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Volumn 8, Issue 5, 2008, Pages 1009-1018

Long term anoxia in rainbow trout investigated by 2-DE and MS/MS

Author keywords

[No Author keywords available]

Indexed keywords

CALPAIN; ISOCITRATE DEHYDROGENASE; MICROTUBULE ASSOCIATED PROTEIN; NITROGEN; OXYGEN; PHOSPHOGLYCERATE MUTASE; RHO GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 41149172603     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200700460     Document Type: Article
Times cited : (27)

References (75)
  • 1
    • 14644442283 scopus 로고    scopus 로고
    • Oxygen, oxidative stress, hypoxia, and heart failure
    • Giordano, F. J., Oxygen, oxidative stress, hypoxia, and heart failure. J. Clin. Invest. 2005, 115, 500-508.
    • (2005) J. Clin. Invest , vol.115 , pp. 500-508
    • Giordano, F.J.1
  • 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
    • 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
  • 4
    • 0036708698 scopus 로고    scopus 로고
    • Hypoxia: From molecular responses to ecosystem responses
    • Wu, R. S., Hypoxia: From molecular responses to ecosystem responses. Mar. Pollut. Bull. 2002, 45, 35-45.
    • (2002) Mar. Pollut. Bull , vol.45 , pp. 35-45
    • Wu, R.S.1
  • 5
    • 3042684300 scopus 로고    scopus 로고
    • Fish consumption and incidence of stroke: A meta-analysis of cohort studies
    • He, K., Song, Y., Daviglus, M. L., Liu, K. et al., Fish consumption and incidence of stroke: A meta-analysis of cohort studies. Stroke 2004, 35, 1538-1542.
    • (2004) Stroke , vol.35 , pp. 1538-1542
    • He, K.1    Song, Y.2    Daviglus, M.L.3    Liu, K.4
  • 6
    • 0032818324 scopus 로고    scopus 로고
    • Fish consumption and coronary heart disease mortality. A systematic review of prospective cohort studies
    • Marckmann, P., Gronbaek, M., Fish consumption and coronary heart disease mortality. A systematic review of prospective cohort studies. Eur. J. Clin. Nutr. 1999, 53, 585-590.
    • (1999) Eur. J. Clin. Nutr , vol.53 , pp. 585-590
    • Marckmann, P.1    Gronbaek, M.2
  • 7
    • 1942456899 scopus 로고    scopus 로고
    • Characterization of a novel fibroblast-like cell line from rainbow trout and responses to sublethal anoxia
    • Ossum, C. G., Hoffmann, E. K., Vijayan, M. M., Holt, S. E., Bols, N. C., Characterization of a novel fibroblast-like cell line from rainbow trout and responses to sublethal anoxia. J. Fish Biol. 2004, 64, 1103-1116.
    • (2004) J. Fish Biol , vol.64 , pp. 1103-1116
    • Ossum, C.G.1    Hoffmann, E.K.2    Vijayan, M.M.3    Holt, S.E.4    Bols, N.C.5
  • 8
    • 0038353381 scopus 로고    scopus 로고
    • Proteome analysis elucidating post-mortem changes in cod (Gadus morhua) muscle proteins
    • Kjaersgard, I. V., Jessen, F., Proteome analysis elucidating post-mortem changes in cod (Gadus morhua) muscle proteins. J. Agric. Food Chem. 2003, 51, 3985-3991.
    • (2003) J. Agric. Food Chem , vol.51 , pp. 3985-3991
    • Kjaersgard, I.V.1    Jessen, F.2
  • 9
    • 33646507653 scopus 로고    scopus 로고
    • Modifications of trout (Oncorhynchus mykiss) muscle proteins by preslaughter activity
    • Morzel, M., Chambon, C., Lefevre, F., Paboeuf, G., Laville, E., Modifications of trout (Oncorhynchus mykiss) muscle proteins by preslaughter activity. J. Agric. Food Chem. 2006, 54, 2997-3001.
    • (2006) J. Agric. Food Chem , vol.54 , pp. 2997-3001
    • Morzel, M.1    Chambon, C.2    Lefevre, F.3    Paboeuf, G.4    Laville, E.5
  • 10
    • 1342283027 scopus 로고    scopus 로고
    • Analysis of expression and post-translational modification of proteins during hypoxia
    • Kumar, G. K., Klein, J. B., Analysis of expression and post-translational modification of proteins during hypoxia. J. Appl. Physiol. 2004, 96, 1178-1186.
    • (2004) J. Appl. Physiol , vol.96 , pp. 1178-1186
    • Kumar, G.K.1    Klein, J.B.2
  • 11
    • 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
  • 12
    • 14644420877 scopus 로고    scopus 로고
    • Effects of hypoxia on the venous circulation in rainbow trout (Oncorhynchus mykiss)
    • Sandblom, E., Axelsson, M., Effects of hypoxia on the venous circulation in rainbow trout (Oncorhynchus mykiss). Comp. Biochem. Physiol. A Mol. Integr. Physiol. 2005, 140, 233-239.
    • (2005) Comp. Biochem. Physiol. A Mol. Integr. Physiol , vol.140 , pp. 233-239
    • Sandblom, E.1    Axelsson, M.2
  • 13
  • 15
    • 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
  • 16
    • 2642548404 scopus 로고    scopus 로고
    • Preconditioning stimuli do not benefit the myocardium of hypoxia-tolerant rainbow trout (Oncorhynchus mykiss)
    • Overgaard, J., Stecyk, J. A., Gesser, H., Wang, T. et al., Preconditioning stimuli do not benefit the myocardium of hypoxia-tolerant rainbow trout (Oncorhynchus mykiss). J. Comp. Physiol. 2004, 174, 329-340.
    • (2004) J. Comp. Physiol , vol.174 , pp. 329-340
    • Overgaard, J.1    Stecyk, J.A.2    Gesser, H.3    Wang, T.4
  • 17
    • 1642267591 scopus 로고    scopus 로고
    • All rainbow trout (Oncorhynchus mykiss) are not created equal: Intra-specific variation in cardiac hypoxia tolerance
    • Faust, H. A., Gamperl, A. K., Rodnick, K. J., All rainbow trout (Oncorhynchus mykiss) are not created equal: Intra-specific variation in cardiac hypoxia tolerance. J. Exp. Biol. 2004, 207, 1005-1015.
    • (2004) J. Exp. Biol , vol.207 , pp. 1005-1015
    • Faust, H.A.1    Gamperl, A.K.2    Rodnick, K.J.3
  • 18
    • 0036010758 scopus 로고    scopus 로고
    • Reversible suppression of protein synthesis in concert with polysome disaggregation during anoxia exposure in Littorina littorea
    • Larade, K., Storey, K. B., Reversible suppression of protein synthesis in concert with polysome disaggregation during anoxia exposure in Littorina littorea. Mol. Cell. Biochem. 2002, 232, 121-127.
    • (2002) Mol. Cell. Biochem , vol.232 , pp. 121-127
    • Larade, K.1    Storey, K.B.2
  • 19
    • 0029973998 scopus 로고    scopus 로고
    • Tissue-specific changes in protein synthesis rates in vivo during anoxia in crucian carp
    • Smith, R. W., Houlihan, D. F., Nilsson, G. E., Brechin, J. G., Tissue-specific changes in protein synthesis rates in vivo during anoxia in crucian carp. Am.J. Physiol. 1996, 271, R897-R904.
    • (1996) Am.J. Physiol , vol.271
    • Smith, R.W.1    Houlihan, D.F.2    Nilsson, G.E.3    Brechin, J.G.4
  • 20
    • 0030683567 scopus 로고    scopus 로고
    • Role of the actin cytoskeleton in ischemia induced cell injury and repair
    • Molitoris, B. A., Leiser, J., Wagner, M. C., Role of the actin cytoskeleton in ischemia induced cell injury and repair. Pediatr. Nephrol. 1997, 11, 761-767.
    • (1997) Pediatr. Nephrol , vol.11 , pp. 761-767
    • Molitoris, B.A.1    Leiser, J.2    Wagner, M.C.3
  • 21
    • 0033948524 scopus 로고    scopus 로고
    • Coincident microvillar actin bundle disruption and perinuclear actin sequestration in anoxic proximal tubule
    • White, P., Doctor, R. B., Dahl, R. H., Chen, J., Coincident microvillar actin bundle disruption and perinuclear actin sequestration in anoxic proximal tubule. Am. J. Physiol. Renal Physiol. 2000, 278, F886-F893.
    • (2000) Am. J. Physiol. Renal Physiol , vol.278
    • White, P.1    Doctor, R.B.2    Dahl, R.H.3    Chen, J.4
  • 22
    • 0034942907 scopus 로고    scopus 로고
    • Crucial role of calpain in hypoxic PC12 cell death: Capain, but not caspases, mediates degradation of cytoskeletal proteins and protein kinase C-alpha and -delta
    • Yamakawa, H., Banno, Y., Nakashima, S., Yoshimura, S. et al., Crucial role of calpain in hypoxic PC12 cell death: Capain, but not caspases, mediates degradation of cytoskeletal proteins and protein kinase C-alpha and -delta. Neurol. Res. 2001, 23, 522-530.
    • (2001) Neurol. Res , vol.23 , pp. 522-530
    • Yamakawa, H.1    Banno, Y.2    Nakashima, S.3    Yoshimura, S.4
  • 23
    • 15544387084 scopus 로고    scopus 로고
    • Rac and Rho play opposing roles in the regulation of hypoxia/reoxygenation-induced permeability changes in pulmonary artery endothelial cells
    • Wojciak-Stothard, B., Tsang, L. Y., Haworth, S. G., Rac and Rho play opposing roles in the regulation of hypoxia/reoxygenation-induced permeability changes in pulmonary artery endothelial cells. Am. J. Physiol. Lung Cell. Mol. Physiol. 2005, 288, L749-L760.
    • (2005) Am. J. Physiol. Lung Cell. Mol. Physiol , vol.288
    • Wojciak-Stothard, B.1    Tsang, L.Y.2    Haworth, S.G.3
  • 24
    • 24144493814 scopus 로고    scopus 로고
    • Mitochondrial complex III is required for hypoxia-induced ROS production and cellular oxygen sensing
    • Guzy, R. D., Hoyos, B., Robin, E., Chen, H. et al., Mitochondrial complex III is required for hypoxia-induced ROS production and cellular oxygen sensing. Cell Metab. 2005, 1, 401-408.
    • (2005) Cell Metab , vol.1 , pp. 401-408
    • Guzy, R.D.1    Hoyos, B.2    Robin, E.3    Chen, H.4
  • 26
    • 0032837481 scopus 로고    scopus 로고
    • Preparation of primary cell cultures from lamprey
    • Ma, C., Collodi, P., Preparation of primary cell cultures from lamprey. Methods Cell Sci. 1999, 21, 39-46.
    • (1999) Methods Cell Sci , vol.21 , pp. 39-46
    • Ma, C.1    Collodi, P.2
  • 27
    • 0034786029 scopus 로고    scopus 로고
    • Limitations to oxygen diffusion and equilibration in in vitro cell exposure systems in hyperoxia and hypoxia
    • Allen, C. B., Schneider, B. K., White, C. W., Limitations to oxygen diffusion and equilibration in in vitro cell exposure systems in hyperoxia and hypoxia. Am. J. Physiol. Lung Cell. Mol. Physiol. 2001, 281, L1021-L1027.
    • (2001) Am. J. Physiol. Lung Cell. Mol. Physiol , vol.281
    • Allen, C.B.1    Schneider, B.K.2    White, C.W.3
  • 28
    • 0017613512 scopus 로고    scopus 로고
    • 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.
    • 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.
  • 31
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O., Mann, M., Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal.Chem. 1996, 68, 850-858.
    • (1996) Anal.Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 32
    • 0033057707 scopus 로고    scopus 로고
    • Sample purification and preparation technique based on nano-scale reversed-phase columns for the sensitive analysis of complex peptide mixtures by matrix-assisted laser desorption/ionization mass spectrometry
    • Gobom, J., Nordhoff, E., Mirgorodskaya, E., Ekman, R., Roepstorff, P., Sample purification and preparation technique based on nano-scale reversed-phase columns for the sensitive analysis of complex peptide mixtures by matrix-assisted laser desorption/ionization mass spectrometry. J. Mass Spectrom. 1999, 34, 105-116.
    • (1999) J. Mass Spectrom , vol.34 , pp. 105-116
    • Gobom, J.1    Nordhoff, E.2    Mirgorodskaya, E.3    Ekman, R.4    Roepstorff, P.5
  • 33
    • 0035514030 scopus 로고    scopus 로고
    • GPMAW - a software tool for analyzing proteins and peptides
    • Peri, S., Steen, H., Pandey, A., GPMAW - a software tool for analyzing proteins and peptides. Trends Biochem. Sci. 2001, 26, 687-689.
    • (2001) Trends Biochem. Sci , vol.26 , pp. 687-689
    • Peri, S.1    Steen, H.2    Pandey, A.3
  • 34
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N., Pappin, D. J., Creasy, D. M., Cottrell, J. S., Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999, 20, 3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 35
    • 33744813523 scopus 로고    scopus 로고
    • Regulation of the mitogen-activated protein kinase p44 ERK activity during anoxia/recovery in rainbow trout hypodermal fibroblasts
    • Ossum, C. G., Wulff, T., Hoffmann, E. K., Regulation of the mitogen-activated protein kinase p44 ERK activity during anoxia/recovery in rainbow trout hypodermal fibroblasts. J. Exp. Biol. 2006, 209, 1765-1776.
    • (2006) J. Exp. Biol , vol.209 , pp. 1765-1776
    • Ossum, C.G.1    Wulff, T.2    Hoffmann, E.K.3
  • 36
    • 0034095972 scopus 로고    scopus 로고
    • The current state of two-dimensional electrophoresis with immobilized pH gradients
    • Gorg, A., Obermaier, C., Boguth, G., Harder, A. 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
  • 37
    • 13344269000 scopus 로고    scopus 로고
    • From proteins to proteomes: Large scale protein identification by two-dimensional electrophoresis and amino acid analysis
    • Wilkins, M. R., Pasquali, C., Appel, R. D., Ou, K. et al., From proteins to proteomes: Large scale protein identification by two-dimensional electrophoresis and amino acid analysis. Biotechnology (NY) 1996, 14, 61-65.
    • (1996) Biotechnology (NY) , vol.14 , pp. 61-65
    • Wilkins, M.R.1    Pasquali, C.2    Appel, R.D.3    Ou, K.4
  • 38
    • 0037427445 scopus 로고    scopus 로고
    • Mitochondria and ischemic reperfusion damage in the adult and in the developing brain
    • Blomgren, K., Zhu, C., Hallin, U., Hagberg, H., Mitochondria and ischemic reperfusion damage in the adult and in the developing brain. Biochem. Biophys. Res. Commun. 2003, 304, 551-559.
    • (2003) Biochem. Biophys. Res. Commun , vol.304 , pp. 551-559
    • Blomgren, K.1    Zhu, C.2    Hallin, U.3    Hagberg, H.4
  • 39
    • 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
  • 40
    • 0034233407 scopus 로고    scopus 로고
    • Oxygen consumption, blood lactate and inter-individual variation in the gulf killifish, Fundulus grandis, during hypoxia and recovery
    • Virani, N. A., Rees, B. B., Oxygen consumption, blood lactate and inter-individual variation in the gulf killifish, Fundulus grandis, during hypoxia and recovery. Comp. Biochem. Physiol. A Mol. Integr. Physiol. 2000, 126, 397-405.
    • (2000) Comp. Biochem. Physiol. A Mol. Integr. Physiol , vol.126 , pp. 397-405
    • Virani, N.A.1    Rees, B.B.2
  • 41
    • 0035799346 scopus 로고    scopus 로고
    • Functional proteomics: Examining the effects of hypoxia on the cytotrophoblast protein repertoire
    • Hoang, V. M., Foulk, R., Clauser, K., Burlingame, A. et al., Functional proteomics: Examining the effects of hypoxia on the cytotrophoblast protein repertoire. Biochemistry 2001, 40, 4077-4086.
    • (2001) Biochemistry , vol.40 , pp. 4077-4086
    • Hoang, V.M.1    Foulk, R.2    Clauser, K.3    Burlingame, A.4
  • 42
    • 0032525935 scopus 로고    scopus 로고
    • Hypoxia-induced expression of phosphoglycerate mutase B in fibroblasts
    • Takahashi, Y., Takahashi, S., Yoshimi, T., Miura, T., Hypoxia-induced expression of phosphoglycerate mutase B in fibroblasts. Eur. J. Biochem. 1998, 254, 497-504.
    • (1998) Eur. J. Biochem , vol.254 , pp. 497-504
    • Takahashi, Y.1    Takahashi, S.2    Yoshimi, T.3    Miura, T.4
  • 43
    • 0022590628 scopus 로고
    • Defense strategies against hypoxia and hypothermia
    • Hochachka, P. W., Defense strategies against hypoxia and hypothermia. Science 1986, 231, 234-241.
    • (1986) Science , vol.231 , pp. 234-241
    • Hochachka, P.W.1
  • 44
    • 0034083353 scopus 로고    scopus 로고
    • Oxygen-dependent energetics of anoxia-tolerant and anoxia-intolerant hepatocytes
    • Krumschnabel, G., Schwarzbaum, P. J., Lisch, J., Biasi, C., Wieser, W., Oxygen-dependent energetics of anoxia-tolerant and anoxia-intolerant hepatocytes. J. Exp. Biol. 2000, 203, 951-959.
    • (2000) J. Exp. Biol , vol.203 , pp. 951-959
    • Krumschnabel, G.1    Schwarzbaum, P.J.2    Lisch, J.3    Biasi, C.4    Wieser, W.5
  • 46
    • 1642349839 scopus 로고    scopus 로고
    • Calpain activity is generally elevated during transformation but has oncogene-specific biological functions
    • Carragher, N. O., Fonseca, B. D., Frame, M. C., Calpain activity is generally elevated during transformation but has oncogene-specific biological functions. Neoplasia 2004, 6, 53-73.
    • (2004) Neoplasia , vol.6 , pp. 53-73
    • Carragher, N.O.1    Fonseca, B.D.2    Frame, M.C.3
  • 48
    • 0033788531 scopus 로고    scopus 로고
    • The calpain small subunit gene is essential: Its inactivation results in embryonic lethality
    • Zimmerman, U. J., Boring, L., Pak, J. H., Mukerjee, N., Wang, K. K., The calpain small subunit gene is essential: Its inactivation results in embryonic lethality. IUBMB Life 2000, 50, 63-68.
    • (2000) IUBMB Life , vol.50 , pp. 63-68
    • Zimmerman, U.J.1    Boring, L.2    Pak, J.H.3    Mukerjee, N.4    Wang, K.K.5
  • 49
    • 0034116930 scopus 로고    scopus 로고
    • Disruption of the murine calpain small subunit gene, Capn4: Calpain is essential for embryonic development but not for cell growth and division
    • Arthur, J. S., Elce, J. S., Hegadorn, C., Williams, K., Greer, P. A., Disruption of the murine calpain small subunit gene, Capn4: Calpain is essential for embryonic development but not for cell growth and division. Mol. Cell. Biol. 2000, 20, 4474-4481.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 4474-4481
    • Arthur, J.S.1    Elce, J.S.2    Hegadorn, C.3    Williams, K.4    Greer, P.A.5
  • 51
    • 33947120556 scopus 로고    scopus 로고
    • Hypoxia-induced cell death of HepG2 cells involves a necrotic cell death mediated by calpain
    • Kim, M. J., Oh, S. J., Park, S. H., Kang, H. J. et al., Hypoxia-induced cell death of HepG2 cells involves a necrotic cell death mediated by calpain. Apoptosis 2006, 12, 707-718.
    • (2006) Apoptosis , vol.12 , pp. 707-718
    • Kim, M.J.1    Oh, S.J.2    Park, S.H.3    Kang, H.J.4
  • 52
    • 0030014211 scopus 로고    scopus 로고
    • Hepatocellular carcinoma cells resist necrosis during anoxia by preventing phospholipase-mediated calpain activation
    • Arora, A. S., de Groen, P. C., Croall, D. E., Emori, Y., Gores, G. J., Hepatocellular carcinoma cells resist necrosis during anoxia by preventing phospholipase-mediated calpain activation. J. Cell. Physiol. 1996, 167, 434-442.
    • (1996) J. Cell. Physiol , vol.167 , pp. 434-442
    • Arora, A.S.1    de Groen, P.C.2    Croall, D.E.3    Emori, Y.4    Gores, G.J.5
  • 53
    • 0034090253 scopus 로고    scopus 로고
    • Calpain inhibitors confer biochemical, but not electrophysiological, protection against anoxia in rat optic nerves
    • Jiang, Q., Stys, P. K., Calpain inhibitors confer biochemical, but not electrophysiological, protection against anoxia in rat optic nerves. J. Neurochem. 2000, 74, 2101-2107.
    • (2000) J. Neurochem , vol.74 , pp. 2101-2107
    • Jiang, Q.1    Stys, P.K.2
  • 54
    • 0033598349 scopus 로고    scopus 로고
    • Progressive impairment of kidneys and reproductive organs in mice lacking Rho GDIalpha
    • Togawa, A., Miyoshi, J., Ishizaki, H., Tanaka, M. et al., Progressive impairment of kidneys and reproductive organs in mice lacking Rho GDIalpha. Oncogene 1999, 18, 5373-5380.
    • (1999) Oncogene , vol.18 , pp. 5373-5380
    • Togawa, A.1    Miyoshi, J.2    Ishizaki, H.3    Tanaka, M.4
  • 56
    • 0033039738 scopus 로고    scopus 로고
    • Rho controls actin cytoskeletal assembly in renal epithelial cells during ATP depletion and recovery
    • Raman, N., Atkinson, S. J., Rho controls actin cytoskeletal assembly in renal epithelial cells during ATP depletion and recovery. Am. J. Physiol. 1999, 276, C1312-C1324.
    • (1999) Am. J. Physiol , vol.276
    • Raman, N.1    Atkinson, S.J.2
  • 57
    • 0038679291 scopus 로고    scopus 로고
    • Rho GTPases show differential sensitivity to nucleotide triphosphate depletion in a model of ischemic cell injury
    • Hallett, M. A., Dagher, P. C., Atkinson, S. J., Rho GTPases show differential sensitivity to nucleotide triphosphate depletion in a model of ischemic cell injury. Am. J. Physiol. Cell Physiol. 2003, 285, C129-C138.
    • (2003) Am. J. Physiol. Cell Physiol , vol.285
    • Hallett, M.A.1    Dagher, P.C.2    Atkinson, S.J.3
  • 58
    • 0035838422 scopus 로고    scopus 로고
    • Critical role for the EB1 and APC interaction in the regulation of microtubule polymerization
    • Nakamura, M., Zhou, X. Z., Lu, K. P., Critical role for the EB1 and APC interaction in the regulation of microtubule polymerization. Curr. Biol. 2001, 11, 1062-1067.
    • (2001) Curr. Biol , vol.11 , pp. 1062-1067
    • Nakamura, M.1    Zhou, X.Z.2    Lu, K.P.3
  • 59
    • 33644865868 scopus 로고    scopus 로고
    • Cooperation of EB1-Mal3 and the Bub1 spindle checkpoint
    • Asakawa, K., Toda, T., Cooperation of EB1-Mal3 and the Bub1 spindle checkpoint. Cell Cycle 2006, 5, 27-30.
    • (2006) Cell Cycle , vol.5 , pp. 27-30
    • Asakawa, K.1    Toda, T.2
  • 60
    • 0034658368 scopus 로고    scopus 로고
    • EB1 proteins regulate microtubule dynamics, cell polarity, and chromosome stability
    • Tirnauer, J. S., Bierer, B. E., EB1 proteins regulate microtubule dynamics, cell polarity, and chromosome stability. J. Cell. Biol. 2000, 149, 761-766.
    • (2000) J. Cell. Biol , vol.149 , pp. 761-766
    • Tirnauer, J.S.1    Bierer, B.E.2
  • 62
    • 1442281893 scopus 로고    scopus 로고
    • Microtubule alteration is an early cellular reaction to the metabolic challenge in ischemic cardiomyocytes
    • Vandroux, D., Schaeffer, C., Tissier, C., Lalande, A. et al., Microtubule alteration is an early cellular reaction to the metabolic challenge in ischemic cardiomyocytes. Mol. Cell. Biochem. 2004, 258, 99-108.
    • (2004) Mol. Cell. Biochem , vol.258 , pp. 99-108
    • Vandroux, D.1    Schaeffer, C.2    Tissier, C.3    Lalande, A.4
  • 63
    • 4444360489 scopus 로고    scopus 로고
    • EB1 and APC bind to mDia to stabilize microtubules downstream of Rho and promote cell migration
    • Wen, Y., Eng, C. H., Schmoranzer, J., Cabrera-Poch, N. et al., EB1 and APC bind to mDia to stabilize microtubules downstream of Rho and promote cell migration. Nat. Cell Biol. 2004, 6, 820-830.
    • (2004) Nat. Cell Biol , vol.6 , pp. 820-830
    • Wen, Y.1    Eng, C.H.2    Schmoranzer, J.3    Cabrera-Poch, N.4
  • 64
    • 0842331443 scopus 로고    scopus 로고
    • Localized stabilization of microtubules by integrin- and FAK-facilitated Rho signaling
    • Palazzo, A. F., Eng, C. H., Schlaepfer, D. D., Marcantonio, E. E., Gundersen, G. G., Localized stabilization of microtubules by integrin- and FAK-facilitated Rho signaling. Science 2004, 303, 836-839.
    • (2004) Science , vol.303 , pp. 836-839
    • Palazzo, A.F.1    Eng, C.H.2    Schlaepfer, D.D.3    Marcantonio, E.E.4    Gundersen, G.G.5
  • 65
    • 33846286901 scopus 로고    scopus 로고
    • Shaping the actin cytoskeleton using microtubule tips
    • Basu, R., Chang, F., Shaping the actin cytoskeleton using microtubule tips. Curr. Opin. Cell Biol. 2006 19, 88-94.
    • (2006) Curr. Opin. Cell Biol , vol.19 , pp. 88-94
    • Basu, R.1    Chang, F.2
  • 67
    • 0036080574 scopus 로고    scopus 로고
    • Ischemia induces alterations in actin filaments in renal vascular smooth muscle cells
    • Kwon, O., Phillips, C. L., Molitoris, B. A., Ischemia induces alterations in actin filaments in renal vascular smooth muscle cells. Am. J. Physiol. Renal Physiol. 2002, 282, F1012-F1019.
    • (2002) Am. J. Physiol. Renal Physiol , vol.282
    • Kwon, O.1    Phillips, C.L.2    Molitoris, B.A.3
  • 68
    • 0343581291 scopus 로고    scopus 로고
    • State of actin filaments is changed by anoxia in cultured rat neocortical neurons
    • Friedman, J. E., Chow, E. J., Haddad, G. G., State of actin filaments is changed by anoxia in cultured rat neocortical neurons. Neuroscience 1998, 82, 421-427.
    • (1998) Neuroscience , vol.82 , pp. 421-427
    • Friedman, J.E.1    Chow, E.J.2    Haddad, G.G.3
  • 69
    • 0033575003 scopus 로고    scopus 로고
    • Direct comparison of GAPDH, beta-actin, cyclophilin, and 28S rRNA as internal standards for quantifying RNA levels under hypoxia
    • Zhong, H., Simons, J. W., Direct comparison of GAPDH, beta-actin, cyclophilin, and 28S rRNA as internal standards for quantifying RNA levels under hypoxia. Biochem. Biophys. Res. Commun. 1999, 259, 523-526.
    • (1999) Biochem. Biophys. Res. Commun , vol.259 , pp. 523-526
    • Zhong, H.1    Simons, J.W.2
  • 70
    • 0032496159 scopus 로고    scopus 로고
    • Intracellular signaling by reactive oxygen species during hypoxia in cardiomyocytes
    • Duranteau, J., Chandel, N. S., Kulisz, A., Shao, Z., Schumacker, P. T., Intracellular signaling by reactive oxygen species during hypoxia in cardiomyocytes. J. Biol. Chem. 1998, 273, 11619-11624.
    • (1998) J. Biol. Chem , vol.273 , pp. 11619-11624
    • Duranteau, J.1    Chandel, N.S.2    Kulisz, A.3    Shao, Z.4    Schumacker, P.T.5
  • 71
    • 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. 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
  • 72
    • 18844400905 scopus 로고    scopus 로고
    • Peroxiredoxin 6, a 1-Cys peroxiredoxin, functions in antioxidant defense and lung phospholipid metabolism
    • Manevich, Y., Fisher, A. B., Peroxiredoxin 6, a 1-Cys peroxiredoxin, functions in antioxidant defense and lung phospholipid metabolism. Free Radic. Biol. Med. 2005, 38, 1422-1432.
    • (2005) Free Radic. Biol. Med , vol.38 , pp. 1422-1432
    • Manevich, Y.1    Fisher, A.B.2
  • 73
    • 33845911313 scopus 로고    scopus 로고
    • Peroxiredoxin 6 is a potent cytoprotective enzyme in the epidermis
    • Kumin, A., Huber, C., Rulicke, T., Wolf, E., Werner, S., Peroxiredoxin 6 is a potent cytoprotective enzyme in the epidermis. Am. J. Pathol. 2006, 169, 1194-1205.
    • (2006) Am. J. Pathol , vol.169 , pp. 1194-1205
    • Kumin, A.1    Huber, C.2    Rulicke, T.3    Wolf, E.4    Werner, S.5
  • 74
    • 0042090273 scopus 로고    scopus 로고
    • Mice with targeted mutation of peroxiredoxin 6 develop normally but are susceptible to oxidative stress
    • Wang, X., Phelan, S. A., Forsman-Semb, K., Taylor, E. F. et al., Mice with targeted mutation of peroxiredoxin 6 develop normally but are susceptible to oxidative stress. J. Biol. Chem. 2003, 278, 25179-25190.
    • (2003) J. Biol. Chem , vol.278 , pp. 25179-25190
    • Wang, X.1    Phelan, S.A.2    Forsman-Semb, K.3    Taylor, E.F.4
  • 75
    • 33645683071 scopus 로고    scopus 로고
    • Transgenic mice overexpressing peroxiredoxin 6 show increased resistance to lung injury in hyperoxia
    • Wang, Y., Phelan, S. A., Manevich, Y., Feinstein, S. I., Fisher, A. B., Transgenic mice overexpressing peroxiredoxin 6 show increased resistance to lung injury in hyperoxia. Am. J. Respir. Cell Mol. Biol. 2006, 34, 481-486.
    • (2006) Am. J. Respir. Cell Mol. Biol , vol.34 , pp. 481-486
    • Wang, Y.1    Phelan, S.A.2    Manevich, Y.3    Feinstein, S.I.4    Fisher, A.B.5


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