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Volumn 586, Issue 3, 2012, Pages 270-276

Anti-diabetic and anti-obesity agent sodium tungstate enhances GCN pathway activation through Glc7p inhibition

Author keywords

Diabetes; Nutrient stress; Phosphatase; Translational control; Tungstate

Indexed keywords

ANTIDIABETIC AGENT; ANTIOBESITY AGENT; GLC7P PHOSPHATASE; HYDROLASE INHIBITOR; INITIATION FACTOR 2ALPHA; PHOSPHOPROTEIN PHOSPHATASE; TUNGSTATE SODIUM; UNCLASSIFIED DRUG;

EID: 84856221597     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2011.12.035     Document Type: Article
Times cited : (7)

References (68)
  • 1
    • 0001598487 scopus 로고    scopus 로고
    • Characterization of a mammalian homolog of the GCN2 eukaryotic initiation factor 2α kinase
    • DOI 10.1046/j.1432-1327.1999.00780.x
    • J.J. Berlanga, J. Santoyo, and C. De Haro Characterization of a mammalian homolog of the GCN2 eukaryotic initiation factor 2alpha kinase Eur. J. Biochem. 265 1999 754 762 (Pubitemid 29489008)
    • (1999) European Journal of Biochemistry , vol.265 , Issue.2 , pp. 754-762
    • Berlanga, J.J.1    Santoyo, J.2    De Haro, C.3
  • 2
    • 0030803256 scopus 로고    scopus 로고
    • Translational regulation of yeast GCN4: A window on factors that control initiator-tRNA binding to the ribosome
    • DOI 10.1074/jbc.272.35.21661
    • A.G. Hinnebusch Translational regulation of yeast GCN4. A window on factors that control initiator-tRNA binding to the ribosome J. Biol. Chem. 272 1997 21661 21664 (Pubitemid 27382774)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.35 , pp. 21661-21664
    • Hinnebusch, A.G.1
  • 3
    • 0034973590 scopus 로고    scopus 로고
    • Transcriptional profiling shows that Gcn4p is a master regulator of gene expression during amino acid starvation in yeast
    • DOI 10.1128/MCB.21.13.4347-4368.2001
    • K. Natarajan, M.R. Meyer, B.M. Jackson, D. Slade, C. Roberts, A.G. Hinnebusch, and M.J. Marton Transcriptional profiling shows that Gcn4p is a master regulator of gene expression during amino acid starvation in yeast Mol. Cell. Biol. 21 2001 4347 4368 (Pubitemid 32565316)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.13 , pp. 4347-4368
    • Natarajan, K.1    Meyer, M.R.2    Jackson, B.M.3    Slade, D.4    Roberts, C.5    Hinnebusch, A.G.6    Marton, M.J.7
  • 4
    • 0034078320 scopus 로고    scopus 로고
    • FK506, an immunosuppressant targeting calcineurin function
    • F.J. Dumont FK506, an immunosuppressant targeting calcineurin function Curr. Med. Chem. 7 2000 731 748 (Pubitemid 30366639)
    • (2000) Current Medicinal Chemistry , vol.7 , Issue.7 , pp. 731-748
    • Dumont, F.J.1
  • 6
    • 0027959012 scopus 로고
    • Two FK506 resistance-conferring genes in Saccharomyces cerevisiae, TAT1 and TAT2, encode amino acid permeases mediating tyrosine and tryptophan uptake
    • A. Schmidt, M.N. Hall, and A. Koller Two FK506 resistance-conferring genes in Saccharomyces cerevisiae, TAT1 and TAT2, encode amino acid permeases mediating tyrosine and tryptophan uptake Mol. Cell. Biol. 14 1994 6597 6606 (Pubitemid 24299728)
    • (1994) Molecular and Cellular Biology , vol.14 , Issue.10 , pp. 6597-6606
    • Schmidt, A.1    Hall, M.N.2    Koller, A.3
  • 9
    • 0027171069 scopus 로고
    • Translation of the yeast transcriptional activator GCN4 is stimulated by purine limitation: Implications for activation of the protein kinase GCN2
    • R.J. Rolfes, and A.G. Hinnebusch Translation of the yeast transcriptional activator GCN4 is stimulated by purine limitation: implications for activation of the protein kinase GCN2 Mol. Cell. Biol. 13 1993 5099 5111 (Pubitemid 23220411)
    • (1993) Molecular and Cellular Biology , vol.13 , Issue.8 , pp. 5099-5111
    • Rolfes, R.J.1    Hinnebusch, A.G.2
  • 10
    • 0034028905 scopus 로고    scopus 로고
    • Glucose limitation induces GCN4 translation by activation of Gcn2 protein kinase
    • DOI 10.1128/MCB.20.8.2706-2717.2000
    • R. Yang, S.A. Wek, and R.C. Wek Glucose limitation induces GCN4 translation by activation of Gcn2 protein kinase Mol. Cell. Biol. 20 2000 2706 2717 (Pubitemid 30183489)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.8 , pp. 2706-2717
    • Yang, R.1    Wek, S.A.2    Wek, R.C.3
  • 11
  • 12
    • 2542489215 scopus 로고    scopus 로고
    • Dimerization is required for activation of eIF2 kinase Gcn2 in response to diverse environmental stress conditions
    • DOI 10.1074/jbc.M402228200
    • J. Narasimhan, K.A. Staschke, and R.C. Wek Dimerization is required for activation of eIF2 kinase Gcn2 in response to diverse environmental stress conditions J. Biol. Chem. 279 2004 22820 22832 (Pubitemid 38685582)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.22 , pp. 22820-22832
    • Narasimhan, J.1    Staschke, K.A.2    Wek, R.C.3
  • 13
    • 0037382865 scopus 로고    scopus 로고
    • Translational control by TOR and TAP42 through dephosphorylation of eIF2α kinase GCN2
    • DOI 10.1101/gad.1069003
    • V.A. Cherkasova, and A.G. Hinnebusch Translational control by TOR and TAP42 through dephosphorylation of eIF2alpha kinase GCN2 Genes Dev. 17 2003 859 872 (Pubitemid 36397374)
    • (2003) Genes and Development , vol.17 , Issue.7 , pp. 859-872
    • Cherkasova, V.A.1    Hinnebusch, A.G.2
  • 14
    • 0037743691 scopus 로고    scopus 로고
    • Rapamycin-induced translational derepression of GCN4 mRNA involves a novel mechanism for activation of the eIF2α kinase GCN2
    • DOI 10.1074/jbc.C300133200
    • H. Kubota, T. Obata, K. Ota, T. Sasaki, and T. Ito Rapamycin-induced translational derepression of GCN4 mRNA involves a novel mechanism for activation of the eIF2 alpha kinase GCN2 J. Biol. Chem. 278 2003 20457 20460 (Pubitemid 36806341)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.23 , pp. 20457-20460
    • Kubota, H.1    Obata, T.2    Ota, K.3    Sasaki, T.4    Ito, T.5
  • 15
    • 0035078505 scopus 로고    scopus 로고
    • TOR modulates GCN4-dependent expression of genes turned on by nitrogen limitation
    • DOI 10.1128/JB.183.7.2331-2334.2001
    • L. Valenzuela, C. Aranda, and A. Gonzalez TOR modulates GCN4-dependent expression of genes turned on by nitrogen limitation J. Bacteriol. 183 2001 2331 2334 (Pubitemid 32240404)
    • (2001) Journal of Bacteriology , vol.183 , Issue.7 , pp. 2331-2334
    • Valenzuela, L.1    Aranda, C.2    Gonzalez, A.3
  • 16
    • 23044493412 scopus 로고    scopus 로고
    • Inhibition of translation initiation by volatile anesthetics involves nutrient-sensitive GCN-independent and -dependent processes in yeast
    • DOI 10.1091/mbc.E05-02-0127
    • L.K. Palmer, J.L. Shoemaker, B.A. Baptiste, D. Wolfe, and R.L. Keil Inhibition of translation initiation by volatile anesthetics involves nutrient-sensitive GCN-independent and -dependent processes in yeast Mol. Biol. Cell 16 2005 3727 3739 (Pubitemid 41077082)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.8 , pp. 3727-3739
    • Palmer, L.K.1    Shoemaker, J.L.2    Baptiste, B.A.3    Wolfe, D.4    Keil, R.L.5
  • 18
    • 0015288961 scopus 로고
    • Infancy-onset diabetes mellitus and multiple epiphyseal dysplasia
    • C.D. Wolcott, and M.L. Rallison Infancy-onset diabetes mellitus and multiple epiphyseal dysplasia J. Pediatr. 80 1972 292 297
    • (1972) J. Pediatr. , vol.80 , pp. 292-297
    • Wolcott, C.D.1    Rallison, M.L.2
  • 19
    • 0020030070 scopus 로고
    • Wolcott-Rallison syndrome: Diabetes mellitus and spondyloepiphyseal dysplasia
    • DOI 10.1007/BF00441137
    • H. Stoss, H.J. Pesch, B. Pontz, A. Otten, and J. Spranger Wolcott-Rallison syndrome: diabetes mellitus and spondyloepiphyseal dysplasia Eur. J. Pediatr. 138 1982 120 129 (Pubitemid 12141763)
    • (1982) European Journal of Pediatrics , vol.138 , Issue.2 , pp. 120-129
    • Stoss, H.1    Pesch, H.J.2    Pontz, B.3
  • 20
    • 0034425698 scopus 로고    scopus 로고
    • EIF2AK3, encoding translation initiation factor 2-α kinase 3, is mutated in patients with Wolcott-Rallison syndrome
    • DOI 10.1038/78085
    • M. Delepine, M. Nicolino, T. Barrett, M. Golamaully, G.M. Lathrop, and C. Julier EIF2AK3, encoding translation initiation factor 2-alpha kinase 3, is mutated in patients with Wolcott-Rallison syndrome Nat. Genet. 25 2000 406 409 (Pubitemid 32983431)
    • (2000) Nature Genetics , vol.25 , Issue.4 , pp. 406-409
    • Delepine, M.1    Nicolino, M.2    Barrett, T.3    Golamaully, M.4    Mark Lathrop, G.5    Julier, C.6
  • 21
    • 0034968330 scopus 로고    scopus 로고
    • Diabetes mellitus and exocrine pancreatic dysfunction in Perk-/- mice reveals a role for translational control in secretory cell survival
    • DOI 10.1016/S1097-2765(01)00264-7
    • H.P. Harding, H. Zeng, Y. Zhang, R. Jungries, P. Chung, H. Plesken, D.D. Sabatini, and D. Ron Diabetes mellitus and exocrine pancreatic dysfunction in perk-/- mice reveals a role for translational control in secretory cell survival Mol. Cell 7 2001 1153 1163 (Pubitemid 32607350)
    • (2001) Molecular Cell , vol.7 , Issue.6 , pp. 1153-1163
    • Harding, H.P.1    Zeng, H.2    Zhang, Y.3    Jungries, R.4    Chung, P.5    Plesken, H.6    Sabatini, D.D.7    Ron, D.8
  • 24
    • 10344222124 scopus 로고    scopus 로고
    • The role of the unfolded protein response in tumour development: Friend or foe?
    • DOI 10.1038/nrc1505
    • Y. Ma, and L.M. Hendershot The role of the unfolded protein response in tumour development: friend or foe? Nat. Rev. Cancer 4 2004 966 977 (Pubitemid 39626220)
    • (2004) Nature Reviews Cancer , vol.4 , Issue.12 , pp. 966-977
    • Ma, Y.1    Hendershot, L.M.2
  • 25
    • 72449160579 scopus 로고    scopus 로고
    • The unfolded protein response and its relevance to connective tissue diseases
    • R.P. Boot-Handford, and M.D. Briggs The unfolded protein response and its relevance to connective tissue diseases Cell Tissue Res 339 2010 197 211
    • (2010) Cell Tissue Res , vol.339 , pp. 197-211
    • Boot-Handford, R.P.1    Briggs, M.D.2
  • 26
    • 74849136799 scopus 로고    scopus 로고
    • Role of ATF4 in regulation of autophagy and resistance to drugs and hypoxia
    • T. Rzymski, M. Milani, D.C. Singleton, and A.L. Harris Role of ATF4 in regulation of autophagy and resistance to drugs and hypoxia Cell Cycle 8 2009 3838 3847
    • (2009) Cell Cycle , vol.8 , pp. 3838-3847
    • Rzymski, T.1    Milani, M.2    Singleton, D.C.3    Harris, A.L.4
  • 27
    • 67349155932 scopus 로고    scopus 로고
    • Cellular stress/the unfolded protein response: Relevance to sleep and sleep disorders
    • N. Naidoo Cellular stress/the unfolded protein response: relevance to sleep and sleep disorders Sleep Med. Rev. 13 2009 195 204
    • (2009) Sleep Med. Rev. , vol.13 , pp. 195-204
    • Naidoo, N.1
  • 28
    • 0026490040 scopus 로고
    • Truncated protein phosphatase GLC7 restores translational activation of GCN4 expression in yeast mutants defective for the eIF-2 alpha kinase GCN2
    • R.C. Wek, J.F. Cannon, T.E. Dever, and A.G. Hinnebusch Truncated protein phosphatase GLC7 restores translational activation of GCN4 expression in yeast mutants defective for the eIF-2 alpha kinase GCN2 Mol. Cell. Biol. 12 1992 5700 5710
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 5700-5710
    • Wek, R.C.1    Cannon, J.F.2    Dever, T.E.3    Hinnebusch, A.G.4
  • 30
  • 31
    • 0028040192 scopus 로고
    • Characterization of glycogen-deficient glc mutants of Saccharomyces cerevisiae
    • J.F. Cannon, J.R. Pringle, A. Fiechter, and M. Khalil Characterization of glycogen-deficient glc mutants of Saccharomyces cerevisiae Genetics 136 1994 485 503 (Pubitemid 24045472)
    • (1994) Genetics , vol.136 , Issue.2 , pp. 485-503
    • Cannon, J.F.1    Pringle, J.R.2    Fiechter, A.3    Khalil, M.4
  • 32
    • 0028102286 scopus 로고
    • The GLC7 type 1 protein phosphatase is required for glucose repression in Saccharomyces cerevisiae
    • J. Tu, and M. Carlson The GLC7 type 1 protein phosphatase is required for glucose repression in Saccharomyces cerevisiae Mol. Cell. Biol. 14 1994 6789 6796 (Pubitemid 24299748)
    • (1994) Molecular and Cellular Biology , vol.14 , Issue.10 , pp. 6789-6796
    • Tu, J.1    Carlson, M.2
  • 33
    • 0036242694 scopus 로고    scopus 로고
    • Protein phosphatase type 1 regulates ion homeostasis in Saccharomyces cerevisiae
    • T. Williams-Hart, X. Wu, and K. Tatchell Protein phosphatase type 1 regulates ion homeostasis in Saccharomyces cerevisiae Genetics 160 2002 1423 1437 (Pubitemid 34454366)
    • (2002) Genetics , vol.160 , Issue.4 , pp. 1423-1437
    • Williams-Hart, T.1    Wu, X.2    Tatchell, K.3
  • 34
    • 73549116091 scopus 로고    scopus 로고
    • Dephosphorylation of gamma H2A by Glc7/protein phosphatase 1 promotes recovery from inhibition of DNA replication
    • M. Bazzi, D. Mantiero, C. Trovesi, G. Lucchini, and M.P. Longhese Dephosphorylation of gamma H2A by Glc7/protein phosphatase 1 promotes recovery from inhibition of DNA replication Mol. Cell Biol 30 2010 131 145
    • (2010) Mol. Cell Biol , vol.30 , pp. 131-145
    • Bazzi, M.1    Mantiero, D.2    Trovesi, C.3    Lucchini, G.4    Longhese, M.P.5
  • 35
    • 0346728803 scopus 로고    scopus 로고
    • Functional Diversity of Protein Phosphatase-1, a Cellular Economizer and Reset Button
    • DOI 10.1152/physrev.00013.2003
    • H. Ceulemans, and M. Bollen Functional diversity of protein phosphatase-1, a cellular economizer and reset button Physiol. Rev. 84 2004 1 39 (Pubitemid 38049874)
    • (2004) Physiological Reviews , vol.84 , Issue.1 , pp. 1-39
    • Ceulemans, H.1    Bollen, M.2
  • 36
    • 0029583122 scopus 로고
    • Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate
    • DOI 10.1006/jmbi.1995.0667
    • M.P. Egloff, P.T. Cohen, P. Reinemer, and D. Barford Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate J. Mol. Biol. 254 1995 942 959 (Pubitemid 26006861)
    • (1995) Journal of Molecular Biology , vol.254 , Issue.5 , pp. 942-959
    • Egloff, M.-P.1    Cohen, P.T.W.2    Reinemer, P.3    Barford, D.4
  • 37
    • 0029780526 scopus 로고    scopus 로고
    • The x-ray crystal structures of Yersinia tyrosine phosphatase with bound tungstate and nitrate. Mechanistic implications
    • DOI 10.1074/jbc.271.31.18780
    • E.B. Fauman, C. Yuvaniyama, H.L. Schubert, J.A. Stuckey, and M.A. Saper The X-ray crystal structures of Yersinia tyrosine phosphatase with bound tungstate and nitrate. Mechanistic implications J. Biol. Chem. 271 1996 18780 18788 (Pubitemid 26322747)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.31 , pp. 18780-18788
    • Fauman, E.B.1    Yuvaniyama, C.2    Schubert, H.L.3    Stuckey, J.A.4    Saper, M.A.5
  • 39
    • 0028122711 scopus 로고
    • Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 A and the complex with tungstate
    • DOI 10.1038/370571a0
    • J.A. Stuckey, H.L. Schubert, E.B. Fauman, Z.Y. Zhang, J.E. Dixon, and M.A. Saper Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 A and the complex with tungstate Nature 370 1994 571 575 (Pubitemid 24264925)
    • (1994) Nature , vol.370 , Issue.6490 , pp. 571-575
    • Stuckey, J.A.1    Schubert, H.L.2    Fauman, E.B.3    Zhang, Z.-Y.4    Dixon, J.E.5    Saper, M.A.6
  • 40
    • 0036693750 scopus 로고    scopus 로고
    • Vanadium and tungsten derivatives as antidiabetic agents: A Review of Their Toxic Effects
    • J.L. Domingo Vanadium and tungsten derivatives as antidiabetic agents: a review of their toxic effects Biol. Trace Elem. Res. 88 2002 97 112 (Pubitemid 35034421)
    • (2002) Biological Trace Element Research , vol.88 , Issue.2 , pp. 97-112
    • Domingo, J.L.1
  • 41
    • 0035061253 scopus 로고    scopus 로고
    • Tungstate is an effective antidiabetic agent in streptozotocin-induced diabetic rats: A long-term study
    • DOI 10.1007/s001250100479
    • A. Barbera, R.R. Gomis, N. Prats, J.E. Rodriguez-Gil, M. Domingo, R. Gomis, and J.J. Guinovart Tungstate is an effective antidiabetic agent in streptozotocin-induced diabetic rats: a long-term study Diabetologia 44 2001 507 513 (Pubitemid 32324363)
    • (2001) Diabetologia , vol.44 , Issue.4 , pp. 507-513
    • Barbera, A.1    Gomis, R.R.2    Prats, N.3    Rodriguez-Gil, J.E.4    Domingo, M.5    Gomis, R.6    Guinovart, J.J.7
  • 42
    • 0031019298 scopus 로고    scopus 로고
    • Effects of tungstate in neonatally streptozotocin-induced diabetic rats: Mechanism leading to normalization of glycaemia
    • DOI 10.1007/s001250050655
    • A. Barbera, J. Fernandez-Alvarez, A. Truc, R. Gomis, and J.J. Guinovart Effects of tungstate in neonatally streptozotocin-induced diabetic rats: mechanism leading to normalization of glycaemia Diabetologia 40 1997 143 149 (Pubitemid 27060285)
    • (1997) Diabetologia , vol.40 , Issue.2 , pp. 143-149
    • Barbera, A.1    Fernandez-Alvarez, J.2    Truc, A.3    Gomis, R.4    Guinovart, J.J.5
  • 43
    • 0028128179 scopus 로고
    • Insulin-like actions of tungstate in diabetic rats. Normalization of hepatic glucose metabolism
    • A. Barbera, J.E. Rodriguez-Gil, and J.J. Guinovart Insulin-like actions of tungstate in diabetic rats. Normalization of hepatic glucose metabolism J. Biol. Chem. 269 1994 20047 20053
    • (1994) J. Biol. Chem. , vol.269 , pp. 20047-20053
    • Barbera, A.1    Rodriguez-Gil, J.E.2    Guinovart, J.J.3
  • 44
    • 0035149832 scopus 로고    scopus 로고
    • Effects of tungstate, a new potential oral antidiabetic agent, in Zucker diabetic fatty rats
    • M.C. Munoz, A. Barbera, J. Dominguez, J. Fernandez-Alvarez, R. Gomis, and J.J. Guinovart Effects of tungstate, a new potential oral antidiabetic agent, in Zucker diabetic fatty rats Diabetes 50 2001 131 138 (Pubitemid 32047991)
    • (2001) Diabetes , vol.50 , Issue.1 , pp. 131-138
    • Munoz, M.C.1    Barbera, A.2    Dominguez, J.3    Fernandez-Alvarez, J.4    Gomis, R.5    Guinovart, J.J.6
  • 45
    • 0038743115 scopus 로고    scopus 로고
    • Modulation of glucose transporters in rat diaphragm by sodium tungstate
    • DOI 10.1016/S0014-5793(03)00352-1
    • M.D. Giron, J.J. Caballero, A.M. Vargas, M.D. Suarez, J.J. Guinovart, and R. Salto Modulation of glucose transporters in rat diaphragm by sodium tungstate FEBS Lett. 542 2003 84 88 (Pubitemid 36555719)
    • (2003) FEBS Letters , vol.542 , Issue.1-3 , pp. 84-88
    • Giron, M.D.1    Caballero, J.J.2    Vargas, A.M.3    Suarez, M.D.4    Guinovart, J.J.5    Salto, R.6
  • 46
    • 0343090412 scopus 로고    scopus 로고
    • Effects of sodium tungstate on insulin and glucagon secretion in the perfused rat pancreas
    • DOI 10.1016/S0014-2999(00)00492-1, PII S0014299900004921
    • J. Rodriguez-Gallardo, R.A. Silvestre, E.M. Egido, and J. Marco Effects of sodium tungstate on insulin and glucagon secretion in the perfused rat pancreas Eur. J. Pharmacol. 402 2000 199 204 (Pubitemid 30625327)
    • (2000) European Journal of Pharmacology , vol.402 , Issue.1-2 , pp. 199-204
    • Rodriguez-Gallardo, J.1    Silvestre, R.A.2    Egido, E.M.3    Marco, J.4
  • 47
    • 24944511514 scopus 로고    scopus 로고
    • Tungstate decreases weight gain and adiposity in obese rats through increased thermogenesis and lipid oxidation
    • DOI 10.1210/en.2005-0385
    • M. Claret, H. Corominola, I. Canals, J. Saura, S. Barcelo-Batllori, J.J. Guinovart, and R. Gomis Tungstate decreases weight gain and adiposity in obese rats through increased thermogenesis and lipid oxidation Endocrinology 146 2005 4362 4369 (Pubitemid 41324032)
    • (2005) Endocrinology , vol.146 , Issue.10 , pp. 4362-4369
    • Claret, M.1    Corominola, H.2    Canals, I.3    Saura, J.4    Barcelo-Batllori, S.5    Guinovart, J.J.6    Gomis, R.7
  • 48
    • 0028954118 scopus 로고
    • Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure
    • R.D. Gietz, R.H. Schiestl, A.R. Willems, and R.A. Woods Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure Yeast 11 1995 355 360
    • (1995) Yeast , vol.11 , pp. 355-360
    • Gietz, R.D.1    Schiestl, R.H.2    Willems, A.R.3    Woods, R.A.4
  • 49
    • 0032169651 scopus 로고    scopus 로고
    • Mutations in the yeast Myb-like protein Bas1p resulting in discrimination between promoters in vivo but not in vitro
    • B. Pinson, I. Sagot, F. Borne, O.S. Gabrielsen, and B. Daignan-Fornier Mutations in the yeast Myb-like protein Bas1p resulting in discrimination between promoters in vivo but not in vitro Nucleic Acids Res. 26 1998 3977 3985 (Pubitemid 28401350)
    • (1998) Nucleic Acids Research , vol.26 , Issue.17 , pp. 3977-3985
    • Pinson, B.1    Sagot, I.2    Borne, F.3    Gabrielsen, O.S.4    Daignan-Fornier, B.5
  • 51
    • 0026731477 scopus 로고
    • A novel and conserved salt-induced protein is an important determinant of salt tolerance in yeast
    • R. Gaxiola, I.F. de Larrinoa, J.M. Villalba, and R. Serrano A novel and conserved salt-induced protein is an important determinant of salt tolerance in yeast EMBO J. 11 1992 3157 3164
    • (1992) EMBO J. , vol.11 , pp. 3157-3164
    • Gaxiola, R.1    De Larrinoa, I.F.2    Villalba, J.M.3    Serrano, R.4
  • 52
    • 0021154718 scopus 로고
    • Isolation and characterization of rabbit skeletal muscle protein phosphatase C-I and C-II
    • S.R. Silberman, M. Speth, R. Nemani, M.K. Ganapathi, V. Dombradi, H. Paris, and E.Y. Lee Isolation and characterization of rabbit skeletal muscle protein phosphatases C-I and C-II J. Biol. Chem. 259 1984 2913 2922 (Pubitemid 14127925)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.5 , pp. 2913-2922
    • Silberman, S.R.1    Speth, M.2    Nemani, R.3
  • 53
    • 0029166109 scopus 로고
    • Regulation of cation transport in Saccharomyces cerevisiae by the salt tolerance gene HAL3
    • A. Ferrando, S.J. Kron, G. Rios, G.R. Fink, and R. Serrano Regulation of cation transport in Saccharomyces cerevisiae by the salt tolerance gene HAL3 Mol. Cell. Biol. 15 1995 5470 5481
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5470-5481
    • Ferrando, A.1    Kron, S.J.2    Rios, G.3    Fink, G.R.4    Serrano, R.5
  • 54
    • 0035877696 scopus 로고    scopus 로고
    • Characterization of the Net1 cell cycle-dependent regulator of the Cdc14 phosphatase from budding yeast
    • E.E. Traverso, C. Baskerville, Y. Liu, W. Shou, P. James, R.J. Deshaies, and H. Charbonneau Characterization of the Net1 cell cycle-dependent regulator of the Cdc14 phosphatase from budding yeast J. Biol. Chem. 276 2001 21924 21931
    • (2001) J. Biol. Chem. , vol.276 , pp. 21924-21931
    • Traverso, E.E.1    Baskerville, C.2    Liu, Y.3    Shou, W.4    James, P.5    Deshaies, R.J.6    Charbonneau, H.7
  • 55
    • 0029079061 scopus 로고
    • Insulin-like action of chromate on glucose transport in isolated rat adipocytes
    • Y. Goto, and K. Kida Insulin-like action of chromate on glucose transport in isolated rat adipocytes Jpn. J. Pharmacol. 67 1995 365 368
    • (1995) Jpn. J. Pharmacol. , vol.67 , pp. 365-368
    • Goto, Y.1    Kida, K.2
  • 56
    • 0028990111 scopus 로고
    • Permolybdate and pertungstate - Potent stimulators of insulin effects in rat adipocytes: Mechanism of action
    • J. Li, G. Elberg, D. Gefel, and Y. Shechter Permolybdate and pertungstate - potent stimulators of insulin effects in rat adipocytes: mechanism of action Biochemistry 34 1995 6218 6225
    • (1995) Biochemistry , vol.34 , pp. 6218-6225
    • Li, J.1    Elberg, G.2    Gefel, D.3    Shechter, Y.4
  • 57
    • 27744521467 scopus 로고    scopus 로고
    • Tungstate stimulates insulin release and inhibits somatostatin output in the perfused rat pancreas
    • DOI 10.1016/j.ejphar.2005.06.028, PII S0014299905006849
    • R.A. Silvestre, E.M. Egido, R. Hernandez, and J. Marco Tungstate stimulates insulin release and inhibits somatostatin output in the perfused rat pancreas Eur. J. Pharmacol. 519 2005 127 134 (Pubitemid 43181175)
    • (2005) European Journal of Pharmacology , vol.519 , Issue.1-2 , pp. 127-134
    • Silvestre, R.A.1    Egido, E.M.2    Hernandez, R.3    Marco, J.4
  • 58
    • 1842866390 scopus 로고    scopus 로고
    • Stable and functional regeneration of pancreatic beta-cell population in nSTZ-rats treated with tungstate
    • DOI 10.1007/s00125-004-1332-8
    • J. Fernandez-Alvarez, A. Barbera, B. Nadal, S. Barcelo-Batllori, S. Piquer, M. Claret, J.J. Guinovart, and R. Gomis Stable and functional regeneration of pancreatic beta-cell population in nSTZ-rats treated with tungstate Diabetologia 47 2004 470 477 (Pubitemid 38491243)
    • (2004) Diabetologia , vol.47 , Issue.3 , pp. 470-477
    • Fernandez-Alvarez, J.1    Barbera, A.2    Nadal, B.3    Barcelo-Batllori, S.4    Piquer, S.5    Claret, M.6    Guinovart, J.J.7    Gomis, R.8
  • 59
    • 22344455195 scopus 로고    scopus 로고
    • Oral administration of sodium tungstate improves cardiac performance in streptozotocin-induced diabetic rats
    • DOI 10.1139/y05-026
    • P.R. Nagareddy, H. Vasudevan, and J.H. McNeill Oral administration of sodium tungstate improves cardiac performance in streptozotocin-induced diabetic rats Can. J. Physiol. Pharmacol. 83 2005 405 411 (Pubitemid 41003315)
    • (2005) Canadian Journal of Physiology and Pharmacology , vol.83 , Issue.5 , pp. 405-411
    • Nagareddy, P.R.1    Vasudevan, H.2    McNeill, J.H.3
  • 61
    • 77955581739 scopus 로고    scopus 로고
    • Sodium tungstate attenuate oxidative stress in brain tissue of streptozotocin-induced diabetic rats
    • A. Nakhaee, M. Bokaeian, A. Akbarzadeh, and M. Hashemi Sodium tungstate attenuate oxidative stress in brain tissue of streptozotocin-induced diabetic rats Biol Trace Elem Res 136 2009 221 231
    • (2009) Biol Trace Elem Res , vol.136 , pp. 221-231
    • Nakhaee, A.1    Bokaeian, M.2    Akbarzadeh, A.3    Hashemi, M.4
  • 62
    • 0024592297 scopus 로고
    • Effects of the tumour promoter okadaic acid on intracellular protein phosphorylation and metabolism
    • DOI 10.1038/337078a0
    • T.A. Haystead, A.T. Sim, D. Carling, R.C. Honnor, Y. Tsukitani, P. Cohen, and D.G. Hardie Effects of the tumour promoter okadaic acid on intracellular protein phosphorylation and metabolism Nature 337 1989 78 81 (Pubitemid 19022553)
    • (1989) Nature , vol.337 , Issue.6202 , pp. 78-81
    • Haystead, T.A.J.1    Sim, A.T.R.2    Carling, D.3    Honnor, R.C.4    Tsukitani, Y.5    Cohen, P.6    Hardie, D.G.7
  • 63
    • 0025851632 scopus 로고
    • The specific protein phosphatase inhibitor okadaic acid differentially modulates insulin action
    • S.L. Hess, C.R. Suchin, and A.R. Saltiel The specific protein phosphatase inhibitor okadaic acid differentially modulates insulin action J. Cell. Biochem. 45 1991 374 380
    • (1991) J. Cell. Biochem. , vol.45 , pp. 374-380
    • Hess, S.L.1    Suchin, C.R.2    Saltiel, A.R.3
  • 64
    • 17144389838 scopus 로고    scopus 로고
    • Phosphorylation of the α-subunit of the eukaryotic initiation factor-2 (eIF2α) reduces protein synthesis and enhances apoptosis in response to proteasome inhibition
    • DOI 10.1074/jbc.M413660200
    • H.Y. Jiang, and R.C. Wek Phosphorylation of the alpha-subunit of the eukaryotic initiation factor-2 (eIF2alpha) reduces protein synthesis and enhances apoptosis in response to proteasome inhibition J. Biol. Chem. 280 2005 14189 14202 (Pubitemid 40517321)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.14 , pp. 14189-14202
    • Jiang, H.-Y.1    Wek, R.C.2
  • 65
    • 1342304043 scopus 로고    scopus 로고
    • Defects in Translational Regulation Mediated by the α Subunit of Eukaryotic Initiation Factor 2 Inhibit Antiviral Activity and Facilitate the Malignant Transformation of Human Fibroblasts
    • DOI 10.1128/MCB.24.5.2025-2040.2004
    • D.J. Perkins, and G.N. Barber Defects in translational regulation mediated by the alpha subunit of eukaryotic initiation factor 2 inhibit antiviral activity and facilitate the malignant transformation of human fibroblasts Mol. Cell. Biol. 24 2004 2025 2040 (Pubitemid 38248942)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.5 , pp. 2025-2040
    • Perkins, D.J.1    Barber, G.N.2
  • 66
    • 0348133608 scopus 로고    scopus 로고
    • RNA sensors: Novel regulators of gene expression
    • DOI 10.1038/sj.embor.7400005
    • R. Kaempfer RNA sensors: novel regulators of gene expression EMBO Rep. 4 2003 1043 1047 (Pubitemid 37527421)
    • (2003) EMBO Reports , vol.4 , Issue.11 , pp. 1043-1047
    • Kaempfer, R.1
  • 68
    • 48549090526 scopus 로고    scopus 로고
    • Aging impairs the unfolded protein response to sleep deprivation and leads to proapoptotic signaling
    • N. Naidoo, M. Ferber, M. Master, Y. Zhu, and A.I. Pack Aging impairs the unfolded protein response to sleep deprivation and leads to proapoptotic signaling J. Neurosci. 28 2008 6539 6548
    • (2008) J. Neurosci. , vol.28 , pp. 6539-6548
    • Naidoo, N.1    Ferber, M.2    Master, M.3    Zhu, Y.4    Pack, A.I.5


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