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Volumn 215, Issue 3, 2012, Pages 543-551

Glycogen synthase kinase-3: Cryoprotection and glycogen metabolism in the freezetolerant wood frog

Author keywords

Cryoprotectant; Freeze tolerance; Glucose; Glycogen synthase kinase 3 (GSK 3); Protein phosphorylation; Rana sylvatica

Indexed keywords

ADENOSINE PHOSPHATE; GLUCOSE; GLYCOGEN; GLYCOGEN SYNTHASE KINASE 3; PHOSPHOENOLPYRUVATE;

EID: 84856597933     PISSN: 00220949     EISSN: None     Source Type: Journal    
DOI: 10.1242/jeb.065961     Document Type: Article
Times cited : (25)

References (51)
  • 1
    • 0035413614 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3: Properties, functions, and regulation
    • DOI 10.1021/cr000110o
    • Ali, A., Hoeflich, K. P. and Woodgett, J. R. (2001). Glycogen synthase kinase-3: Properties, functions, and regulation. Chem. Rev. 101, 2527-2540. (Pubitemid 35373033)
    • (2001) Chemical Reviews , vol.101 , Issue.8 , pp. 2527-2540
    • Ali, A.1    Hoeflich, K.P.2    Woodgett, J.R.3
  • 2
    • 0037677332 scopus 로고    scopus 로고
    • Determination of a large number of kinase activities using peptide substrates, P81 phosphocellulose paper arrays and phosphor imaging
    • DOI 10.1016/S0003-2697(03)00282-3
    • Asensio, C. J. A. and Garcia, R. C. (2003). Determination of a large number of kinase activities using peptide substrates, P81 phosphocellulose paper arrays, and phosphor imaging. Anal. Biochem. 319, 21-33. (Pubitemid 36802139)
    • (2003) Analytical Biochemistry , vol.319 , Issue.1 , pp. 21-33
    • Asensio, C.J.A.1    Garcia, R.C.2
  • 3
    • 0030890234 scopus 로고    scopus 로고
    • Nuclear export of NF-ATc enhanced by glycogen synthase kinase-3
    • DOI 10.1126/science.275.5308.1930
    • Beals, C. A., Sheridan, C. M., Turck, C. W., Gardner, P. and Crabtree, G. R. (1997). Nuclear export of NF-ATc enhanced by glycogen synthase kinase-3. Science 275, 1930-1933. (Pubitemid 27148814)
    • (1997) Science , vol.275 , Issue.5308 , pp. 1930-1933
    • Beals, C.R.1    Sheridan, C.M.2    Turck, C.W.3    Gardner, P.4    Crabtree, G.R.5
  • 4
    • 0017184389 scopus 로고
    • Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976). Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0027092553 scopus 로고
    • A simple computer program with statistical tests for the analysis of enzyme kinetics
    • Brooks, S. P. J. (1992). A simple computer program for the analysis of enzyme kinetics. Biotechniques 13, 906-911. (Pubitemid 23005244)
    • (1992) BioTechniques , vol.13 , Issue.6 , pp. 906-911
    • Brooks, S.P.J.1
  • 7
    • 0031767845 scopus 로고    scopus 로고
    • Freeze tolerance in the wood frog Rana sylvatica is associated with unusual structural features in insulin but not in glucagon
    • Conlon, J. M., Yano, K., Chartrel, N., Vaudry, H. and Storey, K. B. (1998). Freeze tolerance in the wood frog Rana sylvatica is associated with unusual structural features in insulin but not in glucagon. J. Mol. Endrocrinol. 21, 153-159. (Pubitemid 28557080)
    • (1998) Journal of Molecular Endocrinology , vol.21 , Issue.2 , pp. 153-159
    • Conlon, J.M.1    Yano, K.2    Chartrel, N.3    Vaudry, H.4    Storey, K.B.5
  • 8
    • 0023810629 scopus 로고
    • Electrophoretic analysis of liver glycogen phosphorylase activation in the freeze-tolerant wood frog
    • Crerar, M. M., David, E. S. and Storey, K. B. (1988). Electrophoretic analysis of liver glycogen phosphorylase activation in the freeze-tolerant wood frog. Biochim. Biophys. Acta 971, 72-84.
    • (1988) Biochim. Biophys. Acta , vol.971 , pp. 72-84
    • Crerar, M.M.1    David, E.S.2    Storey, K.B.3
  • 9
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • DOI 10.1038/378785a0
    • Cross, D. A., Alessi, D. R., Cohen, P., Andjelkovich, M. and Hemmings, B. A. (1995). Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature 378, 785-789. (Pubitemid 26004411)
    • (1995) Nature , vol.378 , Issue.6559 , pp. 785-789
    • Cross, D.A.E.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Hemmings, B.A.5
  • 10
    • 0025522071 scopus 로고
    • The molecular mechanism by which insulin stimulates glycogen synthesis in mammalian skeletal muscle
    • Dent, P., Lavoinne, A., Nakielny, S., Caudwell, F. B., Watt, P. and Cohen, P. (1990). The molecular mechanism by which insulin stimulates glycogen synthesis in mammalian skeletal muscle. Nature 348, 302-308. (Pubitemid 120029093)
    • (1990) Nature , vol.348 , Issue.6299 , pp. 302-308
    • Dent, P.1    Lavoinne, A.2    Nakielny, S.3    Caudwell, F.B.4    Watt, P.5    Cohen, P.6
  • 11
    • 43549104912 scopus 로고    scopus 로고
    • Regulation of 5α-adenosine monophosphate deaminase in the freeze tolerant wood frog, Rana sylvatica
    • Dieni, C. A. and Storey, K. B. (2008). Regulation of 5α-adenosine monophosphate deaminase in the freeze tolerant wood frog, Rana sylvatica. BMC Biochem. 9, 12.
    • (2008) BMC Biochem. , vol.9 , pp. 12
    • Dieni, C.A.1    Storey, K.B.2
  • 12
    • 60649107179 scopus 로고    scopus 로고
    • Creatine kinase regulation by reversible phosphorylation in frog muscle
    • Dieni, C. A. and Storey, K. B. (2009). Creatine kinase regulation by reversible phosphorylation in frog muscle. Comp. Biochem. Physiol. 152B, 405-412.
    • (2009) Comp. Biochem. Physiol. , vol.152 B , pp. 405-412
    • Dieni, C.A.1    Storey, K.B.2
  • 13
    • 77958491987 scopus 로고    scopus 로고
    • Regulation of glucose-6-phosphate dehydrogenase by reversible phosphorylation in liver of a freeze tolerant frog
    • Dieni, C. A. and Storey, K. B. (2010). Regulation of glucose-6-phosphate dehydrogenase by reversible phosphorylation in liver of a freeze tolerant frog. J. Comp. Physiol. B 180, 1133-1142.
    • (2010) J. Comp. Physiol. B , vol.180 , pp. 1133-1142
    • Dieni, C.A.1    Storey, K.B.2
  • 14
    • 79958822175 scopus 로고    scopus 로고
    • Regulation of hexokinase by reversible phosphorylation in skeletal muscle of a freeze-tolerant frog
    • Dieni, C. A. and Storey, K. B. (2011). Regulation of hexokinase by reversible phosphorylation in skeletal muscle of a freeze-tolerant frog. Comp. Biochem. Physiol. B 159, 236-243.
    • (2011) Comp. Biochem. Physiol. B , vol.159 , pp. 236-243
    • Dieni, C.A.1    Storey, K.B.2
  • 15
    • 0036629249 scopus 로고    scopus 로고
    • Wnt signal transduction: Kinase cogs in a nano-machine?
    • DOI 10.1016/S0968-0004(02)02137-0, PII S0968000402021370
    • Ding, Y. and Dale, T. (2002). Wnt signal transduction: Kinase cogs in a non-machine? Trends Biochem. Sci. 27, 327-329. (Pubitemid 34756510)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.7 , pp. 327-329
    • Ding, Y.1    Dale, T.2
  • 16
    • 0037383322 scopus 로고    scopus 로고
    • GSK-3: Tricks of the trade for a multi-tasking kinase
    • DOI 10.1242/jcs.00384
    • Doble, B. W. and Woodget, J. R. (2003). GSK-3: Tricks of the trade for a multi-tasking kinase. J. Cell Sci. 116, 1175-1186. (Pubitemid 36410657)
    • (2003) Journal of Cell Science , vol.116 , Issue.7 , pp. 1175-1186
    • Doble, B.W.1    Woodgett, J.R.2
  • 17
    • 0029152786 scopus 로고
    • Role of glycogen synthase kinase 3b as a negative regulator of dorsoventral axis formation in Xenopus embryos
    • Dominguez, I., Itoh, K. and Sokol, S. Y. (1995). Role of glycogen synthase kinase 3b as a negative regulator of dorsoventral axis formation in Xenopus embryos. Proc. Natl. Acad. Sci. USA 92, 8498-8502.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8498-8502
    • Dominguez, I.1    Itoh, K.2    Sokol, S.Y.3
  • 18
    • 0019026208 scopus 로고
    • Glycogen synthase kinase-3 from rabbit skeletal muscle. Separation from cyclic-AMP-dependent protein kinase and phosphorylase kinase
    • Embi, N., Rylatt, D. B. and Cohen, P. (1980). Glycogen synthase kinase-3 from rabbit skeletal muscle. Separation from cyclic-AMP-dependent protein kinase and phosphorylase kinase. Eur. J. Biochem. 107, 519-527.
    • (1980) Eur. J. Biochem. , vol.107 , pp. 519-527
    • Embi, N.1    Rylatt, D.B.2    Cohen, P.3
  • 19
    • 2942688147 scopus 로고    scopus 로고
    • Lkb1 and GSK3: Kinases at the center and poles of the action
    • Green, J. B. A. (2004). LKB1 and GSK-3b: Kinases at the center and poles of the action. Cell Cycle 3, 12-14. (Pubitemid 40268576)
    • (2004) Cell Cycle , vol.3 , Issue.1 , pp. 12-14
    • Green, J.B.A.1
  • 20
    • 0029156784 scopus 로고
    • Phosphorylation and inactivation of rat heart glycogen synthase by cAMP-dependent and cAMPindependent protein kinases
    • Grekinis, D., Reimann, E. M. and Schlender, K. K. (1995). Phosphorylation and inactivation of rat heart glycogen synthase by cAMP-dependent and cAMPindependent protein kinases. Int. J. Biochem. Cell Biol. 27, 565-573.
    • (1995) Int. J. Biochem. Cell Biol. , vol.27 , pp. 565-573
    • Grekinis, D.1    Reimann, E.M.2    Schlender, K.K.3
  • 21
    • 0035085644 scopus 로고    scopus 로고
    • Control of glycogen synthesis by glucose, glycogen, and insulin in cultured human muscle cells
    • Halse, R., Bonavaud, S. M., Armstrong, J. L., McCormack, J. G. and Yeaman, S. J. (2001). Control of glycogen synthesis by glucose, glycogen, and insulin in cultured human muscle cells. Diabetes 50, 720-726. (Pubitemid 32242626)
    • (2001) Diabetes , vol.50 , Issue.4 , pp. 720-726
    • Halse, R.1    Bonavaud, S.M.2    Armstrong, J.L.3    McCormack, J.G.4    Yeaman, S.J.5
  • 22
    • 0028649466 scopus 로고
    • Alterations in hepatic adrenergic receptor status in Rana sylvatica in response to freezing and thawing: Implications to the freeze-induced glycemic response
    • Hemmings, S. J. and Storey, K. B. (1994). Alterations in hepatic adrenergic receptor status in Rana sylvatica in response to freezing and thawing: Implications to the freeze-induced glycemic response. Can. J. Physiol. Pharmacol. 72, 1552-1560.
    • (1994) Can. J. Physiol. Pharmacol. , vol.72 , pp. 1552-1560
    • Hemmings, S.J.1    Storey, K.B.2
  • 23
    • 0034996273 scopus 로고    scopus 로고
    • Characterization of sarcolemma and sarcoplasmic reticulum isolated from skeletal muscle of the freeze-tolerant wood frog, Rana sylvatica: The b(2)-adrenergic receptor and calcium transport systems in control, frozen and thawed states
    • Hemmings, S. J. and Storey, K. B. (2001). Characterization of sarcolemma and sarcoplasmic reticulum isolated from skeletal muscle of the freeze-tolerant wood frog, Rana sylvatica: The b(2)-adrenergic receptor and calcium transport systems in control, frozen and thawed states. Cell. Biochem. Function 19, 142-152.
    • (2001) Cell. Biochem. Function , vol.19 , pp. 142-152
    • Hemmings, S.J.1    Storey, K.B.2
  • 24
    • 0020540151 scopus 로고
    • The protein phosphatases involved in cellular regulation: 1. Classification and substrate specificities
    • Ingebritsen, T. S. and Cohen, P. (1983). The protein phosphatases involved in cellular regulation: 1. Classification and substrate specificities. Eur. J. Biochem. 132, 255-261. (Pubitemid 13093422)
    • (1983) European Journal of Biochemistry , vol.132 , Issue.2 , pp. 255-261
    • Ingebritsen, T.S.1    Cohen, P.2
  • 25
    • 0026562948 scopus 로고
    • Glycogen phosphorylase: Control by phosphorylation and allosteric effectors
    • Johnson, L. N. (1992). Glycogen phosphorylase: Control by phosphorylation and allosteric effectors. FASEB J. 2, 2274-2282.
    • (1992) FASEB J. , vol.2 , pp. 2274-2282
    • Johnson, L.N.1
  • 26
  • 27
    • 33646077675 scopus 로고    scopus 로고
    • AMP-activated protein kinase (AMPK) activating agents cause dephosphorylation of Akt and glycogen synthase kinase-3
    • King, T. D., Song, L. and Jope, R. S. (2006). AMP-activated protein kinase (AMPK) activating agents cause dephosphorylation of Akt and glycogen synthase kinase-3. Biochem. Pharmacol. 71, 1637-1647.
    • (2006) Biochem. Pharmacol. , vol.71 , pp. 1637-1647
    • King, T.D.1    Song, L.2    Jope, R.S.3
  • 28
    • 0025244861 scopus 로고
    • Inoculation triggers freezing at high subzero temperatures in a freeze-tolerant frog (Rana sylvatica) and insect (Eurosta solidaginis)
    • Layne, J. R., Jr, Lee, R. E., Jr and Huang, J. L. (1990). Inoculation triggers freezing at high subzero temperatures in a freeze-tolerant frog (Rana sylvatica) and insect (Eurosta solidaginis). Can. J. Zool. 68, 506-510. (Pubitemid 20428185)
    • (1990) Canadian Journal of Zoology , vol.68 , Issue.3 , pp. 506-510
    • Layne Jr., J.R.1    Lee Jr., R.E.2    Huang, J.L.3
  • 29
    • 0033609812 scopus 로고    scopus 로고
    • Insulin and exercise decrease glycogen synthase kinase-3 activity by different mechanisms in rat skeletal muscle
    • Markuns, J. F., Wojtaszewski, J. F. P. and Goodyear, L. J. (1999). Insulin and exercise decrease glycogen synthase kinase-3 activity by different mechanisms in rat skeletal muscle. J. Biol. Chem. 274, 24896-24900.
    • (1999) J. Biol. Chem. , vol.274 , pp. 24896-24900
    • Markuns, J.F.1    Wojtaszewski, J.F.P.2    Goodyear, L.J.3
  • 30
    • 84856619287 scopus 로고    scopus 로고
    • Modulation of GSK-3 as a therapeutic strategy on Tau pathologies
    • Medina, M., Garrido, J. J. and Wandosell, F. G. (2011). Modulation of GSK-3 as a therapeutic strategy on Tau pathologies. Front. Mol. Neurosci. 4, 24.
    • (2011) Front. Mol. Neurosci. , vol.4 , pp. 24
    • Medina, M.1    Garrido, J.J.2    Wandosell, F.G.3
  • 31
    • 0026683691 scopus 로고
    • Hormonal effects on glycogen metabolism in isolated hepatocytes of a freeze-tolerant frog
    • Mommsen, T. P. and Storey, K. B. (1992). Hormonal effects on glycogen metabolism in isolated hepatocytes of a freeze-tolerant frog. Gen. Comp. Endocrinol. 87, 44-53.
    • (1992) Gen. Comp. Endocrinol. , vol.87 , pp. 44-53
    • Mommsen, T.P.1    Storey, K.B.2
  • 32
    • 0020585165 scopus 로고
    • Glycogen synthase from rabbit skeletal muscle; effect of insulin on the state of phosphorylation of the seven phosphoserine residues in vivo
    • Parker, P. J. J., Caudwell, F. B. and Cohen, P. (1983). Glycogen synthase from rabbit skeletal muscle: Effect of insulin on the state of phosphorylation of the seven phosphoserine residues in vivo. Eur. J. Biochem. 130, 227-234. (Pubitemid 13111910)
    • (1983) European Journal of Biochemistry , vol.130 , Issue.1 , pp. 227-234
    • Parker, P.J.1    Caudwell, F.B.2    Cohen, P.3
  • 33
    • 33644961390 scopus 로고    scopus 로고
    • Suppression of Na+K+-ATPase activity during estivation in the land snail Otala lactea
    • Ramnanan, C. J. and Storey, K. B. (2006). Suppression of Na+K+-ATPase activity during estivation in the land snail Otala lactea. J. Exp. Biol. 209, 677-688.
    • (2006) J. Exp. Biol. , vol.209 , pp. 677-688
    • Ramnanan, C.J.1    Storey, K.B.2
  • 34
    • 28244466264 scopus 로고    scopus 로고
    • 5-Aminoimidazole-4-carboxamide-1-D-ribofuranoside inhibits cancer cell proliferation in vitro and in vivo via AMP-activated protein kinase
    • DOI 10.1074/jbc.M507443200
    • Rattan, R., Giri, S., Singh, A. K. and Singh, I. (2005). 5-Aminoimidazole-4- carboxamide-1-b-D-ribofuranoside inhibits cancer cell proliferation in vitro and in vivo via AMP-activated protein kinase. J. Biol. Chem. 280, 39582-39593. (Pubitemid 41713917)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.47 , pp. 39582-39593
    • Rattan, R.1    Giri, S.2    Singh, A.K.3    Singh, I.4
  • 35
    • 33845899087 scopus 로고    scopus 로고
    • Stress-induced activation of the AMP-activated protein kinase in the freeze-tolerant frog Rana sylvatica
    • DOI 10.1016/j.cryobiol.2006.08.001, PII S0011224006001167
    • Rider, M. H., Hussain, N., Horman, S., Dilworth, S. M. and Storey, K. B. (2006). Stress-induced activation of the AMP-activated protein kinase in the freeze-tolerant frog, Rana sylvatica. Cryobiology 53, 297-309. (Pubitemid 46026753)
    • (2006) Cryobiology , vol.53 , Issue.3 , pp. 297-309
    • Rider, M.H.1    Hussain, N.2    Horman, S.3    Dilworth, S.M.4    Storey, K.B.5
  • 36
    • 0025202408 scopus 로고
    • Control of glycogen synthase by hierarchal protein phosphorylation
    • Roach, P. J. (1990). Control of glycogen synthase by hierarchal protein phosphorylation. FASEB J. 4, 2961-2968. (Pubitemid 120012542)
    • (1990) FASEB Journal , vol.4 , Issue.12 , pp. 2961-2968
    • Roach, P.J.1
  • 38
    • 0042037179 scopus 로고
    • Glycogen synthetase and the control of cryoprotectant clearance after thawing in the freeze tolerant wood frog
    • Russell, E. L. and Storey, K. B. (1995). Glycogen synthetase and the control of cryoprotectant clearance after thawing in the freeze tolerant wood frog. Cryo Letters 16, 263-266.
    • (1995) Cryo Letters , vol.16 , pp. 263-266
    • Russell, E.L.1    Storey, K.B.2
  • 39
    • 0019025978 scopus 로고
    • Glycogen synthase from rabbit skeletal muscle. Amino acid sequence at the sites phosphorylated by glycogen synthase kinase-3, and extension of the N-terminal sequence containing the site phosphorylated by phosphorylase kinase
    • Rylatt, D. B., Aitken, A., Bilham, T., Condon, G. D., Embi, N. and Cohen, P. (1980). Glycogen synthase from rabbit skeletal muscle. Amino acid sequence at the sites phosphorylated by glycogen synthase kinase-3, and extension of the N-terminal sequence containing the site phosphorylated by phosphorylase kinase. Eur. J. Biochem. 107, 529-537.
    • (1980) Eur. J. Biochem. , vol.107 , pp. 529-537
    • Rylatt, D.B.1    Aitken, A.2    Bilham, T.3    Condon, G.D.4    Embi, N.5    Cohen, P.6
  • 40
    • 0026448111 scopus 로고
    • Pathways of glycogen repletion
    • Schulman, G. I. and Landau, B. R. (1992). Pathways of glycogen repletion. Physiol. Rev. 72, 1019-1035.
    • (1992) Physiol. Rev. , vol.72 , pp. 1019-1035
    • Schulman, G.I.1    Landau, B.R.2
  • 41
    • 0001384885 scopus 로고
    • Glycolysis and the regulation of cryoprotectant synthesis in liver of the freeze tolerant wood frog
    • Storey, K. B. (1987a). Glycolysis and the regulation of cryoprotectant synthesis in liver of the freeze tolerant wood frog. J. Comp. Physiol. B 157, 373-380.
    • (1987) J. Comp. Physiol. B , vol.157 , pp. 373-380
    • Storey, K.B.1
  • 42
    • 0023635069 scopus 로고
    • Organ-specific metabolism during freezing and thawing in a freeze-tolerant frog
    • Storey, K. B. (1987b). Organ-specific metabolism during freezing and thawing in a freeze-tolerant frog. Am. J. Physiol. Regul. Integr. Comp. Physiol. 253, R292-R297.
    • (1987) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.253
    • Storey, K.B.1
  • 44
    • 0001136401 scopus 로고
    • Triggering of cryoprotectant synthesis by the initiation of ice nucleation in the freeze tolerant frog, Rana sylvatica
    • Storey, J. M. and Storey, K. B. (1985). Triggering of cryoprotectant synthesis by the initiation of ice nucleation in the freeze tolerant frog, Rana sylvatica. J. Comp. Physiol. B 156, 91-195.
    • (1985) J. Comp. Physiol. B , vol.156 , pp. 91-195
    • Storey, J.M.1    Storey, K.B.2
  • 45
    • 0023841438 scopus 로고
    • Freeze tolerance in animals
    • Storey, K. B. and Storey, J. M. (1988). Freeze tolerance in animals. Physiol. Rev. 68, 27-84. (Pubitemid 18036906)
    • (1988) Physiological Reviews , vol.68 , Issue.1 , pp. 27-84
    • Storey, K.B.1    Storey, J.M.2
  • 46
    • 1842721183 scopus 로고    scopus 로고
    • Physiology, biochemistry and molecular biology of vertebrate freeze tolerance: The wood frog
    • (ed. B. E. Fuller and N. Lane) CRC Press, London
    • Storey, K. B. and Storey, J. M. (2004). Physiology, biochemistry and molecular biology of vertebrate freeze tolerance: The wood frog. In Life in the Frozen State (ed. B. E. Fuller and N. Lane), pp. 243-274. CRC Press, London.
    • (2004) Life in the Frozen State , pp. 243-274
    • Storey, K.B.1    Storey, J.M.2
  • 48
    • 0027515127 scopus 로고
    • Inactivation of glycogen synthase kinase-3 by phosphorylation: New kinase connections in insulin and growth-factor signalling
    • Sutherland, C., Leighton, I. A. and Cohen, P. (1993). Inactivation of glycogen synthase kinase-3b by phosphorylation: New kinase connections in insulin and growth-factor signalling. Biochem. J. 296, 15-19. (Pubitemid 23344723)
    • (1993) Biochemical Journal , vol.296 , Issue.1 , pp. 15-19
    • Sutherland, C.1    Leighton, I.A.2    Cohen, P.3
  • 50
    • 0027430039 scopus 로고
    • Glycogen synthase kinase-3 is rapidly inactivated in response to insulin and phosphorylates eukaryotic initiation factor eIF-2B
    • Welsh, G. I. and Proud, C. G. (1993). Glycogen synthase kinase-3 is rapidly inactivated in response to insulin and phosphorylates eukaryotic initiation factor eIF- 2B. Biochem. J. 294, 625-629. (Pubitemid 23286543)
    • (1993) Biochemical Journal , vol.294 , Issue.3 , pp. 625-629
    • Welsh, G.I.1    Proud, C.G.2
  • 51
    • 33644886305 scopus 로고    scopus 로고
    • Vertebrate freezing survival: Regulation of the multicatalytic proteinase complex and controls on protein degradation
    • Woods, A. K. and Storey, K. B. (2006). Vertebrate freezing survival: Regulation of the multicatalytic proteinase complex and controls on protein degradation. Biochim. Biophys. Acta 1760, 395-403.
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 395-403
    • Woods, A.K.1    Storey, K.B.2


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