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Volumn 76, Issue 1, 2003, Pages 28-40

The protein synthesis machinery operates at the same expense in eurythermal and cold stenothermal pectinids

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; GUANOSINE TRIPHOSPHATE; PHENYLALANINE; PROTEIN;

EID: 0038745612     PISSN: 15222152     EISSN: None     Source Type: Journal    
DOI: 10.1086/367945     Document Type: Article
Times cited : (25)

References (66)
  • 2
    • 0014687871 scopus 로고
    • Regulatory significance of transfer RNA charging levels. I. Measurements of charging levels in livers of chow-fed rats, fasting rats, and rats fed balanced or imbalanced mixtures of amino acids
    • Allen R.F.., P.L. Raines, and D.M. Regen. 1969. Regulatory significance of transfer RNA charging levels. I. Measurements of charging levels in livers of chow-fed rats, fasting rats, and rats fed balanced or imbalanced mixtures of amino acids. Biochim Biophys Acta 190:323-336.
    • (1969) Biochim Biophys Acta , vol.190 , pp. 323-336
    • Allen, R.F.1    Raines, P.L.2    Regen, D.M.3
  • 3
    • 0037597315 scopus 로고
    • Studies on fish liver protein synthesis. III. Activity of carp liver polyribosomes in a homologous cell-free system
    • Amthauer R. and M. Krauskopf. 1979. Studies on fish liver protein synthesis. III. Activity of carp liver polyribosomes in a homologous cell-free system. Comp Biochem Physiol B 62:231-236.
    • (1979) Comp Biochem Physiol B , vol.62 , pp. 231-236
    • Amthauer, R.1    Krauskopf, M.2
  • 4
    • 0041696993 scopus 로고
    • Energy cost of whole-body protein synthesis measured in vivo in chicks
    • Aoyagi Y., I. Tasaki, J. Okumura, and T. Muramatsu. 1988. Energy cost of whole-body protein synthesis measured in vivo in chicks. Comp Biochem Physiol A 91:765-768.
    • (1988) Comp Biochem Physiol A , vol.91 , pp. 765-768
    • Aoyagi, Y.1    Tasaki, I.2    Okumura, J.3    Muramatsu, T.4
  • 5
    • 0017206949 scopus 로고
    • Studies on fish liver protein synthesis. II. Factors influencing the aminoacylation of shark liver transfer ribonucleic acid
    • Araya A. and M. Krauskopf. 1976. Studies on fish liver protein synthesis. II. Factors influencing the aminoacylation of shark liver transfer ribonucleic acid. Acta Physiol Latinoam 26:97-105.
    • (1976) Acta Physiol Latinoam , vol.26 , pp. 97-105
    • Araya, A.1    Krauskopf, M.2
  • 6
    • 0023019133 scopus 로고
    • Effect of diabetes on the rates of synthesis and degradation of ribosomes in rat muscle and liver in vivo
    • Ashford A.J. and V.M. Pain. 1986. Effect of diabetes on the rates of synthesis and degradation of ribosomes in rat muscle and liver in vivo. J Biol Chem 261:4059-4065.
    • (1986) J Biol Chem , vol.261 , pp. 4059-4065
    • Ashford, A.J.1    Pain, V.M.2
  • 7
    • 0002920861 scopus 로고
    • The population biology of the Antarctic scallop, Adamussium colbecki (Smith) at New Harbor, Ross Sea
    • K.R. Kerry and G. Hempel, eds. Springer, Berlin
    • Berkman P.A. 1990. The population biology of the Antarctic scallop, Adamussium colbecki (Smith) at New Harbor, Ross Sea. Pp. 281-288 in K.R. Kerry and G. Hempel, eds. Antarctic Ecosystems: Ecological Change and Conservation. Springer, Berlin.
    • (1990) Antarctic Ecosystems: Ecological Change and Conservation , pp. 281-288
    • Berkman, P.A.1
  • 8
    • 0017142438 scopus 로고
    • Comparison of the temperature sensitivity of protein synthesis by cell-free systems from liver of rat and skate (Raja ocellata)
    • Brosnan M.E., D.R. Myron, L.A. Feltham, and B.H. Sells. 1976. Comparison of the temperature sensitivity of protein synthesis by cell-free systems from liver of rat and skate (Raja ocellata). Biochim Biophys Acta 447:360-374.
    • (1976) Biochim Biophys Acta , vol.447 , pp. 360-374
    • Brosnan, M.E.1    Myron, D.R.2    Feltham, L.A.3    Sells, B.H.4
  • 9
    • 0001894811 scopus 로고
    • The energetic efficiency of amino acid metabolism
    • D.J.A. Cole, K.N. Boorman, P.J. Buttery, D. Lewis, R.J. Neal, and H. Swan, eds. Butterworths, London
    • Buttery P.J. and K.N. Boorman. 1976. The energetic efficiency of amino acid metabolism. Pp. 197-206 in D.J.A. Cole, K.N. Boorman, P.J. Buttery, D. Lewis, R.J. Neal, and H. Swan, eds. Protein Metabolism and Nutrition. Butterworths, London.
    • (1976) Protein Metabolism and Nutrition , pp. 197-206
    • Buttery, P.J.1    Boorman, K.N.2
  • 10
    • 0000851518 scopus 로고
    • Acid-base homeostasis: Past and present perspective
    • Cameron J.N. 1989. Acid-base homeostasis: past and present perspective. Physiol Zool 62:845-865.
    • (1989) Physiol Zool , vol.62 , pp. 845-865
    • Cameron, J.N.1
  • 11
    • 0033935886 scopus 로고    scopus 로고
    • Molecular data from the 16S rRNA gene for the phylogeny of Pectinidae (Mollusca: Bivalvia)
    • Canapa A., M. Barucca, A. Marinelli, and E. Olmo. 2000. Molecular data from the 16S rRNA gene for the phylogeny of Pectinidae (Mollusca: Bivalvia). J Mol Evol 50:93-97.
    • (2000) J Mol Evol , vol.50 , pp. 93-97
    • Canapa, A.1    Barucca, M.2    Marinelli, A.3    Olmo, E.4
  • 12
    • 0033135077 scopus 로고    scopus 로고
    • An improved capillary electrophoresis method for measuring tissue metabolites associated with cellular energy state
    • Casey T.M., K.G. Dufall, and P.G. Arthur. 1999. An improved capillary electrophoresis method for measuring tissue metabolites associated with cellular energy state. Eur J Biochem 261:740-745.
    • (1999) Eur J Biochem , vol.261 , pp. 740-745
    • Casey, T.M.1    Dufall, K.G.2    Arthur, P.G.3
  • 13
    • 0029108623 scopus 로고
    • The influence of acclimation and substratum on the metabolism of the Antarctic amphipods Waldeckia obesa (Chevreux 1905) and Bovallia gigantea (Pfeffer 1808)
    • Chapelle G. and L.S. Peck. 1995. The influence of acclimation and substratum on the metabolism of the Antarctic amphipods Waldeckia obesa (Chevreux 1905) and Bovallia gigantea (Pfeffer 1808). Polar Biol 15:225-232.
    • (1995) Polar Biol , vol.15 , pp. 225-232
    • Chapelle, G.1    Peck, L.S.2
  • 14
    • 0035147458 scopus 로고    scopus 로고
    • Antarctic scallop (Adamussium colbecki) spatial population variability along the Victoria Land coast, Antarctica
    • Chiantore M., R. Cattaneo-Vietti, P.A. Berkman, M. Nigro, M.V.S. Schiaparelli, and G. Albertelli. 2001. Antarctic scallop (Adamussium colbecki) spatial population variability along the Victoria Land coast, Antarctica. Polar Biol 24:139-143.
    • (2001) Polar Biol , vol.24 , pp. 139-143
    • Chiantore, M.1    Cattaneo-Vietti, R.2    Berkman, P.A.3    Nigro, M.4    Schiaparelli, M.V.S.5    Albertelli, G.6
  • 15
    • 0026291121 scopus 로고
    • What is cold adaptation and how should we measure it?
    • Clarke A. 1991. What is cold adaptation and how should we measure it? Am Zool 31:81-92.
    • (1991) Am Zool , vol.31 , pp. 81-92
    • Clarke, A.1
  • 16
    • 0032835469 scopus 로고    scopus 로고
    • Scaling of metabolic rate with body mass and temperature in teleost fish
    • Clarke A. and N.M. Johnston 1999. Scaling of metabolic rate with body mass and temperature in teleost fish. J Anim Ecol 68:893-905.
    • (1999) J Anim Ecol , vol.68 , pp. 893-905
    • Clarke, A.1    Johnston, N.M.2
  • 17
    • 0038611445 scopus 로고
    • Nucleases and related enzymes
    • J.N. Davidson, ed. Cox & Wyman, Fakenham, Norfolk, Great Britain
    • Davidson J.N. 1972. Nucleases and related enzymes. Pp. 183-214 in J.N. Davidson, ed. The Biochemistry of the Nucleic Acids. 7th ed. Cox & Wyman, Fakenham, Norfolk, Great Britain.
    • (1972) The Biochemistry of the Nucleic Acids. 7th Ed. , pp. 183-214
    • Davidson, J.N.1
  • 18
    • 0015240299 scopus 로고
    • The effect of cycloheximide on membrane transport in Euglena: A comparative study with nigericin
    • Evans W.R. 1971. The effect of cycloheximide on membrane transport in Euglena: a comparative study with nigericin. J Biol Chem 246:6144-6151.
    • (1971) J Biol Chem , vol.246 , pp. 6144-6151
    • Evans, W.R.1
  • 19
    • 0032005635 scopus 로고    scopus 로고
    • Protein synthesis in the liver of Bufo marinus: Cost and contribution to oxygen consumption
    • Fuery C.J., P.C. Withers, and M. Guppy. 1998. Protein synthesis in the liver of Bufo marinus: cost and contribution to oxygen consumption. Comp Biochem Physiol A 119:459-467.
    • (1998) Comp Biochem Physiol A , vol.119 , pp. 459-467
    • Fuery, C.J.1    Withers, P.C.2    Guppy, M.3
  • 20
    • 0019214262 scopus 로고
    • A rapid and convenient technique for measuring the rate of protein synthesis in tissues by injection of [3H] phenylalanine
    • Garlick P.J., M.A. McNurlan, and V.R. Preedy. 1980. A rapid and convenient technique for measuring the rate of protein synthesis in tissues by injection of [3H] phenylalanine. Biochem J 192:719-723.
    • (1980) Biochem J , vol.192 , pp. 719-723
    • Garlick, P.J.1    McNurlan, M.A.2    Preedy, V.R.3
  • 21
    • 0034000087 scopus 로고    scopus 로고
    • The free guanidine and polyamine pools of bivalve molluscs in relation to their ecology
    • Gasparini S. and C. Audit. 2000. The free guanidine and polyamine pools of bivalve molluscs in relation to their ecology. Biochem Syst Ecol 28:209-218.
    • (2000) Biochem Syst Ecol , vol.28 , pp. 209-218
    • Gasparini, S.1    Audit, C.2
  • 22
    • 0023904916 scopus 로고
    • A high-yield cell-free system of protein synthesis of mouse liver
    • Giannakouros T. and J.G. Georgatsos. 1988. A high-yield cell-free system of protein synthesis of mouse liver. Int J Biochem 20:511-519.
    • (1988) Int J Biochem , vol.20 , pp. 511-519
    • Giannakouros, T.1    Georgatsos, J.G.2
  • 23
    • 0025184907 scopus 로고
    • Concentration-dependent effects of natural polyamines on peptide chain initiation and elongation in a cell-free system of protein synthesis
    • Giannakouros T., H. Nikolakaki, and J.G. Georgatsos 1990. Concentration-dependent effects of natural polyamines on peptide chain initiation and elongation in a cell-free system of protein synthesis. Mol Cell Biochem 99:9-19.
    • (1990) Mol Cell Biochem , vol.99 , pp. 9-19
    • Giannakouros, T.1    Nikolakaki, H.2    Georgatsos, J.G.3
  • 24
    • 0037935196 scopus 로고
    • Temperature dependency of cell-free protein synthetic systems from Antarctic fish
    • Haschemeyer A.E.V. and R.C. Williams, Jr. 1982. Temperature dependency of cell-free protein synthetic systems from Antarctic fish. Mar Biol Lett 3:81-88.
    • (1982) Mar Biol Lett , vol.3 , pp. 81-88
    • Haschemeyer, A.E.V.1    Williams R.C., Jr.2
  • 26
    • 0028100848 scopus 로고
    • Global arrest of translation during invertebrate quiescence
    • Hofmann G.E. and S.C. Hand. 1994. Global arrest of translation during invertebrate quiescence. Proc Natl Acad Sci USA 91:8492-8496.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8492-8496
    • Hofmann, G.E.1    Hand, S.C.2
  • 27
    • 0016177889 scopus 로고
    • Metabolic cold adaptation of polar fish: Fact or artefact
    • Holeton G.F. 1974. Metabolic cold adaptation of polar fish: fact or artefact. Physiol Zool 47:137-152.
    • (1974) Physiol Zool , vol.47 , pp. 137-152
    • Holeton, G.F.1
  • 28
    • 84912426762 scopus 로고
    • The cytoplasmic control of protein synthesis
    • R. Pérez-Bercoff, ed. Plenum, New York
    • Jackson R.J. 1982. The cytoplasmic control of protein synthesis. Pp. 363-418 in R. Pérez-Bercoff, ed. Protein Biosynthesis in Eukaryotes. Plenum, New York.
    • (1982) Protein Biosynthesis in Eukaryotes , pp. 363-418
    • Jackson, R.J.1
  • 29
    • 0025745222 scopus 로고
    • The ATP requirement for initiation of eukaryotic translation varies according to the mRNA species
    • _. 1991. The ATP requirement for initiation of eukaryotic translation varies according to the mRNA species. Eur J Biochem 200:285-294.
    • (1991) Eur J Biochem , vol.200 , pp. 285-294
  • 30
    • 0034672726 scopus 로고    scopus 로고
    • An efficient cell-free protein synthesis system using periplasmic phosphatase-removed S30 extract
    • Kang S.H., T.J. Oh, R.G. Kim, T.J. Kang, S.H. Hwang, E.Y. Lee, and C.Y. Choi. 2000. An efficient cell-free protein synthesis system using periplasmic phosphatase-removed S30 extract. J Microbiol Methods 43:91-96.
    • (2000) J Microbiol Methods , vol.43 , pp. 91-96
    • Kang, S.H.1    Oh, T.J.2    Kim, R.G.3    Kang, T.J.4    Hwang, S.H.5    Lee, E.Y.6    Choi, C.Y.7
  • 31
    • 0028954219 scopus 로고
    • A long-lived batch reaction system of cell-free protein synthesis
    • Kawarasaki Y., T. Kawai, H. Nakano, and T. Yamane. 1995. A long-lived batch reaction system of cell-free protein synthesis. Anal Biochem 226:320-324.
    • (1995) Anal Biochem , vol.226 , pp. 320-324
    • Kawarasaki, Y.1    Kawai, T.2    Nakano, H.3    Yamane, T.4
  • 32
    • 0032513694 scopus 로고    scopus 로고
    • Phosphatase-immunodepleted cell-free protein synthesis system
    • Kawarasaki Y., H. Nakano, and T. Yamane 1998. Phosphatase-immunodepleted cell-free protein synthesis system. J Biotechnol 61:199-208.
    • (1998) J Biotechnol , vol.61 , pp. 199-208
    • Kawarasaki, Y.1    Nakano, H.2    Yamane, T.3
  • 33
    • 0034045838 scopus 로고    scopus 로고
    • Prolonging cell-free protein synthesis by selective reagent additions
    • Kim D.M. and J.R. Swartz 2000. Prolonging cell-free protein synthesis by selective reagent additions. Biotechnol Prog 16:385-390.
    • (2000) Biotechnol Prog , vol.16 , pp. 385-390
    • Kim, D.M.1    Swartz, J.R.2
  • 34
    • 0019162909 scopus 로고
    • Role of ATP in binding and migration of 40S ribosomal subunits
    • Kozak M. 1980. Role of ATP in binding and migration of 40S ribosomal subunits. Cell 22:459-467.
    • (1980) Cell , vol.22 , pp. 459-467
    • Kozak, M.1
  • 35
    • 0024505407 scopus 로고
    • Characterization of translation systems in vitro from three developmental stages of Strongylocentrotus purpuratus
    • Lopo A.C., C.C. Lashbrook, and J.W. Hershey. 1989. Characterization of translation systems in vitro from three developmental stages of Strongylocentrotus purpuratus. Biochem J 258:553-561.
    • (1989) Biochem J , vol.258 , pp. 553-561
    • Lopo, A.C.1    Lashbrook, C.C.2    Hershey, J.W.3
  • 36
    • 0031976451 scopus 로고    scopus 로고
    • Gill protein turnover: Costs of adaptation
    • Lyndon A.R. and D.F. Houlihan. 1998. Gill protein turnover: costs of adaptation. Comp Biochem Physiol A 119:27-34.
    • (1998) Comp Biochem Physiol A , vol.119 , pp. 27-34
    • Lyndon, A.R.1    Houlihan, D.F.2
  • 37
    • 0035831272 scopus 로고    scopus 로고
    • High macromolecular synthesis with low metabolic cost in Antarctic sea urchin embryos
    • Marsh A.G., R.E. Maxson, Jr., and D.T. Manahan. 2001. High macromolecular synthesis with low metabolic cost in Antarctic sea urchin embryos. Science 291:1950-1952.
    • (2001) Science , vol.291 , pp. 1950-1952
    • Marsh, A.G.1    Maxson R.E., Jr.2    Manahan, D.T.3
  • 38
    • 0035431399 scopus 로고    scopus 로고
    • Protein translation during early cell divisions of sea urchin embryos regulated at the level of polypeptide chain elongation and highly sensitive to natural polyamines
    • Monnier A., J. Morales, P. Cormier, S. Boulben, R. Belle, and O. Mulner-Lorillon. 2001. Protein translation during early cell divisions of sea urchin embryos regulated at the level of polypeptide chain elongation and highly sensitive to natural polyamines. Zygote 9:229-236.
    • (2001) Zygote , vol.9 , pp. 229-236
    • Monnier, A.1    Morales, J.2    Cormier, P.3    Boulben, S.4    Belle, R.5    Mulner-Lorillon, O.6
  • 39
    • 0025726541 scopus 로고
    • Characterization of cell-free protein-synthesis systems from undeveloped and developing Artemia embryos
    • Moreno A., R. Mendez, and C. de Haro. 1991. Characterization of cell-free protein-synthesis systems from undeveloped and developing Artemia embryos. Biochem J 276:809-816.
    • (1991) Biochem J , vol.276 , pp. 809-816
    • Moreno, A.1    Mendez, R.2    De Haro, C.3
  • 40
    • 0013877308 scopus 로고
    • Recent developments in the measurement of nucleic acids in biological materials: A supplementary review
    • Munro H.N. and A. Fleck. 1966. Recent developments in the measurement of nucleic acids in biological materials: a supplementary review. Analyst 91:78-88.
    • (1966) Analyst , vol.91 , pp. 78-88
    • Munro, H.N.1    Fleck, A.2
  • 41
    • 0029942135 scopus 로고    scopus 로고
    • Highly productive cell-free protein synthesis system using condensed wheat-germ extract
    • Nakano H., T. Tanaka, Y. Kawarasaki, and T. Yamane. 1996. Highly productive cell-free protein synthesis system using condensed wheat-germ extract. J Biotechnol 46:275-282.
    • (1996) J Biotechnol , vol.46 , pp. 275-282
    • Nakano, H.1    Tanaka, T.2    Kawarasaki, Y.3    Yamane, T.4
  • 42
    • 0031921676 scopus 로고    scopus 로고
    • E. coli-based in vitro transcription/translation: In vivo-specific synthesis rates and high yields in a batch system
    • Patnaik R. and J.R. Swartz. 1998. E. coli-based in vitro transcription/translation: in vivo-specific synthesis rates and high yields in a batch system. Biotechniques 24:862-868.
    • (1998) Biotechniques , vol.24 , pp. 862-868
    • Patnaik, R.1    Swartz, J.R.2
  • 43
    • 0002997670 scopus 로고
    • Summer metabolism and seasonal changes in biochemical composition of the Antarctic brachiopod Liothyrella uva (Broderip 1833)
    • Peck L.S., A. Clarke, and L.J. Holmes 1987. Summer metabolism and seasonal changes in biochemical composition of the Antarctic brachiopod Liothyrella uva (Broderip 1833). J Exp Mar Biol Ecol 114:85-97.
    • (1987) J Exp Mar Biol Ecol , vol.114 , pp. 85-97
    • Peck, L.S.1    Clarke, A.2    Holmes, L.J.3
  • 44
    • 0025025697 scopus 로고
    • Determination of intracellular buffer values after metabolic inhibition by fluoride and nitrilotriacetic acid
    • Pörtner H.O. 1990. Determination of intracellular buffer values after metabolic inhibition by fluoride and nitrilotriacetic acid. Respir Physiol 81:275-288.
    • (1990) Respir Physiol , vol.81 , pp. 275-288
    • Pörtner, H.O.1
  • 45
    • 0001005285 scopus 로고    scopus 로고
    • Ribonuclease A
    • Raines R.T. 1998. Ribonuclease A. Chem Rev 98:1045-1066.
    • (1998) Chem Rev , vol.98 , pp. 1045-1066
    • Raines, R.T.1
  • 46
    • 0000605588 scopus 로고
    • Growth of two Antarctic lamellibranches: Adamussium colbecki and Laternula elliptica
    • Ralph R. and J.G.H. Maxwell. 1977a. Growth of two Antarctic lamellibranches: Adamussium colbecki and Laternula elliptica. Mar Biol 42:171-175.
    • (1977) Mar Biol , vol.42 , pp. 171-175
    • Ralph, R.1    Maxwell, J.G.H.2
  • 47
    • 0002321572 scopus 로고
    • The oxygen consumption of the Antarctic limpet Nacella (Patinigera) concinna
    • _. 1977b. The oxygen consumption of the Antarctic limpet Nacella (Patinigera) concinna. Bull Br Antarct Surv 45:19-23.
    • (1977) Bull Br Antarct Surv , vol.45 , pp. 19-23
  • 48
    • 0002430462 scopus 로고
    • Metabolic basis of energy expenditure with particular reference to protein
    • J.S. Garrow and D. Halliday, eds. John Libbey, London
    • Reeds P.J., M.F. Fuller, and B.A. Nicholson. 1985. Metabolic basis of energy expenditure with particular reference to protein. Pp. 46-57 in J.S. Garrow and D. Halliday, eds. Substrate and Energy Metabolism. John Libbey, London.
    • (1985) Substrate and Energy Metabolism , pp. 46-57
    • Reeds, P.J.1    Fuller, M.F.2    Nicholson, B.A.3
  • 50
    • 0002988584 scopus 로고
    • Climatic adaptation in arctic and tropical poikilotherms
    • Scholander P.F., W. Flagg, V. Walters, and L. Irving. 1953. Climatic adaptation in arctic and tropical poikilotherms. Physiol Zool 26:67-69.
    • (1953) Physiol Zool , vol.26 , pp. 67-69
    • Scholander, P.F.1    Flagg, W.2    Walters, V.3    Irving, L.4
  • 51
    • 0017399861 scopus 로고
    • Effect of starvation on the charging levels of transfer ribonucleic acid and total acceptor capacity in rat liver
    • Shenoy S.T. and Q.R. Rogers 1977. Effect of starvation on the charging levels of transfer ribonucleic acid and total acceptor capacity in rat liver. Biochim Biophys Acta 476:218-227.
    • (1977) Biochim Biophys Acta , vol.476 , pp. 218-227
    • Shenoy, S.T.1    Rogers, Q.R.2
  • 52
    • 0018225639 scopus 로고
    • Effect of dietary amino acids on transfer ribonucleic acid charging levels in rat liver
    • _. 1978. Effect of dietary amino acids on transfer ribonucleic acid charging levels in rat liver. J Nutr 108:1412-1421.
    • (1978) J Nutr , vol.108 , pp. 1412-1421
  • 53
    • 0023082548 scopus 로고
    • Effect of acclimation temperature on the elongation step of protein synthesis in different organs of rainbow trout
    • Simon E. 1987. Effect of acclimation temperature on the elongation step of protein synthesis in different organs of rainbow trout. J Comp Physiol B 157:201-207.
    • (1987) J Comp Physiol B , vol.157 , pp. 201-207
    • Simon, E.1
  • 54
    • 0024297305 scopus 로고
    • A continuous cell-free translation system capable of producing polypeptides in high yield
    • Spirin A.S., V.I. Baranov, L.A. Ryabova, S.Y. Ovodov, and Y.B. Alakhov. 1988. A continuous cell-free translation system capable of producing polypeptides in high yield. Science 242:1162-1164.
    • (1988) Science , vol.242 , pp. 1162-1164
    • Spirin, A.S.1    Baranov, V.I.2    Ryabova, L.A.3    Ovodov, S.Y.4    Alakhov, Y.B.5
  • 55
    • 0000633607 scopus 로고
    • The biology and ecology of the epifaunal scallop Adamussium colbecki on the west side of McMurdo Sound, Antarctica
    • Stockton W.L. 1984. The biology and ecology of the epifaunal scallop Adamussium colbecki on the west side of McMurdo Sound, Antarctica. Mar Biol 78:171-178.
    • (1984) Mar Biol , vol.78 , pp. 171-178
    • Stockton, W.L.1
  • 56
    • 0034810189 scopus 로고    scopus 로고
    • Conditions influencing the precipitation of magnesium ammonium phosphate
    • Stratful I., M.D. Scrimshaw, and J.N. Lester. 2001. Conditions influencing the precipitation of magnesium ammonium phosphate. Water Res 35:4191-4199.
    • (2001) Water Res , vol.35 , pp. 4191-4199
    • Stratful, I.1    Scrimshaw, M.D.2    Lester, J.N.3
  • 57
    • 0021112573 scopus 로고
    • Binding of inosine-substituted mRNA to reticulocyte ribosomes and eukaryotic initiation factors 4A and 4B requires ATP
    • Tahara S.M., M.A. Morgan, and A.J. Shatkin 1983. Binding of inosine-substituted mRNA to reticulocyte ribosomes and eukaryotic initiation factors 4A and 4B requires ATP. J Biol Chem 258:11350-11353.
    • (1983) J Biol Chem , vol.258 , pp. 11350-11353
    • Tahara, S.M.1    Morgan, M.A.2    Shatkin, A.J.3
  • 59
    • 0002690395 scopus 로고
    • Protein turnover in the whole body and in the whole tissue
    • J.C. Waterlow, P.J. Garlick, and D.J. Millward, eds. North-Holland, Amsterdam
    • _. 1978b. Protein turnover in the whole body and in the whole tissue. Pp. 444-476 in J.C. Waterlow, P.J. Garlick, and D.J. Millward, eds. Protein Turnover in Mammalian Tissues and in the Whole Body. North-Holland, Amsterdam.
    • (1978) Protein Turnover in Mammalian Tissues and in the Whole Body , pp. 444-476
  • 60
    • 0002638073 scopus 로고
    • Energy cost of turnover of protein and other cellular constituents
    • W. Wieser and E. Gnaiger, eds. Thieme, Stuttgart
    • Waterlow J.C. and D.J. Millward. 1989. Energy cost of turnover of protein and other cellular constituents. Pp. 277-282 in W. Wieser and E. Gnaiger, eds. Energy Transformation in Cells and Organisms. Thieme, Stuttgart.
    • (1989) Energy Transformation in Cells and Organisms , pp. 277-282
    • Waterlow, J.C.1    Millward, D.J.2
  • 61
    • 0027418991 scopus 로고
    • Toward a model for the interaction between elongation factor Tu and the ribosome
    • Weijland A. and A. Parmeggiani. 1993. Toward a model for the interaction between elongation factor Tu and the ribosome. Science 259:1311-1314.
    • (1993) Science , vol.259 , pp. 1311-1314
    • Weijland, A.1    Parmeggiani, A.2
  • 62
    • 0002069950 scopus 로고
    • Oxygen consumption and nitrogen excretion by the giant Antarctic isopod Glyptonotus antarcticus (Eights) in relation to cold-adapted metabolism in marine polar poikilotherms
    • H. Barnes, ed. University Press, Aberdeen
    • White M.G. 1975. Oxygen consumption and nitrogen excretion by the giant Antarctic isopod Glyptonotus antarcticus (Eights) in relation to cold-adapted metabolism in marine polar poikilotherms. Pp. 707-724 in H. Barnes, ed. Ninth European Marine Biology Symposium. University Press, Aberdeen.
    • (1975) Ninth European Marine Biology Symposium , pp. 707-724
    • White, M.G.1
  • 63
    • 0029959395 scopus 로고    scopus 로고
    • A comparison of the metabolic cost of protein synthesis in stenothermal and eurythermal isopod crustaceans
    • Whiteley N.M., E.W. Taylor, and A.J. el Haj. 1996. A comparison of the metabolic cost of protein synthesis in stenothermal and eurythermal isopod crustaceans. Am J Physiol 271:R1295-R1303.
    • (1996) Am J Physiol , vol.271
    • Whiteley, N.M.1    Taylor, E.W.2    El Haj, A.J.3
  • 64
    • 0035871195 scopus 로고    scopus 로고
    • Hierarchies of ATP-consuming processes: Direct compared with indirect measurements, and comparative aspects
    • Wieser W. and G. Krumschnabel. 2001. Hierarchies of ATP-consuming processes: direct compared with indirect measurements, and comparative aspects. Biochem J 355:389-395.
    • (2001) Biochem J , vol.355 , pp. 389-395
    • Wieser, W.1    Krumschnabel, G.2
  • 65
    • 0000170409 scopus 로고
    • Metabolism of an Antarctic fish and the phenomenon of cold adaptation
    • Wohlschlag D.E. 1960. Metabolism of an Antarctic fish and the phenomenon of cold adaptation. Ecology 41:287-292.
    • (1960) Ecology , vol.41 , pp. 287-292
    • Wohlschlag, D.E.1
  • 66
    • 13144295435 scopus 로고
    • Eine einfache Technik der extrem schnellen Abkühlung grosser Gewebestücke
    • Wollenberger A.O., O. Ristau, and G. Schoffa. 1960. Eine einfache Technik der extrem schnellen Abkühlung grosser Gewebestücke. Pflueg Arch Eur J Physiol 270:399-412.
    • (1960) Pflueg Arch Eur J Physiol , vol.270 , pp. 399-412
    • Wollenberger, A.O.1    Ristau, O.2    Schoffa, G.3


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