: Insulin action is facilitated by insulin-stimulated reactive oxygen species with multiple potential signaling targets
    • Goldstein BJ, Mahadev K, Wu X. 2005. Redox paradox: insulin action is facilitated by insulin-stimulated reactive oxygen species with multiple potential signaling targets. Diabetes 54(2):311-21.
    • (2005) Diabetes , vol.54 , Issue.2 , pp. 311-321
    • Goldstein, B.J.1    Mahadev, K.2    Wu, X.3
  • 49
    • 0037018924 scopus 로고    scopus 로고
    • Positive and negative regulatory role of insulin receptor substrate 1 and 2 (IRS-1 and IRS-2) serine/threonine phosphorylation
    • Greene MW, Garofalo RS. 2002. Positive and negative regulatory role of insulin receptor substrate 1 and 2 (IRS-1 and IRS-2) serine/threonine phosphorylation. Biochemistry 41(22):7082-91.
    • (2002) Biochemistry , vol.41 , Issue.22 , pp. 7082-7091
    • Greene, M.W.1    Garofalo, R.S.2
  • 50
    • 17844377314 scopus 로고    scopus 로고
    • Metabolism: A higher power for insulin
    • Gribble FM. 2005. Metabolism: a higher power for insulin. Nature 434(7036):965-6.
    • (2005) Nature , vol.434 , Issue.7036 , pp. 965-966
    • Gribble, F.M.1
  • 51
    • 0032583122 scopus 로고    scopus 로고
    • Tumor suppressor PTEN inhibits integrin- and growth factor-mediated mitogen-activated protein (MAP) kinase signaling pathways
    • Gu J, Tamura M, Yamada KM. 1998. Tumor suppressor PTEN inhibits integrin- and growth factor-mediated mitogen-activated protein (MAP) kinase signaling pathways. J Cell Biol 143(5):1375-83.
    • (1998) J Cell Biol , vol.143 , Issue.5 , pp. 1375-1383
    • Gu, J.1    Tamura, M.2    Yamada, K.M.3
  • 52
    • 0033606767 scopus 로고    scopus 로고
    • Shc and FAK differentially regulate cell motility and directionality modulated by PTEN
    • Gu J, Tamura M, Pankov R, Danen EH, Takino T, Matsumoto K, Yamada KM. 1999. Shc and FAK differentially regulate cell motility and directionality modulated by PTEN. J Cell Biol 146(2):389-403.
    • (1999) J Cell Biol , vol.146 , Issue.2 , pp. 389-403
    • Gu, J.1    Tamura, M.2    Pankov, R.3    Danen, E.H.4    Takino, T.5    Matsumoto, K.6    Yamada, K.M.7
  • 53
    • 14544271905 scopus 로고    scopus 로고
    • Positive and negative regulation of insulin signaling through IRS-1 phosphorylation
    • Gual P, Le Marchand-Brustel Y, Tanti JF. 2005. Positive and negative regulation of insulin signaling through IRS-1 phosphorylation. Biochimie 87(1):99-109.
    • (2005) Biochimie , vol.87 , Issue.1 , pp. 99-109
    • Gual, P.1    Le Marchand-Brustel, Y.2    Tanti, J.F.3
  • 54
    • 0032541135 scopus 로고    scopus 로고
    • Growth factors and insulin stimulate tyrosine phosphorylation of the 51C/SHIP2 protein
    • Habib T, Hejna JA, Moses RE, Decker SJ. 1998. Growth factors and insulin stimulate tyrosine phosphorylation of the 51C/SHIP2 protein. J Biol Chem 273(29):18605-9.
    • (1998) J Biol Chem , vol.273 , Issue.29 , pp. 18605-18609
    • Habib, T.1    Hejna, J.A.2    Moses, R.E.3    Decker, S.J.4
  • 55
    • 27744608072 scopus 로고    scopus 로고
    • An emerging role for PtdIns(4,5)P2-mediated signalling in human disease
    • Halstead JR, Jalink K, Divecha N. 2005. An emerging role for PtdIns(4,5)P2-mediated signalling in human disease. Trends Pharmacol Sci 26(12):654-60.
    • (2005) Trends Pharmacol Sci , vol.26 , Issue.12 , pp. 654-660
    • Halstead, J.R.1    Jalink, K.2    Divecha, N.3
  • 57
    • 20544460666 scopus 로고    scopus 로고
    • Grb10 and Grb14: Enigmatic regulators of insulin action - and more?
    • Holt LJ, Siddle K. 2005. Grb10 and Grb14: enigmatic regulators of insulin action - and more? Biochem J 388(Pt 2):393-406.
    • (2005) Biochem J , vol.388 , Issue.PART 2 , pp. 393-406
    • Holt, L.J.1    Siddle, K.2
  • 58
    • 0036329397 scopus 로고    scopus 로고
    • Association of SH2-containing inositol phosphatase 2 with the insulin resistance of diabetic db/db mice
    • Hori H, Sasaoka T, Ishihara H, Wada T, Murakami S, Ishiki M, Kobayashi M. 2002. Association of SH2-containing inositol phosphatase 2 with the insulin resistance of diabetic db/db mice. Diabetes 51(8):2387-94.
    • (2002) Diabetes , vol.51 , Issue.8 , pp. 2387-2394
    • Hori, H.1    Sasaoka, T.2    Ishihara, H.3    Wada, T.4    Murakami, S.5    Ishiki, M.6    Kobayashi, M.7
  • 61
    • 0036793214 scopus 로고    scopus 로고
    • Membrane localization of Src homology 2-containing inositol 50-phosphatase 2 via Shc association is required for the negative regulation of insulin signaling in Rat1 fibroblasts overexpressing insulin receptors
    • Ishihara H, Sasaoka T, Ishiki M, Wada T, Hori H, Kagawa S, Kobayashi M. 2002. Membrane localization of Src homology 2-containing inositol 50-phosphatase 2 via Shc association is required for the negative regulation of insulin signaling in Rat1 fibroblasts overexpressing insulin receptors. Mol Endocrinol 16(10):2371-81.
    • (2002) Mol Endocrinol , vol.16 , Issue.10 , pp. 2371-2381
    • Ishihara, H.1    Sasaoka, T.2    Ishiki, M.3    Wada, T.4    Hori, H.5    Kagawa, S.6    Kobayashi, M.7
  • 62
    • 0035861644 scopus 로고    scopus 로고
    • 50-AMP-activated protein kinase phosphorylates IRS-1 on Ser-789 in mouse C2C12 myotubes in response to 5-aminoimidazole-4-carboxamide riboside
    • Jakobsen SN, Hardie DG, Morrice N, Tornqvist HE. 2001. 50-AMP-activated protein kinase phosphorylates IRS-1 on Ser-789 in mouse C2C12 myotubes in response to 5-aminoimidazole-4-carboxamide riboside. J Biol Chem 276(50):46912-6.
    • (2001) J Biol Chem , vol.276 , Issue.50 , pp. 46912-46916
    • Jakobsen, S.N.1    Hardie, D.G.2    Morrice, N.3    Tornqvist, H.E.4
  • 63
    • 0842312945 scopus 로고    scopus 로고
    • Skeletal muscle cells and adipocytes differ in their reliance on TC10 and Rac for insulin-induced actin remodeling
    • JeBailey L, Rudich A, Huang X, Di Ciano-Oliveira C, Kapus A, Klip A. 2004. Skeletal muscle cells and adipocytes differ in their reliance on TC10 and Rac for insulin-induced actin remodeling. Mol Endocrinol 18(2):359-72.
    • (2004) Mol Endocrinol , vol.18 , Issue.2 , pp. 359-372
    • Jebailey, L.1    Rudich, A.2    Huang, X.3    Di Ciano-Oliveira, C.4    Kapus, A.5    Klip, A.6
  • 64
    • 0037773543 scopus 로고    scopus 로고
    • Molecular mechanisms of insulin receptor substrate protein-mediated modulation of insulin signalling
    • Johnston AM, Pirola L, Van Obberghen E. 2003. Molecular mechanisms of insulin receptor substrate protein-mediated modulation of insulin signalling. FEBS Lett 546(1):32-6.
    • (2003) FEBS Lett , vol.546 , Issue.1 , pp. 32-36
    • Johnston, A.M.1    Pirola, L.2    Van Obberghen, E.3
  • 65
    • 0036434431 scopus 로고    scopus 로고
    • Insulin regulation of glucose uptake: A complex interplay of intracellular signalling pathways
    • Khan AH, Pessin JE. 2002. Insulin regulation of glucose uptake: a complex interplay of intracellular signalling pathways. Diabetologia 45(11):1475-83.
    • (2002) Diabetologia , vol.45 , Issue.11 , pp. 1475-1483
    • Khan, A.H.1    Pessin, J.E.2
  • 66
    • 0348031253 scopus 로고    scopus 로고
    • Interaction of the protein tyrosine phosphatase PTPL1 with the PtdIns(3,4)P2-binding adaptor protein TAPP1
    • Kimber WA, Deak M, Prescott AR, Alessi DR. 2003. Interaction of the protein tyrosine phosphatase PTPL1 with the PtdIns(3,4)P2-binding adaptor protein TAPP1. Biochem J 376(Pt 2):525-35.
    • (2003) Biochem J , vol.376 , Issue.PART 2 , pp. 525-535
    • Kimber, W.A.1    Deak, M.2    Prescott, A.R.3    Alessi, D.R.4
  • 67
    • 0031752685 scopus 로고    scopus 로고
    • Global burden of diabetes, 1995-2025: Prevalence, numerical estimates, and projections
    • King H, Aubert RE, Herman WH. 1998. Global burden of diabetes, 1995-2025: prevalence, numerical estimates, and projections. Diabetes Care 21(9):1414-31.
    • (1998) Diabetes Care , vol.21 , Issue.9 , pp. 1414-1431
    • King, H.1    Aubert, R.E.2    Herman, W.H.3
  • 68
    • 0031015986 scopus 로고    scopus 로고
    • A specific product of phosphatidylinositol 3-kinase directly activates the protein kinase Akt through its pleckstrin homology domain
    • Klippel A, Kavanaugh WM, Pot D, Williams LT. 1997. A specific product of phosphatidylinositol 3-kinase directly activates the protein kinase Akt through its pleckstrin homology domain. Mol Cell Biol 17(1):338-44.
    • (1997) Mol Cell Biol , vol.17 , Issue.1 , pp. 338-344
    • Klippel, A.1    Kavanaugh, W.M.2    Pot, D.3    Williams, L.T.4
  • 70
    • 0032189383 scopus 로고    scopus 로고
    • SH2-Balpha is an insulinreceptor adapter protein and substrate that interacts with the activation loop of the insulin-receptor kinase
    • Kotani K, Wilden P, Pillay TS. 1998. SH2-Balpha is an insulinreceptor adapter protein and substrate that interacts with the activation loop of the insulin-receptor kinase. Biochem J 335(Pt 1):103-9.
    • (1998) Biochem J , vol.335 , Issue.PART 1 , pp. 103-109
    • Kotani, K.1    Wilden, P.2    Pillay, T.S.3
  • 71
    • 0033828672 scopus 로고    scopus 로고
    • SOCS: Physiological suppressors of cytokine signaling
    • Krebs DL, Hilton DJ. 2000. SOCS: physiological suppressors of cytokine signaling. J Cell Sci 113(Pt 16):2813-9.
    • (2000) J Cell Sci , vol.113 , Issue.PART 16 , pp. 2813-2819
    • Krebs, D.L.1    Hilton, D.J.2
  • 72
    • 0034801684 scopus 로고    scopus 로고
    • SOCS proteins: Negative regulators of cytokine signaling
    • Krebs DL, Hilton DJ. 2001. SOCS proteins: negative regulators of cytokine signaling. Stem Cells 19(5):378-87.
    • (2001) Stem Cells , vol.19 , Issue.5 , pp. 378-387
    • Krebs, D.L.1    Hilton, D.J.2
  • 73
    • 14844340146 scopus 로고    scopus 로고
    • Insulin hypersensitivity and resistance to streptozotocin-induced diabetes in mice lacking PTEN in adipose tissue
    • Kurlawalla-Martinez C, Stiles B, Wang Y, Devaskar SU, Kahn BB, Wu H. 2005. Insulin hypersensitivity and resistance to streptozotocin-induced diabetes in mice lacking PTEN in adipose tissue. Mol Cell Biol 25(6):2498-510.
    • (2005) Mol Cell Biol , vol.25 , Issue.6 , pp. 2498-2510
    • Kurlawalla-Martinez, C.1    Stiles, B.2    Wang, Y.3    Devaskar, S.U.4    Kahn, B.B.5    Wu, H.6
  • 75
    • 0030905509 scopus 로고    scopus 로고
    • The adapter proteinGrb10 associates preferentially with the insulin receptor as compared with the IGF-I receptor in mouse fibroblasts
    • Laviola L, Giorgino F, Chow JC, Baquero JA, Hansen H, Ooi J, Zhu J,RiedelH, SmithRJ. 1997. The adapter proteinGrb10 associates preferentially with the insulin receptor as compared with the IGF-I receptor in mouse fibroblasts. J Clin Invest 99(5):830-7.
    • (1997) J Clin Invest , vol.99 , Issue.5 , pp. 830-837
    • Laviola, L.1    Giorgino, F.2    Chow, J.C.3    Baquero, J.A.4    Hansen, H.5    Ooi, J.6    Zhu, J.7    Riedel, H.8    Smith, R.J.9
  • 76
    • 0037474274 scopus 로고    scopus 로고
    • c-Jun N-terminal kinase (JNK) mediates feedback inhibition of the insulin signaling cascade
    • Lee YH, Giraud J, Davis RJ, White MF. 2003. c-Jun N-terminal kinase (JNK) mediates feedback inhibition of the insulin signaling cascade. J Biol Chem 278(5):2896-902.
    • (2003) J Biol Chem , vol.278 , Issue.5 , pp. 2896-2902
    • Lee, Y.H.1    Giraud, J.2    Davis, R.J.3    White, M.F.4
  • 77
  • 78
    • 4344684649 scopus 로고    scopus 로고
    • PTEN function: How normal cells control it and tumour cells lose it
    • Leslie NR, Downes CP. 2004. PTEN function: how normal cells control it and tumour cells lose it. Biochem J 382(Pt 1):1-11.
    • (2004) Biochem J , vol.382 , Issue.PART 1 , pp. 1-11
    • Leslie, N.R.1    Downes, C.P.2
  • 79
    • 0033515459 scopus 로고    scopus 로고
    • Modulation of insulin receptor substrate-1 tyrosine phosphorylation by an Akt/phosphatidylinositol 3-kinase pathway
    • Li J, DeFea K, Roth RA. 1999. Modulation of insulin receptor substrate-1 tyrosine phosphorylation by an Akt/phosphatidylinositol 3-kinase pathway. J Biol Chem 274(14):9351-6.
    • (1999) J Biol Chem , vol.274 , Issue.14 , pp. 9351-9356
    • Li, J.1    DeFea, K.2    Roth, R.A.3
  • 81
    • 4544287063 scopus 로고    scopus 로고
    • Insulin induces SOCS-6 expression and its binding to the p85 monomer of phosphoinositide 3-kinase, resulting in improvement in glucose metabolism
    • Li L, Gronning LM, Anderson PO, Li S, Edvardsen K, Johnston J, Kioussis D, Shepherd PR, Wang P. 2004. Insulin induces SOCS-6 expression and its binding to the p85 monomer of phosphoinositide 3-kinase, resulting in improvement in glucose metabolism. J Biol Chem 279(33):34107-14.
    • (2004) J Biol Chem , vol.279 , Issue.33 , pp. 34107-34114
    • Li, L.1    Gronning, L.M.2    Anderson, P.O.3    Li, S.4    Edvardsen, K.5    Johnston, J.6    Kioussis, D.7    Shepherd, P.R.8    Wang, P.9
  • 82
    • 0035957949 scopus 로고    scopus 로고
    • Insulin stimulates PKCzeta-mediated phosphorylation of insulin receptor substrate-1 (IRS-1). A self-attenuated mechanism to negatively regulate the function of IRS proteins
    • Liu YF, Paz K, Herschkovitz A, Alt A, Tennenbaum T, Sampson SR, Ohba M, Kuroki T, LeRoith D, Zick Y. 2001. Insulin stimulates PKCzeta-mediated phosphorylation of insulin receptor substrate-1 (IRS-1). A self-attenuated mechanism to negatively regulate the function of IRS proteins. J Biol Chem 276(17):14459-65.
    • (2001) J Biol Chem , vol.276 , Issue.17 , pp. 14459-14465
    • Liu, Y.F.1    Paz, K.2    Herschkovitz, A.3    Alt, A.4    Tennenbaum, T.5    Sampson, S.R.6    Ohba, M.7    Kuroki, T.8    LeRoith, D.9    Zick, Y.10
  • 83
    • 0141591799 scopus 로고    scopus 로고
    • The roles of Cbl-b and c-Cbl in insulin-stimulated glucose transport
    • Liu J, DeYoung SM, Hwang JB, O'Leary EE, Saltiel AR. 2003. The roles of Cbl-b and c-Cbl in insulin-stimulated glucose transport. J Biol Chem 278(38):36754-62.
    • (2003) J Biol Chem , vol.278 , Issue.38 , pp. 36754-36762
    • Liu, J.1    DeYoung, S.M.2    Hwang, J.B.3    O'Leary, E.E.4    Saltiel, A.R.5
  • 84
    • 21744441932 scopus 로고    scopus 로고
    • Nuclear PTEN-mediated growth suppression is independent of Akt down-regulation
    • Liu JL, Sheng X, Hortobagyi ZK, Mao Z, Gallick GE, Yung WK. 2005. Nuclear PTEN-mediated growth suppression is independent of Akt down-regulation. Mol Cell Biol 25(14):6211-24.
    • (2005) Mol Cell Biol , vol.25 , Issue.14 , pp. 6211-6224
    • Liu, J.L.1    Sheng, X.2    Hortobagyi, Z.K.3    Mao, Z.4    Gallick, G.E.5    Yung, W.K.6
  • 86
    • 0033529502 scopus 로고    scopus 로고
    • Independent SH2-binding sites mediate interaction of Dok-related protein with RasGTPase-activating protein and Nck
    • Lock P, Casagranda F, Dunn AR. 1999. Independent SH2-binding sites mediate interaction of Dok-related protein with RasGTPase-activating protein and Nck. J Biol Chem 274(32):22775-84.
    • (1999) J Biol Chem , vol.274 , Issue.32 , pp. 22775-22784
    • Lock, P.1    Casagranda, F.2    Dunn, A.R.3
  • 87
    • 0032609249 scopus 로고    scopus 로고
    • Differential regulation of signaling pathways for insulin and insulin-like growth factor I
    • Lopaczynski W. 1999. Differential regulation of signaling pathways for insulin and insulin-like growth factor I. Acta Biochim Pol 46(1):51-60.
    • (1999) Acta Biochim Pol , vol.46 , Issue.1 , pp. 51-60
    • Lopaczynski, W.1
  • 89
    • 20444385161 scopus 로고    scopus 로고
    • Knock-down of LAR protein tyrosine phosphatase induces insulin resistance
    • Mander A, Hodgkinson CP, Sale GJ. 2005. Knock-down of LAR protein tyrosine phosphatase induces insulin resistance. FEBS Lett 579(14):3024-8.
    • (2005) FEBS Lett , vol.579 , Issue.14 , pp. 3024-3028
    • Mander, A.1    Hodgkinson, C.P.2    Sale, G.J.3
  • 90
    • 8444224619 scopus 로고    scopus 로고
    • Balancing Akt with S6K: Implications for both metabolic diseases and tumorigenesis
    • Manning BD. 2004. Balancing Akt with S6K: implications for both metabolic diseases and tumorigenesis. J Cell Biol 167(3):399-403.
    • (2004) J Cell Biol , vol.167 , Issue.3 , pp. 399-403
    • Manning, B.D.1
  • 93
    • 0025799454 scopus 로고
    • Abnormal regulation of protein tyrosine phosphatase activities in skeletal muscle of insulin-resistant humans
    • McGuire MC, Fields RM, Nyomba BL, Raz I, Bogardus C, Tonks NK, Sommercorn J. 1991. Abnormal regulation of protein tyrosine phosphatase activities in skeletal muscle of insulin-resistant humans. Diabetes 40(7):939-42.
    • (1991) Diabetes , vol.40 , Issue.7 , pp. 939-942
    • McGuire, M.C.1    Fields, R.M.2    Nyomba, B.L.3    Raz, I.4    Bogardus, C.5    Tonks, N.K.6    Sommercorn, J.7
  • 94
    • 0000714961 scopus 로고    scopus 로고
    • Regulation of protein kinase cascades by protein phosphatase 2A
    • Millward TA, Zolnierowicz S, Hemmings BA. 1999. Regulation of protein kinase cascades by protein phosphatase 2A. Trends Biochem Sci 24(5):186-91.
    • (1999) Trends Biochem Sci , vol.24 , Issue.5 , pp. 186-191
    • Millward, T.A.1    Zolnierowicz, S.2    Hemmings, B.A.3
  • 95
    • 4444228993 scopus 로고    scopus 로고
    • RNAi-based analysis of CAP, Cbl, and CrkII function in the regulation of GLUT4 by insulin
    • Mitra P, Zheng X, Czech MP. 2004. RNAi-based analysis of CAP, Cbl, and CrkII function in the regulation of GLUT4 by insulin. J Biol Chem 279(36):37431-5.
    • (2004) J Biol Chem , vol.279 , Issue.36 , pp. 37431-37435
    • Mitra, P.1    Zheng, X.2    Czech, M.P.3
  • 96
    • 2942623679 scopus 로고    scopus 로고
    • Protein kinase C-zeta-induced phosphorylation of Ser318 in insulin receptor substrate-1 (IRS-1) attenuates the interaction with the insulin receptor and the tyrosine phosphorylation of IRS-1
    • Moeschel K, Beck A, Weigert C, Lammers R, Kalbacher H, Voelter W, Schleicher ED, Haring HU, Lehmann R. 2004. Protein kinase C-zeta-induced phosphorylation of Ser318 in insulin receptor substrate-1 (IRS-1) attenuates the interaction with the insulin receptor and the tyrosine phosphorylation of IRS-1. J Biol Chem 279(24):25157-63.
    • (2004) J Biol Chem , vol.279 , Issue.24 , pp. 25157-25163
    • Moeschel, K.1    Beck, A.2    Weigert, C.3    Lammers, R.4    Kalbacher, H.5    Voelter, W.6    Schleicher, E.D.7    Haring, H.U.8    Lehmann, R.9
  • 97
    • 0035854723 scopus 로고    scopus 로고
    • Suppressors of cytokine signaling-1 and -6 associate with and inhibit the insulin receptor. A potential mechanism for cytokine-mediated insulin resistance
    • Mooney RA, Senn J, Cameron S, Inamdar N, Boivin LM, Shang Y, Furlanetto RW. 2001. Suppressors of cytokine signaling-1 and -6 associate with and inhibit the insulin receptor. A potential mechanism for cytokine-mediated insulin resistance. J Biol Chem 276(28):25889-93.
    • (2001) J Biol Chem , vol.276 , Issue.28 , pp. 25889-25893
    • Mooney, R.A.1    Senn, J.2    Cameron, S.3    Inamdar, N.4    Boivin, L.M.5    Shang, Y.6    Furlanetto, R.W.7
  • 99
    • 15844389443 scopus 로고    scopus 로고
    • Phosphorylation of insulin receptor substrate-1 on multiple serine residues, 612, 632, 662, and 731, modulates insulin action
    • Mothe I, Van Obberghen E. 1996. Phosphorylation of insulin receptor substrate-1 on multiple serine residues, 612, 632, 662, and 731, modulates insulin action. J Biol Chem 271(19):11222-7.
    • (1996) J Biol Chem , vol.271 , Issue.19 , pp. 11222-11227
    • Mothe, I.1    Van Obberghen, E.2
  • 100
    • 3042687456 scopus 로고    scopus 로고
    • Impact of Src homology 2-containing inositol 50-phosphatase 2 on the regulation of insulin signaling leading to protein synthesis in 3T3-L1 adipocytes cultured with excess amino acids
    • Murakami S, Sasaoka T, Wada T, Fukui K, Nagira K, Ishihara H, Usui I, Kobayashi M. 2004. Impact of Src homology 2-containing inositol 50-phosphatase 2 on the regulation of insulin signaling leading to protein synthesis in 3T3-L1 adipocytes cultured with excess amino acids. Endocrinology 145(7):3215-23.
    • (2004) Endocrinology , vol.145 , Issue.7 , pp. 3215-3223
    • Murakami, S.1    Sasaoka, T.2    Wada, T.3    Fukui, K.4    Nagira, K.5    Ishihara, H.6    Usui, I.7    Kobayashi, M.8
  • 101
    • 0027718189 scopus 로고
    • Molecular cloning of pp120/ECTO-ATPase, an endogenous substrate of the insulin receptor kinase
    • Najjar SM, Philippe N, Taylor SI, Accili D. 1993. Molecular cloning of pp120/ECTO-ATPase, an endogenous substrate of the insulin receptor kinase. Adv Exp Med Biol 343:169-74.
    • (1993) Adv Exp Med Biol , vol.343 , pp. 169-174
    • Najjar, S.M.1    Philippe, N.2    Taylor, S.I.3    Accili, D.4
  • 102
    • 0034724747 scopus 로고    scopus 로고
    • The tumor suppressor PTEN negatively regulates insulin signaling in 3T3-L1 adipocytes
    • Nakashima N, Sharma PM, Imamura T, Bookstein R, Olefsky JM. 2000. The tumor suppressor PTEN negatively regulates insulin signaling in 3T3-L1 adipocytes. J Biol Chem 275(17):12889-95.
    • (2000) J Biol Chem , vol.275 , Issue.17 , pp. 12889-12895
    • Nakashima, N.1    Sharma, P.M.2    Imamura, T.3    Bookstein, R.4    Olefsky, J.M.5
  • 103
    • 1042301429 scopus 로고    scopus 로고
    • Role of insulin receptor substrates and protein kinase C-zeta in vascular permeability factor/vascular endothelial growth factor expression in pancreatic cancer cells
    • Neid M, Datta K, Stephan S, Khanna I, Pal S, Shaw L, White M, Mukhopadhyay D. 2004. Role of insulin receptor substrates and protein kinase C-zeta in vascular permeability factor/vascular endothelial growth factor expression in pancreatic cancer cells. J Biol Chem 279(6):3941-8.
    • (2004) J Biol Chem , vol.279 , Issue.6 , pp. 3941-3948
    • Neid, M.1    Datta, K.2    Stephan, S.3    Khanna, I.4    Pal, S.5    Shaw, L.6    White, M.7    Mukhopadhyay, D.8
  • 106
    • 7044272587 scopus 로고    scopus 로고
    • Association of protein tyrosine phosphatase 1B gene polymorphisms with measures of glucose homeostasis in Hispanic Americans: The insulin resistance atherosclerosis study (IRAS) family study
    • Palmer ND, Bento JL, Mychaleckyj JC, Langefeld CD, Campbell JK, Norris JM, Haffner SM, Bergman RN, Bowden DW. 2004. Association of protein tyrosine phosphatase 1B gene polymorphisms with measures of glucose homeostasis in Hispanic Americans: the insulin resistance atherosclerosis study (IRAS) family study. Diabetes 53(11):3013-9.
    • (2004) Diabetes , vol.53 , Issue.11 , pp. 3013-3019
    • Palmer, N.D.1    Bento, J.L.2    Mychaleckyj, J.C.3    Langefeld, C.D.4    Campbell, J.K.5    Norris, J.M.6    Haffner, S.M.7    Bergman, R.N.8    Bowden, D.W.9
  • 107
    • 0035873953 scopus 로고    scopus 로고
    • Tumor suppressor and anti-inflammatory actions of PPARgamma agonists are mediated via upregulation of PTEN
    • Patel L, Pass I, Coxon P, Downes CP, Smith SA, Macphee CH. 2001. Tumor suppressor and anti-inflammatory actions of PPARgamma agonists are mediated via upregulation of PTEN. Curr Biol 11(10):764-8.
    • (2001) Curr Biol , vol.11 , Issue.10 , pp. 764-768
    • Patel, L.1    Pass, I.2    Coxon, P.3    Downes, C.P.4    Smith, S.A.5    Macphee, C.H.6
  • 108
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring, and adaptor proteins
    • Pawson T, Scott JD. 1997. Signaling through scaffold, anchoring, and adaptor proteins. Science 278(5346):2075-80.
    • (1997) Science , vol.278 , Issue.5346 , pp. 2075-2080
    • Pawson, T.1    Scott, J.D.2
  • 109
    • 0030669392 scopus 로고    scopus 로고
    • A molecular basis for insulin resistance. Elevated serine/threonine phosphorylation of IRS-1 and IRS-2 inhibits their binding to the juxtamembrane region of the insulin receptor and impairs their ability to undergo insulin-induced tyrosine phosphorylation
    • Paz K, Hemi R, LeRoith D, Karasik A, Elhanany E, Kanety H, Zick Y. 1997. A molecular basis for insulin resistance. Elevated serine/threonine phosphorylation of IRS-1 and IRS-2 inhibits their binding to the juxtamembrane region of the insulin receptor and impairs their ability to undergo insulin-induced tyrosine phosphorylation. J Biol Chem 272(47):29911-8.
    • (1997) J Biol Chem , vol.272 , Issue.47 , pp. 29911-29918
    • Paz, K.1    Hemi, R.2    LeRoith, D.3    Karasik, A.4    Elhanany, E.5    Kanety, H.6    Zick, Y.7
  • 110
    • 0033214461 scopus 로고    scopus 로고
    • Phosphorylation of insulin receptor substrate-1 (IRS-1) by protein kinase B positively regulates IRS-1 function
    • Paz K, Liu YF, Shorer H, Hemi R, LeRoith D, Quan M, Kanety H, Seger R, Zick Y. 1999. Phosphorylation of insulin receptor substrate-1 (IRS-1) by protein kinase B positively regulates IRS-1 function. J Biol Chem 274(40):28816-22.
    • (1999) J Biol Chem , vol.274 , Issue.40 , pp. 28816-28822
    • Paz, K.1    Liu, Y.F.2    Shorer, H.3    Hemi, R.4    LeRoith, D.5    Quan, M.6    Kanety, H.7    Seger, R.8    Zick, Y.9
  • 111
    • 0035155272 scopus 로고    scopus 로고
    • Serine/threonine phosphorylation of IRS-1 triggers its degradation: Possible regulation by tyrosine phosphorylation
    • Pederson TM, Kramer DL, Rondinone CM. 2001. Serine/threonine phosphorylation of IRS-1 triggers its degradation: possible regulation by tyrosine phosphorylation. Diabetes 50(1):24-31.
    • (2001) Diabetes , vol.50 , Issue.1 , pp. 24-31
    • Pederson, T.M.1    Kramer, D.L.2    Rondinone, C.M.3
  • 113
    • 0033913213 scopus 로고    scopus 로고
    • Signaling pathways in insulin action: Molecular targets of insulin resistance
    • Pessin JE, Saltiel AR. 2000. Signaling pathways in insulin action: molecular targets of insulin resistance. J Clin Invest 106(2):165-9.
    • (2000) J Clin Invest , vol.106 , Issue.2 , pp. 165-169
    • Pessin, J.E.1    Saltiel, A.R.2
  • 115
    • 21344446513 scopus 로고    scopus 로고
    • Steatosis: Co-factor in other liver diseases
    • Powell EE, Jonsson JR, Clouston AD. 2005. Steatosis: co-factor in other liver diseases. Hepatology 42(1):5-13.
    • (2005) Hepatology , vol.42 , Issue.1 , pp. 5-13
    • Powell, E.E.1    Jonsson, J.R.2    Clouston, A.D.3
  • 116
    • 0035793592 scopus 로고    scopus 로고
    • Protein kinase C-zeta phosphorylates insulin receptor substrate-1 and impairs its ability to activate phosphatidylinositol 3-kinase in response to insulin
    • Ravichandran LV, Esposito DL, Chen J, Quon MJ. 2001. Protein kinase C-zeta phosphorylates insulin receptor substrate-1 and impairs its ability to activate phosphatidylinositol 3-kinase in response to insulin. J Biol Chem 276(5):3543-9.
    • (2001) J Biol Chem , vol.276 , Issue.5 , pp. 3543-3549
    • Ravichandran, L.V.1    Esposito, D.L.2    Chen, J.3    Quon, M.J.4
  • 117
    • 0036830636 scopus 로고    scopus 로고
    • SOCS-1 and SOCS-3 block insulin signaling by ubiquitin-mediated degradation of IRS1 and IRS2
    • Rui L, Yuan M, Frantz D, Shoelson S, White MF. 2002. SOCS-1 and SOCS-3 block insulin signaling by ubiquitin-mediated degradation of IRS1 and IRS2. J Biol Chem 277(44):42394-8.
    • (2002) J Biol Chem , vol.277 , Issue.44 , pp. 42394-42398
    • Rui, L.1    Yuan, M.2    Frantz, D.3    Shoelson, S.4    White, M.F.5
  • 118
    • 0034507958 scopus 로고    scopus 로고
    • Molecular basis for the dephosphorylation of the activation segment of the insulin receptor by protein tyrosine phosphatase 1B
    • Salmeen A, Andersen JN, Myers MP, Tonks NK, Barford D. 2000. Molecular basis for the dephosphorylation of the activation segment of the insulin receptor by protein tyrosine phosphatase 1B. Mol Cell 6(6):1401-12.
    • (2000) Mol Cell , vol.6 , Issue.6 , pp. 1401-1412
    • Salmeen, A.1    Andersen, J.N.2    Myers, M.P.3    Tonks, N.K.4    Barford, D.5
  • 119
    • 0035856949 scopus 로고    scopus 로고
    • Insulin signalling and the regulation of glucose and lipid metabolism
    • Saltiel AR, Kahn CR. 2001. Insulin signalling and the regulation of glucose and lipid metabolism. Nature 414(6865):799-806.
    • (2001) Nature , vol.414 , Issue.6865 , pp. 799-806
    • Saltiel, A.R.1    Kahn, C.R.2
  • 120
    • 4344602002 scopus 로고    scopus 로고
    • The biology and clinical relevance of the PTEN tumor suppressor pathway
    • Sansal I, Sellers WR. 2004. The biology and clinical relevance of the PTEN tumor suppressor pathway. J Clin Oncol 22(14):2954-63.
    • (2004) J Clin Oncol , vol.22 , Issue.14 , pp. 2954-2963
    • Sansal, I.1    Sellers, W.R.2
  • 122
    • 0034775501 scopus 로고    scopus 로고
    • SH2-containing inositol phosphatase 2 negatively regulates insulin-induced glycogen synthesis in L6 myotubes
    • Sasaoka T, Hori H, Wada T, Ishiki M, Haruta T, Ishihara H, Kobayashi M. 2001. SH2-containing inositol phosphatase 2 negatively regulates insulin-induced glycogen synthesis in L6 myotubes. Diabetologia 44(10):1258-67.
    • (2001) Diabetologia , vol.44 , Issue.10 , pp. 1258-1267
    • Sasaoka, T.1    Hori, H.2    Wada, T.3    Ishiki, M.4    Haruta, T.5    Ishihara, H.6    Kobayashi, M.7
  • 123
    • 2442553111 scopus 로고    scopus 로고
    • SH2-containing inositol phosphatase 2 predominantly regulates Akt2, and not Akt1, phosphorylation at the plasma membrane in response to insulin in 3T3-L1 adipocytes
    • Sasaoka T, Wada T, Fukui K, Murakami S, Ishihara H, Suzuki R, Tobe K, Kadowaki T, Kobayashi M. 2004. SH2-containing inositol phosphatase 2 predominantly regulates Akt2, and not Akt1, phosphorylation at the plasma membrane in response to insulin in 3T3-L1 adipocytes. J Biol Chem 279(15):14835-43.
    • (2004) J Biol Chem , vol.279 , Issue.15 , pp. 14835-14843
    • Sasaoka, T.1    Wada, T.2    Fukui, K.3    Murakami, S.4    Ishihara, H.5    Suzuki, R.6    Tobe, K.7    Kadowaki, T.8    Kobayashi, M.9
  • 124
  • 125
    • 2342472006 scopus 로고    scopus 로고
    • Phosphatases as small-molecule targets: Inhibiting the endogenous inhibitors of kinases
    • Schmid AC, Woscholski R. 2004. Phosphatases as small-molecule targets: inhibiting the endogenous inhibitors of kinases. Biochem Soc Trans 32(Pt 2):348-9.
    • (2004) Biochem Soc Trans , vol.32 , Issue.PART 2 , pp. 348-349
    • Schmid, A.C.1    Woscholski, R.2
  • 126
    • 0034810894 scopus 로고    scopus 로고
    • Defects of the insulin receptor substrate (IRS) system in human metabolic disorders
    • Sesti G, Federici M, Hribal ML, Lauro D, Sbraccia P, Lauro R. 2001. Defects of the insulin receptor substrate (IRS) system in human metabolic disorders. FASEB J 15(12):2099-111.
    • (2001) FASEB J , vol.15 , Issue.12 , pp. 2099-2111
    • Sesti, G.1    Federici, M.2    Hribal, M.L.3    Lauro, D.4    Sbraccia, P.5    Lauro, R.6
  • 127
    • 13544270853 scopus 로고    scopus 로고
    • Mechanism of SHIP-mediated inhibition of insulin- and platelet-derived growth factor-stimulated mitogen-activated protein kinase activity in 3T3-L1 adipocytes
    • Sharma PM, Son HS, Ugi S, Ricketts W, Olefsky JM. 2005. Mechanism of SHIP-mediated inhibition of insulin- and platelet-derived growth factor-stimulated mitogen-activated protein kinase activity in 3T3-L1 adipocytes. Mol Endocrinol 19(2):421-30.
    • (2005) Mol Endocrinol , vol.19 , Issue.2 , pp. 421-430
    • Sharma, P.M.1    Son, H.S.2    Ugi, S.3    Ricketts, W.4    Olefsky, J.M.5
  • 128
    • 13244252424 scopus 로고    scopus 로고
    • Mechanisms regulating phosphoinositide 3-kinase signalling in insulin-sensitive tissues
    • Shepherd PR. 2005. Mechanisms regulating phosphoinositide 3-kinase signalling in insulin-sensitive tissues. Acta Physiol Scand 183(1):3-12.
    • (2005) Acta Physiol Scand , vol.183 , Issue.1 , pp. 3-12
    • Shepherd, P.R.1
  • 129
    • 0034877139 scopus 로고    scopus 로고
    • Specificity in ligand binding and intracellular signalling by insulin and insulin-like growth factor receptors
    • Siddle K, Urso B, Niesler CA, Cope DL, Molina L, Surinya KH, Soos MA. 2001. Specificity in ligand binding and intracellular signalling by insulin and insulin-like growth factor receptors. Biochem Soc Trans 29(Pt 4):513-25.
    • (2001) Biochem Soc Trans , vol.29 , Issue.PART 4 , pp. 513-525
    • Siddle, K.1    Urso, B.2    Niesler, C.A.3    Cope, D.L.4    Molina, L.5    Surinya, K.H.6    Soos, M.A.7
  • 131
    • 0035100658 scopus 로고    scopus 로고
    • Protein phosphatase 2A: The Trojan Horse of cellular signaling
    • Sontag E. 2001. Protein phosphatase 2A: the Trojan Horse of cellular signaling. Cell Signal 13(1):7-16.
    • (2001) Cell Signal , vol.13 , Issue.1 , pp. 7-16
    • Sontag, E.1
  • 132
    • 0033553433 scopus 로고    scopus 로고
    • Okadaic acid activates atypical protein kinase C (zeta/lambda) in rat and 3T3/L1 adipocytes. An apparent requirement for activation of Glut4 translocation and glucose transport
    • Standaert ML, Bandyopadhyay G, Sajan MP, Cong L, Quon MJ, Farese RV. 1999. Okadaic acid activates atypical protein kinase C (zeta/lambda) in rat and 3T3/L1 adipocytes. An apparent requirement for activation of Glut4 translocation and glucose transport. J Biol Chem 274(20):14074-8.
    • (1999) J Biol Chem , vol.274 , Issue.20 , pp. 14074-14078
    • Standaert, M.L.1    Bandyopadhyay, G.2    Sajan, M.P.3    Cong, L.4    Quon, M.J.5    Farese, R.V.6
  • 135
    • 0005726439 scopus 로고    scopus 로고
    • Serine residues 994 and 1023/25 are important for insulin receptor kinase inhibition by protein kinase C isoforms beta2 and theta
    • Strack V, Hennige AM, Krutzfeldt J, Bossenmaier B, Klein HH, Kellerer M, Lammers R, Haring HU. 2000. Serine residues 994 and 1023/25 are important for insulin receptor kinase inhibition by protein kinase C isoforms beta2 and theta. Diabetologia 43(4):443-9.
    • (2000) Diabetologia , vol.43 , Issue.4 , pp. 443-449
    • Strack, V.1    Hennige, A.M.2    Krutzfeldt, J.3    Bossenmaier, B.4    Klein, H.H.5    Kellerer, M.6    Lammers, R.7    Haring, H.U.8
  • 137
    • 0023941899 scopus 로고
    • Alterations in insulin receptor autophosphorylation in insulin resistance: Correlation with altered sensitivity to glucose transport and antilipolysis to insulin
    • Takayama S, Kahn CR, Kubo K, Foley JE. 1988. Alterations in insulin receptor autophosphorylation in insulin resistance: correlation with altered sensitivity to glucose transport and antilipolysis to insulin. J Clin Endocrinol Metab 66(5):992-9.
    • (1988) J Clin Endocrinol Metab , vol.66 , Issue.5 , pp. 992-999
    • Takayama, S.1    Kahn, C.R.2    Kubo, K.3    Foley, J.E.4
  • 138
    • 20444487358 scopus 로고    scopus 로고
    • PTEN, but not SHIP2, suppresses insulin signaling through the phosphatidylinositol 3-kinase/Akt pathway in 3T3-L1 adipocytes
    • Tang X, Powelka AM, Soriano NA, Czech MP, Guilherme A. 2005. PTEN, but not SHIP2, suppresses insulin signaling through the phosphatidylinositol 3-kinase/Akt pathway in 3T3-L1 adipocytes. J Biol Chem 280(23):22523-9.
    • (2005) J Biol Chem , vol.280 , Issue.23 , pp. 22523-22529
    • Tang, X.1    Powelka, A.M.2    Soriano, N.A.3    Czech, M.P.4    Guilherme, A.5
  • 139
    • 33646434260 scopus 로고    scopus 로고
    • Increased PTEN expression due to transcriptional activation of PPARgamma by Lovastatin and Rosiglitazone
    • Teresi RE, Shaiu CW, Chen CS, Chatterjee VK, Waite KA, Eng C. 2006. Increased PTEN expression due to transcriptional activation of PPARgamma by Lovastatin and Rosiglitazone. Int J Cancer 118(10):2390-8.
    • (2006) Int J Cancer , vol.118 , Issue.10 , pp. 2390-2398
    • Teresi, R.E.1    Shaiu, C.W.2    Chen, C.S.3    Chatterjee, V.K.4    Waite, K.A.5    Eng, C.6
  • 140
    • 0346458780 scopus 로고    scopus 로고
    • Regulation of Cbl-associated protein/Cbl pathway in muscle and adipose tissues of two animal models of insulin resistance
    • Thirone AC, Carvalheira JB, Hirata AE, Velloso LA, Saad MJ. 2004. Regulation of Cbl-associated protein/Cbl pathway in muscle and adipose tissues of two animal models of insulin resistance. Endocrinology 145(1):281-93.
    • (2004) Endocrinology , vol.145 , Issue.1 , pp. 281-293
    • Thirone, A.C.1    Carvalheira, J.B.2    Hirata, A.E.3    Velloso, L.A.4    Saad, M.J.5
  • 141
    • 0033537830 scopus 로고    scopus 로고
    • Oxidative stress disrupts insulin-induced cellular redistribution of insulin receptor substrate-1 and phosphatidylinositol 3-kinase in 3T3-L1 adipocytes. A putative cellular mechanism for impaired protein kinase B activation and GLUT4 translocation
    • Tirosh A, Potashnik R, Bashan N, Rudich A. 1999. Oxidative stress disrupts insulin-induced cellular redistribution of insulin receptor substrate-1 and phosphatidylinositol 3-kinase in 3T3-L1 adipocytes. A putative cellular mechanism for impaired protein kinase B activation and GLUT4 translocation. J Biol Chem 274(15):10595-602.
    • (1999) J Biol Chem , vol.274 , Issue.15 , pp. 10595-10602
    • Tirosh, A.1    Potashnik, R.2    Bashan, N.3    Rudich, A.4
  • 142
    • 0025945356 scopus 로고
    • Purification of proteintyrosine phosphatases from human placenta
    • Tonks NK, Diltz CD, Fischer EH. 1991. Purification of proteintyrosine phosphatases from human placenta. Methods Enzymol 201:427-42.
    • (1991) Methods Enzymol , vol.201 , pp. 427-442
    • Tonks, N.K.1    Diltz, C.D.2    Fischer, E.H.3
  • 143
    • 29144492713 scopus 로고    scopus 로고
    • Role of suppressors of cytokine signaling SOCS-1 and SOCS-3 in hepatic steatosis and the metabolic syndrome
    • Ueki K, Kadowaki T, Kahn CR. 2005. Role of suppressors of cytokine signaling SOCS-1 and SOCS-3 in hepatic steatosis and the metabolic syndrome. Hepatol Res 33(2):185-92.
    • (2005) Hepatol Res , vol.33 , Issue.2 , pp. 185-192
    • Ueki, K.1    Kadowaki, T.2    Kahn, C.R.3
  • 144
    • 0036122481 scopus 로고    scopus 로고
    • Protein phosphatase 2A forms a molecular complex with Shc and regulates Shc tyrosine phosphorylation and downstream mitogenic signaling
    • Ugi S, Imamura T, Ricketts W, Olefsky JM. 2002. Protein phosphatase 2A forms a molecular complex with Shc and regulates Shc tyrosine phosphorylation and downstream mitogenic signaling. Mol Cell Biol 22(7):2375-87.
    • (2002) Mol Cell Biol , vol.22 , Issue.7 , pp. 2375-2387
    • Ugi, S.1    Imamura, T.2    Ricketts, W.3    Olefsky, J.M.4
  • 145
    • 4544314719 scopus 로고    scopus 로고
    • Protein phosphatase 2A negatively regulates insulin's metabolic signaling pathway by inhibiting Akt (protein kinase B) activity in 3T3-L1 adipocytes
    • Ugi S, Imamura T, Maegawa H, Egawa K, Yoshizaki T, Shi K, Obata T, Ebina Y, Kashiwagi A, Olefsky JM. 2004. Protein phosphatase 2A negatively regulates insulin's metabolic signaling pathway by inhibiting Akt (protein kinase B) activity in 3T3-L1 adipocytes. Mol Cell Biol 24(19):8778-89.
    • (2004) Mol Cell Biol , vol.24 , Issue.19 , pp. 8778-8789
    • Ugi, S.1    Imamura, T.2    Maegawa, H.3    Egawa, K.4    Yoshizaki, T.5    Shi, K.6    Obata, T.7    Ebina, Y.8    Kashiwagi, A.9    Olefsky, J.M.10
  • 147
    • 0036182137 scopus 로고    scopus 로고
    • Lipotoxic diseases
    • Unger RH. 2002. Lipotoxic diseases. Annu Rev Med 53:319-36.
    • (2002) Annu Rev Med , vol.53 , pp. 319-336
    • Unger, R.H.1
  • 148
    • 0037427518 scopus 로고    scopus 로고
    • The c-Cbl-associated protein and c-Cbl are two new partners of the SH2-containing inositol polyphosphate 5-phosphatase SHIP2
    • Vandenbroere I, Paternotte N, Dumont JE, Erneux C, Pirson I. 2003. The c-Cbl-associated protein and c-Cbl are two new partners of the SH2-containing inositol polyphosphate 5-phosphatase SHIP2. Biochem Biophys Res Commun 300(2):494-500.
    • (2003) Biochem Biophys Res Commun , vol.300 , Issue.2 , pp. 494-500
    • Vandenbroere, I.1    Paternotte, N.2    Dumont, J.E.3    Erneux, C.4    Pirson, I.5
  • 149
    • 0034653608 scopus 로고    scopus 로고
    • The PI3K-PDK1 connection: More than just a road to PKB
    • Vanhaesebroeck B, Alessi DR. 2000. The PI3K-PDK1 connection: more than just a road to PKB. Biochem J 346 Pt 3:561-76.
    • (2000) Biochem J , vol.346 , Issue.PART 3 , pp. 561-576
    • Vanhaesebroeck, B.1    Alessi, D.R.2
  • 150
    • 0042570843 scopus 로고    scopus 로고
    • Protein - protein interaction in insulin signaling and the molecular mechanisms of insulin resistance
    • Virkamaki A, Ueki K, Kahn CR. 1999. Protein - protein interaction in insulin signaling and the molecular mechanisms of insulin resistance. J Clin Invest 103(7):931-43.
    • (1999) J Clin Invest , vol.103 , Issue.7 , pp. 931-943
    • Virkamaki, A.1    Ueki, K.2    Kahn, C.R.3
  • 151
    • 0035135318 scopus 로고    scopus 로고
    • Overexpression of SH2-containing inositol phosphatase 2 results in negative regulation of insulin-induced metabolic actions in 3T3-L1 adipocytes via its 50-phosphatase catalytic activity
    • Wada T, Sasaoka T, Funaki M, Hori H, Murakami S, Ishiki M, Haruta T, Asano T, Ogawa W, Ishihara H, Kobayashi M. 2001. Overexpression of SH2-containing inositol phosphatase 2 results in negative regulation of insulin-induced metabolic actions in 3T3-L1 adipocytes via its 50-phosphatase catalytic activity. Mol Cell Biol 21(5):1633-46.
    • (2001) Mol Cell Biol , vol.21 , Issue.5 , pp. 1633-1646
    • Wada, T.1    Sasaoka, T.2    Funaki, M.3    Hori, H.4    Murakami, S.5    Ishiki, M.6    Haruta, T.7    Asano, T.8    Ogawa, W.9    Ishihara, H.10    Kobayashi, M.11
  • 152
    • 0035869175 scopus 로고    scopus 로고
    • PTEN inhibits insulin-stimulated MEK/MAPK activation and cell growth by blocking IRS-1 phosphorylation and IRS-1/Grb-2/Sos complex formation in a breast cancer model
    • Weng LP, Smith WM, Brown JL, Eng C. 2001. PTEN inhibits insulin-stimulated MEK/MAPK activation and cell growth by blocking IRS-1 phosphorylation and IRS-1/Grb-2/Sos complex formation in a breast cancer model. Hum Mol Genet 10(6):605-16.
    • (2001) Hum Mol Genet , vol.10 , Issue.6 , pp. 605-616
    • Weng, L.P.1    Smith, W.M.2    Brown, J.L.3    Eng, C.4
  • 153
    • 0037098951 scopus 로고    scopus 로고
    • PTEN blocks insulin-mediated ETS-2 phosphorylation through MAP kinase, independently of the phosphoinositide 3-kinase pathway
    • Weng LP, Brown JL, Baker KM, Ostrowski MC, Eng C. 2002. PTEN blocks insulin-mediated ETS-2 phosphorylation through MAP kinase, independently of the phosphoinositide 3-kinase pathway. Hum Mol Genet 11(15):1687-96.
    • (2002) Hum Mol Genet , vol.11 , Issue.15 , pp. 1687-1696
    • Weng, L.P.1    Brown, J.L.2    Baker, K.M.3    Ostrowski, M.C.4    Eng, C.5
  • 154
    • 0031918624 scopus 로고    scopus 로고
    • The IRS-signalling system: A network of docking proteins that mediate insulin action
    • White MF. 1998. The IRS-signalling system: a network of docking proteins that mediate insulin action. Mol Cell Biochem 182(1-2):3-11.
    • (1998) Mol Cell Biochem , vol.182 , Issue.1-2 , pp. 3-11
    • White, M.F.1
  • 155
    • 0028085078 scopus 로고
    • The insulin signaling system
    • White MF, Kahn CR. 1994. The insulin signaling system. J Biol Chem 269(1):1-4.
    • (1994) J Biol Chem , vol.269 , Issue.1 , pp. 1-4
    • White, M.F.1    Kahn, C.R.2
  • 157
    • 0032431032 scopus 로고    scopus 로고
    • The PTEN/MMAC1 tumor suppressor phosphatase functions as a negative regulator of the phosphoinositide 3-kinase/Akt pathway
    • Wu X, Senechal K, Neshat MS, Whang YE, Sawyers CL. 1998. The PTEN/MMAC1 tumor suppressor phosphatase functions as a negative regulator of the phosphoinositide 3-kinase/Akt pathway. Proc Natl Acad Sci USA 95(26):15587-91.
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.26 , pp. 15587-15591
    • Wu, X.1    Senechal, K.2    Neshat, M.S.3    Whang, Y.E.4    Sawyers, C.L.5
  • 158
    • 0031171216 scopus 로고    scopus 로고
    • The IRS-signalling system during insulin and cytokine action
    • Yenush L, White MF. 1997. The IRS-signalling system during insulin and cytokine action. Bioessays 19(6):491-500.
    • (1997) Bioessays , vol.19 , Issue.6 , pp. 491-500
    • Yenush, L.1    White, M.F.2
  • 159
    • 0029820085 scopus 로고    scopus 로고
    • The pleckstrin homology domain is the principal link between the insulin receptor and IRS-1
    • Yenush L, Makati KJ, Smith-Hall J, Ishibashi O, Myers Jr MG, White MF. 1996. The pleckstrin homology domain is the principal link between the insulin receptor and IRS-1. J Biol Chem 271(39):24300-6.
    • (1996) J Biol Chem , vol.271 , Issue.39 , pp. 24300-24306
    • Yenush, L.1    Makati, K.J.2    Smith-Hall, J.3    Ishibashi, O.4    Myers Jr., M.G.5    White, M.F.6
  • 160
    • 0035979775 scopus 로고    scopus 로고
    • Reversal of obesity- and diet-induced insulin resistance with salicylates or targeted disruption of Ikkbeta
    • Yuan M, Konstantopoulos N, Lee J, Hansen L, Li ZW, Karin M, Shoelson SE. 2001. Reversal of obesity- and diet-induced insulin resistance with salicylates or targeted disruption of Ikkbeta. Science 293(5535):1673-7.
    • (2001) Science , vol.293 , Issue.5535 , pp. 1673-1677
    • Yuan, M.1    Konstantopoulos, N.2    Lee, J.3    Hansen, L.4    Li, Z.W.5    Karin, M.6    Shoelson, S.E.7
  • 162
    • 2642541849 scopus 로고    scopus 로고
    • Transgenic overexpression of protein-tyrosine phosphatase 1B in muscle causes insulin resistance, but overexpression with leukocyte antigen-related phosphatase does not additively impair insulin action
    • Zabolotny JM, Haj FG, Kim YB, Kim HJ, Shulman GI, Kim JK, Neel BG, Kahn BB. 2004. Transgenic overexpression of protein-tyrosine phosphatase 1B in muscle causes insulin resistance, but overexpression with leukocyte antigen-related phosphatase does not additively impair insulin action. J Biol Chem 279(23):24844-51.
    • (2004) J Biol Chem , vol.279 , Issue.23 , pp. 24844-24851
    • Zabolotny, J.M.1    Haj, F.G.2    Kim, Y.B.3    Kim, H.J.4    Shulman, G.I.5    Kim, J.K.6    Neel, B.G.7    Kahn, B.B.8
  • 163
    • 0035500813 scopus 로고    scopus 로고
    • Insulin resistance: A phosphorylation-based uncoupling of insulin signaling
    • Zick Y. 2001. Insulin resistance: a phosphorylation-based uncoupling of insulin signaling. Trends Cell Biol 11(11):437-41.
    • (2001) Trends Cell Biol , vol.11 , Issue.11 , pp. 437-441
    • Zick, Y.1
  • 164
    • 0035856920 scopus 로고    scopus 로고
    • Global and societal implications of the diabetes epidemic
    • Zimmet P, Alberti KG, Shaw J. 2001. Global and societal implications of the diabetes epidemic. Nature 414(6865):782-7.
    • (2001) Nature , vol.414 , Issue.6865 , pp. 782-787
    • Zimmet, P.1    Alberti, K.G.2    Shaw, J.3


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