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Volumn 75, Issue 8, 2012, Pages 2342-2351

Time-dependent changes in protein expression in rainbow trout muscle following hypoxia

Author keywords

Aquaculture; Hypoxia; Oxidative stress; Proteomics; Rainbow trout

Indexed keywords

26S PROTEASE REGULATORY SUBUNIT 6A; 26S PROTEASOME NON ATPASE REGULATORY SUBUNIT 12; 26S PROTEASOME NON ATPASE REGULATORY SUBUNIT 14; 3 OXOACID COENZYME A TRANSFERASE 1A; ADENYLATE KINASE 1; ADENYLATE KINASE 2; ALDEHYDE DEHYDROGENASE; ALPHA 1 ANTIPROTEINASE LIKE PROTEIN; ALPHA 2 ENOLASE 1; ALPHA ENOLASE; CALPHOBINDIN II; COMPLEMENT COMPONENT C9; ENIGMA LIM DOMAIN PROTEIN LIKE; ENOLASE 3 1; ENOLASE 3 2; ENZYME; GLUTATHIONE TRANSFERASE M; HEAT SHOCK COGNATE PROTEIN 70 INTERACTING PROTEIN; HEMOPEXIN LIKE PROTEIN; HYPOXANTHINE PHOSPHORIBOSYLTRANSFERASE 1; METHYLMALONATE SEMIALDEHYDE DEHYDROGENASE; MOESIN; MYOSIN BINDING PROTEIN H LIKE; PEPTIDES AND PROTEINS; PHOSPHOGLUCOMUTASE; PROTEASOME SUBUNIT BETA TYPE 2; PROTEIN SRL; TRANSFERRIN; TUBULIN ALPHA CHAIN; UBIQUITIN SPECIFIC PROTEASE 14; UNCLASSIFIED DRUG;

EID: 84859266460     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2012.02.010     Document Type: Article
Times cited : (36)

References (63)
  • 1
    • 0035925098 scopus 로고    scopus 로고
    • Tumor hypoxia: definitions and current clinical, biologic, and molecular aspects
    • Hockel M., Vaupel P. Tumor hypoxia: definitions and current clinical, biologic, and molecular aspects. J Natl Cancer Inst 2001, 93:266-276.
    • (2001) J Natl Cancer Inst , vol.93 , pp. 266-276
    • Hockel, M.1    Vaupel, P.2
  • 2
    • 2442676752 scopus 로고    scopus 로고
    • Physiological and pathological responses to hypoxia
    • Michiels C. Physiological and pathological responses to hypoxia. Am J Pathol 2004, 164:1875-1882.
    • (2004) Am J Pathol , vol.164 , pp. 1875-1882
    • Michiels, C.1
  • 3
    • 55849092859 scopus 로고    scopus 로고
    • Proteins modulation in human skeletal muscle in the early phase of adaptation to hypobaric hypoxia
    • Vigano A., Ripamonti M., De P.S., Capitanio D., Vasso M., Wait R., et al. Proteins modulation in human skeletal muscle in the early phase of adaptation to hypobaric hypoxia. Proteomics 2008, 8:4668-4679.
    • (2008) Proteomics , vol.8 , pp. 4668-4679
    • Vigano, A.1    Ripamonti, M.2    De, P.S.3    Capitanio, D.4    Vasso, M.5    Wait, R.6
  • 5
    • 0038516974 scopus 로고    scopus 로고
    • Dissociation between skeletal muscle microvascular PO2 and hypoxia-induced microvascular inflammation
    • Shah S., Allen J., Wood J.G., Gonzalez N.C. Dissociation between skeletal muscle microvascular PO2 and hypoxia-induced microvascular inflammation. J Appl Physiol 2003, 94:2323-2329.
    • (2003) J Appl Physiol , vol.94 , pp. 2323-2329
    • Shah, S.1    Allen, J.2    Wood, J.G.3    Gonzalez, N.C.4
  • 7
    • 67349277998 scopus 로고    scopus 로고
    • HIF-1 in the inflammatory microenvironment
    • Dehne N., Brune B. HIF-1 in the inflammatory microenvironment. Exp Cell Res 2009, 315:1791-1797.
    • (2009) Exp Cell Res , vol.315 , pp. 1791-1797
    • Dehne, N.1    Brune, B.2
  • 8
    • 31444444162 scopus 로고    scopus 로고
    • Integration of oxygen signaling at the consensus HRE
    • Wenger R.H., Stiehl D.P., Camenisch G. Integration of oxygen signaling at the consensus HRE. Sci STKE 2005, 2005:re12.
    • (2005) Sci STKE , vol.2005
    • Wenger, R.H.1    Stiehl, D.P.2    Camenisch, G.3
  • 9
    • 0142166332 scopus 로고    scopus 로고
    • Targeting HIF-1 for cancer therapy
    • Semenza G.L. Targeting HIF-1 for cancer therapy. Nat Rev Cancer 2003, 3:721-732.
    • (2003) Nat Rev Cancer , vol.3 , pp. 721-732
    • Semenza, G.L.1
  • 11
    • 0345672740 scopus 로고    scopus 로고
    • Hypoxic upregulation of tyrosine hydroxylase gene expression is paralleled, but not induced, by increased generation of reactive oxygen species in PC12 cells
    • Hohler B., Lange B., Holzapfel B., Goldenberg A., Hanze J., Sell A., et al. Hypoxic upregulation of tyrosine hydroxylase gene expression is paralleled, but not induced, by increased generation of reactive oxygen species in PC12 cells. FEBS Lett 1999, 457:53-56.
    • (1999) FEBS Lett , vol.457 , pp. 53-56
    • Hohler, B.1    Lange, B.2    Holzapfel, B.3    Goldenberg, A.4    Hanze, J.5    Sell, A.6
  • 12
    • 21144440061 scopus 로고    scopus 로고
    • Reactive oxygen species formation in the transition to hypoxia in skeletal muscle
    • Zuo L., Clanton T.L. Reactive oxygen species formation in the transition to hypoxia in skeletal muscle. Am J Physiol Cell Physiol 2005, 289:C207-C216.
    • (2005) Am J Physiol Cell Physiol , vol.289
    • Zuo, L.1    Clanton, T.L.2
  • 13
    • 39749110624 scopus 로고    scopus 로고
    • Oxidative stress and iron homeostasis: mechanistic and health aspects
    • Galaris D., Pantopoulos K. Oxidative stress and iron homeostasis: mechanistic and health aspects. Crit Rev Clin Lab Sci 2008, 45:1-23.
    • (2008) Crit Rev Clin Lab Sci , vol.45 , pp. 1-23
    • Galaris, D.1    Pantopoulos, K.2
  • 14
    • 59449109182 scopus 로고    scopus 로고
    • Iron homeostasis: recently identified proteins provide insight into novel control mechanisms
    • Zhang A.S., Enns C.A. Iron homeostasis: recently identified proteins provide insight into novel control mechanisms. J Biol Chem 2009, 284:711-715.
    • (2009) J Biol Chem , vol.284 , pp. 711-715
    • Zhang, A.S.1    Enns, C.A.2
  • 15
    • 0036024287 scopus 로고    scopus 로고
    • Oxygen-dependent cellular functions-why fishes and their aquatic environment are a prime choice of study
    • Nikinmaa M. Oxygen-dependent cellular functions-why fishes and their aquatic environment are a prime choice of study. Comp Biochem Physiol A Mol Integr Physiol 2002, 133:1-16.
    • (2002) Comp Biochem Physiol A Mol Integr Physiol , vol.133 , pp. 1-16
    • Nikinmaa, M.1
  • 16
    • 0000122454 scopus 로고
    • Metabolic responses of trout (Salmo-gairdneri) to acute environmental hypoxia
    • Dunn J.F., Hochachka P.W. Metabolic responses of trout (Salmo-gairdneri) to acute environmental hypoxia. J Exp Biol 1986, 123:229-242.
    • (1986) J Exp Biol , vol.123 , pp. 229-242
    • Dunn, J.F.1    Hochachka, P.W.2
  • 17
    • 8444238299 scopus 로고    scopus 로고
    • The effects of sustained exercise and hypoxia upon oxygen tensions in the red muscle of rainbow trout
    • McKenzie D.J., Wong S., Randall D.J., Egginton S., Taylor E.W., Farrell A.P. The effects of sustained exercise and hypoxia upon oxygen tensions in the red muscle of rainbow trout. J Exp Biol 2004, 207:3629-3637.
    • (2004) J Exp Biol , vol.207 , pp. 3629-3637
    • McKenzie, D.J.1    Wong, S.2    Randall, D.J.3    Egginton, S.4    Taylor, E.W.5    Farrell, A.P.6
  • 18
    • 33750595807 scopus 로고    scopus 로고
    • Effects of long-term hypoxia on enzymes of carbohydrate metabolism in the Gulf killifish, Fundulus grandis
    • Martinez M.L., Landry C., Boehm R., Manning S., Cheek A.O., Rees B.B. Effects of long-term hypoxia on enzymes of carbohydrate metabolism in the Gulf killifish, Fundulus grandis. J Exp Biol 2006, 209:3851-3861.
    • (2006) J Exp Biol , vol.209 , pp. 3851-3861
    • Martinez, M.L.1    Landry, C.2    Boehm, R.3    Manning, S.4    Cheek, A.O.5    Rees, B.B.6
  • 19
    • 55549126488 scopus 로고    scopus 로고
    • Differential recovery from exercise and hypoxia exposure measured using 31P- and 1H-NMR in white muscle of the common carp Cyprinus carpio
    • Hallman T.M., Rojas-Vargas A.C., Jones D.R., Richards J.G. Differential recovery from exercise and hypoxia exposure measured using 31P- and 1H-NMR in white muscle of the common carp Cyprinus carpio. J Exp Biol 2008, 211:3237-3248.
    • (2008) J Exp Biol , vol.211 , pp. 3237-3248
    • Hallman, T.M.1    Rojas-Vargas, A.C.2    Jones, D.R.3    Richards, J.G.4
  • 20
    • 70449407298 scopus 로고    scopus 로고
    • The response of human skeletal muscle tissue to hypoxia
    • Lundby C., Calbet J.A.L., Robach P. The response of human skeletal muscle tissue to hypoxia. Cell Mol Life Sci 2009, 66:3615-3623.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 3615-3623
    • Lundby, C.1    Calbet, J.A.L.2    Robach, P.3
  • 21
    • 34249292919 scopus 로고    scopus 로고
    • Metabolic modulation induced by chronic hypoxia in rats using a comparative proteomic analysis of skeletal muscle tissue
    • De P.S., Ripamonti M., Vigano A., Moriggi M., Capitanio D., Samaja M., et al. Metabolic modulation induced by chronic hypoxia in rats using a comparative proteomic analysis of skeletal muscle tissue. J Proteome Res 2007, 6:1974-1984.
    • (2007) J Proteome Res , vol.6 , pp. 1974-1984
    • De, P.S.1    Ripamonti, M.2    Vigano, A.3    Moriggi, M.4    Capitanio, D.5    Samaja, M.6
  • 22
    • 65349148426 scopus 로고    scopus 로고
    • Proteomic changes in the crucian carp brain during exposure to anoxia
    • Smith R.W., Cash P., Ellefsen S., Nilsson G.E. Proteomic changes in the crucian carp brain during exposure to anoxia. Proteomics 2009, 9:2217-2229.
    • (2009) Proteomics , vol.9 , pp. 2217-2229
    • Smith, R.W.1    Cash, P.2    Ellefsen, S.3    Nilsson, G.E.4
  • 23
    • 44649161900 scopus 로고    scopus 로고
    • Comparison of two anoxia models in rainbow trout cells by a 2-DE and MS/MS-based proteome approach
    • Wulff T., Hoffmann E.K., Roepstorff P., Jessen F. Comparison of two anoxia models in rainbow trout cells by a 2-DE and MS/MS-based proteome approach. Proteomics 2008, 8:2035-2044.
    • (2008) Proteomics , vol.8 , pp. 2035-2044
    • Wulff, T.1    Hoffmann, E.K.2    Roepstorff, P.3    Jessen, F.4
  • 24
    • 41149172603 scopus 로고    scopus 로고
    • Long term anoxia in rainbow trout investigated by 2-DE and MS/MS
    • Wulff T., Jessen F., Roepstorff P., Hoffmann E.K. Long term anoxia in rainbow trout investigated by 2-DE and MS/MS. Proteomics 2008, 8:1009-1018.
    • (2008) Proteomics , vol.8 , pp. 1009-1018
    • Wulff, T.1    Jessen, F.2    Roepstorff, P.3    Hoffmann, E.K.4
  • 25
    • 17044399794 scopus 로고    scopus 로고
    • Protein expression patterns in zebrafish skeletal muscle: initial characterization and the effects of hypoxic exposure
    • Bosworth C.A., Chou C.W., Cole R.B., Rees B.B. Protein expression patterns in zebrafish skeletal muscle: initial characterization and the effects of hypoxic exposure. Proteomics 2005, 5:1362-1371.
    • (2005) Proteomics , vol.5 , pp. 1362-1371
    • Bosworth, C.A.1    Chou, C.W.2    Cole, R.B.3    Rees, B.B.4
  • 28
    • 32944454622 scopus 로고    scopus 로고
    • Proteome analysis of early post-mortem changes in two bovine muscle types: M. longissimus dorsi and M. semitendinosis
    • Jia X., Hollung K., Therkildsen M., Hildrum K.I., Bendixen E. Proteome analysis of early post-mortem changes in two bovine muscle types: M. longissimus dorsi and M. semitendinosis. Proteomics 2006, 6:936-944.
    • (2006) Proteomics , vol.6 , pp. 936-944
    • Jia, X.1    Hollung, K.2    Therkildsen, M.3    Hildrum, K.I.4    Bendixen, E.5
  • 29
    • 33645976443 scopus 로고    scopus 로고
    • Proteome analysis of the sarcoplasmic fraction of pig semimembranosus muscle: implications on meat color development
    • Sayd T., Morzel M., Chambon C., Franck M., Figwer P., Larzul C., et al. Proteome analysis of the sarcoplasmic fraction of pig semimembranosus muscle: implications on meat color development. J Agric Food Chem 2006, 54:2732-2737.
    • (2006) J Agric Food Chem , vol.54 , pp. 2732-2737
    • Sayd, T.1    Morzel, M.2    Chambon, C.3    Franck, M.4    Figwer, P.5    Larzul, C.6
  • 30
    • 69949156922 scopus 로고    scopus 로고
    • Differential expression of sarcoplasmic and myofibrillar proteins of rat soleus muscle during denervation atrophy
    • Sato Y., Shimizu M., Mizunoya W., Wariishi H., Tatsumi R., Buchman V.L., et al. Differential expression of sarcoplasmic and myofibrillar proteins of rat soleus muscle during denervation atrophy. Biosci Biotechnol Biochem 2009, 73:1748-1756.
    • (2009) Biosci Biotechnol Biochem , vol.73 , pp. 1748-1756
    • Sato, Y.1    Shimizu, M.2    Mizunoya, W.3    Wariishi, H.4    Tatsumi, R.5    Buchman, V.L.6
  • 31
    • 33645082204 scopus 로고    scopus 로고
    • Changes in cod muscle proteins during frozen storage revealed by proteome analysis and multivariate data analysis
    • Kjaersgard I.V., Norrelykke M.R., Jessen F. Changes in cod muscle proteins during frozen storage revealed by proteome analysis and multivariate data analysis. Proteomics 2006, 6:1606-1618.
    • (2006) Proteomics , vol.6 , pp. 1606-1618
    • Kjaersgard, I.V.1    Norrelykke, M.R.2    Jessen, F.3
  • 32
    • 61349120179 scopus 로고    scopus 로고
    • Combination of statistical approaches for analysis of 2-DE data gives complementary results
    • Grove H., Jorgensen B.M., Jessen F., Sondergaard I., Jacobsen S., Hollung K., et al. Combination of statistical approaches for analysis of 2-DE data gives complementary results. J Proteome Res 2008, 7:5119-5124.
    • (2008) J Proteome Res , vol.7 , pp. 5119-5124
    • Grove, H.1    Jorgensen, B.M.2    Jessen, F.3    Sondergaard, I.4    Jacobsen, S.5    Hollung, K.6
  • 33
    • 0042861611 scopus 로고    scopus 로고
    • The role of bioinformatics in two-dimensional gel electrophoresis
    • Dowsey A.W., Dunn M.J., Yang G.Z. The role of bioinformatics in two-dimensional gel electrophoresis. Proteomics 2003, 3:1567-1596.
    • (2003) Proteomics , vol.3 , pp. 1567-1596
    • Dowsey, A.W.1    Dunn, M.J.2    Yang, G.Z.3
  • 35
    • 56149116038 scopus 로고    scopus 로고
    • Contribution of cathepsins B, L and D to muscle protein profiles correlated with texture in rainbow trout (Oncorhynchus mykiss)
    • Godiksen H., Morzel M., Hyldig G., Jessen F. Contribution of cathepsins B, L and D to muscle protein profiles correlated with texture in rainbow trout (Oncorhynchus mykiss). Food Chem 2009, 113:889-896.
    • (2009) Food Chem , vol.113 , pp. 889-896
    • Godiksen, H.1    Morzel, M.2    Hyldig, G.3    Jessen, F.4
  • 37
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al. which is more generally applicable
    • Peterson G.L. A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal Biochem 1977, 83:346-356.
    • (1977) Anal Biochem , vol.83 , pp. 346-356
    • Peterson, G.L.1
  • 38
    • 0024362028 scopus 로고
    • Sensitive protein assay in presence of high-levels of lipid
    • Kaplan R.S., Pedersen P.L. Sensitive protein assay in presence of high-levels of lipid. Methods Enzymol 1989, 172:393-399.
    • (1989) Methods Enzymol , vol.172 , pp. 393-399
    • Kaplan, R.S.1    Pedersen, P.L.2
  • 40
    • 44449102829 scopus 로고    scopus 로고
    • Multivariate data analysis of two-dimensional gel electrophoresis protein patterns from few samples
    • Jensen K.N., Jessen F., Jorgensen B.M. Multivariate data analysis of two-dimensional gel electrophoresis protein patterns from few samples. J Proteome Res 2008, 7:1288-1296.
    • (2008) J Proteome Res , vol.7 , pp. 1288-1296
    • Jensen, K.N.1    Jessen, F.2    Jorgensen, B.M.3
  • 41
    • 0033636234 scopus 로고    scopus 로고
    • Modified jack-knife estimation of parameter uncertainty in bilinear modelling by partial least squares regression (PLSR)
    • Martens H., Martens M. Modified jack-knife estimation of parameter uncertainty in bilinear modelling by partial least squares regression (PLSR). Food Qual Preference 2000, 11:5-16.
    • (2000) Food Qual Preference , vol.11 , pp. 5-16
    • Martens, H.1    Martens, M.2
  • 42
    • 34247339305 scopus 로고    scopus 로고
    • PeakErazor: A windows-based program for improving peptide mass searches
    • Springer Verlag, Berlin, R.M. Kamp, J.J. Calvete, T. Choli-Papadopoulou (Eds.)
    • Hjerno K., Højrup P. PeakErazor: A windows-based program for improving peptide mass searches. Methods in proteome and protein analysis 2004, 359-370. Springer Verlag, Berlin. R.M. Kamp, J.J. Calvete, T. Choli-Papadopoulou (Eds.).
    • (2004) Methods in proteome and protein analysis , pp. 359-370
    • Hjerno, K.1    Højrup, P.2
  • 43
    • 0034095972 scopus 로고    scopus 로고
    • The current state of two-dimensional electrophoresis with immobilized pH gradients
    • Gorg A., Obermaier C., Boguth G., Harder A., Scheibe B., Wildgruber R., et al. The current state of two-dimensional electrophoresis with immobilized pH gradients. Electrophoresis 2000, 21:1037-1053.
    • (2000) Electrophoresis , vol.21 , pp. 1037-1053
    • Gorg, A.1    Obermaier, C.2    Boguth, G.3    Harder, A.4    Scheibe, B.5    Wildgruber, R.6
  • 45
    • 0035001778 scopus 로고    scopus 로고
    • Redox reactions of hemoglobin and myoglobin: biological and toxicological implications
    • Alayash A.I., Patel R.P., Cashon R.E. Redox reactions of hemoglobin and myoglobin: biological and toxicological implications. Antioxid Redox Signal 2001, 3:313-327.
    • (2001) Antioxid Redox Signal , vol.3 , pp. 313-327
    • Alayash, A.I.1    Patel, R.P.2    Cashon, R.E.3
  • 46
    • 0030792094 scopus 로고    scopus 로고
    • Oxygen-regulated transferrin expression is mediated by hypoxia-inducible factor-1
    • Rolfs A., Kvietikova I., Gassmann M., Wenger R.H. Oxygen-regulated transferrin expression is mediated by hypoxia-inducible factor-1. J Biol Chem 1997, 272:20055-20062.
    • (1997) J Biol Chem , vol.272 , pp. 20055-20062
    • Rolfs, A.1    Kvietikova, I.2    Gassmann, M.3    Wenger, R.H.4
  • 47
    • 0142183440 scopus 로고    scopus 로고
    • Effects of iron regulatory protein regulation on iron homeostasis during hypoxia
    • Schneider B.D., Leibold E.A. Effects of iron regulatory protein regulation on iron homeostasis during hypoxia. Blood 2003, 102:3404-3411.
    • (2003) Blood , vol.102 , pp. 3404-3411
    • Schneider, B.D.1    Leibold, E.A.2
  • 48
    • 0015980699 scopus 로고
    • Transfer of heme from ferrihemoglobin and ferrihemoglobin isolated chains to hemopexin
    • Hrkal Z., Vodrazka Z., Kalousek I. Transfer of heme from ferrihemoglobin and ferrihemoglobin isolated chains to hemopexin. Eur J Biochem 1974, 43:73-78.
    • (1974) Eur J Biochem , vol.43 , pp. 73-78
    • Hrkal, Z.1    Vodrazka, Z.2    Kalousek, I.3
  • 49
    • 0035746152 scopus 로고    scopus 로고
    • Muscle tissue adaptations to hypoxia
    • Hoppeler H., Vogt M. Muscle tissue adaptations to hypoxia. J Exp Biol 2001, 204:3133-3139.
    • (2001) J Exp Biol , vol.204 , pp. 3133-3139
    • Hoppeler, H.1    Vogt, M.2
  • 51
    • 0141645435 scopus 로고    scopus 로고
    • The association of glycolytic enzymes with cellular and model membranes
    • Gutowicz J., Terlecki G. The association of glycolytic enzymes with cellular and model membranes. Cell Mol Biol Lett 2003, 8:667-680.
    • (2003) Cell Mol Biol Lett , vol.8 , pp. 667-680
    • Gutowicz, J.1    Terlecki, G.2
  • 52
    • 0032129927 scopus 로고    scopus 로고
    • Effect of hypoxia on the activity and binding of glycolytic and associated enzymes in sea scorpion tissues
    • Lushchak V.I., Bahnjukova T.V., Storey K.B. Effect of hypoxia on the activity and binding of glycolytic and associated enzymes in sea scorpion tissues. Braz J Med Biol Res 1998, 31:1059-1067.
    • (1998) Braz J Med Biol Res , vol.31 , pp. 1059-1067
    • Lushchak, V.I.1    Bahnjukova, T.V.2    Storey, K.B.3
  • 54
    • 54049123250 scopus 로고    scopus 로고
    • Regulation of pyruvate dehydrogenase in the common killifish, Fundulus heteroclitus, during hypoxia exposure
    • Richards J.G., Sardella B.A., Schulte P.M. Regulation of pyruvate dehydrogenase in the common killifish, Fundulus heteroclitus, during hypoxia exposure. Am J Physiol Regul Integr Comp Physiol 2008, 295:R979-R990.
    • (2008) Am J Physiol Regul Integr Comp Physiol , vol.295
    • Richards, J.G.1    Sardella, B.A.2    Schulte, P.M.3
  • 55
    • 0025191301 scopus 로고
    • Evidence for compartmentalized adenylate kinase catalysis serving a high energy phosphoryl transfer function in rat skeletal muscle
    • Zeleznikar R.J., Heyman R.A., Graeff R.M., Walseth T.F., Dawis S.M., Butz E.A., et al. Evidence for compartmentalized adenylate kinase catalysis serving a high energy phosphoryl transfer function in rat skeletal muscle. J Biol Chem 1990, 265:300-311.
    • (1990) J Biol Chem , vol.265 , pp. 300-311
    • Zeleznikar, R.J.1    Heyman, R.A.2    Graeff, R.M.3    Walseth, T.F.4    Dawis, S.M.5    Butz, E.A.6
  • 56
    • 0033612362 scopus 로고    scopus 로고
    • Adenylate kinase-catalyzed phosphotransfer in the myocardium: increased contribution in heart failure
    • Dzeja P.P., Vitkevicius K.T., Redfield M.M., Burnett J.C., Terzic A. Adenylate kinase-catalyzed phosphotransfer in the myocardium: increased contribution in heart failure. Circ Res 1999, 84:1137-1143.
    • (1999) Circ Res , vol.84 , pp. 1137-1143
    • Dzeja, P.P.1    Vitkevicius, K.T.2    Redfield, M.M.3    Burnett, J.C.4    Terzic, A.5
  • 59
    • 0033938994 scopus 로고    scopus 로고
    • Recurring views on the structure and function of the cytoskeleton: a 300-year epic
    • Frixione E. Recurring views on the structure and function of the cytoskeleton: a 300-year epic. Cell Motil Cytoskeleton 2000, 46:73-94.
    • (2000) Cell Motil Cytoskeleton , vol.46 , pp. 73-94
    • Frixione, E.1
  • 62
    • 0029944768 scopus 로고    scopus 로고
    • The relation between cellular sodium, pH and volumes and the activity of Na/H antiport during hypothermic ischemia: multinuclear NMR studies of rat hearts
    • Askenasy N., Vivi A., Tassini M., Navon G. The relation between cellular sodium, pH and volumes and the activity of Na/H antiport during hypothermic ischemia: multinuclear NMR studies of rat hearts. J Mol Cell Cardiol 1996, 28:589-601.
    • (1996) J Mol Cell Cardiol , vol.28 , pp. 589-601
    • Askenasy, N.1    Vivi, A.2    Tassini, M.3    Navon, G.4


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