메뉴 건너뛰기




Volumn 30, Issue 2, 2011, Pages 274-282

Review of recent proteomic applications in aquatic toxicology

Author keywords

Aquatic invertebrates; Aquatic toxicology; Fish; Proteomics

Indexed keywords

AQUATIC INVERTEBRATES; AQUATIC TOXICOLOGY; ECOTOXICOLOGICAL; ENVIRONMENTAL SCIENCE; ENVIRONMENTAL STRESSORS; HIGH-THROUGHPUT; MOLECULAR COMPONENTS; MOLECULAR TOOLS; PROTEOMIC STUDIES; PROTEOMICS; PROTEOMICS RESEARCH; TOXIC ACTION;

EID: 78651349268     PISSN: 07307268     EISSN: 15528618     Source Type: Journal    
DOI: 10.1002/etc.402     Document Type: Review
Times cited : (87)

References (79)
  • 1
    • 1542375217 scopus 로고    scopus 로고
    • Ecotoxicogenomics: The challenge of integrating genomics into aquatic and terrestrial ecotoxicology
    • Snape JR, Maund SJ, Pickford DB, Hutchinson TH. 2004. Ecotoxicogenomics: The challenge of integrating genomics into aquatic and terrestrial ecotoxicology. Aquat Toxicol (Amst) 67: 143-154.
    • (2004) Aquat Toxicol (Amst) , vol.67 , pp. 143-154
    • Snape, J.R.1    Maund, S.J.2    Pickford, D.B.3    Hutchinson, T.H.4
  • 2
    • 8544277251 scopus 로고    scopus 로고
    • Toxicoproteomics: Proteomics applied to toxicology and pathology
    • Wetmore BA, Merrick BA. 2004. Toxicoproteomics: Proteomics applied to toxicology and pathology. Toxicol Pathol 32: 619-642.
    • (2004) Toxicol Pathol , vol.32 , pp. 619-642
    • Wetmore, B.A.1    Merrick, B.A.2
  • 3
    • 33845615517 scopus 로고    scopus 로고
    • Toxicoproteomics-The next step in the evolution of environmental biomarkers?
    • Benninghoff AD. 2007. Toxicoproteomics-The next step in the evolution of environmental biomarkers? Toxicol Sci 95: 1-4.
    • (2007) Toxicol Sci , vol.95 , pp. 1-4
    • Benninghoff, A.D.1
  • 4
    • 0033744461 scopus 로고    scopus 로고
    • Protein expression signatures and lysosomal stability in Mytilus edulis exposed to graded copper concentrations
    • Shepard JL, Bradley BP. 2000. Protein expression signatures and lysosomal stability in Mytilus edulis exposed to graded copper concentrations. Mar Environ Res 50: 457-463.
    • (2000) Mar Environ Res , vol.50 , pp. 457-463
    • Shepard, J.L.1    Bradley, B.P.2
  • 5
    • 0033751418 scopus 로고    scopus 로고
    • Protein expression signatures identified in Mytilus edulis exposed to PCBs, copper and salinity stress
    • Shepard JL, Olsson B, Tedengren M, Bradley BP. 2000. Protein expression signatures identified in Mytilus edulis exposed to PCBs, copper and salinity stress. Mar Environ Res 50: 337-340.
    • (2000) Mar Environ Res , vol.50 , pp. 337-340
    • Shepard, J.L.1    Olsson, B.2    Tedengren, M.3    Bradley, B.P.4
  • 6
    • 66749086312 scopus 로고    scopus 로고
    • Quantitative proteomic profiles of androgen receptor signaling in the liver of fathead minnows (Pimephales promelas)
    • Martyniuk CJ, Alvarez S, McClung S, Villeneuve DL, Ankley GT, Denslow ND. 2009. Quantitative proteomic profiles of androgen receptor signaling in the liver of fathead minnows (Pimephales promelas). J Proteome Res 8: 2186-2200.
    • (2009) J Proteome Res , vol.8 , pp. 2186-2200
    • Martyniuk, C.J.1    Alvarez, S.2    McClung, S.3    Villeneuve, D.L.4    Ankley, G.T.5    Denslow, N.D.6
  • 8
    • 28744445364 scopus 로고    scopus 로고
    • Differential protein expression profiles in anterior gills of Eriocheir sinensis during acclimation to cadmium
    • Silvestre F, Dierick JF, Dumont V, Dieu M, Raes M, Devos P. 2006. Differential protein expression profiles in anterior gills of Eriocheir sinensis during acclimation to cadmium. Aquat Toxicol (Amst) 76: 46-58.
    • (2006) Aquat Toxicol (Amst) , vol.76 , pp. 46-58
    • Silvestre, F.1    Dierick, J.F.2    Dumont, V.3    Dieu, M.4    Raes, M.5    Devos, P.6
  • 11
    • 34548391493 scopus 로고    scopus 로고
    • Proteomic applications in ecotoxicology
    • Monsinjon T, Knigge T. 2007. Proteomic applications in ecotoxicology. Proteomics 7: 2997-3009.
    • (2007) Proteomics , vol.7 , pp. 2997-3009
    • Monsinjon, T.1    Knigge, T.2
  • 12
    • 31144473900 scopus 로고    scopus 로고
    • Toxicogenomics in risk assessment: Applications and needs
    • Boverhof DR, Zacharewski TR. 2006. Toxicogenomics in risk assessment: Applications and needs. Toxicol Sci 89: 352-360.
    • (2006) Toxicol Sci , vol.89 , pp. 352-360
    • Boverhof, D.R.1    Zacharewski, T.R.2
  • 13
    • 33645574501 scopus 로고    scopus 로고
    • Using ecotoxicogenomics to evaluate the impact of chemicals on aquatic organisms
    • Watanabe H, Iguchi T. 2006. Using ecotoxicogenomics to evaluate the impact of chemicals on aquatic organisms. Mar Biol 149: 107-115.
    • (2006) Mar Biol , vol.149 , pp. 107-115
    • Watanabe, H.1    Iguchi, T.2
  • 14
    • 0041351911 scopus 로고    scopus 로고
    • Toxicoproteomics: A parallel approach to identifying biomarkers
    • Merrick BA, Tomer KB. 2003. Toxicoproteomics: A parallel approach to identifying biomarkers. Environ Health Perspect 111: A578-A579.
    • (2003) Environ Health Perspect , vol.111
    • Merrick, B.A.1    Tomer, K.B.2
  • 16
    • 33750591821 scopus 로고    scopus 로고
    • Proteomics as a route to identification of toxicity targets in environmental toxicology
    • Dowling VA, Sheehan D. 2006. Proteomics as a route to identification of toxicity targets in environmental toxicology. Proteomics 6: 5597-5604.
    • (2006) Proteomics , vol.6 , pp. 5597-5604
    • Dowling, V.A.1    Sheehan, D.2
  • 17
    • 35348860923 scopus 로고    scopus 로고
    • Proteomics for the analysis of environmental stress responses in organisms
    • Nesatyy VJ, Suter MJF. 2007. Proteomics for the analysis of environmental stress responses in organisms. Environ Sci Technol 41: 6891-6900.
    • (2007) Environ Sci Technol , vol.41 , pp. 6891-6900
    • Nesatyy, V.J.1    Suter, M.J.F.2
  • 20
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: A single gel method for detecting changes in protein extracts
    • Unlu M, Morgan ME, Minden JS. 1997. Difference gel electrophoresis: A single gel method for detecting changes in protein extracts. Electrophoresis 18: 2071-2077.
    • (1997) Electrophoresis , vol.18 , pp. 2071-2077
    • Unlu, M.1    Morgan, M.E.2    Minden, J.S.3
  • 22
    • 69949105882 scopus 로고    scopus 로고
    • Proteome analysis of a single zebrafish embryo using three different digestion strategies coupled with liquid chromatography-tandem mass spectrometry
    • Lin Y, Chen Y, Yang X, Xu D, Liang S. 2009. Proteome analysis of a single zebrafish embryo using three different digestion strategies coupled with liquid chromatography-tandem mass spectrometry. Anal Biochem 394: 177-185.
    • (2009) Anal Biochem , vol.394 , pp. 177-185
    • Lin, Y.1    Chen, Y.2    Yang, X.3    Xu, D.4    Liang, S.5
  • 23
    • 33645813378 scopus 로고    scopus 로고
    • Mass spectrometry and protein analysis
    • Domon B, Aebersold R. 2006. Mass spectrometry and protein analysis. Science 312: 212-217.
    • (2006) Science , vol.312 , pp. 212-217
    • Domon, B.1    Aebersold, R.2
  • 24
    • 38049088065 scopus 로고    scopus 로고
    • Vitellogenin cleavage products as indicators for toxic stress in zebra fish embryos: A proteomic approach
    • Gündel U, Benndorf D, von Bergen M, Altenberger R, Küster E. 2007. Vitellogenin cleavage products as indicators for toxic stress in zebra fish embryos: A proteomic approach. Proteomics 7: 4541-4554.
    • (2007) Proteomics , vol.7 , pp. 4541-4554
    • Gündel, U.1    Benndorf, D.2    von Bergen, M.3    Altenberger, R.4    Küster, E.5
  • 25
    • 70049105877 scopus 로고    scopus 로고
    • Proteomic studies in zebrafish liver cells exposed to the brominated flame retardants HBCD and TBBPA
    • Kling P, Förlin L. 2009. Proteomic studies in zebrafish liver cells exposed to the brominated flame retardants HBCD and TBBPA. Ecotoxicol Environ Saf 72: 1985-1993.
    • (2009) Ecotoxicol Environ Saf , vol.72 , pp. 1985-1993
    • Kling, P.1    Förlin, L.2
  • 26
    • 67650770098 scopus 로고    scopus 로고
    • Protein profiles in zebrafish (Danio rerio) embryos exposed to perfluorooctane sulfonate
    • Shi X, Yeung LWY, Lam PKS, Wu RSS, Zhou B. 2009. Protein profiles in zebrafish (Danio rerio) embryos exposed to perfluorooctane sulfonate. Toxicol Sci 110: 334-340.
    • (2009) Toxicol Sci , vol.110 , pp. 334-340
    • Shi, X.1    Yeung, L.W.Y.2    Lam, P.K.S.3    Wu, R.S.S.4    Zhou, B.5
  • 27
    • 70350440527 scopus 로고    scopus 로고
    • Comparative proteomics analysis of cardiac muscle samples from pufferfish Takifugu rubripes exposed to excessive fluoride: Initial molecular response to fluorosis
    • Lu J, Xu Q, Zheng J, Liu H, Li J, Chen K. 2009. Comparative proteomics analysis of cardiac muscle samples from pufferfish Takifugu rubripes exposed to excessive fluoride: Initial molecular response to fluorosis. Toxicol Mech Methods 19: 468-475.
    • (2009) Toxicol Mech Methods , vol.19 , pp. 468-475
    • Lu, J.1    Xu, Q.2    Zheng, J.3    Liu, H.4    Li, J.5    Chen, K.6
  • 28
    • 75249106631 scopus 로고    scopus 로고
    • Proteomic analysis of hepatic tissue of zebrafish (Danio rerio) experimentally exposed to chronic microcystin-LR
    • Wang W, Chan LL, Si M, Hong H, Wang D. 2009. Proteomic analysis of hepatic tissue of zebrafish (Danio rerio) experimentally exposed to chronic microcystin-LR. Toxicol Sci 113: 60-69.
    • (2009) Toxicol Sci , vol.113 , pp. 60-69
    • Wang, W.1    Chan, L.L.2    Si, M.3    Hong, H.4    Wang, D.5
  • 29
    • 50949128129 scopus 로고    scopus 로고
    • Gender-specific proteomic responses in zebrafish liver following exposure to a selected mixture of brominated flame retardants
    • Kling P, Norman A, Andersson PL, Norrgren L, Förlin L. 2008. Gender-specific proteomic responses in zebrafish liver following exposure to a selected mixture of brominated flame retardants. Ecotoxicol Environ Saf 71: 319-327.
    • (2008) Ecotoxicol Environ Saf , vol.71 , pp. 319-327
    • Kling, P.1    Norman, A.2    Andersson, P.L.3    Norrgren, L.4    Förlin, L.5
  • 30
    • 71749121372 scopus 로고    scopus 로고
    • Liver proteome response of largemouth bass (Micropterus salmoides) exposed to several environmental contaminants: Potential insights into biomarker development
    • Sanchez BC, Ralston-Hooper KJ, Kowalski KA, Inerowicz HD, Adamec J, Sepúlveda MS. 2009. Liver proteome response of largemouth bass (Micropterus salmoides) exposed to several environmental contaminants: Potential insights into biomarker development. Aquat Toxicol (Amst) 95: 52-59.
    • (2009) Aquat Toxicol (Amst) , vol.95 , pp. 52-59
    • Sanchez, B.C.1    Ralston-Hooper, K.J.2    Kowalski, K.A.3    Inerowicz, H.D.4    Adamec, J.5    Sepúlveda, M.S.6
  • 31
    • 34447565175 scopus 로고    scopus 로고
    • Proteomic analyses indicate induction of hepatic carbonyl reductase/20β-hydroxysteroid dehydrogenase B in rainbow trout exposed to sewage effluent
    • Albertsson E, Kling P, Gunnarsson L, Larsson DGJ, Förlin L. 2007. Proteomic analyses indicate induction of hepatic carbonyl reductase/20β-hydroxysteroid dehydrogenase B in rainbow trout exposed to sewage effluent. Ecotoxicol Environ Saf 68: 33-39.
    • (2007) Ecotoxicol Environ Saf , vol.68 , pp. 33-39
    • Albertsson, E.1    Kling, P.2    Gunnarsson, L.3    Larsson, D.G.J.4    Förlin, L.5
  • 32
    • 45549101986 scopus 로고    scopus 로고
    • Proteomic analysis of hepatic protein profiles in rare minnow (Gobiocypris rarus) exposed to perfluorooctanoic acid
    • Wei Y, Chan LL, Wang D, Zhang H, Wang J, Dai J. 2008. Proteomic analysis of hepatic protein profiles in rare minnow (Gobiocypris rarus) exposed to perfluorooctanoic acid. J Proteome Res 7: 1729-1739.
    • (2008) J Proteome Res , vol.7 , pp. 1729-1739
    • Wei, Y.1    Chan, L.L.2    Wang, D.3    Zhang, H.4    Wang, J.5    Dai, J.6
  • 34
    • 33646252476 scopus 로고    scopus 로고
    • Comparison of protein expression in plasma from nonylphenol and bisphenol A-exposed Atlantic cod (Gadus morhua) turbot (Scophthalmus maximus) by use of SELDI-TOF
    • Larsen BK, Bjørnstad A, Sundt RC, Taban IC, Pampanin DM, Andersen OK. 2006. Comparison of protein expression in plasma from nonylphenol and bisphenol A-exposed Atlantic cod (Gadus morhua) turbot (Scophthalmus maximus) by use of SELDI-TOF. Aquat Toxicol (Amst) 785: S25-S33.
    • (2006) Aquat Toxicol (Amst) , vol.785
    • Larsen, B.K.1    Bjørnstad, A.2    Sundt, R.C.3    Taban, I.C.4    Pampanin, D.M.5    Andersen, O.K.6
  • 36
    • 33646532355 scopus 로고    scopus 로고
    • Acute toxicity profile of cadmium revealed by proteomics in brain tissue of Paralichthys olivaceus: Potential role of transferrin in cadmium toxicity
    • Zhu JY, Huang HQ, Bao XD, Lin QM, Cai Z. 2006. Acute toxicity profile of cadmium revealed by proteomics in brain tissue of Paralichthys olivaceus: Potential role of transferrin in cadmium toxicity. Aquat Toxicol (Amst) 78: 127-135.
    • (2006) Aquat Toxicol (Amst) , vol.78 , pp. 127-135
    • Zhu, J.Y.1    Huang, H.Q.2    Bao, X.D.3    Lin, Q.M.4    Cai, Z.5
  • 37
    • 59649113416 scopus 로고    scopus 로고
    • Proteomic changes in response to acute cadmium toxicity in gill tissue of Paralichthys olivaceus
    • Ling XP, Zhu JY, Huang L, Huang HQ. 2009. Proteomic changes in response to acute cadmium toxicity in gill tissue of Paralichthys olivaceus Environ Toxicol Pharmacol 27: 212-218.
    • (2009) Environ Toxicol Pharmacol , vol.27 , pp. 212-218
    • Ling, X.P.1    Zhu, J.Y.2    Huang, L.3    Huang, H.Q.4
  • 38
    • 38749111845 scopus 로고    scopus 로고
    • Global quantitative analysis of protein expression and phosphorylation status in the liver of the medaka fish (Oryzias latipes) exposed to microcystin-LR I. Balneation study
    • Mezhoud K, Praseuth D, Puiseux-Dao S, François JC, Bernard C, Edery M. 2008. Global quantitative analysis of protein expression and phosphorylation status in the liver of the medaka fish (Oryzias latipes) exposed to microcystin-LR I. Balneation study. Aquat Toxicol (Amst) 86: 166-175.
    • (2008) Aquat Toxicol (Amst) , vol.86 , pp. 166-175
    • Mezhoud, K.1    Praseuth, D.2    Puiseux-Dao, S.3    François, J.C.4    Bernard, C.5    Edery, M.6
  • 39
    • 68249107159 scopus 로고    scopus 로고
    • Proteomic study of the effects of microcystin-LR on organelle and membrane proteins in medaka fish liver
    • Malécot M, Mezhoud K, Marie A, Praseuth D, Puiseux-Dao S, Edery M. 2009. Proteomic study of the effects of microcystin-LR on organelle and membrane proteins in medaka fish liver. Aquat Toxicol (Amst) 94: 153-161.
    • (2009) Aquat Toxicol (Amst) , vol.94 , pp. 153-161
    • Malécot, M.1    Mezhoud, K.2    Marie, A.3    Praseuth, D.4    Puiseux-Dao, S.5    Edery, M.6
  • 40
    • 48949094739 scopus 로고    scopus 로고
    • Utilization of protein expression profiles as indicators of environmental impairment of smallmouth bass (Micropterus dolomieu) from the Shenandoah River, Virginia, USA
    • Ripley J, Iwanowicz L, Blazer V, Foran C. 2008. Utilization of protein expression profiles as indicators of environmental impairment of smallmouth bass (Micropterus dolomieu) from the Shenandoah River, Virginia, USA. Environ Toxicol Chem 27: 1756-1767.
    • (2008) Environ Toxicol Chem , vol.27 , pp. 1756-1767
    • Ripley, J.1    Iwanowicz, L.2    Blazer, V.3    Foran, C.4
  • 41
    • 38949133081 scopus 로고    scopus 로고
    • Proteomic study of the effects of complex environmental stresses in the livers of goldfish (Carassius auratus) that inhabit Gaobeidian Lake in Beijing, China
    • Wang J, Wei Y, Wang D, Chan LL, Dai J. 2008. Proteomic study of the effects of complex environmental stresses in the livers of goldfish (Carassius auratus) that inhabit Gaobeidian Lake in Beijing, China. Ecotoxicology 17: 213-220.
    • (2008) Ecotoxicology , vol.17 , pp. 213-220
    • Wang, J.1    Wei, Y.2    Wang, D.3    Chan, L.L.4    Dai, J.5
  • 42
    • 0037131035 scopus 로고    scopus 로고
    • Growth, mortality, pathological conditions and protein expression of Mytilus edulis and M. galloprovincialis crosses cultured in the Ria de Arousa (NW of Spain)
    • Fuentes J, Lopez JL, Mosquera E, Vazquez J, Villalba A, Alvarez G. 2002. Growth, mortality, pathological conditions and protein expression of Mytilus edulis and M. galloprovincialis crosses cultured in the Ria de Arousa (NW of Spain). Aquaculture 213: 233-251.
    • (2002) Aquaculture , vol.213 , pp. 233-251
    • Fuentes, J.1    Lopez, J.L.2    Mosquera, E.3    Vazquez, J.4    Villalba, A.5    Alvarez, G.6
  • 43
    • 0036934090 scopus 로고    scopus 로고
    • A proteomic approach to the study of the marine mussels Mytilus edulis and M. galloprovincialis
    • Lopez JL, Marina A, Vazquez J, Alvarez G. 2002. A proteomic approach to the study of the marine mussels Mytilus edulis and M. galloprovincialis Mar Biol 141: 217-223.
    • (2002) Mar Biol , vol.141 , pp. 217-223
    • Lopez, J.L.1    Marina, A.2    Vazquez, J.3    Alvarez, G.4
  • 44
    • 0036907894 scopus 로고    scopus 로고
    • Application of proteomics for fast identification of species-specific peptides from marine species
    • Lopez JL, Marina A, Alvarez G, Vazquez J. 2002. Application of proteomics for fast identification of species-specific peptides from marine species. Proteomics 2: 1658-1665.
    • (2002) Proteomics , vol.2 , pp. 1658-1665
    • Lopez, J.L.1    Marina, A.2    Alvarez, G.3    Vazquez, J.4
  • 45
    • 0037791750 scopus 로고    scopus 로고
    • Genetic variability of the marine mussel Mytilus galloprovincialis assessed using two-dimensional electrophoresis
    • Mosquera E, Lopez JL, Alvarez G. 2003. Genetic variability of the marine mussel Mytilus galloprovincialis assessed using two-dimensional electrophoresis. Heredity 90: 432-442.
    • (2003) Heredity , vol.90 , pp. 432-442
    • Mosquera, E.1    Lopez, J.L.2    Alvarez, G.3
  • 46
    • 34347388860 scopus 로고    scopus 로고
    • Evolution of 2-DE protein patterns in a mussel hybrid zone
    • Diz AP, Skibinski DOF. 2007. Evolution of 2-DE protein patterns in a mussel hybrid zone. Proteomics 7: 2111-2120.
    • (2007) Proteomics , vol.7 , pp. 2111-2120
    • Diz, A.P.1    Skibinski, D.O.F.2
  • 47
    • 12344311074 scopus 로고    scopus 로고
    • Role of proteomics in taxonomy: The Mytilus complex as a model of study
    • López JL. 2005. Role of proteomics in taxonomy: The Mytilus complex as a model of study. J Chromatogr B 815: 261-274.
    • (2005) J Chromatogr B , vol.815 , pp. 261-274
    • López, J.L.1
  • 49
    • 70149107068 scopus 로고    scopus 로고
    • Evolution of nacre: Biochemistry and proteomics of the shell organic matrix of the cephalopod Nautilus macromphalus
    • Marie B, Marin F, Marie A, Bédouet L, Dubost L, Alcaraz G, Milet C, Luquet G. 2009. Evolution of nacre: Biochemistry and proteomics of the shell organic matrix of the cephalopod Nautilus macromphalus ChemBioChem 10: 1495-1506.
    • (2009) ChemBioChem , vol.10 , pp. 1495-1506
    • Marie, B.1    Marin, F.2    Marie, A.3    Bédouet, L.4    Dubost, L.5    Alcaraz, G.6    Milet, C.7    Luquet, G.8
  • 50
    • 4444349745 scopus 로고    scopus 로고
    • Surface-enhanced laser desorption/ionization-time of flight-mass spectrometry approach to biomarker discovery in blue mussels (Mytilus edulis) exposed to polyaromatic hydrocarbons and heavy metals under field conditions
    • Knigge T, Monsinjon T, Andersen O-K. 2004. Surface-enhanced laser desorption/ionization-time of flight-mass spectrometry approach to biomarker discovery in blue mussels (Mytilus edulis) exposed to polyaromatic hydrocarbons and heavy metals under field conditions. Proteomics 4: 2722-2727.
    • (2004) Proteomics , vol.4 , pp. 2722-2727
    • Knigge, T.1    Monsinjon, T.2    Andersen, O.3
  • 51
    • 1842529558 scopus 로고    scopus 로고
    • Physiological and proteomic responses in Mytilus edulis exposed to PCBs and PAHs extracted from Baltic Sea sediments
    • Olsson BR, Bradley BP, Gilek M, Reimer O, Shepard JL, Tedengren M. 2004. Physiological and proteomic responses in Mytilus edulis exposed to PCBs and PAHs extracted from Baltic Sea sediments. Hydrobiologia 514: 15-27.
    • (2004) Hydrobiologia , vol.514 , pp. 15-27
    • Olsson, B.R.1    Bradley, B.P.2    Gilek, M.3    Reimer, O.4    Shepard, J.L.5    Tedengren, M.6
  • 53
    • 33646248380 scopus 로고    scopus 로고
    • Protein responses in blue mussels (Mytilus edulis) exposed to organic pollutants: A combined CYP-antibody/proteomic approach
    • Jonsson H, Schiedek D, Grøsvik BE, Goksøyr A. 2006. Protein responses in blue mussels (Mytilus edulis) exposed to organic pollutants: A combined CYP-antibody/proteomic approach. Aquat Toxicol (Amst) 78: S49-S56.
    • (2006) Aquat Toxicol (Amst) , vol.78
    • Jonsson, H.1    Schiedek, D.2    Grøsvik, B.E.3    Goksøyr, A.4
  • 54
    • 33749526135 scopus 로고    scopus 로고
    • Data processing and classification analysis of proteomic changes: A case study of oil pollution in the mussel, Mytilus edulis
    • Monsinjon T, Andersen O, Leboulenger F, Knigge T. 2006. Data processing and classification analysis of proteomic changes: A case study of oil pollution in the mussel, Mytilus edulis Proteome Sci 4: 17.
    • (2006) Proteome Sci , vol.4 , pp. 17
    • Monsinjon, T.1    Andersen, O.2    Leboulenger, F.3    Knigge, T.4
  • 55
    • 20444397400 scopus 로고    scopus 로고
    • Carbonylation and glutathionylation of proteins in the blue mussel Mytilus edulis detected by proteomic analysis and Western blotting: Actin as a target for oxidative stress
    • McDonagh B, Tyther R, Sheehan D. 2005. Carbonylation and glutathionylation of proteins in the blue mussel Mytilus edulis detected by proteomic analysis and Western blotting: Actin as a target for oxidative stress. Aquat Toxicol (Amst) 73: 315-326.
    • (2005) Aquat Toxicol (Amst) , vol.73 , pp. 315-326
    • McDonagh, B.1    Tyther, R.2    Sheehan, D.3
  • 56
    • 34250836448 scopus 로고    scopus 로고
    • Proteomics-based method for the assessment of marine pollution using liquid chromatography coupled with two-dimensional electrophoresis
    • Amelina H, Apraiz I, Sun W, Cristobal S. 2007. Proteomics-based method for the assessment of marine pollution using liquid chromatography coupled with two-dimensional electrophoresis. J Proteome Res 6: 2094-2104.
    • (2007) J Proteome Res , vol.6 , pp. 2094-2104
    • Amelina, H.1    Apraiz, I.2    Sun, W.3    Cristobal, S.4
  • 57
    • 33746308468 scopus 로고    scopus 로고
    • Identification of proteomic signatures of exposure to marine pollutants in mussels (Mytilus edulis)
    • Apraiz I, Mi J, Cristobal S. 2006. Identification of proteomic signatures of exposure to marine pollutants in mussels (Mytilus edulis). Mol Cell Proteomics 5: 1274-1285.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 1274-1285
    • Apraiz, I.1    Mi, J.2    Cristobal, S.3
  • 58
    • 28344444569 scopus 로고    scopus 로고
    • The potential of ecotoxicoproteomics in environmental monitoring: Biomarker profiling in mussel plasma using proteinchip array technology
    • Bjørnstad A, Larsen BK, Skadsheim A, Jones MB, Andersen OK. 2006. The potential of ecotoxicoproteomics in environmental monitoring: Biomarker profiling in mussel plasma using proteinchip array technology. J Toxicol Environ Health Part A 69: 77-96.
    • (2006) J Toxicol Environ Health Part A , vol.69 , pp. 77-96
    • Bjørnstad, A.1    Larsen, B.K.2    Skadsheim, A.3    Jones, M.B.4    Andersen, O.K.5
  • 59
    • 33750586534 scopus 로고    scopus 로고
    • Utility of proteomics to assess pollutant response of clams from the Doñana bank of Guadalquivir Estuary (SW Spain)
    • Romero-Ruiz A, Carrascal M, Alhama J, Gómez-Ariza JL, Abian J, López-Barea J. 2006. Utility of proteomics to assess pollutant response of clams from the Doñana bank of Guadalquivir Estuary (SW Spain). Proteomics 6: S245-S255.
    • (2006) Proteomics , vol.6
    • Romero-Ruiz, A.1    Carrascal, M.2    Alhama, J.3    Gómez-Ariza, J.L.4    Abian, J.5    López-Barea, J.6
  • 62
    • 33645234384 scopus 로고    scopus 로고
    • Protein carbonylation and heat shock response in Ruditapes decussatus following p,p'-dichlorodiphenyldichloroethylene (DDE) exposure: A proteomic approach reveals that DDE causes oxidative stress
    • Dowling V, Hoarau PC, Romeo M, O'Halloran J, van Pelt F, O'Brien N, Sheehan D. 2006. Protein carbonylation and heat shock response in Ruditapes decussatus following p, p'-dichlorodiphenyldichloroethylene (DDE) exposure: A proteomic approach reveals that DDE causes oxidative stress. Aquat Toxicol (Amst) 77: 11-18.
    • (2006) Aquat Toxicol (Amst) , vol.77 , pp. 11-18
    • Dowling, V.1    Hoarau, P.C.2    Romeo, M.3    O'Halloran, J.4    van Pelt, F.5    O'Brien, N.6    Sheehan, D.7
  • 63
    • 33748982067 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis analysis of glutathione affinity-selected proteins from the clam Tapes semidecussatus: Evidence for tissue-specific expression of redox proteins
    • Dowling V, McDonagh B, Cotter EM, O'Brien N, van Pelt F, O'Halloran J, Sheehan D. 2006. Two-dimensional electrophoresis analysis of glutathione affinity-selected proteins from the clam Tapes semidecussatus: Evidence for tissue-specific expression of redox proteins. Comp Biochem Physiol Part D: Genomics Proteomics 1: 267-272.
    • (2006) Comp Biochem Physiol Part D: Genomics Proteomics , vol.1 , pp. 267-272
    • Dowling, V.1    McDonagh, B.2    Cotter, E.M.3    O'Brien, N.4    van Pelt, F.5    O'Halloran, J.6    Sheehan, D.7
  • 64
    • 0042861622 scopus 로고    scopus 로고
    • Changes in protein expression profiles in bivalve molluscs (Chamaelea gallina) exposed to four model environmental pollutants
    • Rodríguez-Ortega MJ, Grøsvik BE, Rodríguez-Ariza A, Goksøyr A, López-Barea J. 2003. Changes in protein expression profiles in bivalve molluscs (Chamaelea gallina) exposed to four model environmental pollutants. Proteomics 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
  • 65
    • 33646255916 scopus 로고    scopus 로고
    • An ecotoxicoproteomic approach (SELDI-TOF mass spectrometry) to biomarker discovery in crab exposed to pollutants under laboratory conditions
    • Gomiero A, Pampanin DM, Bjørnstad A, Larsen BK, Provan F, Lyng E, Andersen OK. 2006. An ecotoxicoproteomic approach (SELDI-TOF mass spectrometry) to biomarker discovery in crab exposed to pollutants under laboratory conditions. Aquat Toxicol (Amst) 78: S34-S41.
    • (2006) Aquat Toxicol (Amst) , vol.78
    • Gomiero, A.1    Pampanin, D.M.2    Bjørnstad, A.3    Larsen, B.K.4    Provan, F.5    Lyng, E.6    Andersen, O.K.7
  • 66
    • 59449094858 scopus 로고    scopus 로고
    • Effect of cadmium exposure on the globin protein expression in 4th instar larvae of Chironomus riparius Mg. (Diptera: Chironomidae): An ecotoxicoproteomics approach
    • Choi J, Ha M-H. 2009. Effect of cadmium exposure on the globin protein expression in 4th instar larvae of Chironomus riparius Mg. (Diptera: Chironomidae): An ecotoxicoproteomics approach. Proteomics 9: 31-39.
    • (2009) Proteomics , vol.9 , pp. 31-39
    • Choi, J.1    Ha, M.2
  • 67
    • 32944463435 scopus 로고    scopus 로고
    • Proteomic evaluation of cadmium toxicity on the midge Chironomus riparius Meigen larvae
    • Lee S-E, Yoo D-H, Son J, Cho K. 2006. Proteomic evaluation of cadmium toxicity on the midge Chironomus riparius Meigen larvae. Proteomics 6: 945-957.
    • (2006) Proteomics , vol.6 , pp. 945-957
    • Lee, S.1    Yoo, D.2    Son, J.3    Cho, K.4
  • 68
    • 67149128374 scopus 로고    scopus 로고
    • 2D gel-based proteome and phosphoproteome analysis during larval metamorphosis in two major marine biofouling invertebrates
    • Thiyagarajan V, Wong T, Qian PY. 2009. 2D gel-based proteome and phosphoproteome analysis during larval metamorphosis in two major marine biofouling invertebrates. J Proteome Res 8: 2708-2719.
    • (2009) J Proteome Res , vol.8 , pp. 2708-2719
    • Thiyagarajan, V.1    Wong, T.2    Qian, P.Y.3
  • 69
    • 49749105216 scopus 로고    scopus 로고
    • Proteomic analysis of larvae during development, attachment, and metamorphosis in the fouling barnacle, Balanus amphitrite
    • Thiyagarajan V, Qian P-Y. 2008. Proteomic analysis of larvae during development, attachment, and metamorphosis in the fouling barnacle, Balanus amphitrite Proteomics 8: 3164-3172.
    • (2008) Proteomics , vol.8 , pp. 3164-3172
    • Thiyagarajan, V.1    Qian, P.2
  • 70
    • 35348936603 scopus 로고    scopus 로고
    • A proteomic study on postdiapaused embryonic development of brine shrimp (Artemia franciscana)
    • Wang W, Meng B, Chen W, Ge X, Liu S, Yu J. 2007. A proteomic study on postdiapaused embryonic development of brine shrimp (Artemia franciscana). Proteomics 7: 3580-3591.
    • (2007) Proteomics , vol.7 , pp. 3580-3591
    • Wang, W.1    Meng, B.2    Chen, W.3    Ge, X.4    Liu, S.5    Yu, J.6
  • 71
    • 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. 2006. 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 (Amst) 79: 325-333.
    • (2006) Aquat Toxicol (Amst) , vol.79 , pp. 325-333
    • McDonagh, B.1    Sheehan, D.2
  • 72
    • 34948844206 scopus 로고    scopus 로고
    • Effect of oxidative stress on protein thiols in the blue mussel Mytilus edulis: Proteomic identification of target proteins
    • McDonagh B, Sheehan D. 2007. Effect of oxidative stress on protein thiols in the blue mussel Mytilus edulis: Proteomic identification of target proteins. Proteomics 7: 3395-3403.
    • (2007) Proteomics , vol.7 , pp. 3395-3403
    • McDonagh, B.1    Sheehan, D.2
  • 73
    • 0043022046 scopus 로고    scopus 로고
    • Characterization of an inducible isoform of the Cu/Zn superoxide dismutase in the blue mussel Mytilus edulis
    • Manduzio H, Monsinjon T, Rocher B, Leboulenger F, Galap C. 2003. Characterization of an inducible isoform of the Cu/Zn superoxide dismutase in the blue mussel Mytilus edulis Aquat Toxicol (Amst) 64: 73-83.
    • (2003) Aquat Toxicol (Amst) , vol.64 , pp. 73-83
    • Manduzio, H.1    Monsinjon, T.2    Rocher, B.3    Leboulenger, F.4    Galap, C.5
  • 74
    • 44749089879 scopus 로고    scopus 로고
    • Effects of oxidative stress on protein thiols and disulphides in Mytilus edulis revealed by proteomics: Actin and protein disulphide isomerase are redox targets
    • McDonagh B, Sheehan D. 2008. Effects of oxidative stress on protein thiols and disulphides in Mytilus edulis revealed by proteomics: Actin and protein disulphide isomerase are redox targets. Mar Environ Res 66: 193-195.
    • (2008) Mar Environ Res , vol.66 , pp. 193-195
    • McDonagh, B.1    Sheehan, D.2
  • 75
    • 27144530363 scopus 로고    scopus 로고
    • Peroxisomal proteomics, a new tool for risk assessment of peroxisome proliferating pollutants in the marine environment
    • Mi J, Orbea A, Syme N, Ahmed M, Cajaraville MP, Cristóbal S. 2005. Peroxisomal proteomics, a new tool for risk assessment of peroxisome proliferating pollutants in the marine environment. Protemics 5: 3954-3965.
    • (2005) Protemics , vol.5 , pp. 3954-3965
    • Mi, J.1    Orbea, A.2    Syme, N.3    Ahmed, M.4    Cajaraville, M.P.5    Cristóbal, S.6
  • 76
    • 65449164977 scopus 로고    scopus 로고
    • LC-MS/MS-based proteome profiling in Daphnia pulex and Daphnia longicephala: The Daphnia pulex genome database as a key for high throughput proteomics in Daphnia
    • Fröhlich T, Arnold GJ, Fritsch R, Mayr T, Laforsch C. 2009. LC-MS/MS-based proteome profiling in Daphnia pulex and Daphnia longicephala: The Daphnia pulex genome database as a key for high throughput proteomics in Daphnia. BMC Genomics 10: 13.
    • (2009) BMC Genomics , vol.10 , pp. 13
    • Fröhlich, T.1    Arnold, G.J.2    Fritsch, R.3    Mayr, T.4    Laforsch, C.5
  • 77
    • 10644230916 scopus 로고    scopus 로고
    • Review: Current two-dimensional electrophoresis technology for proteomics
    • Görg W, Dunn MJ. 2004. Review: Current two-dimensional electrophoresis technology for proteomics. Proteomics 4: 3665-3685.
    • (2004) Proteomics , vol.4 , pp. 3665-3685
    • Görg, W.1    Dunn, M.J.2
  • 78
    • 33746211196 scopus 로고    scopus 로고
    • OMICS-driven biomarker discovery in nutrition and health
    • Kussman M, Raymond F, Affolter M. 2006. OMICS-driven biomarker discovery in nutrition and health. J Biotechnol 124: 758-787.
    • (2006) J Biotechnol , vol.124 , pp. 758-787
    • Kussman, M.1    Raymond, F.2    Affolter, M.3
  • 79
    • 33644845960 scopus 로고    scopus 로고
    • Comparative study of three proteomic quantitative methods, DIGE, CiCAT, and iTRAQ, using 2D gel- or -LC-MALDI TOF/TOF
    • Wu WW, Wang G, Back SJ, Shen R-F. 2006. Comparative study of three proteomic quantitative methods, DIGE, CiCAT, and iTRAQ, using 2D gel- or -LC-MALDI TOF/TOF. J Proteome Res 5: 651-658.
    • (2006) J Proteome Res , vol.5 , pp. 651-658
    • Wu, W.W.1    Wang, G.2    Back, S.J.3    Shen, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.