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Volumn 155, Issue , 2014, Pages 327-336

Proteomic response of mussels Mytilus galloprovincialis exposed to CuO NPs and Cu2+: An exploratory biomarker discovery

Author keywords

CuO NPs; MALDI TOF TOF; Mytilus galloprovincialis; Proteomic analysis; Two dimensional gel electrophoresis

Indexed keywords

ACTIN; ALPHA TUBULIN; ATP SYNTHASE F0 SUBUNIT 6 PROTEIN; BIOLOGICAL MARKER; C1Q DOMAIN CONTAINING PROTEIN; CASPASE 3; CASPASE 7; CATHEPSIN L; CELL PROTEIN; COPPER ION; COPPER OXIDE NANOPARTICLE; GLUTATHIONE; HEAT SHOCK COGNATE PROTEIN 71; HEAT SHOCK PROTEIN; INTERLEUKIN 1BETA CONVERTING ENZYME; NANOPARTICLE; NUCLEAR RECEPTOR SUBFAMILY 1G PROTEIN; PARAMYOSIN; PROCOLLAGEN; PROCOLLAGEN D; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; ZINC FINGER BED DOMAIN CONTAINING PROTEIN 1;

EID: 84905158227     PISSN: 0166445X     EISSN: 18791514     Source Type: Journal    
DOI: 10.1016/j.aquatox.2014.07.015     Document Type: Article
Times cited : (82)

References (64)
  • 1
    • 31144433842 scopus 로고    scopus 로고
    • CDNA cloning and gene expression of ribosoma S9 protein gene in the mollusk Corbicula fluminea: a new potential biomarker of metal contamination up-regulated by cadmium and repressed by zinc
    • Achard-Joris M., Gonzalez P., Marie V., Baudrimont M., Bourdineaud J.-P. cDNA cloning and gene expression of ribosoma S9 protein gene in the mollusk Corbicula fluminea: a new potential biomarker of metal contamination up-regulated by cadmium and repressed by zinc. Environ. Toxicol. Chem. 2006, 25(2):527-533.
    • (2006) Environ. Toxicol. Chem. , vol.25 , Issue.2 , pp. 527-533
    • Achard-Joris, M.1    Gonzalez, P.2    Marie, V.3    Baudrimont, M.4    Bourdineaud, J.-P.5
  • 2
    • 33746308468 scopus 로고    scopus 로고
    • Identification of proteomic signatures of exposure to marine pollutants in mussels (Mytilus edulis)
    • Apraiz I., Mi J., Cristobal S. Identification of proteomic signatures of exposure to marine pollutants in mussels (Mytilus edulis). Mol. Cell. Proteomics 2006, 5(7):1274-1285.
    • (2006) Mol. Cell. Proteomics , vol.5 , Issue.7 , pp. 1274-1285
    • Apraiz, I.1    Mi, J.2    Cristobal, S.3
  • 3
    • 71549116049 scopus 로고    scopus 로고
    • Peroxisomal proteomics: biomonitoring in mussels after the Prestige's oil spill
    • Apraiz I., Cajaraville M.P., Cristobal S. Peroxisomal proteomics: biomonitoring in mussels after the Prestige's oil spill. Mar. Pollut. Bull. 2009, 58(12):1815-1826.
    • (2009) Mar. Pollut. Bull. , vol.58 , Issue.12 , pp. 1815-1826
    • Apraiz, I.1    Cajaraville, M.P.2    Cristobal, S.3
  • 6
    • 78650046570 scopus 로고    scopus 로고
    • Interaction of engineered nanoparticles with various components of the environment and possible strategies for their risk assessment
    • Bhatt I., Tripathi B.N. Interaction of engineered nanoparticles with various components of the environment and possible strategies for their risk assessment. Chemosphere 2011, 82(3):308-317.
    • (2011) Chemosphere , vol.82 , Issue.3 , pp. 308-317
    • Bhatt, I.1    Tripathi, B.N.2
  • 7
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels
    • Blum H., Biere H., Gross H.J. Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 1987, 8:93-99.
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Blum, H.1    Biere, H.2    Gross, H.J.3
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analyt. Biochem. 1976, 72:248-254.
    • (1976) Analyt. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 9
    • 0026452361 scopus 로고
    • Bioavailability, accumulation and effects of heavy metals in sediments with special reference to United Kingdom estuaries: a review
    • Bryan G.W., Langston W.J. Bioavailability, accumulation and effects of heavy metals in sediments with special reference to United Kingdom estuaries: a review. Environ. Pollut. 1992, 76:89-131.
    • (1992) Environ. Pollut. , vol.76 , pp. 89-131
    • Bryan, G.W.1    Langston, W.J.2
  • 15
    • 69949141979 scopus 로고    scopus 로고
    • Evaluation of the toxic impact of silver nanoparticles on Japanese medaka (Oryzias latipes)
    • Chae Y.J., Pham C.H., Lee J., Bae E., Yi J., Gu M.B. Evaluation of the toxic impact of silver nanoparticles on Japanese medaka (Oryzias latipes). Aquat. Toxicol. 2009, 94(4):320-327.
    • (2009) Aquat. Toxicol. , vol.94 , Issue.4 , pp. 320-327
    • Chae, Y.J.1    Pham, C.H.2    Lee, J.3    Bae, E.4    Yi, J.5    Gu, M.B.6
  • 16
    • 84905196338 scopus 로고    scopus 로고
    • Williams, R.J.P. The Biological Chemistry of the Elements: The Inorganic Chemistry of Live, New York, Oxford University Press.
    • da Silva, J.J.R.F., 2001. Williams, R.J.P. The Biological Chemistry of the Elements: The Inorganic Chemistry of Live, New York, Oxford University Press.
    • (2001)
    • da Silva, J.J.R.F.1
  • 17
    • 0035893961 scopus 로고    scopus 로고
    • The actin cytoskeleton response to oxidants: from small heat shock protein phosphorylation to changes in the redox state of actin itself
    • Dalle-Donne I., Rossi R., Milzani A., Di Simplicio P., Colombo R. The actin cytoskeleton response to oxidants: from small heat shock protein phosphorylation to changes in the redox state of actin itself. Free Rad. Biol. Med. 2001, 31(12):1624-1632.
    • (2001) Free Rad. Biol. Med. , vol.31 , Issue.12 , pp. 1624-1632
    • Dalle-Donne, I.1    Rossi, R.2    Milzani, A.3    Di Simplicio, P.4    Colombo, R.5
  • 18
    • 70349399043 scopus 로고    scopus 로고
    • Copper oxide nanoparticles induce oxidative stress and cytotoxicity in airway epithelial cells
    • Fahmy B., Cormier S.A. Copper oxide nanoparticles induce oxidative stress and cytotoxicity in airway epithelial cells. Toxicol. In Vitro 2009, 23:1365-1371.
    • (2009) Toxicol. In Vitro , vol.23 , pp. 1365-1371
    • Fahmy, B.1    Cormier, S.A.2
  • 19
    • 0028854808 scopus 로고
    • Characterization of a glutathione S-transferase and a related glutathione-binding protein from gill of the blue mussel, Mytilus edulis
    • Fitzpatrick P.J., Krag T.O., Hojrup P., Sheehan D. Characterization of a glutathione S-transferase and a related glutathione-binding protein from gill of the blue mussel, Mytilus edulis. Biochem. J. 1995, 305:145-150.
    • (1995) Biochem. J. , vol.305 , pp. 145-150
    • Fitzpatrick, P.J.1    Krag, T.O.2    Hojrup, P.3    Sheehan, D.4
  • 20
    • 0037735344 scopus 로고    scopus 로고
    • Copper toxicity, oxidative stress, and antioxidant nutrients
    • Gaetke L.M., Chow C.K. Copper toxicity, oxidative stress, and antioxidant nutrients. Toxicology 2003, 189:147-163.
    • (2003) Toxicology , vol.189 , pp. 147-163
    • Gaetke, L.M.1    Chow, C.K.2
  • 22
    • 79952445313 scopus 로고    scopus 로고
    • The C1q domain containing proteins of the Mediterranean mussel Mytilus galloprovincialis: a widespread and diverse family of immune-related molecules
    • Gerdol M., Manfrin C., De Moro G., Figueras A., Novoa B., Venier P., Pallavicini A. The C1q domain containing proteins of the Mediterranean mussel Mytilus galloprovincialis: a widespread and diverse family of immune-related molecules. Develop. Comp. Immunol. 2011, 35:635-643.
    • (2011) Develop. Comp. Immunol. , vol.35 , pp. 635-643
    • Gerdol, M.1    Manfrin, C.2    De Moro, G.3    Figueras, A.4    Novoa, B.5    Venier, P.6    Pallavicini, A.7
  • 23
    • 77954089746 scopus 로고    scopus 로고
    • MgC1q, a novel C1q-domain-containing protein involved in the immune response of Mytilus galloprovincialis
    • Gestal C., Pallavicini A., Venier P., Novoa B., Figueras A. MgC1q, a novel C1q-domain-containing protein involved in the immune response of Mytilus galloprovincialis. Develop. Comp. Immunol. 2010, 34:926-934.
    • (2010) Develop. Comp. Immunol. , vol.34 , pp. 926-934
    • Gestal, C.1    Pallavicini, A.2    Venier, P.3    Novoa, B.4    Figueras, A.5
  • 25
    • 84860535497 scopus 로고    scopus 로고
    • Accumulation and toxicity of copper oxide nanoparticles in the digestive gland of Mytilus galloprovincialis
    • Gomes T., Pereira C.G., Cardoso C., Pinheiro J.P., Cancio I., Bebianno M.J. Accumulation and toxicity of copper oxide nanoparticles in the digestive gland of Mytilus galloprovincialis. Aquat. Toxicol. 2012, 118-119:72-79.
    • (2012) Aquat. Toxicol. , pp. 72-79
    • Gomes, T.1    Pereira, C.G.2    Cardoso, C.3    Pinheiro, J.P.4    Cancio, I.5    Bebianno, M.J.6
  • 26
    • 84873082435 scopus 로고    scopus 로고
    • Genotoxicity of copper oxide and silver nanoparticles in the mussel Mytilus galloprovincialis
    • Gomes T., Araújo O., Pereira R., Almeida A.C., Cravo A., Bebianno M.J. Genotoxicity of copper oxide and silver nanoparticles in the mussel Mytilus galloprovincialis. Mar. Environ. Res. 2013, 84:51-59.
    • (2013) Mar. Environ. Res. , vol.84 , pp. 51-59
    • Gomes, T.1    Araújo, O.2    Pereira, R.3    Almeida, A.C.4    Cravo, A.5    Bebianno, M.J.6
  • 27
    • 84877355848 scopus 로고    scopus 로고
    • Differential protein expression in mussels Mytilus galloprovincialis exposed to nano and ionic Ag
    • Gomes T., Pereira C.G., Cardoso C., Bebianno M.J. Differential protein expression in mussels Mytilus galloprovincialis exposed to nano and ionic Ag. Aquat. Toxicol. 2013, 136-137:79-90.
    • (2013) Aquat. Toxicol. , pp. 79-90
    • Gomes, T.1    Pereira, C.G.2    Cardoso, C.3    Bebianno, M.J.4
  • 28
    • 0242361635 scopus 로고    scopus 로고
    • Comparative effects of cadmium, copper, paraquat and benzo[a]pyrene on the actin cytoskeleton and production of reactive oxygen species (ROS) in mussel haemocytes
    • Gómez-Mendikute A., Cajaraville M.P. Comparative effects of cadmium, copper, paraquat and benzo[a]pyrene on the actin cytoskeleton and production of reactive oxygen species (ROS) in mussel haemocytes. Toxicol. In Vitro 2003, 17:539-546.
    • (2003) Toxicol. In Vitro , vol.17 , pp. 539-546
    • Gómez-Mendikute, A.1    Cajaraville, M.P.2
  • 29
    • 59149102096 scopus 로고    scopus 로고
    • Comparison of molecular and histological changes in zebrafish gills exposed to metallic nanoparticles
    • Griffitt R.J., Hyndman K., Denslow N.D., Barber D.S. Comparison of molecular and histological changes in zebrafish gills exposed to metallic nanoparticles. Toxicol. Sci. 2009, 107(2):404-415.
    • (2009) Toxicol. Sci. , vol.107 , Issue.2 , pp. 404-415
    • Griffitt, R.J.1    Hyndman, K.2    Denslow, N.D.3    Barber, D.S.4
  • 30
    • 1242293735 scopus 로고    scopus 로고
    • Effect of cellular uptake of gelatin nanoparticles on adhesion, morphology and cytoskeleton organisation of human fibroblasts
    • Gupta A.K., Gupta M., Yarwood S.J., Curtis A.S.G. Effect of cellular uptake of gelatin nanoparticles on adhesion, morphology and cytoskeleton organisation of human fibroblasts. J. Control. Release 2004, 95:197-207.
    • (2004) J. Control. Release , vol.95 , pp. 197-207
    • Gupta, A.K.1    Gupta, M.2    Yarwood, S.J.3    Curtis, A.S.G.4
  • 34
    • 0034871083 scopus 로고    scopus 로고
    • Zinc finger proteins as potential targets for toxic metal ions: differential effects on structure and function
    • Hartwig A. Zinc finger proteins as potential targets for toxic metal ions: differential effects on structure and function. Antioxid. Redox Sign. 2001, 3(4):625-634.
    • (2001) Antioxid. Redox Sign. , vol.3 , Issue.4 , pp. 625-634
    • Hartwig, A.1
  • 35
    • 78649649690 scopus 로고    scopus 로고
    • Changes in the Daphnia magna midgut upon ingestion of copper oxide nanoparticles: a transmission electron microscopy study
    • Heinlaan M., Kahru A., Kasemets K., Arbeille B., Prensier G., Dubourgier H.-C. Changes in the Daphnia magna midgut upon ingestion of copper oxide nanoparticles: a transmission electron microscopy study. Water Res. 2011, 45:179-190.
    • (2011) Water Res. , vol.45 , pp. 179-190
    • Heinlaan, M.1    Kahru, A.2    Kasemets, K.3    Arbeille, B.4    Prensier, G.5    Dubourgier, H.-C.6
  • 36
    • 67349144664 scopus 로고    scopus 로고
    • Size-dependent toxicity of metal oxide particles-a comparison between nano-and micrometer size
    • Karlsson H.L., Gustafsson J., Cronholm P., Möller L. Size-dependent toxicity of metal oxide particles-a comparison between nano-and micrometer size. Toxicol. Lett. 2009, 188:112-118.
    • (2009) Toxicol. Lett. , vol.188 , pp. 112-118
    • Karlsson, H.L.1    Gustafsson, J.2    Cronholm, P.3    Möller, L.4
  • 37
    • 29744445150 scopus 로고    scopus 로고
    • Acute thermal stress and various heavy metals induce tissue-specific pro-or anti-apoptotic events via the p38-MAPK signal transduction pathway in Mytilus galloprovincialis (Lam.)
    • Kefaloyianni E., Gourgou E., Ferle V., Kotsakis E., Gaitanaki C., Beis I. Acute thermal stress and various heavy metals induce tissue-specific pro-or anti-apoptotic events via the p38-MAPK signal transduction pathway in Mytilus galloprovincialis (Lam.). J. Exp. Biol. 2005, 208:4427-4436.
    • (2005) J. Exp. Biol. , vol.208 , pp. 4427-4436
    • Kefaloyianni, E.1    Gourgou, E.2    Ferle, V.3    Kotsakis, E.4    Gaitanaki, C.5    Beis, I.6
  • 38
    • 44749092578 scopus 로고    scopus 로고
    • Effects of nanoparticles in Mytilus edulis gills and hepatopancreas-a new threat to marine life?
    • Koehler A., Marx U., Broeg K., Bahns S., Bressling J. Effects of nanoparticles in Mytilus edulis gills and hepatopancreas-a new threat to marine life?. Mar. Environ. Res. 2008, 66(1):12-14.
    • (2008) Mar. Environ. Res. , vol.66 , Issue.1 , pp. 12-14
    • Koehler, A.1    Marx, U.2    Broeg, K.3    Bahns, S.4    Bressling, J.5
  • 39
    • 12344311074 scopus 로고    scopus 로고
    • Role of proteomics in taxonomy: the Mytilus complex as a model of study
    • López J.L. Role of proteomics in taxonomy: the Mytilus complex as a model of study. J. Chromatogr. B 2005, 815:261-274.
    • (2005) J. Chromatogr. B , vol.815 , pp. 261-274
    • López, J.L.1
  • 40
    • 0036022290 scopus 로고    scopus 로고
    • A molecular, morphometric and mechanical comparison of the structural elements of byssus from Mytilus edulis and Mytilus galloprovincialis
    • Lucas J.M., Vaccaro E., Waite J.H. A molecular, morphometric and mechanical comparison of the structural elements of byssus from Mytilus edulis and Mytilus galloprovincialis. J. Exp. Biol. 2002, 205:1807-1817.
    • (2002) J. Exp. Biol. , vol.205 , pp. 1807-1817
    • Lucas, J.M.1    Vaccaro, E.2    Waite, J.H.3
  • 41
    • 84855894614 scopus 로고    scopus 로고
    • Contribution of nano-copper particles to in vivo liver dysfunction and cellular damage: Role of IκBα/NF-κB, MAPKs and mitochondrial signal
    • Manna P., Ghosh M., Shosh J., Das J., Sil P.C. Contribution of nano-copper particles to in vivo liver dysfunction and cellular damage: Role of IκBα/NF-κB, MAPKs and mitochondrial signal. Nanotoxicology 2012, 6(1):1-21.
    • (2012) Nanotoxicology , vol.6 , Issue.1 , pp. 1-21
    • Manna, P.1    Ghosh, M.2    Shosh, J.3    Das, J.4    Sil, P.C.5
  • 42
    • 60349099847 scopus 로고    scopus 로고
    • Can estrogenic compounds enhance the activity of cathepsin D and cathepsin L in the mussel, Mytilus galloprovincialis?
    • Margiotta-Casaluci L., Carnevali O. Can estrogenic compounds enhance the activity of cathepsin D and cathepsin L in the mussel, Mytilus galloprovincialis?. Chem. Ecol. 2009, 25(1):49-60.
    • (2009) Chem. Ecol. , vol.25 , Issue.1 , pp. 49-60
    • Margiotta-Casaluci, L.1    Carnevali, O.2
  • 43
    • 79955478142 scopus 로고    scopus 로고
    • Antioxidant and lipid peroxidation responses in Mytilus galloprovincialis exposed to mixtures of benzo(a)pyrene and copper
    • Maria V.L., Bebianno M.J. Antioxidant and lipid peroxidation responses in Mytilus galloprovincialis exposed to mixtures of benzo(a)pyrene and copper. Comp. Biochem. Physiol. C 2011, 154(1):56-63.
    • (2011) Comp. Biochem. Physiol. C , vol.154 , Issue.1 , pp. 56-63
    • Maria, V.L.1    Bebianno, M.J.2
  • 44
    • 84887542517 scopus 로고    scopus 로고
    • Impact of benzo(a)pyrene, Cu and their mixture on the proteomic response of Mytilus galloprovincialis
    • Maria V.L., Gomes T., Barreira L., Bebianno M.J. Impact of benzo(a)pyrene, Cu and their mixture on the proteomic response of Mytilus galloprovincialis. Aquat. Toxicol. 2013, 144-145:284-295.
    • (2013) Aquat. Toxicol. , pp. 284-295
    • Maria, V.L.1    Gomes, T.2    Barreira, L.3    Bebianno, M.J.4
  • 45
    • 33748525920 scopus 로고    scopus 로고
    • Redox proteomics in the blue mussel Mytilus edulis: Carbonylation is not a pre-requisite for ubiquitination in acute free radical-mediated oxidative stress
    • McDonagh B., Sheehan D. Redox proteomics in the blue mussel Mytilus edulis: Carbonylation is not a pre-requisite for ubiquitination in acute free radical-mediated oxidative stress. Aquat. Toxicol. 2006, 79(4):325-333.
    • (2006) Aquat. Toxicol. , vol.79 , Issue.4 , pp. 325-333
    • McDonagh, B.1    Sheehan, D.2
  • 46
    • 77749343664 scopus 로고    scopus 로고
    • Gold nanoparticles cellular toxicity and recovery: effect of size, concentration and exposure time
    • Mironava T., Hadjiargyrou M., Simon M., Jurukovski V., Rafailovich M.H. Gold nanoparticles cellular toxicity and recovery: effect of size, concentration and exposure time. Nanotoxicology 2010, 4(1):120-137.
    • (2010) Nanotoxicology , vol.4 , Issue.1 , pp. 120-137
    • Mironava, T.1    Hadjiargyrou, M.2    Simon, M.3    Jurukovski, V.4    Rafailovich, M.H.5
  • 47
    • 23144436273 scopus 로고    scopus 로고
    • Age-dependent variations of cell response to oxidative stress: proteomic approach to protein expression and phosphorylation
    • Miura Y., Kano M., Abe1 K., Urano S., Suzuki S., Toda T. Age-dependent variations of cell response to oxidative stress: proteomic approach to protein expression and phosphorylation. Electrophoresis 2005, 26:2786-2796.
    • (2005) Electrophoresis , vol.26 , pp. 2786-2796
    • Miura, Y.1    Kano, M.2    Abel, K.3    Urano, S.4    Suzuki, S.5    Toda, T.6
  • 48
    • 33750337188 scopus 로고    scopus 로고
    • Do nanoparticles present ecotoxicological risks for the health of the aquatic environment?
    • Moore M.N. Do nanoparticles present ecotoxicological risks for the health of the aquatic environment?. Environ. Int. 2006, 32:967-976.
    • (2006) Environ. Int. , vol.32 , pp. 967-976
    • Moore, M.N.1
  • 49
    • 10644294514 scopus 로고    scopus 로고
    • Pollution monitoring in Southeast Asia using biomarkers in the mytilid mussel Perna viridis (Mytilidae: Bivalvia)
    • Nicholson S., Lam P.K.S. Pollution monitoring in Southeast Asia using biomarkers in the mytilid mussel Perna viridis (Mytilidae: Bivalvia). Environ. Int. 2005, 31:121-132.
    • (2005) Environ. Int. , vol.31 , pp. 121-132
    • Nicholson, S.1    Lam, P.K.S.2
  • 50
    • 0043027008 scopus 로고    scopus 로고
    • Accumulation of metals in the soft tissues, byssus and shell of the mytilid mussel Perna viridis (Bivalvia: Mytilidae) from polluted and uncontaminated locations in Hong Kong coastal waters
    • Nicholson S., Szefer P. Accumulation of metals in the soft tissues, byssus and shell of the mytilid mussel Perna viridis (Bivalvia: Mytilidae) from polluted and uncontaminated locations in Hong Kong coastal waters. Mar. Pollut. Bull. 2003, 46:1035-1048.
    • (2003) Mar. Pollut. Bull. , vol.46 , pp. 1035-1048
    • Nicholson, S.1    Szefer, P.2
  • 51
    • 0028888954 scopus 로고
    • Glutathione, glutathione-dependent and antioxidant enzymes in mussel, Mytilus galloprovincialis, exposed to metals under field and laboratory conditions: implications for the use of biochemical biomarkers
    • Regoli F., Principato G. Glutathione, glutathione-dependent and antioxidant enzymes in mussel, Mytilus galloprovincialis, exposed to metals under field and laboratory conditions: implications for the use of biochemical biomarkers. Aquat. Toxicol. 1995, 31:143-164.
    • (1995) Aquat. Toxicol. , vol.31 , pp. 143-164
    • Regoli, F.1    Principato, G.2
  • 52
    • 0042861622 scopus 로고    scopus 로고
    • Changes in protein expression profiles in bivalve molluscs (Chamaelea gallina) exposed to four model environmental pollutants
    • Rodríguez-Ortega M.J., Grøsvik B.E., Rodríguez-Ariza A., Goksøyr A., López-Barea J. Changes in protein expression profiles in bivalve molluscs (Chamaelea gallina) exposed to four model environmental pollutants. Proteomics 2003, 3:1535-1543.
    • (2003) Proteomics , vol.3 , pp. 1535-1543
    • Rodríguez-Ortega, M.J.1    Grøsvik, B.E.2    Rodríguez-Ariza, A.3    Goksøyr, A.4    López-Barea, J.5
  • 53
    • 79951821141 scopus 로고    scopus 로고
    • New insights into the apoptotic process in mollusks: characterization of caspase genes in Mytilus galloprovincialis
    • Romero A., Estévez-Calvar N., Dios S., Figueras A., Novoa B. New insights into the apoptotic process in mollusks: characterization of caspase genes in Mytilus galloprovincialis. PLoS ONE 2011, 6(2):e17003.
    • (2011) PLoS ONE , vol.6 , Issue.2
    • Romero, A.1    Estévez-Calvar, N.2    Dios, S.3    Figueras, A.4    Novoa, B.5
  • 54
    • 84858614842 scopus 로고    scopus 로고
    • Nano-copper induces oxidative stress and apoptosis in kidney via both extrinsic and intrinsic pathways
    • Sarkar A., Das J., Manna P., Sil P.C. Nano-copper induces oxidative stress and apoptosis in kidney via both extrinsic and intrinsic pathways. Toxicology 2011, 290:208-217.
    • (2011) Toxicology , vol.290 , pp. 208-217
    • Sarkar, A.1    Das, J.2    Manna, P.3    Sil, P.C.4
  • 55
    • 77954871571 scopus 로고    scopus 로고
    • Review: do engineered nanoparticles pose a significant threat to the aquatic environment?
    • Scown T.M., Aerle R.V., Tyler C.R. Review: do engineered nanoparticles pose a significant threat to the aquatic environment?. Crit. Rev. Toxicol. 2010, 40(7):653-670.
    • (2010) Crit. Rev. Toxicol. , vol.40 , Issue.7 , pp. 653-670
    • Scown, T.M.1    Aerle, R.V.2    Tyler, C.R.3
  • 56
    • 0033744461 scopus 로고    scopus 로고
    • Protein expression signatures and lysosomal stability in Mytilus edulis exposed to graded copper concentrations
    • Shepard J.L., Bradley B.P. Protein expression signatures and lysosomal stability in Mytilus edulis exposed to graded copper concentrations. Mar. Environ. Res. 2000, 50:457-463.
    • (2000) Mar. Environ. Res. , vol.50 , pp. 457-463
    • Shepard, J.L.1    Bradley, B.P.2
  • 57
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko A., Tomas H., Havlis J., Olsen J.V., Mann M. In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat. Protocols 2007, 1(6):2856-2860.
    • (2007) Nat. Protocols , vol.1 , Issue.6 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 58
    • 1642471825 scopus 로고    scopus 로고
    • Heat-shock proteins as regulators of apoptosis
    • Takayama S., Reed J.C., Homma S. Heat-shock proteins as regulators of apoptosis. Oncogene 2003, 22:9041-9047.
    • (2003) Oncogene , vol.22 , pp. 9041-9047
    • Takayama, S.1    Reed, J.C.2    Homma, S.3
  • 59
    • 84856618679 scopus 로고    scopus 로고
    • Proteomic discovery of biomarkers of metal contamination in Sydney Rock oysters (Saccostrea glomerata)
    • Thompson E.L., Taylor D.A., Nair S.V., Birch G., Haynes P.A., Raftos D.A. Proteomic discovery of biomarkers of metal contamination in Sydney Rock oysters (Saccostrea glomerata). Aquat. Toxicol. 2012, 109:202-212.
    • (2012) Aquat. Toxicol. , vol.109 , pp. 202-212
    • Thompson, E.L.1    Taylor, D.A.2    Nair, S.V.3    Birch, G.4    Haynes, P.A.5    Raftos, D.A.6
  • 61
    • 0019644671 scopus 로고
    • Accumulation and detoxification of copper by the mussel Mytilus galloprovincialis Lam: a study of subcellular distribution in the digestive gland cells
    • Viarengo A., Zanicchi G., Moore M.N., Orunesu M. Accumulation and detoxification of copper by the mussel Mytilus galloprovincialis Lam: a study of subcellular distribution in the digestive gland cells. Aquat. Toxicol. 1981, 1:147-157.
    • (1981) Aquat. Toxicol. , vol.1 , pp. 147-157
    • Viarengo, A.1    Zanicchi, G.2    Moore, M.N.3    Orunesu, M.4
  • 62
    • 0033977940 scopus 로고    scopus 로고
    • Complete amino acid sequence of Mytilus anterior byssus retractor paramyosin and its putative phosphorylation site
    • Watabe S., Iwasaki K., Funabara D., Hirayama Y., Nakaya M., Kikuchi K. Complete amino acid sequence of Mytilus anterior byssus retractor paramyosin and its putative phosphorylation site. J. Exp. Zool. 2000, 286:24-35.
    • (2000) J. Exp. Zool. , vol.286 , pp. 24-35
    • Watabe, S.1    Iwasaki, K.2    Funabara, D.3    Hirayama, Y.4    Nakaya, M.5    Kikuchi, K.6
  • 63
    • 0034645728 scopus 로고    scopus 로고
    • Catchin, a novel protein in molluscan catch muscles, is produced by alternative splicing from the myosin heavy chain gene
    • Yamada A., Yoshio M., Oiwa K., Nyitray L. Catchin, a novel protein in molluscan catch muscles, is produced by alternative splicing from the myosin heavy chain gene. J. Mol. Biol. 2000, 295:169-178.
    • (2000) J. Mol. Biol. , vol.295 , pp. 169-178
    • Yamada, A.1    Yoshio, M.2    Oiwa, K.3    Nyitray, L.4
  • 64
    • 84862692310 scopus 로고    scopus 로고
    • Toxic effect on tissues and differentially expressed genes in hepatopancreas identified by suppression subtractive hybridization of Freshwater pearl mussel (Hyriopsis cumingii) following microcystin-LR Challenge
    • Yang Z., Wu H., Li Y. Toxic effect on tissues and differentially expressed genes in hepatopancreas identified by suppression subtractive hybridization of Freshwater pearl mussel (Hyriopsis cumingii) following microcystin-LR Challenge. Environ. Toxicol. 2010, 27(7):393-403.
    • (2010) Environ. Toxicol. , vol.27 , Issue.7 , pp. 393-403
    • Yang, Z.1    Wu, H.2    Li, Y.3


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