메뉴 건너뛰기




Volumn 12, Issue 5, 2006, Pages 549-556

The SHP-1 protein tyrosine phosphatase negatively modulates glucose homeostasis

Author keywords

[No Author keywords available]

Indexed keywords

GLUCOSE; INSULIN; PROTEIN TYROSINE PHOSPHATASE SHP 1; RNA;

EID: 33646551477     PISSN: 10788956     EISSN: 1546170X     Source Type: Journal    
DOI: 10.1038/nm1397     Document Type: Article
Times cited : (124)

References (50)
  • 1
    • 85047684646 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatases: Emerging targets for therapeutic intervention in type 2 diabetes and related states of insulin resistance
    • Goldstein, B.J. Protein-tyrosine phosphatases: emerging targets for therapeutic intervention in type 2 diabetes and related states of insulin resistance. J. Clin. Endocrinol. Metab. 87, 2474-2480 (2002).
    • (2002) J. Clin. Endocrinol. Metab. , vol.87 , pp. 2474-2480
    • Goldstein, B.J.1
  • 2
    • 0037376001 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: The quest for negative regulators of insulin action
    • Asante-Appiah, E. & Kennedy, B.P. Protein tyrosine phosphatases: the quest for negative regulators of insulin action. Am. J. Physiol. Endocrinol. Metab. 284, E663-E670 (2003).
    • (2003) Am. J. Physiol. Endocrinol. Metab. , vol.284
    • Asante-Appiah, E.1    Kennedy, B.P.2
  • 3
    • 0033673994 scopus 로고    scopus 로고
    • Modulation of insulin signaling by protein tyrosine phosphatases
    • Elchebly, M., Cheng, A. & Tremblay, M.L. Modulation of insulin signaling by protein tyrosine phosphatases. J. Mol. Med. 78, 473-482 (2000).
    • (2000) J. Mol. Med. , vol.78 , pp. 473-482
    • Elchebly, M.1    Cheng, A.2    Tremblay, M.L.3
  • 4
    • 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, J.M. et al. 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, 24844-24851 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 24844-24851
    • Zabolotny, J.M.1
  • 5
    • 0033525870 scopus 로고    scopus 로고
    • Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene
    • Elchebly, M. et al. Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene. Science 283, 1544-1548 (1999).
    • (1999) Science , vol.283 , pp. 1544-1548
    • Elchebly, M.1
  • 6
    • 0001334931 scopus 로고    scopus 로고
    • Functional association between the insulin receptor and the transmembrane protein-tyrosine phosphatase LAR in intact cells
    • Ahmad, F. & Goldstein, B.J. Functional association between the insulin receptor and the transmembrane protein-tyrosine phosphatase LAR in intact cells. J. Biol. Chem. 272, 448-457 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 448-457
    • Ahmad, F.1    Goldstein, B.J.2
  • 7
    • 0033942614 scopus 로고    scopus 로고
    • Increased energy expenditure, decreased adiposity, and tissue-specific insulin sensitivity in protein-tyrosine phosphatase 1B-deficient mice
    • Klaman, L.D. et al. Increased energy expenditure, decreased adiposity, and tissue-specific insulin sensitivity in protein-tyrosine phosphatase 1B-deficient mice. Mol. Cell. Biol. 20, 5479-5489 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5479-5489
    • Klaman, L.D.1
  • 8
    • 0028896991 scopus 로고
    • Protein-tyrosine-phosphatase SHPTP2 is a required positive effector for insulin downstream signaling
    • Yamauchi, K., Milarski, K.L., Saltiel, A.R. & Pessin, J.E. Protein-tyrosine-phosphatase SHPTP2 is a required positive effector for insulin downstream signaling. Proc. Natl. Acad. Sci. USA 92, 664-668 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 664-668
    • Yamauchi, K.1    Milarski, K.L.2    Saltiel, A.R.3    Pessin, J.E.4
  • 9
    • 0033570225 scopus 로고    scopus 로고
    • Expression of a dominant negative SHP-2 in transgenic mice induces insulin resistance
    • Maegawa, H. et al. Expression of a dominant negative SHP-2 in transgenic mice induces insulin resistance. J. Biol. Chem. 274, 30236-30243 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 30236-30243
    • Maegawa, H.1
  • 10
    • 0026742211 scopus 로고
    • Characterization of hematopoietic intracellular protein tyrosine phosphatases: Description of a phosphatase containing an SH2 domain and another enriched in proline-, glutamic acid-, serine-, and threonine-rich sequences
    • Matthews, R.J., Bowne, D.B., Flores, E. & Thomas, M.L. Characterization of hematopoietic intracellular protein tyrosine phosphatases: description of a phosphatase containing an SH2 domain and another enriched in proline-, glutamic acid-, serine-, and threonine-rich sequences. Mol. Cell. Biol. 12, 2396-2405 (1992).
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2396-2405
    • Matthews, R.J.1    Bowne, D.B.2    Flores, E.3    Thomas, M.L.4
  • 11
    • 0026516065 scopus 로고
    • Isolation of a src homology 2-containing tyrosine phosphatase
    • Plutzky, J., Neel, B.G. & Rosenberg, R.D. Isolation of a src homology 2-containing tyrosine phosphatase. Proc. Natl. Acad. Sci. USA 89, 1123-1127 (1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 1123-1127
    • Plutzky, J.1    Neel, B.G.2    Rosenberg, R.D.3
  • 12
    • 0025816584 scopus 로고
    • A protein-tyrosine phosphatase with sequence similarity to the SH2 domain of the protein-tyrosine kinases
    • Shen, S.H., Bastien, L., Posner, B.I. & Chretien, P. A protein-tyrosine phosphatase with sequence similarity to the SH2 domain of the protein-tyrosine kinases. Nature 352, 736-739 (1991).
    • (1991) Nature , vol.352 , pp. 736-739
    • Shen, S.H.1    Bastien, L.2    Posner, B.I.3    Chretien, P.4
  • 13
    • 0026547356 scopus 로고
    • Protein tyrosine phosphatase containing SH2 domains: Characterization, preferential expression in hematopoietic cells, and localization to human chromosome 12p12-p13
    • Yi, T.L., Cleveland, J.L. & Ihle, J.N. Protein tyrosine phosphatase containing SH2 domains: characterization, preferential expression in hematopoietic cells, and localization to human chromosome 12p12-p13. Mol. Cell. Biol. 12, 836-846 (1992).
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 836-846
    • Yi, T.L.1    Cleveland, J.L.2    Ihle, J.N.3
  • 14
    • 0029891236 scopus 로고    scopus 로고
    • Regulation of colony-stimulating factor 1 receptor signaling by the SH2 domain-containing tyrosine phosphatase SHPTP1
    • Chen, H.E., Chang, S., Trub, T. & Neel, B.G. Regulation of colony-stimulating factor 1 receptor signaling by the SH2 domain-containing tyrosine phosphatase SHPTP1. Mol. Cell. Biol. 16, 3685-3697 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3685-3697
    • Chen, H.E.1    Chang, S.2    Trub, T.3    Neel, B.G.4
  • 15
    • 0028956353 scopus 로고
    • Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals
    • Klingmuller, U., Lorenz, U., Cantley, L.C., Neel, B.G. & Lodish, H.F. Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals. Cell 80, 729-738 (1995).
    • (1995) Cell , vol.80 , pp. 729-738
    • Klingmuller, U.1    Lorenz, U.2    Cantley, L.C.3    Neel, B.G.4    Lodish, H.F.5
  • 16
    • 0029151931 scopus 로고
    • Association of SH2 domain protein tyrosine phosphatases with the epidermal growth factor receptor in human tumor cells. Phosphatidic acid activates receptor dephosphorylation by PTP1C
    • Tomic, S. et al. Association of SH2 domain protein tyrosine phosphatases with the epidermal growth factor receptor in human tumor cells. Phosphatidic acid activates receptor dephosphorylation by PTP1C. J. Biol. Chem. 270, 21277-21284 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 21277-21284
    • Tomic, S.1
  • 17
    • 0028342629 scopus 로고
    • Insulin stimulates the phosphorylation of Tyr538 and the catalytic activity of PTP1C, a protein tyrosine phosphatase with Src homology-2 domains
    • Uchida, T. et al. Insulin stimulates the phosphorylation of Tyr538 and the catalytic activity of PTP1C, a protein tyrosine phosphatase with Src homology-2 domains. J. Biol. Chem. 269, 12220-12228 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 12220-12228
    • Uchida, T.1
  • 18
    • 0032549589 scopus 로고    scopus 로고
    • sst2 somatostatin receptor mediates negative regulation of insulin receptor signaling through the tyrosine phosphatase SHP-1
    • Bousquet, C. et al. sst2 somatostatin receptor mediates negative regulation of insulin receptor signaling through the tyrosine phosphatase SHP-1. J. Biol. Chem. 273, 7099-7106 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 7099-7106
    • Bousquet, C.1
  • 19
    • 0030962582 scopus 로고    scopus 로고
    • Interleukin-4 (IL-4) induces phosphatidylinositol 3-kinase (p85) dephosphorylation. Implications for the role of SHP-1 in the IL-4-induced signals in human B cells
    • Imani, F., Rager, K.J., Catipovic, B. & Marsh, D.G. Interleukin-4 (IL-4) induces phosphatidylinositol 3-kinase (p85) dephosphorylation. Implications for the role of SHP-1 in the IL-4-induced signals in human B cells. J. Biol. Chem. 272, 7927-7931 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 7927-7931
    • Imani, F.1    Rager, K.J.2    Catipovic, B.3    Marsh, D.G.4
  • 20
    • 0032488828 scopus 로고    scopus 로고
    • SHP-1 associates with both platelet-derived growth factor receptor and the p85 subunit of phosphatidylinositol 3-kinase
    • Yu, Z. et al. SHP-1 associates with both platelet-derived growth factor receptor and the p85 subunit of phosphatidylinositol 3-kinase. J. Biol. Chem. 273, 3687-3694 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 3687-3694
    • Yu, Z.1
  • 21
    • 0033600848 scopus 로고    scopus 로고
    • SHP-1 regulates Lck-induced phosphatidylinositol 3-kinase phosphorylation and activity
    • Cuevas, B. et al. SHP-1 regulates Lck-induced phosphatidylinositol 3-kinase phosphorylation and activity. J. Biol. Chem. 274, 27583-27589 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 27583-27589
    • Cuevas, B.1
  • 22
    • 0031053335 scopus 로고    scopus 로고
    • Association of biliary glycoprotein with protein tyrosine phosphatase SHP-1 in malignant colon epithelial cells
    • Beauchemin, N. et al. Association of biliary glycoprotein with protein tyrosine phosphatase SHP-1 in malignant colon epithelial cells. Oncogene 14, 783-790 (1997).
    • (1997) Oncogene , vol.14 , pp. 783-790
    • Beauchemin, N.1
  • 23
    • 0036009113 scopus 로고    scopus 로고
    • Neisserial binding to CEACAM1 arrests the activation and proliferation of CD4+ T lymphocytes
    • Boulton, I.C. & Gray-Owen, S.D. Neisserial binding to CEACAM1 arrests the activation and proliferation of CD4+ T lymphocytes. Nat. Immunol. 3, 229-236 (2002).
    • (2002) Nat. Immunol. , vol.3 , pp. 229-236
    • Boulton, I.C.1    Gray-Owen, S.D.2
  • 24
    • 0036467540 scopus 로고    scopus 로고
    • Activation-induced expression of carcinoembryonic antigen-cell adhesion molecule 1 regulates mouse T lymphocyte function
    • Nakajima, A. et al. Activation-induced expression of carcinoembryonic antigen-cell adhesion molecule 1 regulates mouse T lymphocyte function. J. Immunol. 168, 1028-1035 (2002).
    • (2002) J. Immunol. , vol.168 , pp. 1028-1035
    • Nakajima, A.1
  • 25
    • 0028822686 scopus 로고
    • Receptor-mediated internalization of insulin. Potential role of pp120/HA4, a substrate of the insulin receptor kinase
    • Formisano, P. et al. Receptor-mediated internalization of insulin. Potential role of pp120/HA4, a substrate of the insulin receptor kinase. J. Biol. Chem. 270, 24073-24077 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 24073-24077
    • Formisano, P.1
  • 26
    • 0030667408 scopus 로고    scopus 로고
    • Differential effect of pp120 on insulin endocytosis by two variant insulin receptor isoforms
    • Li Calzi, S., Choice, C.V. & Najjar, S.M. Differential effect of pp120 on insulin endocytosis by two variant insulin receptor isoforms. Am. J. Physiol. 273, E801-E808 (1997).
    • (1997) Am. J. Physiol. , vol.273
    • Li Calzi, S.1    Choice, C.V.2    Najjar, S.M.3
  • 27
    • 0032557447 scopus 로고    scopus 로고
    • Effect of pp120 on receptor-mediated insulin endocytosis is regulated by the juxtamembrane domain of the insulin receptor
    • Najjar, S.M., Choice, C.V., Soni, P., Whitman, C.M. & Poy, M.N. Effect of pp120 on receptor-mediated insulin endocytosis is regulated by the juxtamembrane domain of the insulin receptor. J. Biol. Chem. 273, 12923-12928 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 12923-12928
    • Najjar, S.M.1    Choice, C.V.2    Soni, P.3    Whitman, C.M.4    Poy, M.N.5
  • 28
    • 0032575650 scopus 로고    scopus 로고
    • Insulin stimulates pp120 endocytosis in cells co-expressing insulin receptors
    • Choice, C.V., Howard, M.J., Poy, M.N., Hankin, M.H. & Najjar, S.M. Insulin stimulates pp120 endocytosis in cells co-expressing insulin receptors. J. Biol. Chem. 273, 22194-22200 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 22194-22200
    • Choice, C.V.1    Howard, M.J.2    Poy, M.N.3    Hankin, M.H.4    Najjar, S.M.5
  • 29
    • 0036510160 scopus 로고    scopus 로고
    • CEACAM1 regulates insulin clearance in liver
    • Poy, M.N. et al. CEACAM1 regulates insulin clearance in liver. Nat. Genet. 30, 270-276 (2002).
    • (2002) Nat. Genet. , vol.30 , pp. 270-276
    • Poy, M.N.1
  • 30
    • 0027195626 scopus 로고
    • Motheaten and viable motheaten mice have mutations in the haematopoietic cell phosphatase gene
    • Tsui, H.W., Siminovitch, K.A., de Souza, L. & Tsui, F.W. Motheaten and viable motheaten mice have mutations in the haematopoietic cell phosphatase gene. Nat. Genet. 4, 124-129 (1993).
    • (1993) Nat. Genet. , vol.4 , pp. 124-129
    • Tsui, H.W.1    Siminovitch, K.A.2    De Souza, L.3    Tsui, F.W.4
  • 31
    • 0030869203 scopus 로고    scopus 로고
    • Expression of protein-tyrosine phosphatases in the major insulin target tissues
    • Norris, K. et al. Expression of protein-tyrosine phosphatases in the major insulin target tissues. FEBS Lett. 415, 243-248 (1997).
    • (1997) FEBS Lett. , vol.415 , pp. 243-248
    • Norris, K.1
  • 32
    • 0035184717 scopus 로고    scopus 로고
    • Role of host phosphotyrosine phosphatase SHP-1 in the development of murine leishmaniasis
    • Forget, G. et al. Role of host phosphotyrosine phosphatase SHP-1 in the development of murine leishmaniasis. Eur. J. Immunol. 31, 3185-3196 (2001).
    • (2001) Eur. J. Immunol. , vol.31 , pp. 3185-3196
    • Forget, G.1
  • 33
    • 0343729328 scopus 로고    scopus 로고
    • Perinuclear localization of the protein-tyrosine phosphatase SHP-1 and inhibition of epidermal growth factor-stimulated STAT1/3 activation in A431 cells
    • Tenev, T. et al. Perinuclear localization of the protein-tyrosine phosphatase SHP-1 and inhibition of epidermal growth factor-stimulated STAT1/3 activation in A431 cells. Eur. J. Cell Biol. 79, 261-271 (2000).
    • (2000) Eur. J. Cell Biol. , vol.79 , pp. 261-271
    • Tenev, T.1
  • 34
    • 0038190977 scopus 로고    scopus 로고
    • Negative regulation of beta-catenin signaling by tyrosine phosphatase SHP-1 in intestinal epithelial cells
    • Duchesne, C., Charland, S., Asselin, C., Nahmias, C. & Rivard, N. Negative regulation of beta-catenin signaling by tyrosine phosphatase SHP-1 in intestinal epithelial cells. J. Biol. Chem. 278, 14274-14283 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 14274-14283
    • Duchesne, C.1    Charland, S.2    Asselin, C.3    Nahmias, C.4    Rivard, N.5
  • 35
    • 3643119742 scopus 로고    scopus 로고
    • The phosphoinositol phosphatase activity of PTEN mediates a serum-sensitive G1 growth arrest in glioma cells
    • Furnari, F.B., Huang, H.J. & Cavenee, W.K. The phosphoinositol phosphatase activity of PTEN mediates a serum-sensitive G1 growth arrest in glioma cells. Cancer Res. 58, 5002-5008 (1998).
    • (1998) Cancer Res. , vol.58 , pp. 5002-5008
    • Furnari, F.B.1    Huang, H.J.2    Cavenee, W.K.3
  • 36
    • 0032506011 scopus 로고    scopus 로고
    • The lipid phosphatase activity of PTEN is critical for its tumor supressor function
    • Myers, M.P. et al. The lipid phosphatase activity of PTEN is critical for its tumor supressor function. Proc. Nat. Acad. Sci. USA 95, 13513-13518 (1998).
    • (1998) Proc. Nat. Acad. Sci. USA , vol.95 , pp. 13513-13518
    • Myers, M.P.1
  • 37
    • 0033794917 scopus 로고    scopus 로고
    • Roles of the SHP-1 tyrosine phosphatase in the negative regulation of cell signalling
    • Zhang, J., Somani, A.K. & Siminovitch, K.A. Roles of the SHP-1 tyrosine phosphatase in the negative regulation of cell signalling. Semin. Immunol. 12, 361-378 (2000).
    • (2000) Semin. Immunol. , vol.12 , pp. 361-378
    • Zhang, J.1    Somani, A.K.2    Siminovitch, K.A.3
  • 38
    • 0033105369 scopus 로고    scopus 로고
    • Expression of dominant-negative src-homology domain 2-containing protein tyrosine phosphatase-1 results in increased Syk tyrosine kinase activity and B cell activation
    • Dustin, L.B. et al. Expression of dominant-negative src-homology domain 2-containing protein tyrosine phosphatase-1 results in increased Syk tyrosine kinase activity and B cell activation. J. Immunol. 162, 2717-2724 (1999).
    • (1999) J. Immunol. , vol.162 , pp. 2717-2724
    • Dustin, L.B.1
  • 39
    • 0023584983 scopus 로고
    • The trafficking and processing of insulin and insulin receptors in cultured rat hepatocytes
    • Levy, J.R. & Olefsky, J.M. The trafficking and processing of insulin and insulin receptors in cultured rat hepatocytes. Endocrinology 121, 2075-2086(1987).
    • (1987) Endocrinology , vol.121 , pp. 2075-2086
    • Levy, J.R.1    Olefsky, J.M.2
  • 40
    • 0026344857 scopus 로고
    • Phosphorylation in vitro of the 85 kDa subunit of phosphatidylinositol 3-kinase and its possible activation by insulin receptor tyrosine kinase
    • Hayashi, H. et al. Phosphorylation in vitro of the 85 kDa subunit of phosphatidylinositol 3-kinase and its possible activation by insulin receptor tyrosine kinase. Biochem. J. 280, 769-775 (1991).
    • (1991) Biochem. J. , vol.280 , pp. 769-775
    • Hayashi, H.1
  • 41
    • 0026563978 scopus 로고
    • Insulin treatment stimulates the tyrosine phosphorylation of the alpha-type 85-kDa subunit of phosphatidylinositol 3-kinase in vivo
    • Hayashi, H. et al. Insulin treatment stimulates the tyrosine phosphorylation of the alpha-type 85-kDa subunit of phosphatidylinositol 3-kinase in vivo. J. Biol. Chem. 267, 22575-22580 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 22575-22580
    • Hayashi, H.1
  • 42
    • 0035920129 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of p85 relieves its inhibitory activity on phosphatidylinositol 3-kinase
    • Cuevas, B.D. et al. Tyrosine phosphorylation of p85 relieves its inhibitory activity on phosphatidylinositol 3-kinase. J. Biol. Chem. 276, 27455-27461 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 27455-27461
    • Cuevas, B.D.1
  • 43
    • 0031887249 scopus 로고    scopus 로고
    • Regulation of the p85/p110 phosphatidylinositol 3′-kinase: Stabilization and inhibition of the p110alpha catalytic subunit by the p85 regulatory subunit
    • Yu, J. et al. Regulation of the p85/p110 phosphatidylinositol 3′-kinase: stabilization and inhibition of the p110alpha catalytic subunit by the p85 regulatory subunit. Mol. Cell. Biol. 18, 1379-1387 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1379-1387
    • Yu, J.1
  • 44
    • 0033780412 scopus 로고    scopus 로고
    • Positive and negative regulation of phosphoinositide 3-kinase-dependent signaling pathways by three different gene products of the p85alpha regulatory subunit
    • Ueki, K., Algenstaedt, P., Mauvais-Jarvis, F. & Kahn, C.R. Positive and negative regulation of phosphoinositide 3-kinase-dependent signaling pathways by three different gene products of the p85alpha regulatory subunit. Mol. Cell. Biol. 20, 8035-8046 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8035-8046
    • Ueki, K.1    Algenstaedt, P.2    Mauvais-Jarvis, F.3    Kahn, C.R.4
  • 45
    • 0141994730 scopus 로고    scopus 로고
    • Src family protein-tyrosine kinases alter the function of PTEN to regulate phosphatidylinositol 3-kinase/AKT cascades
    • Lu, Y. et al. Src family protein-tyrosine kinases alter the function of PTEN to regulate phosphatidylinositol 3-kinase/AKT cascades. J. Biol. Chem. 278, 40057-40066 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 40057-40066
    • Lu, Y.1
  • 46
    • 2342625392 scopus 로고    scopus 로고
    • Analysis of adenovirus sequestration in the liver, transduction of hepatic cells, and innate toxicity after injection of fiber-modified vectors
    • Shayakhmetov, D.M., Li, Z.Y., Ni, S. & Lieber, A. Analysis of adenovirus sequestration in the liver, transduction of hepatic cells, and innate toxicity after injection of fiber-modified vectors. J. Virol. 78, 5368-5381 (2004).
    • (2004) J. Virol. , vol.78 , pp. 5368-5381
    • Shayakhmetov, D.M.1    Li, Z.Y.2    Ni, S.3    Lieber, A.4
  • 47
    • 7244223319 scopus 로고    scopus 로고
    • Interaction between altered insulin and lipid metabolism in CEACAM1-inactive transgenic mice
    • Dai, T. et al. Interaction between altered insulin and lipid metabolism in CEACAM1-inactive transgenic mice. J. Biol. Chem. 279, 45155-45161 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 45155-45161
    • Dai, T.1
  • 48
    • 27244458206 scopus 로고    scopus 로고
    • Insulin acutely decreases hepatic fatty acid synthase activity
    • Najjar, S.M. et al. Insulin acutely decreases hepatic fatty acid synthase activity. Cell Metab. 2, 43-53 (2005).
    • (2005) Cell Metab. , vol.2 , pp. 43-53
    • Najjar, S.M.1
  • 49
    • 12144290761 scopus 로고    scopus 로고
    • Differential effects of interleukin-6 and -10 on skeletal muscle and liver insulin action in vivo
    • Kim, H.J. et al. Differential effects of interleukin-6 and -10 on skeletal muscle and liver insulin action in vivo. Diabetes 53, 1060-1067 (2004).
    • (2004) Diabetes , vol.53 , pp. 1060-1067
    • Kim, H.J.1
  • 50
    • 0034770292 scopus 로고    scopus 로고
    • Targeted disruption of inducible nitric oxide synthase protects against obesity-linked insulin resistance in muscle
    • Perreault, M. & Marette, A. Targeted disruption of inducible nitric oxide synthase protects against obesity-linked insulin resistance in muscle. Nat. Med. 7, 1138-1143 (2001).
    • (2001) Nat. Med. , vol.7 , pp. 1138-1143
    • Perreault, M.1    Marette, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.