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Volumn 118, Issue 4, 1997, Pages 1103-1114

Glycolytic controls in estivation and anoxia: A comparison of metabolic arrest in land and marine molluscs

Author keywords

Enzyme phosphorylation; Glycolysis; Metabolic arrest; Metabolic depression

Indexed keywords

ADAPTATION; ANOXIA; BINDING AFFINITY; CELL SURVIVAL; EFFECTOR CELL; ENZYME PHOSPHORYLATION; ENZYME SUBSTRATE; GLYCOLYSIS; METABOLIC INHIBITION; METABOLIC RATE; METABOLIC REGULATION; MOLLUSC; NONHUMAN; PRIORITY JOURNAL; REVIEW;

EID: 0031425659     PISSN: 03009629     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-9629(97)00237-5     Document Type: Review
Times cited : (120)

References (88)
  • 1
    • 0000817680 scopus 로고
    • Respiratory gas tensions and gas exchange in active and dormant land snails, Otala lactea
    • Barnhart, M.C. Respiratory gas tensions and gas exchange in active and dormant land snails, Otala lactea. Physiol. Zool. 59: 733-745;1986.
    • (1986) Physiol. Zool. , vol.59 , pp. 733-745
    • Barnhart, M.C.1
  • 2
    • 0001330271 scopus 로고
    • Discontinuous carbon dioxide release and metabolic depression in dormant land snails
    • Barnhart, M.C.; McMahon, B.R. Discontinuous carbon dioxide release and metabolic depression in dormant land snails. J. Exp. Biol. 128:123-138;1987.
    • (1987) J. Exp. Biol. , vol.128 , pp. 123-138
    • Barnhart, M.C.1    McMahon, B.R.2
  • 3
    • 0024253227 scopus 로고
    • Multiple isozymes of cyclic nucleotide phosphodiesterase
    • Greengard, P.; Robinson, G.A. (eds). New York: Raven Press
    • Beavo, J.A. Multiple isozymes of cyclic nucleotide phosphodiesterase. In: Greengard, P.; Robinson, G.A. (eds). Advances in Second Messenger and Phosphoprotein Research. New York: Raven Press; 1988:1-35.
    • (1988) Advances in Second Messenger and Phosphoprotein Research , pp. 1-35
    • Beavo, J.A.1
  • 5
    • 0025342803 scopus 로고
    • Cycle AMP as a modulator of NaCl transport in gills of the euryhaline Chinese crab Eriocheir sinensis
    • Bianchini, A.; Gilles, R. Cycle AMP as a modulator of NaCl transport in gills of the euryhaline Chinese crab Eriocheir sinensis. Marine Biol. 104:191-195;1990.
    • (1990) Marine Biol. , vol.104 , pp. 191-195
    • Bianchini, A.1    Gilles, R.2
  • 6
    • 0027199345 scopus 로고
    • Inhibition of brain calcium channels by plasma proteins from anoxic turtles
    • Bickler, P.E.; Gallego, S.M. Inhibition of brain calcium channels by plasma proteins from anoxic turtles. Am. J. Physiol265:R277-R281;1993.
    • (1993) Am. J. Physiol , vol.265
    • Bickler, P.E.1    Gallego, S.M.2
  • 7
    • 0025776217 scopus 로고
    • Inactivation of 6-phosphofructo-2-kinase during anaerobiosis in the marine whelk Busycon canaliculatum
    • Bosca, L.; Storey, K.B. Inactivation of 6-phosphofructo-2-kinase during anaerobiosis in the marine whelk Busycon canaliculatum. Am. J. Physiol. 260:R1168-R1175;1991.
    • (1991) Am. J. Physiol. , vol.260
    • Bosca, L.1    Storey, K.B.2
  • 8
    • 0024282507 scopus 로고
    • Anoxic brain function: Molecular mechanisms of metabolic depression
    • Brooks, S.P.J.; Storey, K.B. Anoxic brain function: Molecular mechanisms of metabolic depression. FEBS Lett. 232:214-216;1988a.
    • (1988) FEBS Lett. , vol.232 , pp. 214-216
    • Brooks, S.P.J.1    Storey, K.B.2
  • 9
    • 0023710694 scopus 로고
    • Subcellular enzyme binding in glycolytic control: In vivo studies with fish muscle
    • Brooks, S.P.J.; Storey, K.B. Subcellular enzyme binding in glycolytic control: in vivo studies with fish muscle. Am. J. Physiol. 255:R289-R294;1988b.
    • (1988) Am. J. Physiol. , vol.255
    • Brooks, S.P.J.1    Storey, K.B.2
  • 10
    • 13144255420 scopus 로고    scopus 로고
    • Regulation of glycolytic enzymes during anoxia in the turtle Pseudemys scripta
    • Brooks, S.P.J.; Storey, K.B. Regulation of glycolytic enzymes during anoxia in the turtle Pseudemys scripta. Am. J. Physiol. 257:R278-R283.
    • Am. J. Physiol. , vol.257
    • Brooks, S.P.J.1    Storey, K.B.2
  • 11
    • 0343247532 scopus 로고
    • Influence of hormones, second messengers and pH on the expression of metabolic responses to anoxia in a marine whelk
    • Brooks, S.P.J.; Storey, K.B. Influence of hormones, second messengers and pH on the expression of metabolic responses to anoxia in a marine whelk. J. Exp. Biol. 145:31-43;1989.
    • (1989) J. Exp. Biol. , vol.145 , pp. 31-43
    • Brooks, S.P.J.1    Storey, K.B.2
  • 12
    • 0025046194 scopus 로고
    • Glycolytic enzyme binding and metabolic control in estivation and anoxia in the land snail Otala lactea
    • Brooks, S.P.J.; Storey, K.B. Glycolytic enzyme binding and metabolic control in estivation and anoxia in the land snail Otala lactea. J. Exp. Biol. 151:193-204;1990.
    • (1990) J. Exp. Biol. , vol.151 , pp. 193-204
    • Brooks, S.P.J.1    Storey, K.B.2
  • 13
    • 0025130389 scopus 로고
    • cGMP-stimulated protein kinase phosphorylates pyruvate kinase in an anoxia-tolerant marine mollusc
    • Brooks, S.P.J.; Storey, K.B. cGMP-stimulated protein kinase phosphorylates pyruvate kinase in an anoxia-tolerant marine mollusc. J. Comp. Physiol. 160B:309-316;1990.
    • (1990) J. Comp. Physiol. , vol.160 B , pp. 309-316
    • Brooks, S.P.J.1    Storey, K.B.2
  • 14
    • 0025957990 scopus 로고    scopus 로고
    • Where is the glycolytic complex? A critical evaluation of present data from muscle tissues
    • Brooks, S.P.J.; Storey, K.B. Where is the glycolytic complex? A critical evaluation of present data from muscle tissues. FEBS Lett. 278:135-138.
    • FEBS Lett. , vol.278 , pp. 135-138
    • Brooks, S.P.J.1    Storey, K.B.2
  • 15
    • 0025971230 scopus 로고
    • The role of protein kinases in anoxia tolerance in facultative anaerobes: Purification and characterization of a protein kinase that phosphorylates pyruvate kinase
    • Brooks, S.P.J.; Storey, K.B. The role of protein kinases in anoxia tolerance in facultative anaerobes: Purification and characterization of a protein kinase that phosphorylates pyruvate kinase. Biochim. Biophys. Acta 1073:253-259;1991.
    • (1991) Biochim. Biophys. Acta , vol.1073 , pp. 253-259
    • Brooks, S.P.J.1    Storey, K.B.2
  • 16
    • 0003110036 scopus 로고
    • Mechanisms of glycolytic control during hibernation in the ground squirrel Spermophilus lateralls
    • Brooks, S.P.J.; Storey, K.B. Mechanisms of glycolytic control during hibernation in the ground squirrel Spermophilus lateralls. J. Comp. Physiol. 162B:23-28;1992.
    • (1992) J. Comp. Physiol. , vol.162 B , pp. 23-28
    • Brooks, S.P.J.1    Storey, K.B.2
  • 17
    • 0000669664 scopus 로고
    • Properties of pyruvate dehydrogenase from the land snail, Otala lactea: Control of enzyme activity during estivation
    • Brooks, S.P.J.; Storey, K.B. Properties of pyruvate dehydrogenase from the land snail, Otala lactea: Control of enzyme activity during estivation. Physiol. Zool. 65:620-633;1992.
    • (1992) Physiol. Zool. , vol.65 , pp. 620-633
    • Brooks, S.P.J.1    Storey, K.B.2
  • 18
    • 0028500931 scopus 로고
    • Metabolic depression in land snails: In vitro analysis of protein kinase involvement in pyruvate kinase control in isolated Otala lactea tissues
    • Brooks, S.P.J.; Storey, K.B. Metabolic depression in land snails: In vitro analysis of protein kinase involvement in pyruvate kinase control in isolated Otala lactea tissues. J. Exp. Zool. 269:507-514;1994a.
    • (1994) J. Exp. Zool. , vol.269 , pp. 507-514
    • Brooks, S.P.J.1    Storey, K.B.2
  • 19
    • 0027948837 scopus 로고
    • Patterns of protein synthesis and phosphorylation during anoxia in the land snail Otala lactea
    • Brooks, S.P.J.; Storey, K.B. Patterns of protein synthesis and phosphorylation during anoxia in the land snail Otala lactea. Can. J. Zool. 72:856-862;1994.
    • (1994) Can. J. Zool. , vol.72 , pp. 856-862
    • Brooks, S.P.J.1    Storey, K.B.2
  • 20
    • 0028966768 scopus 로고
    • Protein phosphorylation patterns during aestivation in the land snail Otala lactea
    • Brooks, S.P.J.; Storey, K.B. Protein phosphorylation patterns during aestivation in the land snail Otala lactea. Mol. Cell. Biochem. 143:7-13;1995.
    • (1995) Mol. Cell. Biochem. , vol.143 , pp. 7-13
    • Brooks, S.P.J.1    Storey, K.B.2
  • 21
    • 0000926765 scopus 로고
    • Differential survival of Venus gallina and Scapharca inaequivalvis during anoxic stress: Covalent modification ot phosphofructokinase and glycogen phosphorylase during anoxia
    • Brooks, S.P.J.; de Zwaan, A.; van den Thillart, G.; Cattani, O.; Cortesi, P.; Storey, K.B. Differential survival of Venus gallina and Scapharca inaequivalvis during anoxic stress: covalent modification ot phosphofructokinase and glycogen phosphorylase during anoxia. J. Comp. Physiol. 161B:207-212;1991.
    • (1991) J. Comp. Physiol. , vol.161 B , pp. 207-212
    • Brooks, S.P.J.1    De Zwaan, A.2    Van Den Thillart, G.3    Cattani, O.4    Cortesi, P.5    Storey, K.B.6
  • 22
    • 0027484140 scopus 로고
    • Anoxic suppression of Na/K ATPase and constant membrane potential in hepatocytes: Support for channel arrest
    • Buck, L.T.; Hochachka, P.W. Anoxic suppression of Na/K ATPase and constant membrane potential in hepatocytes: Support for channel arrest. Am. J. Physiol. 265:R1020-R1025;1993.
    • (1993) Am. J. Physiol. , vol.265
    • Buck, L.T.1    Hochachka, P.W.2
  • 23
    • 0025807890 scopus 로고
    • Quantification of ATP-producing and consuming processes in quiescent pig spleen lymphocytes
    • Buttgereit, F.; Muller, M.; Rapoport, S.M. Quantification of ATP-producing and consuming processes in quiescent pig spleen lymphocytes. Biochem. Int. 24:59-67;1991.
    • (1991) Biochem. Int. , vol.24 , pp. 59-67
    • Buttgereit, F.1    Muller, M.2    Rapoport, S.M.3
  • 24
    • 0000290117 scopus 로고
    • Intermediary energy metabolism during dormancy and anoxia in the land snail Otala lactea
    • Churchill, T.A.; Storey, K.B. Intermediary energy metabolism during dormancy and anoxia in the land snail Otala lactea. Physiol. Zool. 62:1015-1030;1989.
    • (1989) Physiol. Zool. , vol.62 , pp. 1015-1030
    • Churchill, T.A.1    Storey, K.B.2
  • 25
    • 0019324511 scopus 로고
    • Effect of electrical stimulation post-mortem of bovine muscle on the binding of glycolytic enzymes
    • Clarke, P.M.; Shaw, F.D.; Morton, D.J. Effect of electrical stimulation post-mortem of bovine muscle on the binding of glycolytic enzymes. Biochem. J. 186:105-109;1980.
    • (1980) Biochem. J. , vol.186 , pp. 105-109
    • Clarke, P.M.1    Shaw, F.D.2    Morton, D.J.3
  • 26
    • 0021321626 scopus 로고
    • Metabolic dependence of glycolytic enzyme binding in rat and sheep heart
    • Clarke, F.M.; Stephan, P.; Huxham, G.; Hamilton, D.; Morton, D.J. Metabolic dependence of glycolytic enzyme binding in rat and sheep heart. Eur. J. Biochem. 138:643-649;1984.
    • (1984) Eur. J. Biochem. , vol.138 , pp. 643-649
    • Clarke, F.M.1    Stephan, P.2    Huxham, G.3    Hamilton, D.4    Morton, D.J.5
  • 27
    • 0023546694 scopus 로고
    • Hormonal regulation of fluxes through pyruvate dehydrogenase and the citric acid cycle in mammalian tissues
    • Denton, R.M.; McCormack, J.G.; Midgley, P.J.W.; Rutter, G.A. Hormonal regulation of fluxes through pyruvate dehydrogenase and the citric acid cycle in mammalian tissues. Biochem. Soc. Symp. 54:127-143;1987.
    • (1987) Biochem. Soc. Symp. , vol.54 , pp. 127-143
    • Denton, R.M.1    McCormack, J.G.2    Midgley, P.J.W.3    Rutter, G.A.4
  • 29
    • 0013604875 scopus 로고
    • Role of enzyme binding in muscle metabolism of the goldfish
    • Duncan, J.A.; Storey, K.B. Role of enzyme binding in muscle metabolism of the goldfish. Can. J. Zool. 69:1571-1576;1991.
    • (1991) Can. J. Zool. , vol.69 , pp. 1571-1576
    • Duncan, J.A.1    Storey, K.B.2
  • 30
    • 0026522118 scopus 로고
    • Subcellular enzyme binding and the regulation of glycolysis in anoxic turtle brain
    • Duncan, J.A.; Storey, K.B. Subcellular enzyme binding and the regulation of glycolysis in anoxic turtle brain. Am. J. Physiol. 262:R517-R523;1992.
    • (1992) Am. J. Physiol. , vol.262
    • Duncan, J.A.1    Storey, K.B.2
  • 31
    • 13144270947 scopus 로고
    • Phosphorus nuclear magnetic resonance studies of energy metabolism in molluscan tissues
    • Ellington, W.R. Phosphorus nuclear magnetic resonance studies of energy metabolism in molluscan tissues. J. Comp. Physiol. 137:165-171;1983.
    • (1983) J. Comp. Physiol. , vol.137 , pp. 165-171
    • Ellington, W.R.1
  • 32
    • 84986505520 scopus 로고
    • The extent of intracellular acidification during anoxia in the catch muscles of two bivalve molluscs
    • Ellington, W.R. The extent of intracellular acidification during anoxia in the catch muscles of two bivalve molluscs. J. Exp. Zool. 227:313-317;1983.
    • (1983) J. Exp. Zool. , vol.227 , pp. 313-317
    • Ellington, W.R.1
  • 33
    • 0024248684 scopus 로고
    • Tissue-specific biochemical responses during anoxia and recovery in the channelled whelk
    • Eberlee, J.C.; Storey, K.B. Tissue-specific biochemical responses during anoxia and recovery in the channelled whelk. J. Exp. Mar. Biol. Ecol. 121:165-176;1988.
    • (1988) J. Exp. Mar. Biol. Ecol. , vol.121 , pp. 165-176
    • Eberlee, J.C.1    Storey, K.B.2
  • 35
    • 0025606551 scopus 로고
    • Time-course of covalent modification of pyruvate kinase during anaerobiosis in the mantle muscle and the hepatopancreas of the limpet Patella caerulea (L.)
    • Gaitanaki, C.; Papadopoulos, A.; Beis, I. Time-course of covalent modification of pyruvate kinase during anaerobiosis in the mantle muscle and the hepatopancreas of the limpet Patella caerulea (L.). J. Comp. Physiol. 160B:529-535;1990.
    • (1990) J. Comp. Physiol. , vol.160 B , pp. 529-535
    • Gaitanaki, C.1    Papadopoulos, A.2    Beis, I.3
  • 37
    • 0001571454 scopus 로고
    • Anaerobic dormancy quantified in Anemia embryos: A calorimetric test of the control mechanism
    • Hand, S.C.; Gnaiger, E. Anaerobic dormancy quantified in Anemia embryos: A calorimetric test of the control mechanism. Science 239:1425-1427;1988.
    • (1988) Science , vol.239 , pp. 1425-1427
    • Hand, S.C.1    Gnaiger, E.2
  • 38
    • 0016170049 scopus 로고
    • Intracellular actions of 5-hydroxytryptamine on the bivalve myocardium-II. Cyclic nucleotide-dependent protein kinase and microsomal calcium uptake
    • Higgins, W.J.; Greenberg, M.J. Intracellular actions of 5-hydroxytryptamine on the bivalve myocardium-II. Cyclic nucleotide-dependent protein kinase and microsomal calcium uptake. J. Exp. Zool. 190:305-316;1974.
    • (1974) J. Exp. Zool. , vol.190 , pp. 305-316
    • Higgins, W.J.1    Greenberg, M.J.2
  • 39
    • 0343432413 scopus 로고
    • Regulation of pyruvate kinase and phosphoenolpyruvate carboxykinase activity during anaerobiosis in Mytitus edulis L
    • Holwerda, D.A.; Druitwagen, E.C.J.; de Bont, A.M.Th. Regulation of pyruvate kinase and phosphoenolpyruvate carboxykinase activity during anaerobiosis in Mytitus edulis L. Mol. Physiol. 1:165-171;1981.
    • (1981) Mol. Physiol. , vol.1 , pp. 165-171
    • Holwerda, D.A.1    Druitwagen, E.C.J.2    De Bont, A.M.Th.3
  • 40
    • 0020581564 scopus 로고
    • Modification of mussel pyruvate kinase during anaerobiosis and after temperature acclimation
    • Holwerda, D.A.; Veenhof, P.R.; van Heugten, H.A.A.; Zandee, D.I. Modification of mussel pyruvate kinase during anaerobiosis and after temperature acclimation. Mol. Physiol. 3:225-234;1983.
    • (1983) Mol. Physiol. , vol.3 , pp. 225-234
    • Holwerda, D.A.1    Veenhof, P.R.2    Van Heugten, H.A.A.3    Zandee, D.I.4
  • 42
    • 0023655408 scopus 로고
    • Role of fructose 2,6-bisphosphate in the control of glycolysis in mammalian tissues
    • Hue, L.; Rider, M.H. Role of fructose 2,6-bisphosphate in the control of glycolysis in mammalian tissues. Biochem. J. 245: 313-324;1987.
    • (1987) Biochem. J. , vol.245 , pp. 313-324
    • Hue, L.1    Rider, M.H.2
  • 43
    • 0028119727 scopus 로고
    • Protein turnover during metabolic arrest in turtle hepatocytes: Role and energy dependence of proteolysis
    • Land, S.C.; Hochachka, P.W. Protein turnover during metabolic arrest in turtle hepatocytes: Role and energy dependence of proteolysis. Am. J. Physiol. 266:C1028-C1036;1994.
    • (1994) Am. J. Physiol. , vol.266
    • Land, S.C.1    Hochachka, P.W.2
  • 44
    • 0027244326 scopus 로고
    • Response of protein synthesis to anoxia and recovery in anoxia-tolerant hepatocytes
    • Land, S.C.; Buck, L.T.; Hochachka, P.W. Response of protein synthesis to anoxia and recovery in anoxia-tolerant hepatocytes. Am. J. Physiol. 265:R41-R48;1993.
    • (1993) Am. J. Physiol. , vol.265
    • Land, S.C.1    Buck, L.T.2    Hochachka, P.W.3
  • 45
    • 0026080004 scopus 로고
    • Oxidation of cysteines activates cGMP-dependent protein kinase
    • Landgraf, W.; Regulla, S.; Meyer, H.E.; Hofmann, F. Oxidation of cysteines activates cGMP-dependent protein kinase. J. Biol. Chem. 266:16305-16311;1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16305-16311
    • Landgraf, W.1    Regulla, S.2    Meyer, H.E.3    Hofmann, F.4
  • 46
    • 0342664290 scopus 로고
    • Regulation of phosphofructokinase in the foot muscle of Patella caerulea (L.) during exposure to air
    • Lazou, A. Regulation of phosphofructokinase in the foot muscle of Patella caerulea (L.) during exposure to air. J. Exp. Zool. 259:202-208;1991.
    • (1991) J. Exp. Zool. , vol.259 , pp. 202-208
    • Lazou, A.1
  • 47
    • 0019321173 scopus 로고
    • Activation of rabbit muscle phosphofructokinase by f-actin and reconstituted thin filaments
    • Liou, R.-S.; Anderson, S. Activation of rabbit muscle phosphofructokinase by f-actin and reconstituted thin filaments. Biochemistry 19:2684-2688;1980.
    • (1980) Biochemistry , vol.19 , pp. 2684-2688
    • Liou, R.-S.1    Anderson, S.2
  • 48
    • 0022973976 scopus 로고
    • The role of phosphorylation in the interaction of rabbit muscle phosphofructokinase with f-actin
    • Luther, M.A.; Lee, J.C. The role of phosphorylation in the interaction of rabbit muscle phosphofructokinase with f-actin. J. Biol. Chem. 261:1753-1759;1986.
    • (1986) J. Biol. Chem. , vol.261 , pp. 1753-1759
    • Luther, M.A.1    Lee, J.C.2
  • 49
    • 0025051204 scopus 로고
    • Phosphofructokinase from the anterior byssus rectractor muscle of Mytilus edulis: Modification of the enzyme in anoxia and by endogenous protein kinases
    • Michaelidis, B.; Storey, K.B. Phosphofructokinase from the anterior byssus rectractor muscle of Mytilus edulis: Modification of the enzyme in anoxia and by endogenous protein kinases. Int. J. Biochem. 22:759-765;1990.
    • (1990) Int. J. Biochem. , vol.22 , pp. 759-765
    • Michaelidis, B.1    Storey, K.B.2
  • 50
    • 0026019041 scopus 로고
    • Evidence for phosphorylation-dephosphorylation control of phosphofructokinase from organs of the anoxia-tolerant sea mussel Mytilus edulis
    • Michaelidis, B.; Storey, K.B. Evidence for phosphorylation-dephosphorylation control of phosphofructokinase from organs of the anoxia-tolerant sea mussel Mytilus edulis. J. Exp. Zool. 257:1-9;1991.
    • (1991) J. Exp. Zool. , vol.257 , pp. 1-9
    • Michaelidis, B.1    Storey, K.B.2
  • 51
    • 0000032107 scopus 로고
    • Adenosine release in the anoxic turtle brain: A possible mechanism for anoxic survival
    • Nilsson, G.E.; Lutz, P.L. Adenosine release in the anoxic turtle brain: A possible mechanism for anoxic survival. J. Exp. Biol. 162:345-351;1992.
    • (1992) J. Exp. Biol. , vol.162 , pp. 345-351
    • Nilsson, G.E.1    Lutz, P.L.2
  • 52
    • 0026355413 scopus 로고
    • Protein kinase phosphorylation site sequences and consensus specificity motifs: Tabulations
    • Hunter, T.; Sefton, B.M. (eds). New York: Academic Press
    • Pearson, R.B.; Kemp, B.E. Protein kinase phosphorylation site sequences and consensus specificity motifs: Tabulations. In: Hunter, T.; Sefton, B.M. (eds). Methods in Enzymology, Vol. 200. New York: Academic Press; 1991:62-81.
    • (1991) Methods in Enzymology , vol.200 , pp. 62-81
    • Pearson, R.B.1    Kemp, B.E.2
  • 53
    • 0026518612 scopus 로고
    • Downregulation of sodium channels during anoxia: A putative survival strategy of turtle brain
    • Peréz-Pinón, M.A.; Rosenthal, M.; Sick, T.J.; Lutz, P.L.; Pablo, J.; Mash, D. Downregulation of sodium channels during anoxia: A putative survival strategy of turtle brain. Am. J. Physiol. 262:R712-R715;1992.
    • (1992) Am. J. Physiol. , vol.262
    • Peréz-Pinón, M.A.1    Rosenthal, M.2    Sick, T.J.3    Lutz, P.L.4    Pablo, J.5    Mash, D.6
  • 54
    • 77956900538 scopus 로고
    • Enzymes of the fructose 6-phosphate-fructose 1,6-bisphosphate substrate cycle
    • Boyer, P.D.; Krebs, E.G. (eds). New York: Academic Press
    • Pilkis, S.J.; Claus, T.H.; Kountz, P.D.; el-Maghradi, M.R. Enzymes of the fructose 6-phosphate-fructose 1,6-bisphosphate substrate cycle. In: Boyer, P.D.; Krebs, E.G. (eds). The Enzymes. New York: Academic Press; 1987:3-45.
    • (1987) The Enzymes , pp. 3-45
    • Pilkis, S.J.1    Claus, T.H.2    Kountz, P.D.3    El-Maghradi, M.R.4
  • 55
    • 0021754360 scopus 로고
    • Phosphorylation in vivo of red-muscle pyruvate kinase from the channelled whelk, Busycotypus canaliculatum, in response to anoxic stress
    • Plaxton, W.C.; Storey, K.B. Phosphorylation in vivo of red-muscle pyruvate kinase from the channelled whelk, Busycotypus canaliculatum, in response to anoxic stress. Eur. J. Biochem. 143:267-272;1984.
    • (1984) Eur. J. Biochem. , vol.143 , pp. 267-272
    • Plaxton, W.C.1    Storey, K.B.2
  • 56
    • 0011365199 scopus 로고
    • Tissue specific isozymes of pyruvate kinase in the channelled whelk Busycotypus canaliculatum: Enzyme modification in response to environmental anoxia
    • Plaxton, W.C.; Storey, K.B. Tissue specific isozymes of pyruvate kinase in the channelled whelk Busycotypus canaliculatum: Enzyme modification in response to environmental anoxia. J. Comp. Physiol. 155B:291-296;1985.
    • (1985) J. Comp. Physiol. , vol.155 B , pp. 291-296
    • Plaxton, W.C.1    Storey, K.B.2
  • 57
    • 0000488594 scopus 로고
    • Glycolytic enzyme binding and metabolic control in anaerobiosis
    • Plaxton, W.C.; Storey, K.B. Glycolytic enzyme binding and metabolic control in anaerobiosis. J. Comp. Physiol. 156B: 635-640;1986.
    • (1986) J. Comp. Physiol. , vol.156 B , pp. 635-640
    • Plaxton, W.C.1    Storey, K.B.2
  • 58
    • 34250109980 scopus 로고
    • Anaerobiosis and acid-base status in marine invertebrates: Effect of environmental hypoxia on extracellular and intercellular pH in Sipunculus nudus L
    • Pörtner, H.O.; Grieshaber, M.K.; Heisler, N. Anaerobiosis and acid-base status in marine invertebrates: Effect of environmental hypoxia on extracellular and intercellular pH in Sipunculus nudus L. J. Comp. Physiol. 155:11-20;1984.
    • (1984) J. Comp. Physiol. , vol.155 , pp. 11-20
    • Pörtner, H.O.1    Grieshaber, M.K.2    Heisler, N.3
  • 59
    • 0001663364 scopus 로고
    • Role of covalent modification in the control of glycolytic enzymes in response to environmental anoxia in goldfish
    • Rahman, M.S.; Storey, K.B. Role of covalent modification in the control of glycolytic enzymes in response to environmental anoxia in goldfish. J. Comp. Physiol. 157B:815-820;1988.
    • (1988) J. Comp. Physiol. , vol.157 B , pp. 815-820
    • Rahman, M.S.1    Storey, K.B.2
  • 60
    • 0025098398 scopus 로고
    • Metabolic consequences of glucogenic transamination in aestivating snail, Pila globosa (Swainson): Neuroendocrine involvement
    • Reddy, G.R.; Babu, G.R.V.; Chetty, C.S. Metabolic consequences of glucogenic transamination in aestivating snail, Pila globosa (Swainson): Neuroendocrine involvement. Biochem. Int. 20:287-290;1990.
    • (1990) Biochem. Int. , vol.20 , pp. 287-290
    • Reddy, G.R.1    Babu, G.R.V.2    Chetty, C.S.3
  • 61
    • 0025259747 scopus 로고
    • Modulations of protein metabolism during aestivation: Possible occurrence of hyperproteinaemic and hyperaminoacidaemic factors in the central nervous system of freshwater snail Pila glohosa
    • Reddy, G.R.; Babu, G.R.V.; Chetty, C.S. Modulations of protein metabolism during aestivation: possible occurrence of hyperproteinaemic and hyperaminoacidaemic factors in the central nervous system of freshwater snail Pila glohosa. Biochem. Int. 20:471-477;1990.
    • (1990) Biochem. Int. , vol.20 , pp. 471-477
    • Reddy, G.R.1    Babu, G.R.V.2    Chetty, C.S.3
  • 62
    • 0025149052 scopus 로고
    • Heat dissipation, gas exchange and acid-base status in the land snail Oreohelix during short-term estivation
    • Rees, B.B.; Hand, S.C. Heat dissipation, gas exchange and acid-base status in the land snail Oreohelix during short-term estivation. J. Exp. Biol. 152:77-92;1990.
    • (1990) J. Exp. Biol. , vol.152 , pp. 77-92
    • Rees, B.B.1    Hand, S.C.2
  • 63
    • 0000747867 scopus 로고
    • Biochemical correlates of estivation tolerance in the mountain snail Oreohelix (Pulmonata: Oreohelicidae)
    • Rees, B.B.; Hand, S.C. Biochemical correlates of estivation tolerance in the mountain snail Oreohelix (Pulmonata: Oreohelicidae). Biol. Bull. 184:230-242;1995.
    • (1995) Biol. Bull. , vol.184 , pp. 230-242
    • Rees, B.B.1    Hand, S.C.2
  • 64
    • 0018816350 scopus 로고
    • Biochemical properties of hormone-sensitive adenylate cyclase
    • Ross, E.M.; Gillman, A.G. Biochemical properties of hormone-sensitive adenylate cyclase. Ann. Rev. Biochem. 49: 533-564;1980.
    • (1980) Ann. Rev. Biochem. , vol.49 , pp. 533-564
    • Ross, E.M.1    Gillman, A.G.2
  • 65
    • 0021759150 scopus 로고
    • Differences in kinetic properties of phospho and dephospho forms of fructose-6-phosphate, 2-kinase and fructose 2,6-bisphosphatase
    • Sakakibara, R.; Kitajima, S.; Uyeda, K. Differences in kinetic properties of phospho and dephospho forms of fructose-6-phosphate, 2-kinase and fructose 2,6-bisphosphatase. J. Biol. Chem. 259:41-46;1984.
    • (1984) J. Biol. Chem. , vol.259 , pp. 41-46
    • Sakakibara, R.1    Kitajima, S.2    Uyeda, K.3
  • 66
    • 0002438856 scopus 로고
    • Anoxic metabolic rate in the mussel Mytilus edulis L. estimated by simultaneous direct calorimetry and biochemical analysis
    • Shick, J.M.; de Zwaan, A.; de Bont, A.M.T. Anoxic metabolic rate in the mussel Mytilus edulis L. estimated by simultaneous direct calorimetry and biochemical analysis. Physiol. Zool. 56: 56-63;1983.
    • (1983) Physiol. Zool. , vol.56 , pp. 56-63
    • Shick, J.M.1    De Zwaan, A.2    De Bont, A.M.T.3
  • 67
    • 0021731179 scopus 로고
    • Phosphofructokinase from foot muscle of the whelk, Busycotypus canaliculatum: Evidence for covalent modification of the enzyme during anaerobiosis
    • Storey, K.B. Phosphofructokinase from foot muscle of the whelk, Busycotypus canaliculatum: Evidence for covalent modification of the enzyme during anaerobiosis. Arch. Biochem. Biophys. 235:665-672;1984.
    • (1984) Arch. Biochem. Biophys. , vol.235 , pp. 665-672
    • Storey, K.B.1
  • 68
    • 0010456369 scopus 로고
    • A re-evaluation of the Pasteur effect: New mechanisms in anaerobic metabolism
    • Storey, K.B. A re-evaluation of the Pasteur effect: New mechanisms in anaerobic metabolism. Mol. Physiol. 8:439-461; 1985.
    • (1985) Mol. Physiol. , vol.8 , pp. 439-461
    • Storey, K.B.1
  • 69
    • 0023644534 scopus 로고
    • Regulation of liver metabolism by enzyme phosphorylation during mammalian hibernation
    • Storey, K.B. Regulation of liver metabolism by enzyme phosphorylation during mammalian hibernation. J. Biol. Chem. 262:1670-1673;1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1670-1673
    • Storey, K.B.1
  • 70
    • 1542509752 scopus 로고
    • Investigation of the mechanisms of glycolytic control during hibernation
    • Storey, K.B. Investigation of the mechanisms of glycolytic control during hibernation. Can. J. Zool. 65:3079-3083;1987.
    • (1987) Can. J. Zool. , vol.65 , pp. 3079-3083
    • Storey, K.B.1
  • 71
    • 0001040956 scopus 로고
    • Mechanisms of glycolytic control during facultative anaerobiosis in a marine mollusc: Tissue-specific analysis of glycogen phosphorylase and fructose 2,6-bisphosphate
    • Storey, K.B. Mechanisms of glycolytic control during facultative anaerobiosis in a marine mollusc: Tissue-specific analysis of glycogen phosphorylase and fructose 2,6-bisphosphate. Can. J. Zool. 66:1767-1771;1988.
    • (1988) Can. J. Zool. , vol.66 , pp. 1767-1771
    • Storey, K.B.1
  • 72
    • 0002052376 scopus 로고
    • Integrated control of metabolic rate depression via reversible phosphorylation of enzymes in hibernating mammals
    • Malan, A.; Canguilhem, B. (eds). London: John Libbey Eurotext
    • Storey, K.B. Integrated control of metabolic rate depression via reversible phosphorylation of enzymes in hibernating mammals. In: Malan, A.; Canguilhem, B. (eds). Living in the Cold II. London: John Libbey Eurotext; 1989:309-319.
    • (1989) Living in the Cold II , pp. 309-319
    • Storey, K.B.1
  • 73
    • 0025442575 scopus 로고    scopus 로고
    • Metabolic rate depression and biochemical adaptation in anaerobiosis, hibernation and estivation
    • Storey, K.B.; Storey, J.M. Metabolic rate depression and biochemical adaptation in anaerobiosis, hibernation and estivation. Q. Rev. Biol. 65:145-174.
    • Q. Rev. Biol. , vol.65 , pp. 145-174
    • Storey, K.B.1    Storey, J.M.2
  • 74
    • 0001231144 scopus 로고
    • Anaerobiosis and organ-specific regulation of glycolysis in a marine whelk
    • Storey, K.B.; Kelly, D.A.; Duncan, J.A.; Storey, J.M. Anaerobiosis and organ-specific regulation of glycolysis in a marine whelk. Can. J. Zool. 68:974-980;1990.
    • (1990) Can. J. Zool. , vol.68 , pp. 974-980
    • Storey, K.B.1    Kelly, D.A.2    Duncan, J.A.3    Storey, J.M.4
  • 76
    • 0016380711 scopus 로고
    • Regulation of pyruvate dehydrogenase in rat liver mitochondria by phosphorylation-dephosphorylation
    • Walajtys, E.I.; Gottesman, D.P.; Williamson, J.R. Regulation of pyruvate dehydrogenase in rat liver mitochondria by phosphorylation-dephosphorylation. J. Biol. Chem. 249:1857-1865;1974.
    • (1974) J. Biol. Chem. , vol.249 , pp. 1857-1865
    • Walajtys, E.I.1    Gottesman, D.P.2    Williamson, J.R.3
  • 77
    • 0000738301 scopus 로고
    • Acid-base balance in the sea mussel, Mytilus edulis, II. Effects of hypoxia and air exposure on intracellular acid-base status
    • Walsh, P.J.; McDonald, D.G.; Booth, C.E. Acid-base balance in the sea mussel, Mytilus edulis, II. Effects of hypoxia and air exposure on intracellular acid-base status. Mar. Biol. Lett. 5: 359-369;1984.
    • (1984) Mar. Biol. Lett. , vol.5 , pp. 359-369
    • Walsh, P.J.1    McDonald, D.G.2    Booth, C.E.3
  • 78
    • 0025962636 scopus 로고
    • Motifs of protein phosphorylation and mechanisms of reversible covalent regulation
    • Walsh, D.A.; Newsholme, P.; Cawley, K. C.; van Patten, S. M.; Angeles, K. L. Motifs of protein phosphorylation and mechanisms of reversible covalent regulation. Physiol. Rev. 71:285-315;1991.
    • (1991) Physiol. Rev. , vol.71 , pp. 285-315
    • Walsh, D.A.1    Newsholme, P.2    Cawley, K.C.3    Van Patten, S.M.4    Angeles, K.L.5
  • 80
    • 0039853570 scopus 로고
    • General features of metabolic control as applied to the erythrocyte
    • Williamson, J.R. General features of metabolic control as applied to the erythrocyte. Adv. Biol. Med. 6:117-136;1970.
    • (1970) Adv. Biol. Med. , vol.6 , pp. 117-136
    • Williamson, J.R.1
  • 81
    • 0343868151 scopus 로고
    • Organ-specific analysis of the time course of covalent modification of pyruvate kinase during anaerobiosis in a marine whelk
    • Whitwam, R.E.; Storey, K.B. Organ-specific analysis of the time course of covalent modification of pyruvate kinase during anaerobiosis in a marine whelk. Physiol. Zool. 63:222-234; 1990.
    • (1990) Physiol. Zool. , vol.63 , pp. 222-234
    • Whitwam, R.E.1    Storey, K.B.2
  • 82
    • 0025203742 scopus 로고
    • Pyruvate kinase from the land snail Otala lactea: Regulation by reversible phosphorylation during estivation and anoxia
    • Whitwam, R.E.; Storey, K.B. Pyruvate kinase from the land snail Otala lactea: Regulation by reversible phosphorylation during estivation and anoxia. J. Exp. Biol. 154:321-337;1990.
    • (1990) J. Exp. Biol. , vol.154 , pp. 321-337
    • Whitwam, R.E.1    Storey, K.B.2
  • 83
    • 0004173566 scopus 로고
    • Organ-specific regulation of phosphofructokinase during facultative anaerobiosis in the marine whelk Busycotypus canaliculatum
    • Whitwam, R.E.; Storey, K.B. Organ-specific regulation of phosphofructokinase during facultative anaerobiosis in the marine whelk Busycotypus canaliculatum. Can. J. Zool. 69:70-75;1991.
    • (1991) Can. J. Zool. , vol.69 , pp. 70-75
    • Whitwam, R.E.1    Storey, K.B.2
  • 84
    • 0011462629 scopus 로고
    • Regulation of phosphofructokinase during estivation and anoxia in the land snail, Otala lactea
    • Whitwam, R.E.; Storey, K.B. Regulation of phosphofructokinase during estivation and anoxia in the land snail, Otala lactea. Physiol. Zool. 64:595-610;1991.
    • (1991) Physiol. Zool. , vol.64 , pp. 595-610
    • Whitwam, R.E.1    Storey, K.B.2
  • 86
    • 33747744622 scopus 로고
    • Substrate specificity of cyclic AMP-dependent protein kinase
    • Kemp, B.E. (ed). Boca Raton, FL: CRC Press
    • Zetterqvist, O.; Ragnarsson, U.; Engstrom, L. Substrate specificity of cyclic AMP-dependent protein kinase. In: Kemp, B.E. (ed). Peptides and Protein Phosphorylation. Boca Raton, FL: CRC Press; 1990:171-187.
    • (1990) Peptides and Protein Phosphorylation , pp. 171-187
    • Zetterqvist, O.1    Ragnarsson, U.2    Engstrom, L.3
  • 87
    • 0000259201 scopus 로고
    • Anaerobic energy metabolism in bivalve molluscs
    • de Zwaan, A. Anaerobic energy metabolism in bivalve molluscs. Oceanogr. Mar. Biol. Ann. Rev. 15:103-187;1977.
    • (1977) Oceanogr. Mar. Biol. Ann. Rev. , vol.15 , pp. 103-187
    • De Zwaan, A.1
  • 88
    • 0000804693 scopus 로고
    • Carbohydrate metabolism in bivalves
    • Wilbur, K.M. (ed). New York: Academic Press
    • de Zwaan, A. Carbohydrate metabolism in bivalves. In: Wilbur, K.M. (ed). The Mollusca, Vol. 1. New York: Academic Press; 1983:137-175.
    • (1983) The Mollusca , vol.1 , pp. 137-175
    • De Zwaan, A.1


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