메뉴 건너뛰기




Volumn 1, Issue 6, 2003, Pages 381-398

Carbon metabolite sensing and signalling

Author keywords

carbohydrates; cross talk; hexokinase; SnRK1; sugar sensing; sugar transporters; trehalose

Indexed keywords


EID: 2942586276     PISSN: 14677644     EISSN: 14677652     Source Type: Journal    
DOI: 10.1046/j.1467-7652.2003.00046.x     Document Type: Review
Times cited : (98)

References (167)
  • 1
    • 0000569611 scopus 로고
    • cDNA clone encoding yeast SNF4-like protein from Phaseolus vulgaris
    • Abe, H., Kamiya, Y. and Sakurai, A.A. (1995) cDNA clone encoding yeast SNF4-like protein from Phaseolus vulgaris. Plant Phys. 110, 336.
    • (1995) Plant Phys , vol.110 , pp. 336
    • Abe, H.1    Kamiya, Y.2    Sakurai, A.A.3
  • 2
    • 0025936416 scopus 로고
    • Complementation of snf1, a mutation affecting global regulation of carbon metabolism in yeast, by a plant protein kinase cDNA
    • pmid/1924320
    • Alderson, A., Sabelli, P.A., Dickinson, J.R., Cole, D., Richardson, M., Kreis, M., Shewry, P.R. and Halford, N.G. (1991) Complementation of snf1, a mutation affecting global regulation of carbon metabolism in yeast, by a plant protein kinase cDNA. Proc. Natl Acad. Sci. USA, 88, 8602–8605.pmid/1924320
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 8602-8605
    • Alderson, A.1    Sabelli, P.A.2    Dickinson, J.R.3    Cole, D.4    Richardson, M.5    Kreis, M.6    Shewry, P.R.7    Halford, N.G.8
  • 3
    • 0000180202 scopus 로고
    • Uptake and utilization of sugars in cultured rice cells
    • Amino, S. and Tazawa, M. (1988) Uptake and utilization of sugars in cultured rice cells. Plant Cell Phys. 29, 483–487.
    • (1988) Plant Cell Phys , vol.29 , pp. 483-487
    • Amino, S.1    Tazawa, M.2
  • 4
    • 0026498186 scopus 로고
    • Isolation of a wheat cDNA clone for an abscisic acid-inducible transcript with homology to protein kinases
    • pmid/1438207
    • Anderberg, R.J. and Walker-Simmons, M.K. (1992) Isolation of a wheat cDNA clone for an abscisic acid-inducible transcript with homology to protein kinases. Proc. Natl Acad. Sci. USA, 89, 10183–10187.pmid/1438207
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 10183-10187
    • Anderberg, R.J.1    Walker-Simmons, M.K.2
  • 5
    • 0032932580 scopus 로고    scopus 로고
    • Quantitation of the effects of disruption of catabolite (de) repression genes on the cell cycle behaviour of Saccharomyces cerevisiae
    • pmid/9841784
    • Aon, M.G. and Cortassa, S. (1999) Quantitation of the effects of disruption of catabolite (de) repression genes on the cell cycle behaviour of Saccharomyces cerevisiae. Curr. Microbiol. 38, 57–60.pmid/9841784
    • (1999) Curr. Microbiol , vol.38 , pp. 57-60
    • Aon, M.G.1    Cortassa, S.2
  • 6
    • 0034664087 scopus 로고    scopus 로고
    • Analysis of Arabidopsis glucose insensitive mutants, gin5 and gin6, reveals a central role of the plant hormone ABA in the regulation of plant vegetative development by sugar
    • pmid/10950871
    • Arenas-Huertero, F., Arroyo, A., Zhou, L., Sheen, J. and Leon, P. (2000) Analysis of Arabidopsis glucose insensitive mutants, gin5 and gin6, reveals a central role of the plant hormone ABA in the regulation of plant vegetative development by sugar. Genes Dev. 14, 2085–2096.pmid/10950871
    • (2000) Genes Dev , vol.14 , pp. 2085-2096
    • Arenas-Huertero, F.1    Arroyo, A.2    Zhou, L.3    Sheen, J.4    Leon, P.5
  • 7
    • 0029924885 scopus 로고    scopus 로고
    • The inhibitor protein of phosphorylated nitrate reductase from spinach (Spinaea oleracea) leaves is a 14-3-3 protein
    • Bachmann, M., Huber, J.L., Liao, P.C., Gage, D.A. and Huber, S.C. (1996a) The inhibitor protein of phosphorylated nitrate reductase from spinach (Spinaea oleracea) leaves is a 14-3-3 protein. FEBS Letts. 387, 127–131.
    • (1996) FEBS Letts , vol.387 , pp. 127-131
    • Bachmann, M.1    Huber, J.L.2    Liao, P.C.3    Gage, D.A.4    Huber, S.C.5
  • 8
    • 0030096855 scopus 로고    scopus 로고
    • Identification of Ser-543 as the major regulatory phosphorylation site in spinach leaf nitrate reductase
    • pmid/8721752
    • Bachmann, M., Shiraishi, N., Campbell, W.H., Yoo, B.C., Harmon, A.C. and Huber, S.C. (1996b) Identification of Ser-543 as the major regulatory phosphorylation site in spinach leaf nitrate reductase. Plant Cell, 8, 505–517.pmid/8721752
    • (1996) Plant Cell , vol.8 , pp. 505-517
    • Bachmann, M.1    Shiraishi, N.2    Campbell, W.H.3    Yoo, B.C.4    Harmon, A.C.5    Huber, S.C.6
  • 9
    • 0029583202 scopus 로고
    • Immunological evidence that HMG-CoA reductase kinase-A is the cauliflower homologue of the RKIN1 subfamily of plant protein kinases
    • Ball, K.L., Barker, J.H.A., Halford, N.G. and Hardie, D.G. (1995) Immunological evidence that HMG-CoA reductase kinase-A is the cauliflower homologue of the RKIN1 subfamily of plant protein kinases. FEBS Letts. 377, 189–192.
    • (1995) FEBS Letts , vol.377 , pp. 189-192
    • Ball, K.L.1    Barker, J.H.A.2    Halford, N.G.3    Hardie, D.G.4
  • 10
    • 0027954963 scopus 로고
    • Biochemical characterisation of two forms of 3-hydroxy-3-methyl-glutaryl CoA reductase kinase from cauliflower (Brassica oleracea)
    • pmid/8112324
    • Ball, K.L., Dale, S., Weekes, J. and Hardie, D.G. (1994) Biochemical characterisation of two forms of 3-hydroxy-3-methyl-glutaryl CoA reductase kinase from cauliflower (Brassica oleracea). Eur. J. Biochem. 219, 743–750.pmid/8112324
    • (1994) Eur. J. Biochem , vol.219 , pp. 743-750
    • Ball, K.L.1    Dale, S.2    Weekes, J.3    Hardie, D.G.4
  • 12
    • 0030296153 scopus 로고    scopus 로고
    • Evidence that barley 3-hydroxy-3-methylglutaryl-Coenzyme A reductase kinase is a member of the sucrose nonfermenting-1-related protein kinase family
    • pmid/8938414
    • Barker, J.H.A., Slocombe, S.P., Ball, K.L., Hardie, D.G., Shewry, P.R. and Halford, N.G. (1996) Evidence that barley 3-hydroxy-3-methylglutaryl-Coenzyme A reductase kinase is a member of the sucrose nonfermenting-1-related protein kinase family. Plant Physiol. 112, 1141–1149.pmid/8938414
    • (1996) Plant Physiol , vol.112 , pp. 1141-1149
    • Barker, J.H.A.1    Slocombe, S.P.2    Ball, K.L.3    Hardie, D.G.4    Shewry, P.R.5    Halford, N.G.6
  • 13
    • 0033555685 scopus 로고    scopus 로고
    • Nim1-related kinases coordinate cell cycle progression with the organization of the peripheral cytoskeleton in yeast
    • pmid/9925642
    • Barral, Y., Parra, M., Bidlingmaier, S. and Snyder, M. (1999) Nim1-related kinases coordinate cell cycle progression with the organization of the peripheral cytoskeleton in yeast. Genes Dev. 13, 176–187.pmid/9925642
    • (1999) Genes Dev , vol.13 , pp. 176-187
    • Barral, Y.1    Parra, M.2    Bidlingmaier, S.3    Snyder, M.4
  • 14
    • 0015864346 scopus 로고
    • Modulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity with cAMP and with protein fractions of rat liver cytosol
    • pmid/4356818
    • Beg, Z.H., Allmann, D.W. and Gibson, D.M. (1973) Modulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity with cAMP and with protein fractions of rat liver cytosol. Biochem. Biophys. Res. Commun. 54, 1362–1369.pmid/4356818
    • (1973) Biochem. Biophys. Res. Commun , vol.54 , pp. 1362-1369
    • Beg, Z.H.1    Allmann, D.W.2    Gibson, D.M.3
  • 15
  • 16
    • 0030953385 scopus 로고    scopus 로고
    • The molecular genetics of hexose transport in yeasts
    • pmid/9299703
    • Boles, E. and Hollenberg, C.P. (1997) The molecular genetics of hexose transport in yeasts. FEMS Microbiol. Rev. 21, 85–111.pmid/9299703
    • (1997) FEMS Microbiol. Rev , vol.21 , pp. 85-111
    • Boles, E.1    Hollenberg, C.P.2
  • 17
    • 0034663598 scopus 로고    scopus 로고
    • Expression of Escherichia coli otsA in a Saccharomyces tps1 mutant restores growth and fermentation with glucose and control of glucose influx into glycolysis
    • pmid/10926852
    • Bonini, B.M., Van Vaeck, C., Larsson, C., Gustafsson, L., Ma, P., Winderickx, J., Van Dijck, P. and Thevelein, J.M. (2000) Expression of Escherichia coli otsA in a Saccharomyces tps1 mutant restores growth and fermentation with glucose and control of glucose influx into glycolysis. Biochem. J. 350, 261–268.pmid/10926852
    • (2000) Biochem. J , vol.350 , pp. 261-268
    • Bonini, B.M.1    Van Vaeck, C.2    Larsson, C.3    Gustafsson, L.4    Ma, P.5    Winderickx, J.6    Van Dijck, P.7    Thevelein, J.M.8
  • 18
    • 0033152684 scopus 로고    scopus 로고
    • Arabidopsis thaliana homologues of the yeast SIP and SNF4 proteins interact with AKINα1, a SNF1-like protein kinase
    • pmid/10417704
    • Bouly, J.P., Gissot, L., Lessard, P., Kreis, M. and Thomas, M. (1999) Arabidopsis thaliana homologues of the yeast SIP and SNF4 proteins interact with AKINα1, a SNF1-like protein kinase. Plant J. 18, 541–550.pmid/10417704
    • (1999) Plant J , vol.18 , pp. 541-550
    • Bouly, J.P.1    Gissot, L.2    Lessard, P.3    Kreis, M.4    Thomas, M.5
  • 19
    • 0028310837 scopus 로고
    • Mammalian AMP-activated protein kinase is homologous to yeast and plant protein kinases involved in the regulation of carbon metabolism
    • pmid/7908907
    • Carling, D., Aguan, K., Woods, A., Verhoeven, A.J.M., Beri, R.K., Brennan, C.H., Sidebottom, C., Davison, M.D. and Scott, J. (1994) Mammalian AMP-activated protein kinase is homologous to yeast and plant protein kinases involved in the regulation of carbon metabolism. J. Biol. Chem. 269, 11442–11448.pmid/7908907
    • (1994) J. Biol. Chem , vol.269 , pp. 11442-11448
    • Carling, D.1    Aguan, K.2    Woods, A.3    Verhoeven, A.J.M.4    Beri, R.K.5    Brennan, C.H.6    Sidebottom, C.7    Davison, M.D.8    Scott, J.9
  • 20
    • 0024786438 scopus 로고
    • Purification and characterisation of the AMP-activated protein kinase – co-purification of acetyl-CoA carboxylase and 3-hydroxy-3-methylglutaryl CoA reductase kinase activity
    • pmid/2598924
    • Carling, D., Clarke, P.R., Zammit, V.A. and Hardie, D.G. (1989) Purification and characterisation of the AMP-activated protein kinase – co-purification of acetyl-CoA carboxylase and 3-hydroxy-3-methylglutaryl CoA reductase kinase activity. Eur. J. Biochem. 186, 129–136.pmid/2598924
    • (1989) Eur. J. Biochem , vol.186 , pp. 129-136
    • Carling, D.1    Clarke, P.R.2    Zammit, V.A.3    Hardie, D.G.4
  • 21
    • 0023642627 scopus 로고
    • A common bicyclic protein kinase cascade inactivates the regulatory enzymes of fatty acid and cholesterol biosynthesis
    • pmid/2889619
    • Carling, D., Zammit, V.A. and Hardie, D.G. (1987) A common bicyclic protein kinase cascade inactivates the regulatory enzymes of fatty acid and cholesterol biosynthesis. FEBS Lett. 223, 217–222.pmid/2889619
    • (1987) FEBS Lett , vol.223 , pp. 217-222
    • Carling, D.1    Zammit, V.A.2    Hardie, D.G.3
  • 22
    • 0015918822 scopus 로고
    • Regulation of hepatic acetyl coenzyme A carboxylase by phosphorylation and dephosphorylation
    • pmid/4692841
    • Carlson, C.A. and Kim, K.H. (1973) Regulation of hepatic acetyl coenzyme A carboxylase by phosphorylation and dephosphorylation. J. Biol. Chem. 248, 378–380.pmid/4692841
    • (1973) J. Biol. Chem , vol.248 , pp. 378-380
    • Carlson, C.A.1    Kim, K.H.2
  • 23
    • 0022534202 scopus 로고
    • A yeast gene that is essential for release from glucose repression encodes a protein kinase
    • pmid/3526554
    • Celenza, J.L. and Carlson, M. (1986) A yeast gene that is essential for release from glucose repression encodes a protein kinase. Science, 233, 1175–1180.pmid/3526554
    • (1986) Science , vol.233 , pp. 1175-1180
    • Celenza, J.L.1    Carlson, M.2
  • 24
    • 0024325465 scopus 로고
    • Molecular analysis of the Snf4 gene of Saccharomyces cerevisiae – evidence for the physical association of the Snf4 protein with the Snf1 protein kinase
    • pmid/2481228
    • Celenza, J.L., Eng, F.J. and Carlson, M. (1989) Molecular analysis of the Snf4 gene of Saccharomyces cerevisiae – evidence for the physical association of the Snf4 protein with the Snf1 protein kinase. Molec. Cell. Biol. 9, 5045–5054.pmid/2481228
    • (1989) Molec. Cell. Biol , vol.9 , pp. 5045-5054
    • Celenza, J.L.1    Eng, F.J.2    Carlson, M.3
  • 25
    • 0026541075 scopus 로고
    • Sucrose mimics the light induction of Arabidopsis nitrate reductase gene transcription
    • pmid/1542684
    • Cheng, C.-L., Acedo, G.N., Cristinsin, M. and Conkling, M.A. (1992) Sucrose mimics the light induction of Arabidopsis nitrate reductase gene transcription. Proc. Natl Acad. Sci. USA, 89, 1861–1864.pmid/1542684
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 1861-1864
    • Cheng, C.-L.1    Acedo, G.N.2    Cristinsin, M.3    Conkling, M.A.4
  • 26
    • 0017034186 scopus 로고
    • The enzymatic deficiency conditioned by the Shrunken-1 mutations in maize
    • pmid/1016220
    • Chourey, P.S. and Nelson, O.E. (1976) The enzymatic deficiency conditioned by the Shrunken-1 mutations in maize. Biochem. Genet. 14, 1041–1055.pmid/1016220
    • (1976) Biochem. Genet , vol.14 , pp. 1041-1055
    • Chourey, P.S.1    Nelson, O.E.2
  • 27
    • 0025310576 scopus 로고
    • Regulation of HMG-CoA reductase: identification of the site phosphorylated by the AMP-activated protein kinase in vitro and in intact rat liver
    • pmid/2369897
    • Clarke, P.R. and Hardie, D.G. (1990) Regulation of HMG-CoA reductase: identification of the site phosphorylated by the AMP-activated protein kinase in vitro and in intact rat liver. EMBO J. 9, 2439–2446.pmid/2369897
    • (1990) EMBO J , vol.9 , pp. 2439-2446
    • Clarke, P.R.1    Hardie, D.G.2
  • 28
    • 0028406897 scopus 로고
    • Role of the AMP-activated protein kinase in the cellular stress response
    • pmid/7922340
    • Corton, J.M., Gillespie, J.G. and Hardie, D.G. (1994) Role of the AMP-activated protein kinase in the cellular stress response. Curr. Biol. 4, 315–324.pmid/7922340
    • (1994) Curr. Biol , vol.4 , pp. 315-324
    • Corton, J.M.1    Gillespie, J.G.2    Hardie, D.G.3
  • 29
    • 85047689953 scopus 로고
    • 5-Aminoimidazole-4-carboxamide ribonucleoside: a specific method for activating AMP-activated protein kinase in intact cells?
    • pmid/7744080
    • Corton, J.M., Gillespie, J.G., Hawley, S.A. and Hardie, D.G. (1995) 5-Aminoimidazole-4-carboxamide ribonucleoside: a specific method for activating AMP-activated protein kinase in intact cells? Eur. J. Biochem. 229, 558–565.pmid/7744080
    • (1995) Eur. J. Biochem , vol.229 , pp. 558-565
    • Corton, J.M.1    Gillespie, J.G.2    Hawley, S.A.3    Hardie, D.G.4
  • 30
    • 0035321194 scopus 로고    scopus 로고
    • Cloning of DNA encoding a catalytic subunit of SNF1-related protein kinase-1 (SnRK1-α1) and immunological analysis of multiple forms of the kinase in spinach leaf
    • Crawford, R.M., Halford, N.G. and Hardie, D.G. (2001) Cloning of DNA encoding a catalytic subunit of SNF1-related protein kinase-1 (SnRK1-α1) and immunological analysis of multiple forms of the kinase in spinach leaf. Plant Molec. Biol. 45, 731–741.
    • (2001) Plant Molec. Biol , vol.45 , pp. 731-741
    • Crawford, R.M.1    Halford, N.G.2    Hardie, D.G.3
  • 31
    • 0028834801 scopus 로고
    • Bacterial expression of the catalytic domain of 3-hydroxy-3-methylglutaryl CoA reductase (isoform HMGR1) from Arabidopsis, and its inactivation by phosphorylation at serine-577 by Brassica oleracea 3-hydroxy-3-methylglutaryl CoA reductase kinase
    • pmid/7588795
    • Dale, S., Arró, M., Becerra, B., Morrice, N.G., Boronat, A., Hardie, D.G. and Ferrer, A. (1995a) Bacterial expression of the catalytic domain of 3-hydroxy-3-methylglutaryl CoA reductase (isoform HMGR1) from Arabidopsis, and its inactivation by phosphorylation at serine-577 by Brassica oleracea 3-hydroxy-3-methylglutaryl CoA reductase kinase. Eur. J. Biochem. 233, 506–513.pmid/7588795
    • (1995) Eur. J. Biochem , vol.233 , pp. 506-513
    • Dale, S.1    Arró, M.2    Becerra, B.3    Morrice, N.G.4    Boronat, A.5    Hardie, D.G.6    Ferrer, A.7
  • 32
    • 0028942747 scopus 로고
    • Similar substrate recognition motifs for mammalian AMP-activated protein kinase, higher plant HMG-CoA reductase kinase-A, yeast SNF1, and mammalian calmodulin-dependent protein kinase I
    • Dale, S., Wilson, W.A., Edelman, A.M. and Hardie, D.G. (1995b) Similar substrate recognition motifs for mammalian AMP-activated protein kinase, higher plant HMG-CoA reductase kinase-A, yeast SNF1, and mammalian calmodulin-dependent protein kinase I. FEBS Letts. 361, 191–195.
    • (1995) FEBS Letts , vol.361 , pp. 191-195
    • Dale, S.1    Wilson, W.A.2    Edelman, A.M.3    Hardie, D.G.4
  • 33
    • 0024839973 scopus 로고
    • Tissue distribution of the AMP-activated protein kinase, and lack of activation by cyclic AMP-dependent protein kinase, studies using a specific and sensitive peptide assay
    • pmid/2574667
    • Davies, S.P., Carling, D. and Hardie, D.G. (1989) Tissue distribution of the AMP-activated protein kinase, and lack of activation by cyclic AMP-dependent protein kinase, studies using a specific and sensitive peptide assay. Eur. J. Biochem. 186, 123–128.pmid/2574667
    • (1989) Eur. J. Biochem , vol.186 , pp. 123-128
    • Davies, S.P.1    Carling, D.2    Hardie, D.G.3
  • 34
    • 0026605017 scopus 로고
    • Diurnal rhythm of phosphorylation of rat-liver acetyl-CoA carboxylase by the AMP-activated protein kinase, demonstrated using freeze-clamping – effects of high-fat diets
    • pmid/1346520
    • Davies, S.P., Carling, D., Munday, M.R. and Hardie, D.G. (1992) Diurnal rhythm of phosphorylation of rat-liver acetyl-CoA carboxylase by the AMP-activated protein kinase, demonstrated using freeze-clamping – effects of high-fat diets. Eur. J. Biochem. 203, 615–623.pmid/1346520
    • (1992) Eur. J. Biochem , vol.203 , pp. 615-623
    • Davies, S.P.1    Carling, D.2    Munday, M.R.3    Hardie, D.G.4
  • 35
    • 0028068882 scopus 로고
    • Purification of the AMP-activated protein kinase on ATP-g-Sepharose and analysis of its subunit structure
    • pmid/8055903
    • Davies, S.P., Hawley, S.A., Woods, A., Carling, D., Haystead, T.A.J. and Hardie, D.G. (1994) Purification of the AMP-activated protein kinase on ATP-g-Sepharose and analysis of its subunit structure. Eur. J. Biochem. 223, 351–357.pmid/8055903
    • (1994) Eur. J. Biochem , vol.223 , pp. 351-357
    • Davies, S.P.1    Hawley, S.A.2    Woods, A.3    Carling, D.4    Haystead, T.A.J.5    Hardie, D.G.6
  • 36
    • 0029561919 scopus 로고
    • 5′-AMP inhibits dephosphorylation, as well as promoting phosphorylation, of the AMP-activated protein kinase. Studies using bacterially expressed human protein phosphatase-2Cα and native bovine protein phosphatase-2A(C)
    • Davies, S.P., Helps, N.R., Cohen, P.T.W. and Hardie, D.G. (1995) 5′-AMP inhibits dephosphorylation, as well as promoting phosphorylation, of the AMP-activated protein kinase. Studies using bacterially expressed human protein phosphatase-2Cα and native bovine protein phosphatase-2A(C). FEBS Letts. 377, 421–425.
    • (1995) FEBS Letts , vol.377 , pp. 421-425
    • Davies, S.P.1    Helps, N.R.2    Cohen, P.T.W.3    Hardie, D.G.4
  • 37
    • 0025192341 scopus 로고
    • Location and function of three sites phosphorylated on rat acetyl-CoA carboxylase by the AMP-activated protein kinase
    • pmid/1967580
    • Davies, S.P., Sim, A.T.R. and Hardie, D.G. (1990) Location and function of three sites phosphorylated on rat acetyl-CoA carboxylase by the AMP-activated protein kinase. Eur. J. Biochem. 187, 183–190.pmid/1967580
    • (1990) Eur. J. Biochem , vol.187 , pp. 183-190
    • Davies, S.P.1    Sim, A.T.R.2    Hardie, D.G.3
  • 38
    • 0030883032 scopus 로고    scopus 로고
    • Regulated nuclear translocation of the Mig1 repressor
    • pmid/9285828
    • DeVit, M.J., Waddle, J.A. and Johnston, M. (1997) Regulated nuclear translocation of the Mig1 repressor. Molec. Biol. Cell, 8, 1603–1618.pmid/9285828
    • (1997) Molec. Biol. Cell , vol.8 , pp. 1603-1618
    • DeVit, M.J.1    Waddle, J.A.2    Johnston, M.3
  • 39
    • 0001953368 scopus 로고    scopus 로고
    • Carbon metabolism
    • Dickinson, J.R., Schweizer, M., eds), London & Philadelphia, PA, Taylor & Francis
    • Dickinson, J.R. (1999) Carbon metabolism. In: The Metabolism and Molecular Physiology of Saccharomyces Cerevisiae (Dickinson, J.R. and Schweizer, M., eds), pp. 23–55. London & Philadelphia, PA: Taylor & Francis.
    • (1999) The Metabolism and Molecular Physiology of Saccharomyces Cerevisiae , pp. 23-55
    • Dickinson, J.R.1
  • 40
    • 10144234981 scopus 로고
    • Slow growth phenotype of transgenic tomato expressing apoplastic invertase
    • Dickinson, C.C., Altabella, T. and Chrispeels, M.J. (1991) Slow growth phenotype of transgenic tomato expressing apoplastic invertase. Plant Physiol. 95, 420–425.
    • (1991) Plant Physiol , vol.95 , pp. 420-425
    • Dickinson, C.C.1    Altabella, T.2    Chrispeels, M.J.3
  • 41
    • 0032826189 scopus 로고    scopus 로고
    • A cell cycle role for a plant sucrose nonfermenting-1-related protein kinase (SnRK1) is indicated by expression in yeast
    • Dickinson, J.R., Cole, D. and Halford, N.G. (1999) A cell cycle role for a plant sucrose nonfermenting-1-related protein kinase (SnRK1) is indicated by expression in yeast. Plant Growth Reg. 28, 169–174.
    • (1999) Plant Growth Reg , vol.28 , pp. 169-174
    • Dickinson, J.R.1    Cole, D.2    Halford, N.G.3
  • 42
    • 0029583746 scopus 로고
    • Identification of a regulatory phosphorylation site in the hinge 1 region of nitrate reductase from spinach (Spinacea oleracea) leaves
    • Douglas, P., Morrice, N. and MacKintosh, C. (1995) Identification of a regulatory phosphorylation site in the hinge 1 region of nitrate reductase from spinach (Spinacea oleracea) leaves. FEBS Letts. 377, 113–117.
    • (1995) FEBS Letts , vol.377 , pp. 113-117
    • Douglas, P.1    Morrice, N.2    MacKintosh, C.3
  • 44
    • 0027143058 scopus 로고
    • The occurrence of trehalose in the leaves of the desiccation tolerant angiosperm Myrothamnus flabellifolius Welw
    • Drennan, P.M., Smith, M.T., Goldsworthy, D. and Van Staden, J. (1993) The occurrence of trehalose in the leaves of the desiccation tolerant angiosperm Myrothamnus flabellifolius Welw. J. Plant Physiol. 142, 493–496.
    • (1993) J. Plant Physiol , vol.142 , pp. 493-496
    • Drennan, P.M.1    Smith, M.T.2    Goldsworthy, D.3    Van Staden, J.4
  • 45
    • 0028446540 scopus 로고
    • Separate cis sequences and trans factors direct metabolic and developmental regulation of a potato tuber storage protein gene
    • pmid/8054988
    • Du Grierson, C.J.S., Zabala, M.D., Beggs, K., Smith, C., Holdsworth, M. and Bevan, M. (1994) Separate cis sequences and trans factors direct metabolic and developmental regulation of a potato tuber storage protein gene. Plant J. 5, 815–826.pmid/8054988
    • (1994) Plant J , vol.5 , pp. 815-826
    • Du Grierson, C.J.S.1    Zabala, M.D.2    Beggs, K.3    Smith, C.4    Holdsworth, M.5    Bevan, M.6
  • 46
    • 0036007980 scopus 로고    scopus 로고
    • Trehalose-6-phosphate 1, which catalyses the first step in trehalose synthesis, is essential for Arabidopsis embryo development
    • pmid/11851922
    • Eastmond, P.J., Van Dijken, A.J., Spielman, M., Kerr, A., Tissier, A.F., Dickinson, H.G., Jones, J.D., Smeekens, S.C. and Graham, I.A. (2002) Trehalose-6-phosphate 1, which catalyses the first step in trehalose synthesis, is essential for Arabidopsis embryo development. Plant J. 29, 225–235.pmid/11851922
    • (2002) Plant J , vol.29 , pp. 225-235
    • Eastmond, P.J.1    Van Dijken, A.J.2    Spielman, M.3    Kerr, A.4    Tissier, A.F.5    Dickinson, H.G.6    Jones, J.D.7    Smeekens, S.C.8    Graham, I.A.9
  • 47
    • 0018969294 scopus 로고
    • Genetic and biochemical evidence for hexokinase PII as a key enzyme involved in carbon catabolite repression in yeast
    • pmid/6993859
    • Entian, K.D. (1980) Genetic and biochemical evidence for hexokinase PII as a key enzyme involved in carbon catabolite repression in yeast. Mol. Gen. Genet. 178, 633–637.pmid/6993859
    • (1980) Mol. Gen. Genet , vol.178 , pp. 633-637
    • Entian, K.D.1
  • 48
    • 0035986769 scopus 로고    scopus 로고
    • A novel higher plant protein tyrosine phosphatase interacts with SNF1-related protein kinases via a KIS (kinase interaction sequence) domain
    • pmid/12148529
    • Fordham-Skelton, A.P., Chilley, P., Lumbreras, V., Reignoux, S., Fenton, T.R., Dahm, C.C., Pages, M. and Gatehouse, J.A. (2002) A novel higher plant protein tyrosine phosphatase interacts with SNF1-related protein kinases via a KIS (kinase interaction sequence) domain. Plant J. 29, 705–715.pmid/12148529
    • (2002) Plant J , vol.29 , pp. 705-715
    • Fordham-Skelton, A.P.1    Chilley, P.2    Lumbreras, V.3    Reignoux, S.4    Fenton, T.R.5    Dahm, C.C.6    Pages, M.7    Gatehouse, J.A.8
  • 49
    • 0034979938 scopus 로고    scopus 로고
    • Induction of APL3 expression by trehalose complements the starch-deficient Arabidopsis mutant adg2-1 lacking ApL1, the large subunit of ADP-glucose pyrophosphorylase
    • pmid/11402215
    • Fritzius, T., Aeschbacher, R., Wiemken, A. and Wingler, A. (2001) Induction of APL3 expression by trehalose complements the starch-deficient Arabidopsis mutant adg2-1 lacking ApL1, the large subunit of ADP-glucose pyrophosphorylase. Plant Physiol. 126, 883–889.pmid/11402215
    • (2001) Plant Physiol , vol.126 , pp. 883-889
    • Fritzius, T.1    Aeschbacher, R.2    Wiemken, A.3    Wingler, A.4
  • 50
    • 0029360594 scopus 로고
    • Sink- and vascular-associated sucrose synthase functions are encoded by different gene classes in potato
    • pmid/8589622
    • Fu, H. and Park, W.D. (1995) Sink- and vascular-associated sucrose synthase functions are encoded by different gene classes in potato. Plant Cell, 7, 1369–1385.pmid/8589622
    • (1995) Plant Cell , vol.7 , pp. 1369-1385
    • Fu, H.1    Park, W.D.2
  • 52
    • 0028961963 scopus 로고
    • Catalytic subunits of the porcine and rat 5′-AMP-activated protein kinase are members of the SNF1 protein kinase family
    • pmid/7718624
    • Gao, G., Widmer, J., Stapleton, D., The, T., Cox, T., Kemp, B.E. and Witters, L.A. (1995) Catalytic subunits of the porcine and rat 5′-AMP-activated protein kinase are members of the SNF1 protein kinase family. Biochim. Biophys. Acta, 1266, 73–82.pmid/7718624
    • (1995) Biochim. Biophys. Acta , vol.1266 , pp. 73-82
    • Gao, G.1    Widmer, J.2    Stapleton, D.3    The, T.4    Cox, T.5    Kemp, B.E.6    Witters, L.A.7
  • 53
    • 0037058918 scopus 로고    scopus 로고
    • Trehalose accumulation in rice plants confers high tolerance levels to different abiotic stresses
    • pmid/12456878
    • Garg, A.K., Kim, J.-K., Owens, T.G., Ranwala, A.P., Choi, Y.D., Kochian, L.V. and Wu, R.J. (2002) Trehalose accumulation in rice plants confers high tolerance levels to different abiotic stresses. Proc. Natl Acad. Sci. USA, 99, 15898–15903.pmid/12456878
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 15898-15903
    • Garg, A.K.1    Kim, J.-K.2    Owens, T.G.3    Ranwala, A.P.4    Choi, Y.D.5    Kochian, L.V.6    Wu, R.J.7
  • 54
    • 0026740903 scopus 로고
    • Phosphorylation and inactivation of HMG-CoA reductase at the AMP-activated protein kinase site in response to fructose treatment of isolated rat hepatocytes
    • Gillespie, J.G. and Hardie, D.G. (1992) Phosphorylation and inactivation of HMG-CoA reductase at the AMP-activated protein kinase site in response to fructose treatment of isolated rat hepatocytes. FEBS Letts. 306, 59–62.
    • (1992) FEBS Letts , vol.306 , pp. 59-62
    • Gillespie, J.G.1    Hardie, D.G.2
  • 55
    • 0032053108 scopus 로고    scopus 로고
    • Sensing trehalose biosynthesis in plants
    • pmid/9628011
    • Goddijn, O.J. and Smeekens, S.C.M. (1998) Sensing trehalose biosynthesis in plants. Plant J. 14, 143–146.pmid/9628011
    • (1998) Plant J , vol.14 , pp. 143-146
    • Goddijn, O.J.1    Smeekens, S.C.M.2
  • 56
    • 0033178759 scopus 로고    scopus 로고
    • Trehalose metabolism in plants
    • pmid/10431221
    • Goddijn, O.J. and Van Dun, K. (1999) Trehalose metabolism in plants. Trends Plant Sci. 4, 315–319.pmid/10431221
    • (1999) Trends Plant Sci , vol.4 , pp. 315-319
    • Goddijn, O.J.1    Van Dun, K.2
  • 57
    • 0033573898 scopus 로고    scopus 로고
    • An abscisic acid-induced protein kinase, PKABA1, mediates abscisic acid-suppressed gene expression in barley aleurone layers
    • pmid/9990099
    • Gómez-Cadenas, A., Verhey, S.D., Holappa, L.D., Shen, Q., Ho, T.-H.D. and Walker-Simmons, M.K. (1999) An abscisic acid-induced protein kinase, PKABA1, mediates abscisic acid-suppressed gene expression in barley aleurone layers. Proc. Natl Acad. Sci. USA, 96, 1767–1772.pmid/9990099
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 1767-1772
    • Gómez-Cadenas, A.1    Verhey, S.D.2    Holappa, L.D.3    Shen, Q.4    Ho, T.-H.D.5    Walker-Simmons, M.K.6
  • 58
    • 0028152032 scopus 로고
    • Carbon catabolite repression regulates glyoxylate cycle gene expression in cucumber
    • pmid/12244257
    • Graham, I.A., Denby, K.J. and Leaver, C.J. (1994) Carbon catabolite repression regulates glyoxylate cycle gene expression in cucumber. Plant Cell, 6, 761–772.pmid/12244257
    • (1994) Plant Cell , vol.6 , pp. 761-772
    • Graham, I.A.1    Denby, K.J.2    Leaver, C.J.3
  • 59
    • 0032127148 scopus 로고    scopus 로고
    • SNF1-related protein kinases: global regulators of carbon metabolism in plants?
    • pmid/9678569
    • Halford, N.G. and Hardie, D.G. (1998) SNF1-related protein kinases: global regulators of carbon metabolism in plants? Plant Mol. Biol. 37, 735–748.pmid/9678569
    • (1998) Plant Mol. Biol , vol.37 , pp. 735-748
    • Halford, N.G.1    Hardie, D.G.2
  • 60
    • 0037239022 scopus 로고    scopus 로고
    • Metabolic signalling and carbon partitioning: Role of Snf1-related (SnRK1) protein kinase
    • pmid/12508057
    • Halford, N.G., Hey, S., Jhurreea, D., Laurie, S., McKibbin, R.S., Paul, M.J. and Zhang, Y. (2003a) Metabolic signalling and carbon partitioning: Role of Snf1-related (SnRK1) protein kinase. J. Exp. Bot. 54, 467–475.pmid/12508057
    • (2003) J. Exp. Bot , vol.54 , pp. 467-475
    • Halford, N.G.1    Hey, S.2    Jhurreea, D.3    Laurie, S.4    McKibbin, R.S.5    Paul, M.J.6    Zhang, Y.7
  • 62
    • 0033035539 scopus 로고    scopus 로고
    • Is hexokinase really a sugar sensor in plants?
    • pmid/10322544
    • Halford, N.G., Purcell, P.C. and Hardie, D.G. (1999) Is hexokinase really a sugar sensor in plants? Trends Plant Sci. 4, 117–120.pmid/10322544
    • (1999) Trends Plant Sci , vol.4 , pp. 117-120
    • Halford, N.G.1    Purcell, P.C.2    Hardie, D.G.3
  • 63
    • 0034724180 scopus 로고    scopus 로고
    • The arabidopsis SOS2 protein kinase physically interacts with and is activated by the calcium-binding protein, SOS3
    • Halfter, U., Ishitani, M. and Shu, J.-K. (2000) The arabidopsis SOS2 protein kinase physically interacts with and is activated by the calcium-binding protein, SOS3. Proc. Natl Acad. Sci. USA, 97, 3535–3740.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 3535-3740
    • Halfter, U.1    Ishitani, M.2    Shu, J.-K.3
  • 64
    • 23044523930 scopus 로고    scopus 로고
    • Plant protein serine/threonine protein kinases: Classification into subfamilies and overview of function
    • Hardie, D.G. (2000) Plant protein serine/threonine protein kinases: Classification into subfamilies and overview of function. Adv. Bot. Res. Inc. Adv. Plant Path. 32, 1–44.
    • (2000) Adv. Bot. Res. Inc. Adv. Plant Path , vol.32 , pp. 1-44
    • Hardie, D.G.1
  • 65
    • 0031007065 scopus 로고    scopus 로고
    • The AMP-activated protein kinase: fuel gauge of the mammalian cell?
    • pmid/9208914
    • Hardie, D.G. and Carling, D. (1997) The AMP-activated protein kinase: fuel gauge of the mammalian cell? Eur. J. Biochem. 246, 259–273.pmid/9208914
    • (1997) Eur. J. Biochem , vol.246 , pp. 259-273
    • Hardie, D.G.1    Carling, D.2
  • 66
    • 0000370670 scopus 로고
    • Light and sucrose-dependent gene expression in photomixotrophic cell suspension cultures and protoplasts of rape
    • Harter, K., Talke-Messerer, C., Barz, W. and Schäfer, E. (1993) Light and sucrose-dependent gene expression in photomixotrophic cell suspension cultures and protoplasts of rape. Plant J. 4, 507–516.
    • (1993) Plant J , vol.4 , pp. 507-516
    • Harter, K.1    Talke-Messerer, C.2    Barz, W.3    Schäfer, E.4
  • 67
    • 0029910018 scopus 로고    scopus 로고
    • Characterization of the AMP-activated protein kinase kinase from rat liver, and identification of threonine-172 as the major site at which it phosphorylates and activates AMP-activated protein kinase
    • pmid/8910387
    • Hawley, S.A., Davison, M., Woods, A., Davies, S.P., Beri, R.K., Carling, D. and Hardie, D.G. (1996) Characterization of the AMP-activated protein kinase kinase from rat liver, and identification of threonine-172 as the major site at which it phosphorylates and activates AMP-activated protein kinase. J. Biol. Chem. 271, 27879–27887.pmid/8910387
    • (1996) J. Biol. Chem , vol.271 , pp. 27879-27887
    • Hawley, S.A.1    Davison, M.2    Woods, A.3    Davies, S.P.4    Beri, R.K.5    Carling, D.6    Hardie, D.G.7
  • 69
    • 0028039637 scopus 로고
    • Accumulation of hexoses in leaf vacuoles: studies with transgenic tobacco plants expressing yeast-derived invertase in the cytosol, vacuole or cytoplasm
    • Heineke, D., Wildenberger, K., Sonnewald, U., Willmitzer, L. and Heldt, H.W. (1994) Accumulation of hexoses in leaf vacuoles: studies with transgenic tobacco plants expressing yeast-derived invertase in the cytosol, vacuole or cytoplasm. Planta, 194, 29–33.
    • (1994) Planta , vol.194 , pp. 29-33
    • Heineke, D.1    Wildenberger, K.2    Sonnewald, U.3    Willmitzer, L.4    Heldt, H.W.5
  • 70
    • 0000020414 scopus 로고    scopus 로고
    • Systemic acquired resistance mediated by the ectopic expression of invertase: Possible hexose sensing in the secretory pathway
    • pmid/12239401
    • Herbers, K., Meuwly, P., Frommer, W.B., Metraux, J.P. and Sonnewald, U. (1996) Systemic acquired resistance mediated by the ectopic expression of invertase: Possible hexose sensing in the secretory pathway. Plant Cell, 8, 793–803.pmid/12239401
    • (1996) Plant Cell , vol.8 , pp. 793-803
    • Herbers, K.1    Meuwly, P.2    Frommer, W.B.3    Metraux, J.P.4    Sonnewald, U.5
  • 71
    • 0345647082 scopus 로고    scopus 로고
    • The hexokinase 2 protein participates in regulatory DNA-protein complexes necessary for glucose repression of the SUC2 gene in Saccharomyces cerevisiae
    • pmid/9738454
    • Herrero, P., Martinez-Campa, C. and Moreno, F. (1998) The hexokinase 2 protein participates in regulatory DNA-protein complexes necessary for glucose repression of the SUC2 gene in Saccharomyces cerevisiae. FEBS Lett. 434, 71–76.pmid/9738454
    • (1998) FEBS Lett , vol.434 , pp. 71-76
    • Herrero, P.1    Martinez-Campa, C.2    Moreno, F.3
  • 72
    • 0001634436 scopus 로고
    • General and pathway-specific regulatory mechanisms controlling the synthesis of amino acid biosynthetic enzymes in Saccharomyces cerevisiae
    • Gene Expression, Jones, E.W., Pringle, J.R., Broach, J.B., eds), New York, Cold Spring Harbor Laboratory Press
    • Hinnebusch, A.G. (1992) General and pathway-specific regulatory mechanisms controlling the synthesis of amino acid biosynthetic enzymes in Saccharomyces cerevisiae. In: Molecular Cell Biology Yeast Saccharomyces, Vol. 2Gene Expression (Jones, E.W., Pringle, J.R. and Broach, J.B., eds), pp. 319–414. New York: Cold Spring Harbor Laboratory Press.
    • (1992) Molecular Cell Biology Yeast Saccharomyces , vol.2 , pp. 319-414
    • Hinnebusch, A.G.1
  • 73
    • 0028151657 scopus 로고
    • Translational control of GCN4 – an in vivo barometer of initiation factor activity
    • pmid/7817398
    • Hinnebusch, A.G. (1994) Translational control of GCN4 – an in vivo barometer of initiation factor activity. Trends. Biochem. Sci. 19, 409–414.pmid/7817398
    • (1994) Trends. Biochem. Sci , vol.19 , pp. 409-414
    • Hinnebusch, A.G.1
  • 74
    • 0030803256 scopus 로고    scopus 로고
    • Translational regulation of yeast GCN4 – A window on factors that control initiator-tRNA binding to the ribosome
    • pmid/9268289
    • Hinnebusch, A.G. (1997) Translational regulation of yeast GCN4 – A window on factors that control initiator-tRNA binding to the ribosome. J. Biol. Chem. 272, 21661–21664.pmid/9268289
    • (1997) J. Biol. Chem , vol.272 , pp. 21661-21664
    • Hinnebusch, A.G.1
  • 75
    • 0029948606 scopus 로고    scopus 로고
    • Evidence for trehalose 6-phosphate dependent and independent mechanisms in the control of sugar influx into yeast glycolysis
    • pmid/8809751
    • Hohmann, S., Bell, W., Neves, M.J., Valckx, D. and Thevelein, J.M. (1996) Evidence for trehalose 6-phosphate dependent and independent mechanisms in the control of sugar influx into yeast glycolysis. Mol. Microbiol. 20, 981–991.pmid/8809751
    • (1996) Mol. Microbiol , vol.20 , pp. 981-991
    • Hohmann, S.1    Bell, W.2    Neves, M.J.3    Valckx, D.4    Thevelein, J.M.5
  • 76
    • 0031830719 scopus 로고    scopus 로고
    • SNF1 kinase connects nutritional pathways controlling meiosis in Saccharomyces cereviseae
    • pmid/9671464
    • Honigberg, S.M. and Lee, R.H. (1998) SNF1 kinase connects nutritional pathways controlling meiosis in Saccharomyces cereviseae. Mol. Cell. Biol. 18, 4548–4555.pmid/9671464
    • (1998) Mol. Cell. Biol , vol.18 , pp. 4548-4555
    • Honigberg, S.M.1    Lee, R.H.2
  • 78
    • 0027690401 scopus 로고
    • Metabolic regulation of α-amylase gene expression in transgenic cell cultures of rice (Oryza sativa L.)
    • Huang, N., Chandler, J., Thomas, B.R., Koizumi, N. and Rodriguez, R.L. (1993) Metabolic regulation of α-amylase gene expression in transgenic cell cultures of rice (Oryza sativa L.). Plant Molec. Biol. 23, 737–747.
    • (1993) Plant Molec. Biol , vol.23 , pp. 737-747
    • Huang, N.1    Chandler, J.2    Thomas, B.R.3    Koizumi, N.4    Rodriguez, R.L.5
  • 79
    • 0034757497 scopus 로고    scopus 로고
    • Phosphorylation of synthetic peptides by a CDPK and plant SNF1-related protein kinase. Influence of proline and basic amino acid residues at selected positions
    • pmid/11673623
    • Huang, J.Z. and Huber, S.C. (2001) Phosphorylation of synthetic peptides by a CDPK and plant SNF1-related protein kinase. Influence of proline and basic amino acid residues at selected positions. Plant Cell Physiol. 42, 1079–1087.pmid/11673623
    • (2001) Plant Cell Physiol , vol.42 , pp. 1079-1087
    • Huang, J.Z.1    Huber, S.C.2
  • 80
    • 0035960031 scopus 로고    scopus 로고
    • Two-component circuitry in Arabidopsis signal transduction
    • pmid/11574878
    • Hwang, I. and Sheen, J. (2001) Two-component circuitry in Arabidopsis signal transduction. Nature, 413, 383–389.pmid/11574878
    • (2001) Nature , vol.413 , pp. 383-389
    • Hwang, I.1    Sheen, J.2
  • 81
    • 1842376846 scopus 로고    scopus 로고
    • Hexokinase as a sugar sensor in higher plants
    • pmid/9014361
    • Jang, J.-C., Leon, P., Zhou, L. and Sheen, J. (1997) Hexokinase as a sugar sensor in higher plants. Plant Cell, 9, 5–19.pmid/9014361
    • (1997) Plant Cell , vol.9 , pp. 5-19
    • Jang, J.-C.1    Leon, P.2    Zhou, L.3    Sheen, J.4
  • 82
    • 0028534751 scopus 로고
    • Sugar sensing in higher plants
    • pmid/7827498
    • Jang, J.C. and Sheen, J. (1994) Sugar sensing in higher plants. Plant Cell, 6, 1665–1679.pmid/7827498
    • (1994) Plant Cell , vol.6 , pp. 1665-1679
    • Jang, J.C.1    Sheen, J.2
  • 83
    • 0030974632 scopus 로고    scopus 로고
    • Sugar sensing in higher plants
    • Jang, J.C. and Sheen, J. (1997) Sugar sensing in higher plants. Trends Plant Sci. 2, 208–214.
    • (1997) Trends Plant Sci , vol.2 , pp. 208-214
    • Jang, J.C.1    Sheen, J.2
  • 84
    • 0030468365 scopus 로고    scopus 로고
    • Glucose regulates protein interactions within the yeast Snf1 protein kinase complex
    • pmid/8985180
    • Jiang, R. and Carlson, M. (1996) Glucose regulates protein interactions within the yeast Snf1 protein kinase complex. Genes Dev. 10, 3105–3115.pmid/8985180
    • (1996) Genes Dev , vol.10 , pp. 3105-3115
    • Jiang, R.1    Carlson, M.2
  • 85
    • 0030953974 scopus 로고    scopus 로고
    • The Snf1 protein kinase and its activating subunit, Snf4, interact with distinct domains of the Sip1/ Sip2/Gal83 component in the kinase complex
    • pmid/9121458
    • Jiang, R. and Carlson, M. (1997) The Snf1 protein kinase and its activating subunit, Snf4, interact with distinct domains of the Sip1/ Sip2/Gal83 component in the kinase complex. Molec. Cell. Biol. 17, 2099–2106.pmid/9121458
    • (1997) Molec. Cell. Biol , vol.17 , pp. 2099-2106
    • Jiang, R.1    Carlson, M.2
  • 86
    • 0026893753 scopus 로고
    • Metabolic regulation of rice α-amylase and sucrose synthase genes in plants
    • pmid/1344888
    • Karrer, E.E. and Rodriguez, R.L. (1992) Metabolic regulation of rice α-amylase and sucrose synthase genes in plants. Plant J. 2, 517–523.pmid/1344888
    • (1992) Plant J , vol.2 , pp. 517-523
    • Karrer, E.E.1    Rodriguez, R.L.2
  • 87
    • 0033901074 scopus 로고    scopus 로고
    • Functional identification of an Arabidopsis SNF4 orthologue by screening for heterologous multicopy suppressors of snf4 deficiency in yeast
    • pmid/10929106
    • Kleinow, T., Bhalerao, R., Breuer, F., Umeda, M., Salchert, K. and Koncz, C. (2000) Functional identification of an Arabidopsis SNF4 orthologue by screening for heterologous multicopy suppressors of snf4 deficiency in yeast. Plant J. 23, 115–122.pmid/10929106
    • (2000) Plant J , vol.23 , pp. 115-122
    • Kleinow, T.1    Bhalerao, R.2    Breuer, F.3    Umeda, M.4    Salchert, K.5    Koncz, C.6
  • 88
    • 0003329817 scopus 로고
    • Regulation of the expression of rbcS and other photosynthetic genes by carbohydrates: a mechanism for the ‘sink’ regulation of photosynthesis?
    • Krapp, A., Hofmann, B., Schäfer, C. and Stitt, M. (1993) Regulation of the expression of rbcS and other photosynthetic genes by carbohydrates: a mechanism for the ‘sink’ regulation of photosynthesis? Plant J. 3, 817–828.
    • (1993) Plant J , vol.3 , pp. 817-828
    • Krapp, A.1    Hofmann, B.2    Schäfer, C.3    Stitt, M.4
  • 89
    • 0029798141 scopus 로고    scopus 로고
    • The hexose transporter family of Saccharomyces cerevisiae
    • pmid/8929273
    • Kruckeberg, A.L. (1996) The hexose transporter family of Saccharomyces cerevisiae. Arch. Microbiol. 166, 283–292.pmid/8929273
    • (1996) Arch. Microbiol , vol.166 , pp. 283-292
    • Kruckeberg, A.L.1
  • 90
    • 0029093341 scopus 로고
    • High rates of fatty acid oxidation during reperfusion of ischemic hearts are associated with a decrease in malonyl-CoA levels due to an increase in 5′-AMP-activated protein kinase inhibition of acetyl-CoA carboxylase
    • pmid/7615556
    • Kudo, N., Barr, A.J., Barr, R.L., Desai, S. and Lopaschuk, G.D. (1995) High rates of fatty acid oxidation during reperfusion of ischemic hearts are associated with a decrease in malonyl-CoA levels due to an increase in 5′-AMP-activated protein kinase inhibition of acetyl-CoA carboxylase. J. Biol. Chem. 270, 17513–17520.pmid/7615556
    • (1995) J. Biol. Chem , vol.270 , pp. 17513-17520
    • Kudo, N.1    Barr, A.J.2    Barr, R.L.3    Desai, S.4    Lopaschuk, G.D.5
  • 91
    • 0033103452 scopus 로고    scopus 로고
    • Potato StubSNF1 interacts with StubGAL83: a plant protein kinase complex with yeast and mammalian counterparts
    • pmid/10205910
    • Lakatos, L., Klein, M., Hofgen, R. and Banfalvi, Z. (1999) Potato StubSNF1 interacts with StubGAL83: a plant protein kinase complex with yeast and mammalian counterparts. Plant J. 17, 569–574.pmid/10205910
    • (1999) Plant J , vol.17 , pp. 569-574
    • Lakatos, L.1    Klein, M.2    Hofgen, R.3    Banfalvi, Z.4
  • 92
    • 0032720694 scopus 로고    scopus 로고
    • The dual function of plant sugar carriers in transport and in nutrient sensing
    • pmid/10213788
    • Lalonde, S., Boles, E., Hellmann, H., Barker, L., Patrick, J.W., Frommer, W.B. and Ward, J.M. (1999) The dual function of plant sugar carriers in transport and in nutrient sensing. Plant Cell, 11, 707–726.pmid/10213788
    • (1999) Plant Cell , vol.11 , pp. 707-726
    • Lalonde, S.1    Boles, E.2    Hellmann, H.3    Barker, L.4    Patrick, J.W.5    Frommer, W.B.6    Ward, J.M.7
  • 94
    • 0037321018 scopus 로고    scopus 로고
    • Antisense SNF1-related (SnRK1) protein kinase gene represses transient activity of an α-amylase (α-Amy2) gene promoter in cultured wheat embryos
    • pmid/12554717
    • Laurie, S., McKibbin, R.S. and Halford, N.G. (2003) Antisense SNF1-related (SnRK1) protein kinase gene represses transient activity of an α-amylase (α-Amy2) gene promoter in cultured wheat embryos. J. Exp. Bot. 54, 739–747.pmid/12554717
    • (2003) J. Exp. Bot , vol.54 , pp. 739-747
    • Laurie, S.1    McKibbin, R.S.2    Halford, N.G.3
  • 95
    • 0032541083 scopus 로고    scopus 로고
    • The 5′-AMP-activated protein kinase inhibits the transcriptional stimulation by glucose in liver cells, acting through the glucose response complex
    • pmid/9708898
    • Leclerc, I., Mar. Albà, M., Kleinow, T., Koncz, C. and Pagès, M. (1998) The 5′-AMP-activated protein kinase inhibits the transcriptional stimulation by glucose in liver cells, acting through the glucose response complex. FEBS Lett. 431, 180–184.pmid/9708898
    • (1998) FEBS Lett , vol.431 , pp. 180-184
    • Leclerc, I.1    Mar. Albà, M.2    Kleinow, T.3    Koncz, C.4    Pagès, M.5
  • 96
    • 0034724210 scopus 로고    scopus 로고
    • The Arabidopsis thaliana SOS2 gene encodes a protein kinase that is required for salt tolerance
    • pmid/10725382
    • Liu, J., Ishitani, M., Halfter, U., Kim, C.-S. and Shu, J.-K. (2000) The Arabidopsis thaliana SOS2 gene encodes a protein kinase that is required for salt tolerance. Proc. Natl Acad. Sci. USA, 97, 3730–3734.pmid/10725382
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 3730-3734
    • Liu, J.1    Ishitani, M.2    Halfter, U.3    Kim, C.-S.4    Shu, J.-K.5
  • 97
    • 0035093444 scopus 로고    scopus 로고
    • Domain fusion between SNF1-related kinase subunits during plant evolution
    • pmid/11252725
    • Lumbreras, V., Mar. Albà, M., Kleinow, T., Koncz, C. and Pagès, M. (2001) Domain fusion between SNF1-related kinase subunits during plant evolution. EMBO Rep. 2, 55–60.pmid/11252725
    • (2001) EMBO Rep. , vol.2 , pp. 55-60
    • Lumbreras, V.1    Mar. Albà, M.2    Kleinow, T.3    Koncz, C.4    Pagès, M.5
  • 98
    • 0024313495 scopus 로고
    • The residual enzymatic phosphorylation activity of hexokinase II mutants is correlated with glucose repression in Saccharomyces cerevisiae
    • pmid/2685572
    • Ma, H., Bloom, L.M., Walsh, C.T. and Botstein, D. (1989) The residual enzymatic phosphorylation activity of hexokinase II mutants is correlated with glucose repression in Saccharomyces cerevisiae. Mol. Cell. Biol. 9, 5643–5649.pmid/2685572
    • (1989) Mol. Cell. Biol , vol.9 , pp. 5643-5649
    • Ma, H.1    Bloom, L.M.2    Walsh, C.T.3    Botstein, D.4
  • 99
    • 0026440171 scopus 로고
    • Evidence for a protein kinase cascade in higher plants: 3-hydroxy-3-methylglutaryl-CoA reductase kinase
    • pmid/1358611
    • MacKintosh, R.W., Davies, S.P., Clarke, P.R., Weekes, J., Gillespie, J.G., Gibb, B.J. and Hardie, D.G. (1992) Evidence for a protein kinase cascade in higher plants: 3-hydroxy-3-methylglutaryl-CoA reductase kinase. Eur. J. Biochem. 209, 923–931.pmid/1358611
    • (1992) Eur. J. Biochem , vol.209 , pp. 923-931
    • MacKintosh, R.W.1    Davies, S.P.2    Clarke, P.R.3    Weekes, J.4    Gillespie, J.G.5    Gibb, B.J.6    Hardie, D.G.7
  • 100
    • 0031149601 scopus 로고    scopus 로고
    • Potato SNF1-related protein kinase: molecular cloning, expression analysis and peptide kinase activity measurements
    • pmid/9177310
    • Man, A.L., Purcell, P.C., Hannappel, U. and Halford, N.G. (1997) Potato SNF1-related protein kinase: molecular cloning, expression analysis and peptide kinase activity measurements. Plant Mol. Biol. 34, 31–43.pmid/9177310
    • (1997) Plant Mol. Biol , vol.34 , pp. 31-43
    • Man, A.L.1    Purcell, P.C.2    Hannappel, U.3    Halford, N.G.4
  • 101
    • 0033555954 scopus 로고    scopus 로고
    • Crop Scientist seeks a new revolution
    • Mann, G.C. (1999) Crop Scientist seeks a new revolution. Science, 283, 310–314.
    • (1999) Science , vol.283 , pp. 310-314
    • Mann, G.C.1
  • 102
    • 0029257520 scopus 로고
    • Sugar-inducible expression of a gene for β-amylase in Arabidopsis
    • pmid/7716246
    • Mita, S., Suzuki-Fujii, K. and Nakamura, K. (1995) Sugar-inducible expression of a gene for β-amylase in Arabidopsis. Plant Physiol. 107, 895–904.pmid/7716246
    • (1995) Plant Physiol , vol.107 , pp. 895-904
    • Mita, S.1    Suzuki-Fujii, K.2    Nakamura, K.3
  • 103
    • 0027932717 scopus 로고
    • Mammalian AMP-activated protein kinase shares structural and functional homology with the catalytic domain of yeast Snf1 protein kinase
    • pmid/7905477
    • Mitchelhill, K.I., Stapleton, D., Gao, G., House, C., Michell, B., Katsis, F., Witters, L.A. and Kemp, B.E. (1994) Mammalian AMP-activated protein kinase shares structural and functional homology with the catalytic domain of yeast Snf1 protein kinase. J. Biol. Chem. 269, 2361–2364.pmid/7905477
    • (1994) J. Biol. Chem , vol.269 , pp. 2361-2364
    • Mitchelhill, K.I.1    Stapleton, D.2    Gao, G.3    House, C.4    Michell, B.5    Katsis, F.6    Witters, L.A.7    Kemp, B.E.8
  • 104
    • 0025915269 scopus 로고
    • AMP triggers phosphorylation as well as direct allosteric activation of rat liver AMP-activated protein kinase. A sensitive mechanism to protect the cell against ATP depletion
    • pmid/1678349
    • Moore, F., Weekes, J. and Hardie, D.G. (1991) AMP triggers phosphorylation as well as direct allosteric activation of rat liver AMP-activated protein kinase. A sensitive mechanism to protect the cell against ATP depletion. Eur. J. Biochem. 199, 691–697.pmid/1678349
    • (1991) Eur. J. Biochem , vol.199 , pp. 691-697
    • Moore, F.1    Weekes, J.2    Hardie, D.G.3
  • 105
    • 0037432789 scopus 로고    scopus 로고
    • Role of the Arabidopsis glucose sensor HXK1 in nutrient, light and hormonal signalling
    • pmid/12690200
    • Moore, B., Zhou, L., Rolland, F., Hall, Q., Cheng, W.-H., Liu, Y.-X., Hwang, I., Jones, T. and Sheen, J. (2003) Role of the Arabidopsis glucose sensor HXK1 in nutrient, light and hormonal signalling. Science, 300, 332–336.pmid/12690200
    • (2003) Science , vol.300 , pp. 332-336
    • Moore, B.1    Zhou, L.2    Rolland, F.3    Hall, Q.4    Cheng, W.-H.5    Liu, Y.-X.6    Hwang, I.7    Jones, T.8    Sheen, J.9
  • 106
    • 0030250857 scopus 로고    scopus 로고
    • Phosphorylated nitrate reductase from spinach leaves is inhibited by 14-3-3 proteins and activated by fusicoccin
    • pmid/8805370
    • Moorhead, G., Douglas, P., Morrice, N., Scarabel, M., Aitken, A. and MacKintosh, C. (1996) Phosphorylated nitrate reductase from spinach leaves is inhibited by 14-3-3 proteins and activated by fusicoccin. Curr. Biol. 6, 1104–1113.pmid/8805370
    • (1996) Curr. Biol , vol.6 , pp. 1104-1113
    • Moorhead, G.1    Douglas, P.2    Morrice, N.3    Scarabel, M.4    Aitken, A.5    MacKintosh, C.6
  • 107
    • 0031655386 scopus 로고    scopus 로고
    • Trehalose affects sucrose synthase and invertase activities in soybean (Glycine max L. Merr.) roots
    • Muller, J., Boller, T. and Wiemken, A. (1998) Trehalose affects sucrose synthase and invertase activities in soybean (Glycine max L. Merr.) roots. J. Plant Physiol. 153, 255–257.
    • (1998) J. Plant Physiol , vol.153 , pp. 255-257
    • Muller, J.1    Boller, T.2    Wiemken, A.3
  • 108
    • 0028274294 scopus 로고
    • Characterisation of the tobacco protein kinase NPK5, a homologue of Saccharomyces cerevisiae SNF1 that constitutively activates expression of the glucose-repressible SUC2 gene for a secreted invertase of S. cerevisiae
    • pmid/8164654
    • Muranaka, T., Banno, H. and Machida, Y. (1994) Characterisation of the tobacco protein kinase NPK5, a homologue of Saccharomyces cerevisiae SNF1 that constitutively activates expression of the glucose-repressible SUC2 gene for a secreted invertase of S. cerevisiae. Mol. Cell. Biol. 14, 2958–2965.pmid/8164654
    • (1994) Mol. Cell. Biol , vol.14 , pp. 2958-2965
    • Muranaka, T.1    Banno, H.2    Machida, Y.3
  • 109
    • 0034973590 scopus 로고    scopus 로고
    • Transcriptional profiling shows that Gcn4p is a master regulator of gene expression during amino acid starvation in yeast
    • pmid/11390663
    • Natarajan, K., Meyer, M.R., Jackson, B.M., Slade, D., Roberts, C., Hinnebusch, A.G. and Marton, M.J. (2001) Transcriptional profiling shows that Gcn4p is a master regulator of gene expression during amino acid starvation in yeast. Mol. Cell. Biol. 21, 4347–4368.pmid/11390663
    • (2001) Mol. Cell. Biol , vol.21 , 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
  • 110
    • 0033927803 scopus 로고    scopus 로고
    • Reconstitution of ethanolic fermentation in permeabilised spheroplasts of wild type and trehalose 6-phosphate synthase mutants of the yeast Saccharomyces cerevisiae
    • pmid/10880982
    • Noubhani, A., Bunoust, O., Rigoulet, M. and Thevelein, J.M. (2000) Reconstitution of ethanolic fermentation in permeabilised spheroplasts of wild type and trehalose 6-phosphate synthase mutants of the yeast Saccharomyces cerevisiae. Eur. J. Biochem. 267, 4566–4576.pmid/10880982
    • (2000) Eur. J. Biochem , vol.267 , pp. 4566-4576
    • Noubhani, A.1    Bunoust, O.2    Rigoulet, M.3    Thevelein, J.M.4
  • 111
    • 0032519837 scopus 로고    scopus 로고
    • Negative control of the Mig1p repressor by Snf1p-dependent phosphorylation in the absence of glucose
    • pmid/9523726
    • Östling, J. and Ronne, H. (1998) Negative control of the Mig1p repressor by Snf1p-dependent phosphorylation in the absence of glucose. Eur. J. Biochem. 252, 162–168.pmid/9523726
    • (1998) Eur. J. Biochem , vol.252 , pp. 162-168
    • Östling, J.1    Ronne, H.2
  • 112
    • 0029813252 scopus 로고    scopus 로고
    • Two different repressors collaborate to restrict expression of yeast glucose transporter genes HXT2 and HXT4 to low levels of glucose
    • pmid/8816466
    • Ozcan, S. and Johnston, M. (1996) Two different repressors collaborate to restrict expression of yeast glucose transporter genes HXT2 and HXT4 to low levels of glucose. Mol. Cell. Biol. 16, 5536–5545.pmid/8816466
    • (1996) Mol. Cell. Biol , vol.16 , pp. 5536-5545
    • Ozcan, S.1    Johnston, M.2
  • 113
    • 0031910069 scopus 로고    scopus 로고
    • Growth-independent regulation of CLN3 mRNA levels by nutrients in Saccharomyces cerevisiae
    • pmid/9440509
    • Parviz, F. and Heideman, W. (1998) Growth-independent regulation of CLN3 mRNA levels by nutrients in Saccharomyces cerevisiae. J. Bacteriol. 180, 225–230.pmid/9440509
    • (1998) J. Bacteriol , vol.180 , pp. 225-230
    • Parviz, F.1    Heideman, W.2
  • 114
    • 0035209371 scopus 로고    scopus 로고
    • Enhancing photosynthesis with sugar signals
    • pmid/11335171
    • Paul, M.J., Pellny, T. and Goddijn, O. (2001) Enhancing photosynthesis with sugar signals. Trends Plant Sci. 6, 197–200.pmid/11335171
    • (2001) Trends Plant Sci , vol.6 , pp. 197-200
    • Paul, M.J.1    Pellny, T.2    Goddijn, O.3
  • 116
    • 0031861675 scopus 로고    scopus 로고
    • Antisense expression of a sucrose nonfermenting-1-related protein kinase sequence in potato results in decreased expression of sucrose synthase in tubers and loss of sucrose-inducibility of sucrose synthase transcripts in leaves
    • Purcell, P.C., Smith, A.M. and Halford, N.G. (1998) Antisense expression of a sucrose nonfermenting-1-related protein kinase sequence in potato results in decreased expression of sucrose synthase in tubers and loss of sucrose-inducibility of sucrose synthase transcripts in leaves. Plant J. 14, 195–202.
    • (1998) Plant J , vol.14 , pp. 195-202
    • Purcell, P.C.1    Smith, A.M.2    Halford, N.G.3
  • 117
    • 0035985938 scopus 로고    scopus 로고
    • The CLN3/SWI6/CLN2 pathway and SNF1 act sequentially to regulate meiotic initiation in Saccharomyces cerevisiae
    • pmid/12081645
    • Purnapatre, K., Piccirillo, S., Schneider, B.L. and Honigberg, S.M. (2002) The CLN3/SWI6/CLN2 pathway and SNF1 act sequentially to regulate meiotic initiation in Saccharomyces cerevisiae. Genes Cells, 7, 675–691.pmid/12081645
    • (2002) Genes Cells , vol.7 , pp. 675-691
    • Purnapatre, K.1    Piccirillo, S.2    Schneider, B.L.3    Honigberg, S.M.4
  • 118
    • 0032478569 scopus 로고    scopus 로고
    • Hexokinase PII has a double cytosolic-nuclear localisation in Saccharomyces cerevisiae
    • pmid/9563516
    • Randez-Gil, F., Herrero, P., Sanz, P., Prieto, J.A. and Moreno, F. (1998) Hexokinase PII has a double cytosolic-nuclear localisation in Saccharomyces cerevisiae. FEBS Lett. 425, 475–478.pmid/9563516
    • (1998) FEBS Lett , vol.425 , pp. 475-478
    • Randez-Gil, F.1    Herrero, P.2    Sanz, P.3    Prieto, J.A.4    Moreno, F.5
  • 119
    • 0030891998 scopus 로고    scopus 로고
    • Kinetic characterization of individual hexose transporters of Saccharomyces cerevisiae and their relation to the triggering mechanisms of glucose repression
    • pmid/9151960
    • Reifenberger, E., Boles, E. and Ciriacy, M. (1997) Kinetic characterization of individual hexose transporters of Saccharomyces cerevisiae and their relation to the triggering mechanisms of glucose repression. Eur. J. Biochem. 245, 324–333.pmid/9151960
    • (1997) Eur. J. Biochem , vol.245 , pp. 324-333
    • Reifenberger, E.1    Boles, E.2    Ciriacy, M.3
  • 120
    • 0035984056 scopus 로고    scopus 로고
    • Protein–protein interactions between sucrose transporters of different affinities co-localized in the same enucleate sieve element
    • pmid/12119375
    • Reinders, A., Schulze, W., Kühn, C., Barker, L., Schulz, A., Ward, J.M. and Frommer, W.B. (2002) Protein–protein interactions between sucrose transporters of different affinities co-localized in the same enucleate sieve element. Plant Cell, 14, 1567–1577.pmid/12119375
    • (2002) Plant Cell , vol.14 , pp. 1567-1577
    • Reinders, A.1    Schulze, W.2    Kühn, C.3    Barker, L.4    Schulz, A.5    Ward, J.M.6    Frommer, W.B.7
  • 121
    • 0034042485 scopus 로고    scopus 로고
    • Sugar control of the plant cell cycle: differential regulation of Arabidopsis d-type cyclin gene expression
    • pmid/10848578
    • Riou-Khamlichi, C., Menges, M., Healy, J.M.S. and Murray, J.A.H. (2000) Sugar control of the plant cell cycle: differential regulation of Arabidopsis d-type cyclin gene expression. Mol. Cell. Biol. 20, 4513–4521.pmid/10848578
    • (2000) Mol. Cell. Biol , vol.20 , pp. 4513-4521
    • Riou-Khamlichi, C.1    Menges, M.2    Healy, J.M.S.3    Murray, J.A.H.4
  • 122
    • 0035336970 scopus 로고    scopus 로고
    • Glucose-sensing mechanisms in eukaryotic cells
    • pmid/11343924
    • Rolland, F., Winderickx, J. and Thevelein, J.M. (2001) Glucose-sensing mechanisms in eukaryotic cells. Trends Biochem. Sci. 26, 310–317.pmid/11343924
    • (2001) Trends Biochem. Sci , vol.26 , pp. 310-317
    • Rolland, F.1    Winderickx, J.2    Thevelein, J.M.3
  • 123
    • 0037238979 scopus 로고    scopus 로고
    • Genetic approaches to understanding sugar-response pathways
    • pmid/12508060
    • Rook, F. and Bevan, M.W. (2003) Genetic approaches to understanding sugar-response pathways. J. Exp. Bot. 54, 495–501.pmid/12508060
    • (2003) J. Exp. Bot , vol.54 , pp. 495-501
    • Rook, F.1    Bevan, M.W.2
  • 124
    • 0034930631 scopus 로고    scopus 로고
    • Impaired sucrose-induction mutants reveal the modulation of sugar-induced starch biosynthetic gene expression by abscisic acid signalling
    • pmid/11439129
    • Rook, F., Corke, F., Card, R., Munz, G., Smith, C. and Bevan, M.W. (2001) Impaired sucrose-induction mutants reveal the modulation of sugar-induced starch biosynthetic gene expression by abscisic acid signalling. Plant J. 26, 421–433.pmid/11439129
    • (2001) Plant J , vol.26 , pp. 421-433
    • Rook, F.1    Corke, F.2    Card, R.3    Munz, G.4    Smith, C.5    Bevan, M.W.6
  • 125
    • 0025772770 scopus 로고
    • Glucose repression in Saccharomyces cerevisiae is directly associated with hexose phosphorylation by hexokinase PI and PII
    • pmid/1868842
    • Rose, M., Albig, W. and Entian, K.D. (1991) Glucose repression in Saccharomyces cerevisiae is directly associated with hexose phosphorylation by hexokinase PI and PII. Eur. J. Biochem. 199, 511–518.pmid/1868842
    • (1991) Eur. J. Biochem , vol.199 , pp. 511-518
    • Rose, M.1    Albig, W.2    Entian, K.D.3
  • 126
    • 0024787402 scopus 로고
    • The steady-state level of potato sucrose synthase mRNA is dependant on wounding, anaerobiosis and sucrose concentration
    • pmid/2532612
    • Salanoubat, M. and Belliard, G. (1989) The steady-state level of potato sucrose synthase mRNA is dependant on wounding, anaerobiosis and sucrose concentration. Gene, 84, 181–185.pmid/2532612
    • (1989) Gene , vol.84 , pp. 181-185
    • Salanoubat, M.1    Belliard, G.2
  • 127
    • 0027428833 scopus 로고
    • Replacement of Serine-871 of hamster 3-hydroxy-3-methylglutaryl CoA reductase prevents phosphorylation by AMP-activated protein kinase and blocks inhibition of sterol synthesis induced by ATP depletion
    • pmid/8415689
    • Sato, R., Goldstein, J.L. and Brown, M.S. (1993) Replacement of Serine-871 of hamster 3-hydroxy-3-methylglutaryl CoA reductase prevents phosphorylation by AMP-activated protein kinase and blocks inhibition of sterol synthesis induced by ATP depletion. Proc. Natl Acad. Sci. USA, 90, 9261–9265.pmid/8415689
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 9261-9265
    • Sato, R.1    Goldstein, J.L.2    Brown, M.S.3
  • 128
    • 0025171655 scopus 로고
    • Expression of a yeast-derived invertase in the cell wall of tobacco and arabidopsis plants leads to accumulation of carbohydrate and inhibition of photosynthesis and strongly influences growth and phenotype of transgenic tobacco plants
    • pmid/2209536
    • Von Schaewen, A., Stitt, M., Sonnewald, U. and Willmitzer, L. (1990) Expression of a yeast-derived invertase in the cell wall of tobacco and arabidopsis plants leads to accumulation of carbohydrate and inhibition of photosynthesis and strongly influences growth and phenotype of transgenic tobacco plants. EMBO J. 9, 3033–3044.pmid/2209536
    • (1990) EMBO J , vol.9 , pp. 3033-3044
    • Von Schaewen, A.1    Stitt, M.2    Sonnewald, U.3    Willmitzer, L.4
  • 129
    • 0037636377 scopus 로고    scopus 로고
    • Trehalose 6-phosphate is indispensable for carbohydrate utilization and growth in Arabidopsis thaliana
    • pmid/12748379
    • Schluepmann, H., Pellny, T., Van Dijken, A., Smeekens, S. and Paul, M. (2003) Trehalose 6-phosphate is indispensable for carbohydrate utilization and growth in Arabidopsis thaliana. Proc. Natl Acad. Sci. USA, 100, 6849–6854.pmid/12748379
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 6849-6854
    • Schluepmann, H.1    Pellny, T.2    Van Dijken, A.3    Smeekens, S.4    Paul, M.5
  • 130
    • 0025495624 scopus 로고
    • Metabolic repression of transcription in higher plants
    • pmid/2136626
    • Sheen, J. (1990) Metabolic repression of transcription in higher plants. Plant Cell, 2, 1027–1038.pmid/2136626
    • (1990) Plant Cell , vol.2 , pp. 1027-1038
    • Sheen, J.1
  • 131
    • 0001685824 scopus 로고
    • Feedback control of gene expression
    • Sheen, J. (1994) Feedback control of gene expression. Photosynth. Res. 39, 427–438.
    • (1994) Photosynth. Res , vol.39 , pp. 427-438
    • Sheen, J.1
  • 132
    • 0037241454 scopus 로고    scopus 로고
    • Roles of cell-wall invertases and monosaccharide transporters in the growth and development of Arabidopsis
    • pmid/12508063
    • Sherson, S.M., Alford, H.L., Forbes, S.M., Wallace, G. and Smith, S.M. (2003) Roles of cell-wall invertases and monosaccharide transporters in the growth and development of Arabidopsis. J. Exp. Bot. 54, 525–531.pmid/12508063
    • (2003) J. Exp. Bot , vol.54 , pp. 525-531
    • Sherson, S.M.1    Alford, H.L.2    Forbes, S.M.3    Wallace, G.4    Smith, S.M.5
  • 133
    • 0036010843 scopus 로고    scopus 로고
    • Molecular cloning of SnIP1, a novel protein that interacts with SNF1-related protein kinase (SnRK1)
    • pmid/12008897
    • Slocombe, S.P., Laurie, S., Bertini, L., Beaudoin, F., Dickinson, J.R. and Halford, N.G. (2002) Molecular cloning of SnIP1, a novel protein that interacts with SNF1-related protein kinase (SnRK1). Plant Mol. Biol. 49, 31–44.pmid/12008897
    • (2002) Plant Mol. Biol , vol.49 , pp. 31-44
    • Slocombe, S.P.1    Laurie, S.2    Bertini, L.3    Beaudoin, F.4    Dickinson, J.R.5    Halford, N.G.6
  • 135
    • 0001655794 scopus 로고
    • Induction of sucrose synthase in potato tissue culture: Effect of carbon source and metabolic regulators on sink strength
    • Sowokinos, J.R. and Varns, J.L. (1992) Induction of sucrose synthase in potato tissue culture: Effect of carbon source and metabolic regulators on sink strength. J. Plant Physiol. 139, 672–679.
    • (1992) J. Plant Physiol , vol.139 , pp. 672-679
    • Sowokinos, J.R.1    Varns, J.L.2
  • 136
    • 0030095876 scopus 로고    scopus 로고
    • Identification in vitro of a post-translational regulatory site in the hinge 1 region of Arabidopsis nitrate reductase
    • pmid/8721753
    • Su, W., Huber, S.C. and Crawford, N.M. (1996) Identification in vitro of a post-translational regulatory site in the hinge 1 region of Arabidopsis nitrate reductase. Plant Cell, 8, 519–527.pmid/8721753
    • (1996) Plant Cell , vol.8 , pp. 519-527
    • Su, W.1    Huber, S.C.2    Crawford, N.M.3
  • 137
    • 0033180353 scopus 로고    scopus 로고
    • Regulation of spinach SNF1-related (SnRK1) kinases by protein kinases and phosphatases is associated with phosphorylation of the T loop and is regulated by 5′-AMP
    • pmid/10504565
    • Sugden, C., Crawford, R.M., Halford, N.G. and Hardie, D.G. (1999a) Regulation of spinach SNF1-related (SnRK1) kinases by protein kinases and phosphatases is associated with phosphorylation of the T loop and is regulated by 5′-AMP. Plant J. 19, 433–439.pmid/10504565
    • (1999) Plant J , vol.19 , pp. 433-439
    • Sugden, C.1    Crawford, R.M.2    Halford, N.G.3    Hardie, D.G.4
  • 138
    • 0033134243 scopus 로고    scopus 로고
    • Two SNF1-related protein kinases from spinach leaf phosphorylate and inactivate 3-hydroxy-3-methylglutaryl-coenzyme A reductase, nitrate reductase and sucrose phosphate synthase in vitro
    • pmid/10318703
    • Sugden, C., Donaghy, P., Halford, N.G. and Hardie, D.G. (1999b) Two SNF1-related protein kinases from spinach leaf phosphorylate and inactivate 3-hydroxy-3-methylglutaryl-coenzyme A reductase, nitrate reductase and sucrose phosphate synthase in vitro. Plant Physiol. 120, 257–274.pmid/10318703
    • (1999) Plant Physiol , vol.120 , pp. 257-274
    • Sugden, C.1    Donaghy, P.2    Halford, N.G.3    Hardie, D.G.4
  • 139
    • 0034028458 scopus 로고    scopus 로고
    • Source metabolism dominates the control of source to sink carbon flux in tuberising potato plants throughout the diurnal cycle and under a range of environmental conditions
    • Sweetlove, L.J. and Hill, S.A. (2000) Source metabolism dominates the control of source to sink carbon flux in tuberising potato plants throughout the diurnal cycle and under a range of environmental conditions. Plant Cell Environ. 23, 523–529.
    • (2000) Plant Cell Environ , vol.23 , pp. 523-529
    • Sweetlove, L.J.1    Hill, S.A.2
  • 140
    • 0030256014 scopus 로고    scopus 로고
    • Nik1, a Nim1-like protein kinase of S. cerevisiae, interacts with the Cdc28 complex and regulates cell cycle progression
    • pmid/9077450
    • Tanaka, S. and Nojima, H. (1996) Nik1, a Nim1-like protein kinase of S. cerevisiae, interacts with the Cdc28 complex and regulates cell cycle progression. Genes Cells, 1, 905–921.pmid/9077450
    • (1996) Genes Cells , vol.1 , pp. 905-921
    • Tanaka, S.1    Nojima, H.2
  • 141
    • 0028985536 scopus 로고
    • Trehalose synthase: guard to the gate of glycolysis in yeast?
    • pmid/7878741
    • Thevelein, J. and Hohmann, S. (1995) Trehalose synthase: guard to the gate of glycolysis in yeast? Trends Biochem. Sci. 20, 3–10.pmid/7878741
    • (1995) Trends Biochem. Sci , vol.20 , pp. 3-10
    • Thevelein, J.1    Hohmann, S.2
  • 142
    • 0026054752 scopus 로고
    • Deletion of SNF1 affects the nutrient response of yeast and resembles mutations which activate the adenylate cyclase pathway
    • Thompson-Jaeger, S., Francois, J., Gaughran, J.P. and Tatchell, K. (1991) Deletion of SNF1 affects the nutrient response of yeast and resembles mutations which activate the adenylate cyclase pathway. Genetics, 12, 697–706.
    • (1991) Genetics , vol.12 , pp. 697-706
    • Thompson-Jaeger, S.1    Francois, J.2    Gaughran, J.P.3    Tatchell, K.4
  • 143
    • 0035686071 scopus 로고    scopus 로고
    • GLUT2 in pancreatic and extra-pancreatic gluco-detection
    • Thorens, B. (2001) GLUT2 in pancreatic and extra-pancreatic gluco-detection. Mol. Membrane Biol. 18, 265–273.
    • (2001) Mol. Membrane Biol , vol.18 , pp. 265-273
    • Thorens, B.1
  • 144
    • 0036743460 scopus 로고    scopus 로고
    • Starch synthesis in potato tubers is regulated by post-translational redox modification of ADP-glucose pyrophosphorylase: a novel regulatory mechanism linking starch synthesis to the sucrose supply
    • pmid/12215515
    • Tiessen, A., Hendriks, J.H.M., Stitt, M., Branscheid, A., Gibon, Y., Farre, E.M. and Geigenberger, P. (2002) Starch synthesis in potato tubers is regulated by post-translational redox modification of ADP-glucose pyrophosphorylase: a novel regulatory mechanism linking starch synthesis to the sucrose supply. Plant Cell, 14, 2191–2213.pmid/12215515
    • (2002) Plant Cell , vol.14 , pp. 2191-2213
    • Tiessen, A.1    Hendriks, J.H.M.2    Stitt, M.3    Branscheid, A.4    Gibon, Y.5    Farre, E.M.6    Geigenberger, P.7
  • 145
    • 0042352390 scopus 로고    scopus 로고
    • Evidence that SNF1 related kinase and hexokinase are involved in separate sugar signalling pathways modulating posttranslational redox activation of ADP-glucose pyrophosphorylase in potato tubers
    • pmid/12904211
    • Tiessen, A., Prescha, K., Branscheid, A., Palacios, N., McKibbin, R., Halford, N.G. and Geigenberger, P. (2003) Evidence that SNF1 related kinase and hexokinase are involved in separate sugar signalling pathways modulating posttranslational redox activation of ADP-glucose pyrophosphorylase in potato tubers. Plant J., 35, 490–500.pmid/12904211
    • (2003) Plant J , vol.35 , pp. 490-500
    • Tiessen, A.1    Prescha, K.2    Branscheid, A.3    Palacios, N.4    McKibbin, R.5    Halford, N.G.6    Geigenberger, P.7
  • 146
    • 0034073253 scopus 로고    scopus 로고
    • Regulation of a plant SNF1-related protein kinase by glucose-6-phosphate
    • pmid/10806257
    • Toroser, D., Plaut, Z. and Huber, S.C. (2000) Regulation of a plant SNF1-related protein kinase by glucose-6-phosphate. Plant Physiol. 123, 403–411.pmid/10806257
    • (2000) Plant Physiol , vol.123 , pp. 403-411
    • Toroser, D.1    Plaut, Z.2    Huber, S.C.3
  • 147
    • 0032077442 scopus 로고    scopus 로고
    • The danger of metabolic pathways with turbo design
    • pmid/9612078
    • Teusink, B., Walsh, M.C., Van Dam, K. and Westerhoff, H.V. (1998) The danger of metabolic pathways with turbo design. Trends Biochem. Sci. 23, 162–169.pmid/9612078
    • (1998) Trends Biochem. Sci , vol.23 , pp. 162-169
    • Teusink, B.1    Walsh, M.C.2    Van Dam, K.3    Westerhoff, H.V.4
  • 149
    • 0017404565 scopus 로고
    • Characterisation of a regulatory mutant of fructose 1,6-bisphosphate in Saccharomyces carlsbergensis
    • Van de Poll, K.W. and Schamhart, D. (1974) Characterisation of a regulatory mutant of fructose 1,6-bisphosphate in Saccharomyces carlsbergensis. Mol. Gen. Genet. 154, 61–66.
    • (1974) Mol. Gen. Genet , vol.154 , pp. 61-66
    • Van de Poll, K.W.1    Schamhart, D.2
  • 150
    • 0029981144 scopus 로고    scopus 로고
    • 2 through feedback regulation of gene expression: climate of opinion
    • 2 through feedback regulation of gene expression: climate of opinion. Photosynth. Res. 48, 353–365.
    • (1996) Photosynth. Res , vol.48 , pp. 353-365
    • Van Oosten, J.-J.1    Besford, R.T.2
  • 151
    • 0030161090 scopus 로고    scopus 로고
    • Sucrose metabolism during cotyledon development of Vicia faba L. is controlled by the concerted action of both sucrose phosphate synthase and sucrose synthase: expression patterns, metabolic regulation and implications for seed development
    • pmid/8696364
    • Weber, H., Buchner, P., Borisjuk, L. and Wobus, U. (1996) Sucrose metabolism during cotyledon development of Vicia faba L. is controlled by the concerted action of both sucrose phosphate synthase and sucrose synthase: expression patterns, metabolic regulation and implications for seed development. Plant J. 9, 841–850.pmid/8696364
    • (1996) Plant J , vol.9 , pp. 841-850
    • Weber, H.1    Buchner, P.2    Borisjuk, L.3    Wobus, U.4
  • 152
    • 0027440990 scopus 로고
    • Specificity determinants for the AMP-activated protein kinase and its plant homologue analyzed using synthetic peptides
    • pmid/7902296
    • Weekes, J., Ball, K.L., Caudwell, F.B. and Hardie, D.G. (1993) Specificity determinants for the AMP-activated protein kinase and its plant homologue analyzed using synthetic peptides. FEBS Lett. 334, 335–339.pmid/7902296
    • (1993) FEBS Lett , vol.334 , pp. 335-339
    • Weekes, J.1    Ball, K.L.2    Caudwell, F.B.3    Hardie, D.G.4
  • 153
    • 0033823573 scopus 로고    scopus 로고
    • A new subfamily of sucrose transporters, SUT4, with low affinity/high capacity localized in enucleate sieve elements of plants
    • pmid/10948254
    • Weise, A., Barker, L., Kühn, C., Lalonde, S., Buschmann, H., Frommer, W.B. and Ward, J.M. (2000) A new subfamily of sucrose transporters, SUT4, with low affinity/high capacity localized in enucleate sieve elements of plants. Plant Cell, 12, 1345–1355.pmid/10948254
    • (2000) Plant Cell , vol.12 , pp. 1345-1355
    • Weise, A.1    Barker, L.2    Kühn, C.3    Lalonde, S.4    Buschmann, H.5    Frommer, W.B.6    Ward, J.M.7
  • 154
    • 0030293885 scopus 로고    scopus 로고
    • The mechanism of glucose repression/derepression in yeast: SNF1 protein kinase is activated by phosphorylation under derepressing conditions, and this correlates with a high AMP: ATP ratio
    • pmid/8939604
    • Wilson, W.A., Hawley, S.A. and Hardie, D.G. (1996) The mechanism of glucose repression/derepression in yeast: SNF1 protein kinase is activated by phosphorylation under derepressing conditions, and this correlates with a high AMP: ATP ratio. Curr. Biol. 6, 1426–1434.pmid/8939604
    • (1996) Curr. Biol , vol.6 , pp. 1426-1434
    • Wilson, W.A.1    Hawley, S.A.2    Hardie, D.G.3
  • 155
    • 0029978799 scopus 로고    scopus 로고
    • Inactivation of acetyl-CoA carboxylase and activation of AMP-activated protein kinase in muscle during exercise
    • pmid/8779952
    • Winder, W.W. and Hardie, D.G. (1996) Inactivation of acetyl-CoA carboxylase and activation of AMP-activated protein kinase in muscle during exercise. Am. J. Physiol. 270, E299–E304.pmid/8779952
    • (1996) Am. J. Physiol , vol.270 , pp. E299-E304
    • Winder, W.W.1    Hardie, D.G.2
  • 156
    • 0033825641 scopus 로고    scopus 로고
    • Trehalose induces the ADP-glucose pyrophosphorylase gene, ApL3, and starch synthesis in Arabidopsis
    • pmid/10982426
    • Wingler, A., Fritzius, T., Wiemken, A., Boller, T. and Aeschbacher, R.A. (2000) Trehalose induces the ADP-glucose pyrophosphorylase gene, ApL3, and starch synthesis in Arabidopsis. Plant Physiol. 124, 105–114.pmid/10982426
    • (2000) Plant Physiol , vol.124 , pp. 105-114
    • Wingler, A.1    Fritzius, T.2    Wiemken, A.3    Boller, T.4    Aeschbacher, R.A.5
  • 157
    • 0031760039 scopus 로고    scopus 로고
    • Regulation of leaf senescence by cytokinin, sugars and light. Effects on NADH-dependent hdroxypyruvate reductase
    • Wingler, A., Von Schaewen, A., Leegood, R.C., Lea, P.J. and Quick, W.P. (1998) Regulation of leaf senescence by cytokinin, sugars and light. Effects on NADH-dependent hdroxypyruvate reductase. Plant Physiol. 116, 329–335.
    • (1998) Plant Physiol , vol.116 , pp. 329-335
    • Wingler, A.1    Von Schaewen, A.2    Leegood, R.C.3    Lea, P.J.4    Quick, W.P.5
  • 158
    • 0026350712 scopus 로고
    • Regulation of intracellular acetyl-CoA carboxylase by ATP depletors mimics the action of the 5′-AMP-activated protein kinase
    • pmid/1684896
    • Witters, L.A., Nordlund, A.C. and Marshall, L. (1991) Regulation of intracellular acetyl-CoA carboxylase by ATP depletors mimics the action of the 5′-AMP-activated protein kinase. Biochem. Biophys. Res. Commun. 181, 1486–1492.pmid/1684896
    • (1991) Biochem. Biophys. Res. Commun , vol.181 , pp. 1486-1492
    • Witters, L.A.1    Nordlund, A.C.2    Marshall, L.3
  • 159
    • 0033815967 scopus 로고    scopus 로고
    • Characterization of the role of AMP-activated protein kinase in the regulation of glucose-activated gene expression using constitutively active and dominant negative forms of the kinase
    • pmid/10958668
    • Woods, A., Azzout-Marniche, D., Foretz, M., Stein, S.C., Lemarchand, P., Ferre, P., Foufelle, F. and Carling, D. (2000) Characterization of the role of AMP-activated protein kinase in the regulation of glucose-activated gene expression using constitutively active and dominant negative forms of the kinase. Mol. Cell. Biol. 20, 6704–6711.pmid/10958668
    • (2000) Mol. Cell. Biol , vol.20 , pp. 6704-6711
    • Woods, A.1    Azzout-Marniche, D.2    Foretz, M.3    Stein, S.C.4    Lemarchand, P.5    Ferre, P.6    Foufelle, F.7    Carling, D.8
  • 160
    • 0029925785 scopus 로고    scopus 로고
    • Characterisation of AMP-activated protein kinase β and γ subunits: assembly of the heterotrimeric complex in vitro
    • pmid/8626596
    • Woods, A., Cheung, P.C.F., Smith, F.C., Davison, M.D., Scott, J., Beri, R.K. and Carling, D. (1996) Characterisation of AMP-activated protein kinase β and γ subunits: assembly of the heterotrimeric complex in vitro. J. Biol. Chem. 271, 10282–10290.pmid/8626596
    • (1996) J. Biol. Chem , vol.271 , pp. 10282-10290
    • Woods, A.1    Cheung, P.C.F.2    Smith, F.C.3    Davison, M.D.4    Scott, J.5    Beri, R.K.6    Carling, D.7
  • 161
    • 0028070457 scopus 로고
    • Yeast SNF1 is functionally related to mammalian AMP-activated protein kinase and regulates acetyl-CoA carboxylase in vivo
    • pmid/7913470
    • Woods, A., Munday, M.R., Scott, J., Yang, X., Carlson, M. and Carling, D. (1994) Yeast SNF1 is functionally related to mammalian AMP-activated protein kinase and regulates acetyl-CoA carboxylase in vivo. J. Biol. Chem. 269, 19509–19515.pmid/7913470
    • (1994) J. Biol. Chem , vol.269 , pp. 19509-19515
    • Woods, A.1    Munday, M.R.2    Scott, J.3    Yang, X.4    Carlson, M.5    Carling, D.6
  • 162
    • 0028559507 scopus 로고
    • A family of proteins containing a conserved domain that mediates interaction with the yeast Snf1 protein kinase complex
    • pmid/7813428
    • Yang, X., Jiang, R. and Carlson, M. (1994) A family of proteins containing a conserved domain that mediates interaction with the yeast Snf1 protein kinase complex. EMBO J. 13, 5878–5886.pmid/7813428
    • (1994) EMBO J , vol.13 , pp. 5878-5886
    • Yang, X.1    Jiang, R.2    Carlson, M.3
  • 163
    • 0034028905 scopus 로고    scopus 로고
    • Glucose limitation induces GCN4 translation by activation of gcn2 protein kinase
    • pmid/10733573
    • Yang, R.J., Wek, S.A. and Wek, R.C. (2000) Glucose limitation induces GCN4 translation by activation of gcn2 protein kinase. Mol. Cell. Biol. 20, 2706–2717.pmid/10733573
    • (2000) Mol. Cell. Biol , vol.20 , pp. 2706-2717
    • Yang, R.J.1    Wek, S.A.2    Wek, R.C.3
  • 164
    • 0025718505 scopus 로고
    • Metabolic derepression of α-amylase gene expression in suspension-cultured cells of rice
    • pmid/1939156
    • Yu, S.-M., Kuo, Y.-H., Sheu, G., Sheu, Y.-J. and Liu, L.-F. (1991) Metabolic derepression of α-amylase gene expression in suspension-cultured cells of rice. J. Biol. Chem. 266, 21131–21137.pmid/1939156
    • (1991) J. Biol. Chem , vol.266 , pp. 21131-21137
    • Yu, S.-M.1    Kuo, Y.-H.2    Sheu, G.3    Sheu, Y.-J.4    Liu, L.-F.5
  • 165
    • 0042352484 scopus 로고    scopus 로고
    • Molecular cloning of an arabidopsis homologue of GCN2, a protein kinase involved in co-ordinated response to amino acid starvation
    • Zhang, Y., Dickinson, J.R., Paul, M.J. and Halford, N.G. (2003) Molecular cloning of an arabidopsis homologue of GCN2, a protein kinase involved in co-ordinated response to amino acid starvation. Planta, DOI: 10.1007/s00425-003-1025–4.
    • (2003) Planta
    • Zhang, Y.1    Dickinson, J.R.2    Paul, M.J.3    Halford, N.G.4
  • 166
    • 0035543420 scopus 로고    scopus 로고
    • Expression of antisense SnRK1 protein kinase sequence causes abnormal pollen development and male sterility in transgenic barley
    • pmid/11737780
    • Zhang, Y., Shewry, P.R., Jones, H., Barcelo, P., Lazzeri, P.A. and Halford, N.G. (2001) Expression of antisense SnRK1 protein kinase sequence causes abnormal pollen development and male sterility in transgenic barley. Plant J. 28, 431–442.pmid/11737780
    • (2001) Plant J , vol.28 , pp. 431-442
    • Zhang, Y.1    Shewry, P.R.2    Jones, H.3    Barcelo, P.4    Lazzeri, P.A.5    Halford, N.G.6
  • 167
    • 0029107792 scopus 로고
    • Evidence of the crucial role of sucrose synthase for sink strength using transgenic potato plants (Solanum tuberosum L.)
    • pmid/7894514
    • Zrenner, R., Salanoubat, M., Willmitzer, L. and Sonnewald, U. (1995) Evidence of the crucial role of sucrose synthase for sink strength using transgenic potato plants (Solanum tuberosum L.). Plant J. 7, 97–107.pmid/7894514
    • (1995) Plant J , vol.7 , pp. 97-107
    • Zrenner, R.1    Salanoubat, M.2    Willmitzer, L.3    Sonnewald, U.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.