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Volumn 113, Issue 1, 2009, Pages 60-69

Proteomic analysis of hepatic tissue of zebrafish (Danio rerio) experimentally exposed to chronic microcystin-LR

Author keywords

Chronic toxicity; Microcystin LR; Protein phosphatase; Proteomics; Ultrastructure

Indexed keywords

DRINKING WATER; MICROCYSTIN LR; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHOPROTEIN PHOSPHATASE 2A; REACTIVE OXYGEN METABOLITE;

EID: 75249106631     PISSN: 10966080     EISSN: 10960929     Source Type: Journal    
DOI: 10.1093/toxsci/kfp248     Document Type: Article
Times cited : (92)

References (59)
  • 1
    • 0022656473 scopus 로고
    • Succinate thiokinase in pigeon breast muscle mitochondria
    • Allen, D. A., and Ottaway, J. H. (1986). Succinate thiokinase in pigeon breast muscle mitochondria. FEBS Lett. 194, 171-175.
    • (1986) FEBS Lett. , vol.194 , pp. 171-175
    • Allen, D.A.1    Ottaway, J.H.2
  • 2
    • 9244223606 scopus 로고    scopus 로고
    • A comparative study on microcystin-LR induced behavioural changes of two fish species (Danio rerio and Leucaspius delineatus)
    • Baganz, D., Staaks, G., Pflugmacher, S., and Steinberg, C. E. W. (2004). A comparative study on microcystin-LR induced behavioural changes of two fish species (Danio rerio and Leucaspius delineatus). Environ. Toxicol. 19, 564-570.
    • (2004) Environ. Toxicol. , vol.19 , pp. 564-570
    • Baganz, D.1    Staaks, G.2    Pflugmacher, S.3    Steinberg, C.E.W.4
  • 3
    • 24044450575 scopus 로고    scopus 로고
    • High crustacean toxicity of microcystin congeners does not correlate with high protein phosphatase inhibitory activity
    • Blom, J. F., and Jüttner, F. (2005). High crustacean toxicity of microcystin congeners does not correlate with high protein phosphatase inhibitory activity. Toxicon 46, 465-470.
    • (2005) Toxicon. , vol.46 , pp. 465-470
    • Blom, J.F.1    Jüttner, F.2
  • 4
    • 0025806526 scopus 로고
    • Inhibition of cell proliferation by a-tocopherol. Role of protein kinase C
    • Boscoboinik, D., Szewczyk, A., Hensey, C., and Azzi, A. (1991). Inhibition of cell proliferation by a-tocopherol. Role of protein kinase C. J. Biol. Chem. 266, 6188-6194.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6188-6194
    • Boscoboinik, D.1    Szewczyk, A.2    Hensey, C.3    Azzi, A.4
  • 5
    • 0019843141 scopus 로고
    • Non-muscle a-actinins are calciumsensitive actin-binding proteins
    • Burridge, K., and Feramisco, J. R. (1981). Non-muscle a-actinins are calciumsensitive actin-binding proteins. Nature 294, 565-567.
    • (1981) Nature , vol.294 , pp. 565-567
    • Burridge, K.1    Feramisco, J.R.2
  • 7
    • 34247120229 scopus 로고    scopus 로고
    • Elucidation and short-term forecasting of microcystin concentrations in Lake Suwa (Japan) by means of artificial neural networks and evolutionary algorithms
    • Chan, W. S., Recknagel, F., Cao, H. Q., and Park, H. D. (2007). Elucidation and short-term forecasting of microcystin concentrations in Lake Suwa (Japan) by means of artificial neural networks and evolutionary algorithms. Water Res. 41, 2247-2255.
    • (2007) Water Res. , vol.41 , pp. 2247-2255
    • Chan, W.S.1    Recknagel, F.2    Cao, H.Q.3    Park, H.D.4
  • 8
    • 32044462755 scopus 로고    scopus 로고
    • Identification of human liver mitochondrial aldehyde dehydrogenase as a potential target for microcystin-LR
    • Chen, T., Cui, J., Liang, Y., Xin, X. B., Young, D. O., Chen, C., and Shen, P. P. (2006). Identification of human liver mitochondrial aldehyde dehydrogenase as a potential target for microcystin-LR. Toxicology 220, 71-80.
    • (2006) Toxicology , vol.220 , pp. 71-80
    • Chen, T.1    Cui, J.2    Liang, Y.3    Xin, X.B.4    Young, D.O.5    Chen, C.6    Shen, P.P.7
  • 10
    • 0028939160 scopus 로고
    • Microcystin-LR induced an inhibition of protein synthesis in isolated rat hepatocytes
    • Claeyssens, S., Francois, A., Chedeville, A., and Lavoinne, A. (1995). Microcystin-LR induced an inhibition of protein synthesis in isolated rat hepatocytes. Biochem. J. 306, 693-696.
    • (1995) Biochem. J. , vol.306 , pp. 693-696
    • Claeyssens, S.1    Francois, A.2    Chedeville, A.3    Lavoinne, A.4
  • 11
    • 0032853037 scopus 로고    scopus 로고
    • Identification of the cDNA encoding human 6-phosphogluconolactonase, the enzyme catalyzing the second step of the pentose phosphate pathway
    • Collard, F., Collet, J., Gerin, I., Veiga-da-Cunha, M., and Van Schaftingen, E. (1999). Identification of the cDNA encoding human 6-phosphogluconolactonase, the enzyme catalyzing the second step of the pentose phosphate pathway. FEBS Lett. 459, 223-226.
    • (1999) FEBS Lett. , vol.459 , pp. 223-226
    • Collard, F.1    Collet, J.2    Gerin, I.3    Veiga-da-Cunha, M.4    Van Schaftingen, E.5
  • 12
    • 39149094295 scopus 로고    scopus 로고
    • Microcystin accumulation in liver and muscle of tilapia in two large Brazilian hydroelectric reservoirs
    • Deblois, C. P., Aranda-Rodriguez, R., Giani, A., and Bird, D. F. (2008). Microcystin accumulation in liver and muscle of tilapia in two large Brazilian hydroelectric reservoirs. Toxicon 51, 435-448.
    • (2008) Toxicon. , vol.51 , pp. 435-448
    • Deblois, C.P.1    Aranda-Rodriguez, R.2    Giani, A.3    Bird, D.F.4
  • 13
    • 0035941161 scopus 로고    scopus 로고
    • Critical role of reactive oxygen species formation in microcystin-induced cytoskeleton disruption in primary cultured hepatocytes
    • Ding, W. X., Shen, H. M., and Ong, C. N. (2001). Critical role of reactive oxygen species formation in microcystin-induced cytoskeleton disruption in primary cultured hepatocytes. J. Toxicol. Environ. Health 64, 507-519.
    • (2001) J. Toxicol. Environ. Health , vol.64 , pp. 507-519
    • Ding, W.X.1    Shen, H.M.2    Ong, C.N.3
  • 14
    • 33750591821 scopus 로고    scopus 로고
    • Proteomics as a route to identification of toxicity targets in environmental toxicology
    • Dowling, V. A., and Sheehan, D. (2006). Proteomics as a route to identification of toxicity targets in environmental toxicology. Proteomics 6(20), 5597-5604.
    • (2006) Proteomics , vol.6 , Issue.20 , pp. 5597-5604
    • Dowling, V.A.1    Sheehan, D.2
  • 15
    • 4744344805 scopus 로고    scopus 로고
    • Cytoplasmic nonsense-mediated mRNA decay for a nonsense (W262X) transcript of the gene responsible for hereditary tyrosinemia, fumarylacetoacetate hydrolase
    • Dreumont, N., Maresca, A., Khandjian, E. W., Baklouti, F., and Tanguay, R. M. (2004). Cytoplasmic nonsense-mediated mRNA decay for a nonsense (W262X) transcript of the gene responsible for hereditary tyrosinemia, fumarylacetoacetate hydrolase. Biochem. Biophys. Res. Commun. 324, 186-192.
    • (2004) Biochem. Biophys. Res. Commun. , vol.324 , pp. 186-192
    • Dreumont, N.1    Maresca, A.2    Khandjian, E.W.3    Baklouti, F.4    Tanguay, R.M.5
  • 18
    • 0030897513 scopus 로고    scopus 로고
    • Role of long-chain fatty acyl-CoAs esters in the regulation of metabolism and cell signaling
    • Faergeman, N. J., and Knudsen, J. (1997). Role of long-chain fatty acyl-CoAs esters in the regulation of metabolism and cell signaling. Biochem. J. 323, 1-12.
    • (1997) Biochem. J. , vol.323 , pp. 1-12
    • Faergeman, N.J.1    Knudsen, J.2
  • 20
    • 0034176293 scopus 로고    scopus 로고
    • Pathological and biochemical characterization of microcystin-induced hepatopancreas and kidney damage in carp (Cyprinus carpio)
    • Fischer, W. J., and Dietrich, D. R. (2000). Pathological and biochemical characterization of microcystin-induced hepatopancreas and kidney damage in carp (Cyprinus carpio). Toxicol. Appl. Pharmacol. 164, 73-81.
    • (2000) Toxicol. Appl. Pharmacol. , vol.164 , pp. 73-81
    • Fischer, W.J.1    Dietrich, D.R.2
  • 22
    • 1642559254 scopus 로고    scopus 로고
    • Microcystin-LR and okadaic acid-induced cellular effects: a dualistic response
    • Gehringer, M. M. (2004). Microcystin-LR and okadaic acid-induced cellular effects: a dualistic response. FEBS Lett. 557, 1-8.
    • (2004) FEBS Lett. , vol.557 , pp. 1-8
    • Gehringer, M.M.1
  • 26
    • 0031543318 scopus 로고    scopus 로고
    • Cancer preventive selenocompounds induce a specific redox modification of cysteine-rich regions in calcium-dependent isoenzymes of protein kinase C
    • Gopalakrishna, R., Gundimeda, U., and Chen, Z. H. (1997). Cancer preventive selenocompounds induce a specific redox modification of cysteine-rich regions in calcium-dependent isoenzymes of protein kinase C. Arch. Biochem. Biophys. 348, 25-36.
    • (1997) Arch. Biochem. Biophys. , vol.348 , pp. 25-36
    • Gopalakrishna, R.1    Gundimeda, U.2    Chen, Z.H.3
  • 27
    • 67349085803 scopus 로고    scopus 로고
    • Analysis of dissolved microcystins in surface water samples from Kovada Lake, Turkey
    • Gurbuz, F., Metcalf, J. S., Karahan, A. G., and Codd, G. A. (2009). Analysis of dissolved microcystins in surface water samples from Kovada Lake, Turkey. Sci. Total Environ. 407, 4038-4046.
    • (2009) Sci. Total Environ. , vol.407 , pp. 4038-4046
    • Gurbuz, F.1    Metcalf, J.S.2    Karahan, A.G.3    Codd, G.A.4
  • 28
    • 0038696373 scopus 로고    scopus 로고
    • Inhibition of nuclear protein phosphatase activity in mouse hepatocytes by the cyanobacterial toxin microcystin-LR
    • Guzman, R. E., Solter, P. F., and Runnegar, M. T. (2003). Inhibition of nuclear protein phosphatase activity in mouse hepatocytes by the cyanobacterial toxin microcystin-LR. Toxicon 41, 773-781.
    • (2003) Toxicon. , vol.41 , pp. 773-781
    • Guzman, R.E.1    Solter, P.F.2    Runnegar, M.T.3
  • 29
    • 0025008805 scopus 로고
    • Purification of profilin from Saccharomyces cerevisiae and analysis of profilin-deficient cells
    • Haarer, B. K., Lillie, S. H., Adams, A. E. M., Magdolen, V., Bandlow, W., and Brown, S. S. (1990). Purification of profilin from Saccharomyces cerevisiae and analysis of profilin-deficient cells. J. Cell Biol. 110, 105-114.
    • (1990) J. Cell Biol. , vol.110 , pp. 105-114
    • Haarer, B.K.1    Lillie, S.H.2    Adams, A.E.M.3    Magdolen, V.4    Bandlow, W.5    Brown, S.S.6
  • 30
    • 14744268901 scopus 로고    scopus 로고
    • Occurrence and elimination of cyanobacterial toxins in drinking water treatment plants
    • Hoeger, S. J., Hitzfeld, B. C., and Dietrich, D. R. (2005). Occurrence and elimination of cyanobacterial toxins in drinking water treatment plants. Toxicol. Appl. Pharmacol. 203, 231-242.
    • (2005) Toxicol. Appl. Pharmacol. , vol.203 , pp. 231-242
    • Hoeger, S.J.1    Hitzfeld, B.C.2    Dietrich, D.R.3
  • 32
    • 55249124257 scopus 로고    scopus 로고
    • Ectopic expression of an annexin from Brassica juncea confers tolerance to abiotic and biotic stress treatments in transgenic tobacco
    • Jami, S. K., Clark, G. B., Turlapati, S. A., Handley, C., Roux, S. J., and Kirti, P. B. (2008). Ectopic expression of an annexin from Brassica juncea confers tolerance to abiotic and biotic stress treatments in transgenic tobacco. Plant Physiol. Biochem. 46, 1019-1030.
    • (2008) Plant Physiol. Biochem. , vol.46 , pp. 1019-1030
    • Jami, S.K.1    Clark, G.B.2    Turlapati, S.A.3    Handley, C.4    Roux, S.J.5    Kirti, P.B.6
  • 33
    • 0017735655 scopus 로고
    • The action of human pancreatic and salivary isoamylases on starch and glycogen
    • Kaczmarek, M. J., and Rosenmund, H. (1977). The action of human pancreatic and salivary isoamylases on starch and glycogen. Clin. Chim. Acta 79, 69-73.
    • (1977) Clin. Chim. Acta. , vol.79 , pp. 69-73
    • Kaczmarek, M.J.1    Rosenmund, H.2
  • 36
    • 23844494323 scopus 로고    scopus 로고
    • The effects of harmful algal blooms on aquatic organisms
    • Landsberg, J. H. (2002). The effects of harmful algal blooms on aquatic organisms. Fish. Sci. 10, 113-390.
    • (2002) Fish. Sci. , vol.10 , pp. 113-390
    • Landsberg, J.H.1
  • 37
    • 0034598662 scopus 로고    scopus 로고
    • Influence of microcystin-YR and nodularin on the activity of some proteolytic enzymes in mouse liver
    • Lankoff, A., and Kolataj, A. (2001). Influence of microcystin-YR and nodularin on the activity of some proteolytic enzymes in mouse liver. Toxicon 39, 419-423.
    • (2001) Toxicon. , vol.39 , pp. 419-423
    • Lankoff, A.1    Kolataj, A.2
  • 38
    • 34547144685 scopus 로고    scopus 로고
    • Sequential ultrastructural and biochemical changes induced in vivo by the hepatotoxic microcystins in liver of the phytoplanktivorous silver carp Hypophthalmichthys molitrix
    • Li, L., Xie, P., Li, S. X., Qiu, T., and Guo, L. G. (2007). Sequential ultrastructural and biochemical changes induced in vivo by the hepatotoxic microcystins in liver of the phytoplanktivorous silver carp Hypophthalmichthys molitrix. Comp. Biochem. Physiol. C: Pharmacol. Toxicol. 146, 357-367.
    • (2007) Comp. Biochem. Physiol. C: Pharmacol. Toxicol. , vol.146 , pp. 357-367
    • Li, L.1    Xie, P.2    Li, S.X.3    Qiu, T.4    Guo, L.G.5
  • 39
    • 8644230019 scopus 로고    scopus 로고
    • Subchronic oral toxicity of microcystin in common carp (Cyprinus carpio L.) exposed to microcystis under laboratory conditions
    • Li, X. Y., Chung, I. K., Kim, J. I., and Lee, J. A. (2004). Subchronic oral toxicity of microcystin in common carp (Cyprinus carpio L.) exposed to microcystis under laboratory conditions. Toxicon 44, 821-827.
    • (2004) Toxicon. , vol.44 , pp. 821-827
    • Li, X.Y.1    Chung, I.K.2    Kim, J.I.3    Lee, J.A.4
  • 40
    • 0141543868 scopus 로고    scopus 로고
    • Responses of antioxidant systems in the hepatocytes of common carp (Cyprinus carpio L.) to the toxicity of microcystin-LR
    • Li, X. Y., Liu, Y. D., Song, L. R., and Liu, J. T. (2003). Responses of antioxidant systems in the hepatocytes of common carp (Cyprinus carpio L.) to the toxicity of microcystin-LR. Toxicon 42, 85-89.
    • (2003) Toxicon. , vol.42 , pp. 85-89
    • Li, X.Y.1    Liu, Y.D.2    Song, L.R.3    Liu, J.T.4
  • 42
    • 8644262199 scopus 로고    scopus 로고
    • Effect of microcystin-LR on protein phosphatase activity and glycogen content in isolated hepatocytes of fed and fasted juvenile goldfish Carassius auratus L
    • Malbrouck, C., Trausch, G., Devos, P., and Kestemont, P. (2004). Effect of microcystin-LR on protein phosphatase activity and glycogen content in isolated hepatocytes of fed and fasted juvenile goldfish Carassius auratus L. Toxicon 44, 927-932.
    • (2004) Toxicon. , vol.44 , pp. 927-932
    • Malbrouck, C.1    Trausch, G.2    Devos, P.3    Kestemont, P.4
  • 43
    • 60449099557 scopus 로고    scopus 로고
    • Differential protein expression in Corbicula fluminea upon exposure to a Microcystis aeruginosa toxic strain
    • Martins, J. C., Leão, P. N., and Vasconcelos, V. (2009). Differential protein expression in Corbicula fluminea upon exposure to a Microcystis aeruginosa toxic strain. Toxicon 53, 409-416.
    • (2009) Toxicon. , vol.53 , pp. 409-416
    • Martins, J.C.1    Leão, P.N.2    Vasconcelos, V.3
  • 44
    • 0024212517 scopus 로고
    • Superoxide dismutase: the first twenty years (1968-1988)
    • McCord, J. M., and Fridovich, I. (1988). Superoxide dismutase: the first twenty years (1968-1988). Free Radic. Biol. Med. 5, 363-369.
    • (1988) Free Radic. Biol. Med. , vol.5 , pp. 363-369
    • McCord, J.M.1    Fridovich, I.2
  • 46
    • 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., Francxois, J. C., Bernard, C., and Edery, M. (2008b). 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. 86, 166-175.
    • (2008) Aquat. Toxicol. , vol.86 , pp. 166-175
    • Mezhoud, K.1    Praseuth, D.2    Puiseux-Dao, S.3    Francxois, J.C.4    Bernard, C.5    Edery, M.6
  • 48
    • 20444468492 scopus 로고    scopus 로고
    • Determination of microcystins in fish by solvent extraction and liquid chromatography
    • Moreno, I. M., Molina, R., Jos, A., Picó, Y., and Cameán, A. M. (2005). Determination of microcystins in fish by solvent extraction and liquid chromatography. J. Chromatogr. A 1080, 199-203.
    • (2005) J. Chromatogr. A. , vol.1080 , pp. 199-203
    • Moreno, I.M.1    Molina, R.2    Jos, A.3    Picó, Y.4    Cameán, A.M.5
  • 49
    • 0032159462 scopus 로고    scopus 로고
    • Physiologic importance of protein phosphatase inhibitors
    • Oliver, C. J., and Shenolikar, S. (1998). Physiologic importance of protein phosphatase inhibitors. Front Biosci. 3, 961-972.
    • (1998) Front Biosci. , vol.3 , pp. 961-972
    • Oliver, C.J.1    Shenolikar, S.2
  • 50
    • 33646109817 scopus 로고    scopus 로고
    • Hepatocytes nuclear structure and subcellular distribution of copper in zebrafish Brachydanio rerio and roach Rutilus rutilus (Teleostei, Cyprinidae) exposed to copper sulphate
    • Paris-Palacios, S., and Biagianti-Risbourg, S. (2006). Hepatocytes nuclear structure and subcellular distribution of copper in zebrafish Brachydanio rerio and roach Rutilus rutilus (Teleostei, Cyprinidae) exposed to copper sulphate. Aquat. Toxicol. 77, 306-313.
    • (2006) Aquat. Toxicol. , vol.77 , pp. 306-313
    • Paris-Palacios, S.1    Biagianti-Risbourg, S.2
  • 51
    • 0034046609 scopus 로고    scopus 로고
    • Annexin I is a stress protein induced by heat, oxidative stress and a sulfhydryl-reactive agent
    • Rhee, H. J., Kim, G. Y., Huh, J. W., Kim, S. W., and Na, D. S. (2000). Annexin I is a stress protein induced by heat, oxidative stress and a sulfhydryl-reactive agent. Eur. J. Biochem. 267, 3220-3225.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 3220-3225
    • Rhee, H.J.1    Kim, G.Y.2    Huh, J.W.3    Kim, S.W.4    Na, D.S.5
  • 52
    • 0036346564 scopus 로고    scopus 로고
    • Intracellular localization of endothelial cell annexins is differentially regulated by oxidative stress
    • Sacre, S. M., and Moss, S. E. (2002). Intracellular localization of endothelial cell annexins is differentially regulated by oxidative stress. Exp. Cell Res. 274, 254-263.
    • (2002) Exp. Cell Res. , vol.274 , pp. 254-263
    • Sacre, S.M.1    Moss, S.E.2
  • 54
    • 34249949759 scopus 로고    scopus 로고
    • Distribution and bioaccumulation of microcystins in water columns: a systematic investigation into the environmental fate and the risks associated with microcystins in Meiliang Bay, Lake Taihu
    • Song, L. R., Chen, W., Peng, L., Wan, N., Gan, N. Q., and Zhang, X. M. (2007). Distribution and bioaccumulation of microcystins in water columns: a systematic investigation into the environmental fate and the risks associated with microcystins in Meiliang Bay, Lake Taihu. Water Res. 41, 2853-2864.
    • (2007) Water Res. , vol.41 , pp. 2853-2864
    • Song, L.R.1    Chen, W.2    Peng, L.3    Wan, N.4    Gan, N.Q.5    Zhang, X.M.6
  • 55
    • 2542627411 scopus 로고    scopus 로고
    • Redox regulation of annexin 2 and its implications for oxidative stress-induced renal carcinogenesis and metastasis
    • Tanaka, T., Akatsuka, S., Ozeki, M., Shirase, T., Hiai, H., and Toyokuni, S. (2004). Redox regulation of annexin 2 and its implications for oxidative stress-induced renal carcinogenesis and metastasis. Oncogene 23, 3980-3989.
    • (2004) Oncogene , vol.23 , pp. 3980-3989
    • Tanaka, T.1    Akatsuka, S.2    Ozeki, M.3    Shirase, T.4    Hiai, H.5    Toyokuni, S.6
  • 56
    • 0030006616 scopus 로고    scopus 로고
    • Detection of microcystins, a blue-green algal hepatotoxin in drinking water sampled in Haimen and Fusui, endemic areas of primary liver cancer in China, by highly sensitive immunoassay
    • Ueno, Y., Nagata, S., Tsutsumi, T., Hasegawa, A., Watanabe, M. F., Park, H. D., Chen, G. C., and Yu, S. H. (1996). Detection of microcystins, a blue-green algal hepatotoxin in drinking water sampled in Haimen and Fusui, endemic areas of primary liver cancer in China, by highly sensitive immunoassay. Carcinogenesis 17, 1317-1321.
    • (1996) Carcinogenesis , vol.17 , pp. 1317-1321
    • Ueno, Y.1    Nagata, S.2    Tsutsumi, T.3    Hasegawa, A.4    Watanabe, M.F.5    Park, H.D.6    Chen, G.C.7    Yu, S.H.8
  • 57
    • 67349258548 scopus 로고    scopus 로고
    • Comparative studies of four protein preparation methods for proteomic study of the dinoflagellate Alexandrium sp. using two-dimensional electrophoresis
    • Wang, D. Z., Lin, L., Chan, L. L., and Hong, H. S. (2009). Comparative studies of four protein preparation methods for proteomic study of the dinoflagellate Alexandrium sp. using two-dimensional electrophoresis. Harmful Algae 8, 685-691.
    • (2009) Harmful Algae , vol.8 , pp. 685-691
    • Wang, D.Z.1    Lin, L.2    Chan, L.L.3    Hong, H.S.4
  • 58
    • 0036316242 scopus 로고    scopus 로고
    • Refsum's disease: a peroxisomal disorder affecting phytanic acid alpha-oxidation
    • Wierzbicki, A. S., Lloyd, M. D., Schofield, C. J., Feher, M. D., and Gibberd, F. B. (2002). Refsum's disease: a peroxisomal disorder affecting phytanic acid alpha-oxidation. J. Neurochem. 80, 727-735.
    • (2002) J. Neurochem. , vol.80 , pp. 727-735
    • Wierzbicki, A.S.1    Lloyd, M.D.2    Schofield, C.J.3    Feher, M.D.4    Gibberd, F.B.5
  • 59
    • 41149175685 scopus 로고    scopus 로고
    • Structural mechanism of demethylation and inactivation of protein phosphatase 2A
    • Xing, Y. N., Li, Z., Chen, Y., Stock, J. B., Jeffrey, P. D., and Shi, Y. G. (2008). Structural mechanism of demethylation and inactivation of protein phosphatase 2A. Cell 133, 154-163.
    • (2008) Cell , vol.133 , pp. 154-163
    • Xing, Y.N.1    Li, Z.2    Chen, Y.3    Stock, J.B.4    Jeffrey, P.D.5    Shi, Y.G.6


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