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Volumn 35, Issue 11, 2011, Pages

Haemocyte protein expression profiling of scallop Chlamys farreri response to acute viral necrosis virus (AVNV) infection

Author keywords

Acute viral necrosis virus; Haemocyte; Host response; Infection; Proteomic analysis

Indexed keywords

ACTIN; ADENYLATE KINASE; ARGININE KINASE; CALMODULIN; CALRETICULIN; CHAPERONE; CYTOSKELETON PROTEIN; HEAT SHOCK COGNATE PROTEIN 70; HEAT SHOCK PROTEIN; MYOSIN LIGHT CHAIN; PHOSPHOGLYCERATE DEHYDROGENASE; PROFILIN; TROPOMYOSIN; TROPONIN C;

EID: 80053330193     PISSN: 0145305X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dci.2011.03.022     Document Type: Article
Times cited : (26)

References (71)
  • 1
    • 0000049318 scopus 로고
    • Molluscan hemocyte-mediated cytotoxicity: the role of reactive oxygen intermediates
    • Adema C.M., Van der Knaap W.P.W., Sminia T. Molluscan hemocyte-mediated cytotoxicity: the role of reactive oxygen intermediates. Rev. Aquat. Sci. 1991, 4:201-223.
    • (1991) Rev. Aquat. Sci. , vol.4 , pp. 201-223
    • Adema, C.M.1    Van der Knaap, W.P.W.2    Sminia, T.3
  • 2
    • 85190490605 scopus 로고    scopus 로고
    • Partial cloning of the genome of the acute viral necrobiotic virus from Chlamys farreri and the nucleic acid diagnosing methods. Ocean University of China Master Thesis, Qingdao.
    • Ai, H.X., 2004. Partial cloning of the genome of the acute viral necrobiotic virus from Chlamys farreri and the nucleic acid diagnosing methods. Ocean University of China Master Thesis, Qingdao.
    • (2004)
    • Ai, H.X.1
  • 3
    • 32644458346 scopus 로고    scopus 로고
    • Artificial infection of cultured scallop Chlamys farreri by pathogen from acute virus necrobiotic disease
    • Ai H.X., Wang C.M., Wang X.H., Liu Y.J., Li Y., Huang J.Y., He G.Z., Song W.B. Artificial infection of cultured scallop Chlamys farreri by pathogen from acute virus necrobiotic disease. J. Fish Sci. China 2003, 10:386-391.
    • (2003) J. Fish Sci. China , vol.10 , pp. 386-391
    • Ai, H.X.1    Wang, C.M.2    Wang, X.H.3    Liu, Y.J.4    Li, Y.5    Huang, J.Y.6    He, G.Z.7    Song, W.B.8
  • 4
    • 0030018117 scopus 로고    scopus 로고
    • Molecular cloning of thi-4, a gene necessary for the biosynthesis of thiamine in Neurospora crassa
    • Akiyama M., Nakashima H. Molecular cloning of thi-4, a gene necessary for the biosynthesis of thiamine in Neurospora crassa. Curr. Genet. 1996, 30:62-67.
    • (1996) Curr. Genet. , vol.30 , pp. 62-67
    • Akiyama, M.1    Nakashima, H.2
  • 6
    • 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. Proteomics-based method for the assessment of marine pollution using liquid chromatography coupled with two dimensional electrophoresis. J. Proteome Res. 2007, 6:2094-2104.
    • (2007) J. Proteome Res. , vol.6 , pp. 2094-2104
    • Amelina, H.1    Apraiz, I.2    Sun, W.3    Cristobal, S.4
  • 7
    • 0029168863 scopus 로고
    • Short-term and long-term alterations in the energy budget of young oyster Ostrea edulis L. in response to temperature change
    • Beiras R., Camacho P., Albentosa M. Short-term and long-term alterations in the energy budget of young oyster Ostrea edulis L. in response to temperature change. J. Exp. Mar. Biol. Ecol. 1995, 186:221-236.
    • (1995) J. Exp. Mar. Biol. Ecol. , vol.186 , pp. 221-236
    • Beiras, R.1    Camacho, P.2    Albentosa, M.3
  • 8
    • 4344588192 scopus 로고    scopus 로고
    • A core catalytic domain of the TyrA protein family: arogenate dehydrogenase from Synechocystis
    • Bonner C.A., Jensen R.A., Gander J.E., Keyhani N.O. A core catalytic domain of the TyrA protein family: arogenate dehydrogenase from Synechocystis. Biochem. J. 2004, 382:279-291.
    • (2004) Biochem. J. , vol.382 , pp. 279-291
    • Bonner, C.A.1    Jensen, R.A.2    Gander, J.E.3    Keyhani, N.O.4
  • 9
    • 43049084373 scopus 로고    scopus 로고
    • Proteomic analysis of altered proteins in lymphoid organ of yellow head virus infected Penaeus monodon
    • Bourchookarn A., Havanapan P.O., Thongboonkerd V., Krittanai C. Proteomic analysis of altered proteins in lymphoid organ of yellow head virus infected Penaeus monodon. Biochim. Biophys. Acta 2008, 1784:504-511.
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 504-511
    • Bourchookarn, A.1    Havanapan, P.O.2    Thongboonkerd, V.3    Krittanai, C.4
  • 10
    • 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.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 11
    • 69249213971 scopus 로고    scopus 로고
    • Proteomic approach envisaged to analyze the bases of oyster tolerance/resistance to bonamiosis
    • Cao A., Fuentes J., Comesana P., Casas S.M., Villalba A.A. Proteomic approach envisaged to analyze the bases of oyster tolerance/resistance to bonamiosis. Aquaculture 2009, 295:149-156.
    • (2009) Aquaculture , vol.295 , pp. 149-156
    • Cao, A.1    Fuentes, J.2    Comesana, P.3    Casas, S.M.4    Villalba, A.A.5
  • 12
    • 0001552047 scopus 로고    scopus 로고
    • Hemocytes: forms and functions
    • Maryland Sea Grant, College Park, MD, USA, V.S. Kennedy, R.I.E. Newell, A.F. Eble (Eds.)
    • Cheng T.C. Hemocytes: forms and functions. The Eastern Oyster Crassostrea virginica 1996, 299-333. Maryland Sea Grant, College Park, MD, USA. V.S. Kennedy, R.I.E. Newell, A.F. Eble (Eds.).
    • (1996) The Eastern Oyster Crassostrea virginica , pp. 299-333
    • Cheng, T.C.1
  • 13
    • 0034256090 scopus 로고    scopus 로고
    • Calmodulin: a prototypical calcium sensor
    • Chin D., Means A.R. Calmodulin: a prototypical calcium sensor. Trends Cell. Biol. 2000, 10:322-328.
    • (2000) Trends Cell. Biol. , vol.10 , pp. 322-328
    • Chin, D.1    Means, A.R.2
  • 16
    • 77954957023 scopus 로고    scopus 로고
    • Allograft inflammatory factor-1 in disk abalone (Haliotis discus discus): molecular cloning, transcriptional regulation against immune challenge and tissue injury
    • De Zoysa M., Nikapitiya C., Kim Y., Oh C., Kang D.H., Whang I., Kim S.J., Lee J.S., Choi C.Y., Lee J. Allograft inflammatory factor-1 in disk abalone (Haliotis discus discus): molecular cloning, transcriptional regulation against immune challenge and tissue injury. Fish Shellfish Immunol. 2010, 29:319-326.
    • (2010) Fish Shellfish Immunol. , vol.29 , pp. 319-326
    • De Zoysa, M.1    Nikapitiya, C.2    Kim, Y.3    Oh, C.4    Kang, D.H.5    Whang, I.6    Kim, S.J.7    Lee, J.S.8    Choi, C.Y.9    Lee, J.10
  • 17
    • 0037070630 scopus 로고    scopus 로고
    • The allograft inflammatory factor-1 family of proteins
    • Deininger M.H., Meyermann R., Schluesener H.J. The allograft inflammatory factor-1 family of proteins. FEBS J. 2002, 514:115-121.
    • (2002) FEBS J. , vol.514 , pp. 115-121
    • Deininger, M.H.1    Meyermann, R.2    Schluesener, H.J.3
  • 18
    • 85190485357 scopus 로고    scopus 로고
    • Cytoskeleton
    • Higher Education Press, Beijing, Z.H. Di, X.Z. Wang, M.X. Ding (Eds.)
    • Di Z.H. Cytoskeleton. Cell Biology 2003, 318-355. Higher Education Press, Beijing. Z.H. Di, X.Z. Wang, M.X. Ding (Eds.).
    • (2003) Cell Biology , pp. 318-355
    • Di, Z.H.1
  • 19
    • 33645234384 scopus 로고    scopus 로고
    • Protein carbonilation 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 P.C., Romeo M., O'Halloran J., van Pelt F., O'Brien N., Sheehan D. Protein carbonilation and heat shock response in Ruditapes decussatus following p,p′-dichlorodiphenyldichloroethylene (DDE) exposure: a proteomic approach reveals that DDE causes oxidative stress. Aquat. Toxicol. 2006, 77:11-18.
    • (2006) Aquat. Toxicol. , 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
  • 22
    • 0001786337 scopus 로고
    • Structure and functions of oyster haemocytes
    • Springer-Verlag, Berlin, Heidelberg, M. Brehélin (Ed.)
    • Fisher W.S. Structure and functions of oyster haemocytes. Immunity in Invertebrates 1986, 25-35. Springer-Verlag, Berlin, Heidelberg. M. Brehélin (Ed.).
    • (1986) Immunity in Invertebrates , pp. 25-35
    • Fisher, W.S.1
  • 23
    • 34547663446 scopus 로고    scopus 로고
    • Impact of brown ring disease on the energy budget of the Manila clam Ruditapes philippinarum
    • Flye-Sainte-Marie J., Pouvreau S., Paillard C., Jean F. Impact of brown ring disease on the energy budget of the Manila clam Ruditapes philippinarum. J. Exp. Mar. Biol. Ecol. 2007, 349:378-389.
    • (2007) J. Exp. Mar. Biol. Ecol. , vol.349 , pp. 378-389
    • Flye-Sainte-Marie, J.1    Pouvreau, S.2    Paillard, C.3    Jean, F.4
  • 24
    • 0027959156 scopus 로고
    • Protein disulphide isomerase: building bridges in protein folding
    • Freedman R.B., Hirst T.R., Tuite M.F. Protein disulphide isomerase: building bridges in protein folding. Trends Biochem. Sci. 1994, 19:331-336.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 331-336
    • Freedman, R.B.1    Hirst, T.R.2    Tuite, M.F.3
  • 25
    • 22044457595 scopus 로고    scopus 로고
    • Monoclonal antibodies developed for detection of an epizootic virus associated with mass mortalities of cultured scallop Chlamys farreri
    • Fu C.L., Song W.B., Li Y. Monoclonal antibodies developed for detection of an epizootic virus associated with mass mortalities of cultured scallop Chlamys farreri. Dis. Aquat. Organ. 2005, 65:17-22.
    • (2005) Dis. Aquat. Organ. , vol.65 , pp. 17-22
    • Fu, C.L.1    Song, W.B.2    Li, Y.3
  • 26
    • 0037131035 scopus 로고    scopus 로고
    • Growth, mortality, pathological conditions and protein expression of Mytilus edulis and M. galloprovincialis crosses cultured in the Ríade Arousa (NW of Spain)
    • Fuentes J., López J.L., Mosquera E., Vázquez J., Villalba A., álvarez G. Growth, mortality, pathological conditions and protein expression of Mytilus edulis and M. galloprovincialis crosses cultured in the Ríade Arousa (NW of Spain). Aquaculture 2002, 213:233-251.
    • (2002) Aquaculture , vol.213 , pp. 233-251
    • Fuentes, J.1    López, J.L.2    Mosquera, E.3    Vázquez, J.4    Villalba, A.5    álvarez, G.6
  • 27
    • 40149107404 scopus 로고    scopus 로고
    • Molecular cloning, characterization and expression of heat shock protein 90 gene in the haemocytes of bay scallop Argopecten irradians
    • Gao Q., Zhao J.M., Song L.S., Qiu L.M., Yu Y.D., Zhang H., Ni D.J. Molecular cloning, characterization and expression of heat shock protein 90 gene in the haemocytes of bay scallop Argopecten irradians. Fish Shellfish Immunol. 2008, 24:379-385.
    • (2008) Fish Shellfish Immunol. , vol.24 , pp. 379-385
    • Gao, Q.1    Zhao, J.M.2    Song, L.S.3    Qiu, L.M.4    Yu, Y.D.5    Zhang, H.6    Ni, D.J.7
  • 29
    • 0032926319 scopus 로고    scopus 로고
    • Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts
    • Göthel S.F., Marahiel M.A. Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts. Cell. Mol. Life Sci. 1999, 55:423-436.
    • (1999) Cell. Mol. Life Sci. , vol.55 , pp. 423-436
    • Göthel, S.F.1    Marahiel, M.A.2
  • 30
    • 77956294288 scopus 로고    scopus 로고
    • Characterization of myosin light chain in shrimp hemocytic phagocytosis
    • Han F., Wang Z.Y., Wang X.Q. Characterization of myosin light chain in shrimp hemocytic phagocytosis. Fish Shellfish Immunol. 2010, 29:875-883.
    • (2010) Fish Shellfish Immunol. , vol.29 , pp. 875-883
    • Han, F.1    Wang, Z.Y.2    Wang, X.Q.3
  • 32
    • 32644488871 scopus 로고
    • The cause and its prevention of mortalities in cultured scallop Chlamys farreri
    • Liu Z.C., Wu J.Q., Jin F.J. The cause and its prevention of mortalities in cultured scallop Chlamys farreri. Mar. Sci. 1992, 6:9-10.
    • (1992) Mar. Sci. , vol.6 , pp. 9-10
    • Liu, Z.C.1    Wu, J.Q.2    Jin, F.J.3
  • 33
    • 0035915521 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis of Mytilus galloprovincialis: differences in protein expression between intertidal and cultured mussels
    • López J.L., Mosquera E., Fuentes J., Marina A., Vázquez J., Alvarez G. Two-dimensional gel electrophoresis of Mytilus galloprovincialis: differences in protein expression between intertidal and cultured mussels. Mar. Ecol. Prog. Ser. 2001, 224:149-156.
    • (2001) Mar. Ecol. Prog. Ser. , vol.224 , pp. 149-156
    • López, J.L.1    Mosquera, E.2    Fuentes, J.3    Marina, A.4    Vázquez, J.5    Alvarez, G.6
  • 34
    • 24144470553 scopus 로고    scopus 로고
    • Proteomic approach to probe for larval proteins of the mussel Mytilus galloprovincialis
    • López J.L., Abalde S.L., Fuentes J. Proteomic approach to probe for larval proteins of the mussel Mytilus galloprovincialis. Mar. Biotechnol. 2005, 7:396-404.
    • (2005) Mar. Biotechnol. , vol.7 , pp. 396-404
    • López, J.L.1    Abalde, S.L.2    Fuentes, J.3
  • 35
    • 34447299940 scopus 로고    scopus 로고
    • Characterization and expression analysis of aralichthys olivaceus voltage-dependent anion channel (VDAC) gene in response to virus infection
    • Lü A.J., Dong C.W., Du C.S., Zhang Q.Y. Characterization and expression analysis of aralichthys olivaceus voltage-dependent anion channel (VDAC) gene in response to virus infection. Fish Shellfish Immunol. 2007, 23:601-613.
    • (2007) Fish Shellfish Immunol. , vol.23 , pp. 601-613
    • Lü, A.J.1    Dong, C.W.2    Du, C.S.3    Zhang, Q.Y.4
  • 36
    • 3242788127 scopus 로고    scopus 로고
    • Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes
    • Mackintosh C. Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes. Biochem. J. 2004, 381:329-342.
    • (2004) Biochem. J. , vol.381 , pp. 329-342
    • Mackintosh, C.1
  • 37
    • 0035067475 scopus 로고    scopus 로고
    • Phagocytosis and the actin cytoskeleton
    • May R.C., Machesky L.M. Phagocytosis and the actin cytoskeleton. J. Cell. Sci. 2001, 114:1061-1077.
    • (2001) J. Cell. Sci. , vol.114 , pp. 1061-1077
    • May, R.C.1    Machesky, L.M.2
  • 38
    • 34147139944 scopus 로고    scopus 로고
    • Peroxisomal proteomic approach for protein profiling in blue mussels (Mytilus edulis) exposed to crude oil
    • Mi J., Apraiz I., Cristóbal S. Peroxisomal proteomic approach for protein profiling in blue mussels (Mytilus edulis) exposed to crude oil. Biomarkers 2007, 12:47-60.
    • (2007) Biomarkers , vol.12 , pp. 47-60
    • Mi, J.1    Apraiz, I.2    Cristóbal, S.3
  • 39
    • 0037791750 scopus 로고    scopus 로고
    • Genetic variability of the marine mussel Mytilus galloprovincialis assessed using two-dimensional electrophoresis
    • Mosquera E., López J.L., álvarez G. Genetic variability of the marine mussel Mytilus galloprovincialis assessed using two-dimensional electrophoresis. Heredity 2003, 90:432-442.
    • (2003) Heredity , vol.90 , pp. 432-442
    • Mosquera, E.1    López, J.L.2    álvarez, G.3
  • 41
    • 0025965545 scopus 로고
    • Cloning and characterization of a pair of novel genes that regulate production of extracellular enzymes in Bacillus subtilis
    • Pang A.S., Nathoo S., Wong S.L. Cloning and characterization of a pair of novel genes that regulate production of extracellular enzymes in Bacillus subtilis. J. Bacteriol. 1991, 173:46-54.
    • (1991) J. Bacteriol. , vol.173 , pp. 46-54
    • Pang, A.S.1    Nathoo, S.2    Wong, S.L.3
  • 42
    • 0000233354 scopus 로고    scopus 로고
    • The effects of Perkinsus marinus infection on physiological processes in the eastern oyster, Crassostrea virginica
    • Paynter K.T. The effects of Perkinsus marinus infection on physiological processes in the eastern oyster, Crassostrea virginica. J. Shellfish Res. 1996, 15:119-125.
    • (1996) J. Shellfish Res. , vol.15 , pp. 119-125
    • Paynter, K.T.1
  • 43
    • 0031127256 scopus 로고    scopus 로고
    • Proteome analysis: from protein characterization to biological function
    • Pennington S.R. Proteome analysis: from protein characterization to biological function. Trends Cell. Biol. 1997, 7:168-173.
    • (1997) Trends Cell. Biol. , vol.7 , pp. 168-173
    • Pennington, S.R.1
  • 44
    • 85190485166 scopus 로고    scopus 로고
    • Detection methods, sequence of the complete genome of acute viral necrobiotic virus isolated from scallop Chlamys farreri. Ocean University of China Doctor Thesis, Qingdao.
    • Ren, W.C., 2009. Detection methods, sequence of the complete genome of acute viral necrobiotic virus isolated from scallop Chlamys farreri. Ocean University of China Doctor Thesis, Qingdao.
    • (2009)
    • Ren, W.C.1
  • 45
    • 80053317751 scopus 로고    scopus 로고
    • Development and application of a FQ-PCR assay for detection of Chlamys farreri acute viral necrobiotic virus
    • Ren W.C., Wang C.M., Sun S.C., Cai Y.Y., Li Y., Yu Z.A. Development and application of a FQ-PCR assay for detection of Chlamys farreri acute viral necrobiotic virus. J. Fish Sci. China 2009, 16:564-571.
    • (2009) J. Fish Sci. China , vol.16 , pp. 564-571
    • Ren, W.C.1    Wang, C.M.2    Sun, S.C.3    Cai, Y.Y.4    Li, Y.5    Yu, Z.A.6
  • 46
    • 0033106065 scopus 로고    scopus 로고
    • Defense mechanisms and disease prevention in farmed marine invertebrates
    • Roch P. Defense mechanisms and disease prevention in farmed marine invertebrates. Aquaculture 1999, 172:125-145.
    • (1999) Aquaculture , vol.172 , pp. 125-145
    • Roch, P.1
  • 48
    • 2542427376 scopus 로고    scopus 로고
    • New research progress on massive mortality of cultured scallop Chlamys farreri
    • Song W.B., Wang C.M., Wang X.H., Li Y., Li J. New research progress on massive mortality of cultured scallop Chlamys farreri. Mar. Sci. 2001, 25:23-26.
    • (2001) Mar. Sci. , vol.25 , pp. 23-26
    • Song, W.B.1    Wang, C.M.2    Wang, X.H.3    Li, Y.4    Li, J.5
  • 49
    • 33745642911 scopus 로고    scopus 로고
    • The cDNA cloning and mRNA expression of heat shock protein 70 gene in the haemocytes of bay scallop (Argopecten irradians, Lamarck 1819) responding to bacteria challenge and naphthalin stress
    • Song L.S., Wu L.T., Ni D.J., Chang Y.Q. The cDNA cloning and mRNA expression of heat shock protein 70 gene in the haemocytes of bay scallop (Argopecten irradians, Lamarck 1819) responding to bacteria challenge and naphthalin stress. Fish Shellfish Immunol. 2006, 21:335-345.
    • (2006) Fish Shellfish Immunol. , vol.21 , pp. 335-345
    • Song, L.S.1    Wu, L.T.2    Ni, D.J.3    Chang, Y.Q.4
  • 50
    • 27644471767 scopus 로고    scopus 로고
    • The cDNA cloning and mRNA expression of a potential selenium-binding protein gene in the scallop Chlamys farreri
    • Song L.S., Zou H.B., Chang Y.Q., Xu W., Wu L.T. The cDNA cloning and mRNA expression of a potential selenium-binding protein gene in the scallop Chlamys farreri. Dev. Comp. Immunol. 2006, 30:265-273.
    • (2006) Dev. Comp. Immunol. , vol.30 , pp. 265-273
    • Song, L.S.1    Zou, H.B.2    Chang, Y.Q.3    Xu, W.4    Wu, L.T.5
  • 51
    • 0018895694 scopus 로고
    • Distribution of actin-binding protein and myosin in macrophages during spreading and phagocytosis
    • Stendahl O.I., Hartwig J.H., Brotschi E.A., Stossel T.P. Distribution of actin-binding protein and myosin in macrophages during spreading and phagocytosis. J. Cell. Biol. 1980, 84:215-224.
    • (1980) J. Cell. Biol. , vol.84 , pp. 215-224
    • Stendahl, O.I.1    Hartwig, J.H.2    Brotschi, E.A.3    Stossel, T.P.4
  • 53
    • 77955029360 scopus 로고    scopus 로고
    • Physiological and immune responses of zhikong scallop Chlamys farreri to the acute viral necrobiotic virus infection
    • Tang B.J., Liu B.Z., Wang X.M., Yue X., Xiang J.H. Physiological and immune responses of zhikong scallop Chlamys farreri to the acute viral necrobiotic virus infection. Fish Shellfish Immunol. 2010, 29:42-48.
    • (2010) Fish Shellfish Immunol. , vol.29 , pp. 42-48
    • Tang, B.J.1    Liu, B.Z.2    Wang, X.M.3    Yue, X.4    Xiang, J.H.5
  • 54
    • 0842266604 scopus 로고    scopus 로고
    • Oxidative protein folding in eukaryotes: mechanisms and consequences
    • Tu B.P., Weissman J.S. Oxidative protein folding in eukaryotes: mechanisms and consequences. J. Cell. Biol. 2004, 164:341-346.
    • (2004) J. Cell. Biol. , vol.164 , pp. 341-346
    • Tu, B.P.1    Weissman, J.S.2
  • 55
    • 0029664416 scopus 로고    scopus 로고
    • Allograft inflammatory factor-1, a cytokine-responsive macrophage molecule expressed in trans-planted human hearts
    • Utans U., Quist W.C., McManus B.M., Wilson J.E., Arceci R.J. Allograft inflammatory factor-1, a cytokine-responsive macrophage molecule expressed in trans-planted human hearts. Transplant 1996, 61:1387-1392.
    • (1996) Transplant , vol.61 , pp. 1387-1392
    • Utans, U.1    Quist, W.C.2    McManus, B.M.3    Wilson, J.E.4    Arceci, R.J.5
  • 56
    • 0019435848 scopus 로고
    • Distribution of actin-binding protein and myosin in polymorphonuclear leukocytes during locomotion and phagocytosis
    • Valerius N.H., Stendahl O., Hartwig J.H., Stossel T.P. Distribution of actin-binding protein and myosin in polymorphonuclear leukocytes during locomotion and phagocytosis. Cell 1981, 24:195-202.
    • (1981) Cell , vol.24 , pp. 195-202
    • Valerius, N.H.1    Stendahl, O.2    Hartwig, J.H.3    Stossel, T.P.4
  • 57
    • 0034788964 scopus 로고    scopus 로고
    • 14-3-3 proteins: key regulators of cell division, signaling and apoptosis
    • van Hemert M.J., Steensma H.Y., van Heusden G.P. 14-3-3 proteins: key regulators of cell division, signaling and apoptosis. Bioassays 2001, 23:936-946.
    • (2001) Bioassays , vol.23 , pp. 936-946
    • van Hemert, M.J.1    Steensma, H.Y.2    van Heusden, G.P.3
  • 58
    • 32644474747 scopus 로고    scopus 로고
    • Purification and ultrastructure of a spherical virus in cultured scallop Chlamys farreri
    • Wang C.M., Wang X.H., Song X.L., Huang J., Song W.B. Purification and ultrastructure of a spherical virus in cultured scallop Chlamys farreri. J. Fish China 2002, 26:180-184.
    • (2002) J. Fish China , vol.26 , pp. 180-184
    • Wang, C.M.1    Wang, X.H.2    Song, X.L.3    Huang, J.4    Song, W.B.5
  • 59
    • 2542487226 scopus 로고    scopus 로고
    • Epidemiological study on massive death of the cultured scallop Chlamys farreri in the Jiaozhou Bay
    • Wang X.H., Wang C.M., Li J., Wang X.H., Zheng G.L., Hu X.Z., Gong J., Song W.B. Epidemiological study on massive death of the cultured scallop Chlamys farreri in the Jiaozhou Bay. J. Fish China 2002, 26:149-155.
    • (2002) J. Fish China , vol.26 , pp. 149-155
    • Wang, X.H.1    Wang, C.M.2    Li, J.3    Wang, X.H.4    Zheng, G.L.5    Hu, X.Z.6    Gong, J.7    Song, W.B.8
  • 60
    • 0142154798 scopus 로고    scopus 로고
    • Preparation of polyclonal antibody of AVND virus and analysis by ELISA technique
    • Wang X.H., He G.Z., Li Y., Wang C.M., Song W.B. Preparation of polyclonal antibody of AVND virus and analysis by ELISA technique. High Technol. Lett. 2003, 9:84-88.
    • (2003) High Technol. Lett. , vol.9 , pp. 84-88
    • Wang, X.H.1    He, G.Z.2    Li, Y.3    Wang, C.M.4    Song, W.B.5
  • 62
    • 80051957652 scopus 로고    scopus 로고
    • Pathological observation andanalysis of acute viral necrobiotic disease in Chlamys farreri
    • Wang C.M., Liu Y.J., Wang X.H., Li Y. Pathological observation andanalysis of acute viral necrobiotic disease in Chlamys farreri. Mar. Fish Res. 2007, 28:1-8.
    • (2007) Mar. Fish Res. , vol.28 , pp. 1-8
    • Wang, C.M.1    Liu, Y.J.2    Wang, X.H.3    Li, Y.4
  • 63
    • 33947732449 scopus 로고    scopus 로고
    • Protein expression profiling of the shrimp cellular response to white spot syndrome virus infection
    • Wang H.C., Wang H.C., Leu J.H., Kou G.H., Wang A.H.J., Lo C.F. Protein expression profiling of the shrimp cellular response to white spot syndrome virus infection. Dev. Comp. Immunol. 2007, 31:672-686.
    • (2007) Dev. Comp. Immunol. , vol.31 , pp. 672-686
    • Wang, H.C.1    Wang, H.C.2    Leu, J.H.3    Kou, G.H.4    Wang, A.H.J.5    Lo, C.F.6
  • 64
    • 77955058678 scopus 로고    scopus 로고
    • The Marsupenaeus japonicus voltage-dependent anion channel (MjVDAC) protein is involved in white spot syndrome virus (WSSV) pathogenesis
    • Wang K.C.H.C., Kondo H., Hirono I., Aoki T. The Marsupenaeus japonicus voltage-dependent anion channel (MjVDAC) protein is involved in white spot syndrome virus (WSSV) pathogenesis. Fish Shellfish Immunol. 2010, 29:94-103.
    • (2010) Fish Shellfish Immunol. , vol.29 , pp. 94-103
    • Wang, K.C.H.C.1    Kondo, H.2    Hirono, I.3    Aoki, T.4
  • 65
    • 0035168274 scopus 로고    scopus 로고
    • Allograft in ammatory factor-1 augments production of interleukin-6-10 and -12 by a mouse macrophage line
    • Watano K., Iwabuchi K., Fujii S., Ishimori N., Mitsuhashi S., Ato M. Allograft in ammatory factor-1 augments production of interleukin-6-10 and -12 by a mouse macrophage line. Immunology 2001, 104:307-316.
    • (2001) Immunology , vol.104 , pp. 307-316
    • Watano, K.1    Iwabuchi, K.2    Fujii, S.3    Ishimori, N.4    Mitsuhashi, S.5    Ato, M.6
  • 66
    • 55949101724 scopus 로고    scopus 로고
    • Variations of enzyme activities in the haemocytes of scallop Chlamys farreri after infection with the acute virus necrobiotic virus (AVNV)
    • Xing J., Lin T.T., Zhan W.B. Variations of enzyme activities in the haemocytes of scallop Chlamys farreri after infection with the acute virus necrobiotic virus (AVNV). Fish Shellfish Immunol. 2008, 25:847-852.
    • (2008) Fish Shellfish Immunol. , vol.25 , pp. 847-852
    • Xing, J.1    Lin, T.T.2    Zhan, W.B.3
  • 68
    • 77954957948 scopus 로고    scopus 로고
    • Proteomic analysis of differentially expressed proteins in lymphoid organ of Fenneropenaeus chinensis response to Vibrio anguillarum stimulation
    • Zhang J.K., Li F.H., Jiang H., Yu Y., Liu C.Z., Li S.H., Wang B., Xiang J.H. Proteomic analysis of differentially expressed proteins in lymphoid organ of Fenneropenaeus chinensis response to Vibrio anguillarum stimulation. Fish Shellfish Immunol. 2010, 29:186-194.
    • (2010) Fish Shellfish Immunol. , vol.29 , pp. 186-194
    • Zhang, J.K.1    Li, F.H.2    Jiang, H.3    Yu, Y.4    Liu, C.Z.5    Li, S.H.6    Wang, B.7    Xiang, J.H.8
  • 69
    • 78650700819 scopus 로고    scopus 로고
    • Cloning and characterization of allograft inflammatory factor-1 (AIF-1) from manila clam Venerupis philippinarum
    • Zhang L., Zhao J.M., Li C.H., Su X.R., Chen A.Q., Li T.W., Qin S. Cloning and characterization of allograft inflammatory factor-1 (AIF-1) from manila clam Venerupis philippinarum. Fish Shellfish Immunol. 2011, 30:148-153.
    • (2011) Fish Shellfish Immunol. , vol.30 , pp. 148-153
    • Zhang, L.1    Zhao, J.M.2    Li, C.H.3    Su, X.R.4    Chen, A.Q.5    Li, T.W.6    Qin, S.7
  • 70
    • 1442327526 scopus 로고    scopus 로고
    • Essential role of the voltage-dependent anion channel (VDAC) in mitochondrial permeability transition pore opening and cytochrome c release induced by arsenic trioxide
    • Zheng Y., Shi Y., Tian C., Jiang C., Jin H., Chen J., Almasan A., Tang H., Chen Q. Essential role of the voltage-dependent anion channel (VDAC) in mitochondrial permeability transition pore opening and cytochrome c release induced by arsenic trioxide. Oncogene 2004, 23:1239-1247.
    • (2004) Oncogene , vol.23 , pp. 1239-1247
    • Zheng, Y.1    Shi, Y.2    Tian, C.3    Jiang, C.4    Jin, H.5    Chen, J.6    Almasan, A.7    Tang, H.8    Chen, Q.9
  • 71
    • 77949491169 scopus 로고    scopus 로고
    • A proteomics based approach to assessing the toxicity of bisphenol A and diallyl phthalate to the abalone (Haliotis diversicolor supertexta)
    • Zhou J., Cai Z.H., Li L., Gao Y.F., Hutchinson T.H. A proteomics based approach to assessing the toxicity of bisphenol A and diallyl phthalate to the abalone (Haliotis diversicolor supertexta). Chemosphere 2010, 79:595-604.
    • (2010) Chemosphere , vol.79 , pp. 595-604
    • Zhou, J.1    Cai, Z.H.2    Li, L.3    Gao, Y.F.4    Hutchinson, T.H.5


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