메뉴 건너뛰기




Volumn 32, Issue 1, 2012, Pages 161-169

Effect of infectious hypodermal and haematopoietic necrosis virus (IHHNV) infection on caspase 3c expression and activity in freshwater prawn Macrobrachium rosenbergii

Author keywords

Caspase; Gene expression; Hydrolyzing activity; IHHNV; Macrobrachium rosenbergii

Indexed keywords

ESCHERICHIA COLI; INFECTIOUS HYPODERMAL AND HEMATOPOIETIC NECROSIS VIRUS; MACROBRACHIUM ROSENBERGII; PROKARYOTA;

EID: 84858332370     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2011.11.006     Document Type: Article
Times cited : (36)

References (55)
  • 1
    • 77949912133 scopus 로고    scopus 로고
    • First molecular cloning of a molluscan caspase from variously colored abalone (Haliotis diversicolor) and gene expression analysis with bacterial challenge
    • Huang W.B., Ren H.L., Gopalakrishnan S., Xu D.D., Qiao K., Wang K.J. First molecular cloning of a molluscan caspase from variously colored abalone (Haliotis diversicolor) and gene expression analysis with bacterial challenge. Fish Shellfish Immunol 2010, 28:587-595.
    • (2010) Fish Shellfish Immunol , vol.28 , pp. 587-595
    • Huang, W.B.1    Ren, H.L.2    Gopalakrishnan, S.3    Xu, D.D.4    Qiao, K.5    Wang, K.J.6
  • 2
    • 0030947095 scopus 로고    scopus 로고
    • Programmed cell death in animal development
    • Jacobson M.D., Weil M., Raff M.C. Programmed cell death in animal development. Cell 1997, 88:347-354.
    • (1997) Cell , vol.88 , pp. 347-354
    • Jacobson, M.D.1    Weil, M.2    Raff, M.C.3
  • 3
    • 32344434220 scopus 로고    scopus 로고
    • Molecular cloning and expression of caspase from white shrimp Penaeus merguiensis
    • Phongdara A., Wanna W., Chotigeat W. Molecular cloning and expression of caspase from white shrimp Penaeus merguiensis. Aquaculture 2006, 252:114-120.
    • (2006) Aquaculture , vol.252 , pp. 114-120
    • Phongdara, A.1    Wanna, W.2    Chotigeat, W.3
  • 4
    • 33748785440 scopus 로고    scopus 로고
    • Molecular cloning and characterisation of sea bass (Dicentrarchus labrax L.) caspase-3 gene
    • Reis M.I.R., Diana S., Nascimento Vale A.D., Silva M.T., Nuno M.S., Santos D. Molecular cloning and characterisation of sea bass (Dicentrarchus labrax L.) caspase-3 gene. Mol Immunol 2007, 44:774-783.
    • (2007) Mol Immunol , vol.44 , pp. 774-783
    • Reis, M.I.R.1    Diana, S.2    Nascimento Vale, A.D.3    Silva, M.T.4    Nuno, M.S.5    Santos, D.6
  • 6
    • 0035123705 scopus 로고    scopus 로고
    • Cloning and sequencing of caspase 6 in rainbow trout, Oncorhynchus mykiss, and analysis of its expression under conditions known to induce apoptosis
    • Laing K.J., Hollanda J., Bonillaa S., Cunninghamb C., Secombes C.J. Cloning and sequencing of caspase 6 in rainbow trout, Oncorhynchus mykiss, and analysis of its expression under conditions known to induce apoptosis. Dev Comp Immunol 2001, 25:303-312.
    • (2001) Dev Comp Immunol , vol.25 , pp. 303-312
    • Laing, K.J.1    Hollanda, J.2    Bonillaa, S.3    Cunninghamb, C.4    Secombes, C.J.5
  • 7
    • 0030931876 scopus 로고    scopus 로고
    • Caspases: the executioners of apoptosis
    • Cohen G.M. Caspases: the executioners of apoptosis. Biochem J 1997, 326:1-6.
    • (1997) Biochem J , vol.326 , pp. 1-6
    • Cohen, G.M.1
  • 10
    • 0036372121 scopus 로고    scopus 로고
    • Caspases: their role in apoptosis and other physiological processes as revealed by knock-out studies
    • Sadowski-Debbing K., Coy J.F., Mier W., Hug H., Los M. Caspases: their role in apoptosis and other physiological processes as revealed by knock-out studies. Arch Immunol Therapiae Expt 2002, 50:19-34.
    • (2002) Arch Immunol Therapiae Expt , vol.50 , pp. 19-34
    • Sadowski-Debbing, K.1    Coy, J.F.2    Mier, W.3    Hug, H.4    Los, M.5
  • 11
    • 0344234438 scopus 로고    scopus 로고
    • Apoptosis in zebrafish development
    • Yamashita M. Apoptosis in zebrafish development. Comp Biochem Physiol Part B 2003, 136:731-742.
    • (2003) Comp Biochem Physiol Part B , vol.136 , pp. 731-742
    • Yamashita, M.1
  • 12
    • 0242361218 scopus 로고    scopus 로고
    • Homocysteine-induced changes in brain membrane composition correlate with increased brain caspase-3 activities and reduced chick embryo viability
    • Robert R.M., Christina M.L., Emily E.P., Kevin D.B. Homocysteine-induced changes in brain membrane composition correlate with increased brain caspase-3 activities and reduced chick embryo viability. Comp Biochem Physiol Part B 2003, 136:521-532.
    • (2003) Comp Biochem Physiol Part B , vol.136 , pp. 521-532
    • Robert, R.M.1    Christina, M.L.2    Emily, E.P.3    Kevin, D.B.4
  • 13
    • 20544450481 scopus 로고    scopus 로고
    • Hyperglycemia-induced changes in hepatic membrane fatty acid composition correlate with increased caspase-3 activities and reduced chick embryo viability
    • Robert R.M., Allison L.B., Megan E.L., James D.H. Hyperglycemia-induced changes in hepatic membrane fatty acid composition correlate with increased caspase-3 activities and reduced chick embryo viability. Comp Biochem Physiol Part B 2005, 141:323-330.
    • (2005) Comp Biochem Physiol Part B , vol.141 , pp. 323-330
    • Robert, R.M.1    Allison, L.B.2    Megan, E.L.3    James, D.H.4
  • 14
    • 33646525220 scopus 로고    scopus 로고
    • Cloning and characterization of the executioner caspases 3, 6, 7 and Hsp70 in hyperthermic Atlantic salmon (Salmo salar) embryos
    • Takle H., McLeod A., Andersen O. Cloning and characterization of the executioner caspases 3, 6, 7 and Hsp70 in hyperthermic Atlantic salmon (Salmo salar) embryos. Comp Biochem Physiol Part B 2006, 144:188-198.
    • (2006) Comp Biochem Physiol Part B , vol.144 , pp. 188-198
    • Takle, H.1    McLeod, A.2    Andersen, O.3
  • 16
    • 33751258003 scopus 로고    scopus 로고
    • First molecular cloning and characterisation of caspase-9 gene in fish and its involvement in a gram negative septicaemia
    • Reis M.I.R., Vale A.D., Pinto C., Nascimento Diana S., Ramos C.C., et al. First molecular cloning and characterisation of caspase-9 gene in fish and its involvement in a gram negative septicaemia. Mol Immunol 2007, 44:1754-1764.
    • (2007) Mol Immunol , vol.44 , pp. 1754-1764
    • Reis, M.I.R.1    Vale, A.D.2    Pinto, C.3    Nascimento, D.S.4    Ramos, C.C.5
  • 17
    • 79952185199 scopus 로고    scopus 로고
    • Molecular cloning and characterization of caspase-3 in large yellow croaker (Pseudosciaena crocea)
    • Li M., Ding Y., Mu Y., Ao J., Chen X. Molecular cloning and characterization of caspase-3 in large yellow croaker (Pseudosciaena crocea). Fish Shellfish Immunol 2011, 30:910-916.
    • (2011) Fish Shellfish Immunol , vol.30 , pp. 910-916
    • Li, M.1    Ding, Y.2    Mu, Y.3    Ao, J.4    Chen, X.5
  • 18
    • 54849442293 scopus 로고    scopus 로고
    • The effect of Vibrio lginolyticus infection on caspase-3 expression and activity in white shrimp Litopenaeus vannamei
    • Chang C.C., Yeh M.S., Lin H.K., Cheng W. The effect of Vibrio lginolyticus infection on caspase-3 expression and activity in white shrimp Litopenaeus vannamei. Fish Shellfish Immunol 2008, 25:672-678.
    • (2008) Fish Shellfish Immunol , vol.25 , pp. 672-678
    • Chang, C.C.1    Yeh, M.S.2    Lin, H.K.3    Cheng, W.4
  • 19
    • 77955057057 scopus 로고    scopus 로고
    • Molecular cloning of sea bass (Dicentrarchus labrax L.) caspase-8 gene and its involvement in Photobacterium damselae ssp. piscicida triggered apoptosis
    • Reis M.I.R., Costa-Ramos C., Vale A.D., Nuno M.S., Santos D. Molecular cloning of sea bass (Dicentrarchus labrax L.) caspase-8 gene and its involvement in Photobacterium damselae ssp. piscicida triggered apoptosis. Fish Shellfish Immunol 2010, 29:58-65.
    • (2010) Fish Shellfish Immunol , vol.29 , pp. 58-65
    • Reis, M.I.R.1    Costa-Ramos, C.2    Vale, A.D.3    Nuno, M.S.4    Santos, D.5
  • 20
    • 35649028361 scopus 로고    scopus 로고
    • Molecular cloning, expression, and functional analysis of caspase-10 from Japanese flounder Paralichthys olivaceus
    • Kurobe T., Hirono I., Kondo H., Yamashita M., Aoki T. Molecular cloning, expression, and functional analysis of caspase-10 from Japanese flounder Paralichthys olivaceus. Fish Shellfish Immunol 2007, 23:1266-1274.
    • (2007) Fish Shellfish Immunol , vol.23 , pp. 1266-1274
    • Kurobe, T.1    Hirono, I.2    Kondo, H.3    Yamashita, M.4    Aoki, T.5
  • 21
    • 38649105206 scopus 로고    scopus 로고
    • Penaeus monodon caspase is targeted by a white spot syndrome virus anti-apoptosis protein
    • Leu J.H., Wang H.C., Kou G.H., Loa C.F. Penaeus monodon caspase is targeted by a white spot syndrome virus anti-apoptosis protein. Dev Comp Immunol 2008, 32:476-486.
    • (2008) Dev Comp Immunol , vol.32 , pp. 476-486
    • Leu, J.H.1    Wang, H.C.2    Kou, G.H.3    Loa, C.F.4
  • 22
    • 34447266005 scopus 로고    scopus 로고
    • Cloning and characterization of a caspase gene from black tiger shrimp (Penaeus monodon) infected with white spot syndrome virus (WSSV)
    • Wongprasert K., Sangsuriya P., Phongdara A., Senapin S. Cloning and characterization of a caspase gene from black tiger shrimp (Penaeus monodon) infected with white spot syndrome virus (WSSV). J Biotech 2007, 131:9-19.
    • (2007) J Biotech , vol.131 , pp. 9-19
    • Wongprasert, K.1    Sangsuriya, P.2    Phongdara, A.3    Senapin, S.4
  • 23
    • 78650705528 scopus 로고    scopus 로고
    • Molecular cloning, characterization and expression analysis of two apoptosis genes, caspase and nm23, involved in the antibacterial response in Chinese mitten crab, Eriocheir sinensis
    • Jin X.K., Li W.W., He L., Lu W., Chen L.L., Wang Y., et al. Molecular cloning, characterization and expression analysis of two apoptosis genes, caspase and nm23, involved in the antibacterial response in Chinese mitten crab, Eriocheir sinensis. Fish Shellfish Immunol 2011, 30:263-272.
    • (2011) Fish Shellfish Immunol , vol.30 , pp. 263-272
    • Jin, X.K.1    Li, W.W.2    He, L.3    Lu, W.4    Chen, L.L.5    Wang, Y.6
  • 24
    • 73249119069 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of caspase 9 in large yellow croaker (Pseudosciaena crocea)
    • Mu Y., Xiao X., Zhang J., Ao J., Chen X. Molecular cloning and functional characterization of caspase 9 in large yellow croaker (Pseudosciaena crocea). Dev Comp Immunol 2010, 34:300-307.
    • (2010) Dev Comp Immunol , vol.34 , pp. 300-307
    • Mu, Y.1    Xiao, X.2    Zhang, J.3    Ao, J.4    Chen, X.5
  • 25
    • 0025624530 scopus 로고
    • Freshwater prawn culture: a review
    • New M.B. Freshwater prawn culture: a review. Aquaculture 1990, 88:99-143.
    • (1990) Aquaculture , vol.88 , pp. 99-143
    • New, M.B.1
  • 26
    • 0033505308 scopus 로고
    • The penaeid shrimp viruses TSV, IHHNV, WSSV, and YHV current status in the Americas, available diagnostic methods, and management strategies
    • Lightner V.D. The penaeid shrimp viruses TSV, IHHNV, WSSV, and YHV current status in the Americas, available diagnostic methods, and management strategies. J Appl Aquacult 1990, 9:27-52.
    • (1990) J Appl Aquacult , vol.9 , pp. 27-52
    • Lightner, V.D.1
  • 27
    • 0025272240 scopus 로고
    • Rapid and sensitive sequence comparison with FASTP and FASTA
    • Pearson W.R. Rapid and sensitive sequence comparison with FASTP and FASTA. Meth Enzymol 1990, 183:63-98.
    • (1990) Meth Enzymol , vol.183 , pp. 63-98
    • Pearson, W.R.1
  • 28
    • 0027968068 scopus 로고
    • CLUSTALW: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTALW: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acid Res 1994, 22:4673-4680.
    • (1994) Nucleic Acid Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 29
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using realtime quantitative PCR and the 2(-Delta Delta C(T)) method
    • Livak K.J., Schmittgen T.D. Analysis of relative gene expression data using realtime quantitative PCR and the 2(-Delta Delta C(T)) method. Methods 2001, 25:402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 31
    • 79957854747 scopus 로고    scopus 로고
    • Gene profiling and characterization of arginine kinase-1 (MrAK-1) from freshwater giant prawn (Macrobrachium rosenbergii)
    • Arockiaraj J., Vanaraja P., Easwvaran S., Singh A., Alinejaid T., Othman R.Y., et al. Gene profiling and characterization of arginine kinase-1 (MrAK-1) from freshwater giant prawn (Macrobrachium rosenbergii). Fish Shellfish Immunol 2011, 31:81-89.
    • (2011) Fish Shellfish Immunol , vol.31 , pp. 81-89
    • Arockiaraj, J.1    Vanaraja, P.2    Easwvaran, S.3    Singh, A.4    Alinejaid, T.5    Othman, R.Y.6
  • 32
    • 62949088018 scopus 로고    scopus 로고
    • Arginine kinase from Litopenaeus vannamei: cloning, expression and catalytic properties
    • Yao C.L., Ji P.F., Kong P., Wang Z.Y., Xiang J.H. Arginine kinase from Litopenaeus vannamei: cloning, expression and catalytic properties. Fish Shellfish Immunol 2009, 26:553-558.
    • (2009) Fish Shellfish Immunol , vol.26 , pp. 553-558
    • Yao, C.L.1    Ji, P.F.2    Kong, P.3    Wang, Z.Y.4    Xiang, J.H.5
  • 33
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Mann M., Aebersold R. Mass spectrometry-based proteomics. Nature 2003, 422:198-207.
    • (2003) Nature , vol.422 , pp. 198-207
    • Mann, M.1    Aebersold, R.2
  • 34
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantification 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
  • 35
    • 0035890676 scopus 로고    scopus 로고
    • Characterization of zebrafish caspase-3 and induction of apoptosis through ceramide generation in fish fathead minnow tailbud cells and zebrafish embryo
    • Yabu T., Kishi S., Okazaki T., Yamashita M. Characterization of zebrafish caspase-3 and induction of apoptosis through ceramide generation in fish fathead minnow tailbud cells and zebrafish embryo. Biochem J 2001, 360:39-47.
    • (2001) Biochem J , vol.360 , pp. 39-47
    • Yabu, T.1    Kishi, S.2    Okazaki, T.3    Yamashita, M.4
  • 36
    • 79551649498 scopus 로고    scopus 로고
    • Molluscan death effector domain (DED) containing caspase-8 gene from disk abalone (Haliotis discus discus): molecular characterization and expression analysis
    • Lee Y., De Zoysa M., Whang I., Lee S., Kim Y., Oh C., et al. Molluscan death effector domain (DED) containing caspase-8 gene from disk abalone (Haliotis discus discus): molecular characterization and expression analysis. Fish Shellfish Immunol 2011, 30:480-487.
    • (2011) Fish Shellfish Immunol , vol.30 , pp. 480-487
    • Lee, Y.1    De Zoysa, M.2    Whang, I.3    Lee, S.4    Kim, Y.5    Oh, C.6
  • 37
    • 0033575255 scopus 로고    scopus 로고
    • Suicidal tendencies: apoptotic cell death by caspase family proteinases
    • Wolf B.B., Green D.R. Suicidal tendencies: apoptotic cell death by caspase family proteinases. J Biol Chem 1999, 274:2004-2052.
    • (1999) J Biol Chem , vol.274 , pp. 2004-2052
    • Wolf, B.B.1    Green, D.R.2
  • 38
    • 0036205587 scopus 로고    scopus 로고
    • Mechanisms of caspase activation and inhibition during apoptosis
    • Shi Y. Mechanisms of caspase activation and inhibition during apoptosis. Mol Cell 2002, 9:459-470.
    • (2002) Mol Cell , vol.9 , pp. 459-470
    • Shi, Y.1
  • 39
    • 0030702084 scopus 로고    scopus 로고
    • Caspases: intracellular signaling by proteolysis
    • Salvesen G.S., Dixit V.M. Caspases: intracellular signaling by proteolysis. Cell 1997, 91:443-446.
    • (1997) Cell , vol.91 , pp. 443-446
    • Salvesen, G.S.1    Dixit, V.M.2
  • 40
    • 0031001092 scopus 로고    scopus 로고
    • Identification of a Drosophila melanogaster ICE/CED-3-related protease, drICE
    • Fraser A.G., Evan G.I. Identification of a Drosophila melanogaster ICE/CED-3-related protease, drICE. EMBO J 1997, 16:2805-2813.
    • (1997) EMBO J , vol.16 , pp. 2805-2813
    • Fraser, A.G.1    Evan, G.I.2
  • 41
    • 0031023782 scopus 로고    scopus 로고
    • DCP-1, a Drosophila cell death protease essential for development
    • Song Z.K., Mc Call K., Steller H. DCP-1, a Drosophila cell death protease essential for development. Science 1997, 275:536-540.
    • (1997) Science , vol.275 , pp. 536-540
    • Song, Z.K.1    Mc Call, K.2    Steller, H.3
  • 42
    • 0029871920 scopus 로고    scopus 로고
    • Cleavage of sterol regulatory element binding proteins (SREBPs) by CPP32 during apoptosis
    • Wang X., Zelenski N.G., Yang J., Sakai J., Brown M.S., Goldstein J.L. Cleavage of sterol regulatory element binding proteins (SREBPs) by CPP32 during apoptosis. EMBO J 1996, 15:1012-1020.
    • (1996) EMBO J , vol.15 , pp. 1012-1020
    • Wang, X.1    Zelenski, N.G.2    Yang, J.3    Sakai, J.4    Brown, M.S.5    Goldstein, J.L.6
  • 43
    • 39149109572 scopus 로고    scopus 로고
    • Knocking down caspase-3 by RNAi reduces mortality in Pacific white shrimp Penaeus (Litopenaeus) vannamei challenged with a low dose of white-spot syndrome virus
    • Rijiravanich A., Browdy C.L., Withyachumnarnkul B. Knocking down caspase-3 by RNAi reduces mortality in Pacific white shrimp Penaeus (Litopenaeus) vannamei challenged with a low dose of white-spot syndrome virus. Fish Shellfish Immunol 2008, 24:308-313.
    • (2008) Fish Shellfish Immunol , vol.24 , pp. 308-313
    • Rijiravanich, A.1    Browdy, C.L.2    Withyachumnarnkul, B.3
  • 44
    • 39049084854 scopus 로고    scopus 로고
    • Requirement for shrimp caspase in apoptosis against virus infection
    • Wang L., Zhi B., Wu W., Zhang X. Requirement for shrimp caspase in apoptosis against virus infection. Dev Comp Immunol 2008, 32:706-715.
    • (2008) Dev Comp Immunol , vol.32 , pp. 706-715
    • Wang, L.1    Zhi, B.2    Wu, W.3    Zhang, X.4
  • 45
    • 0344053451 scopus 로고    scopus 로고
    • In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains
    • Fernandes-Alnemri T., Armstrong R.C., Krebs J., Srinivasula S.M., Wang L., Bullrich F., et al. In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains. Proc Natl Acad Sci USA 1996, 93:7464-7469.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 7464-7469
    • Fernandes-Alnemri, T.1    Armstrong, R.C.2    Krebs, J.3    Srinivasula, S.M.4    Wang, L.5    Bullrich, F.6
  • 46
    • 0035862551 scopus 로고    scopus 로고
    • Cloning and characterization of three novel genes, ALS2CR1, ALS2CR2, and ALS2CR3, in the juvenile amyotrophic lateral sclerosis (ALS2) critical region at chromosome 2q33eq34: candidate genes for ALS2
    • Hadano S., Yanagisawa Y., Skaug J., Fichter K., Nasir J., Martindale D., et al. Cloning and characterization of three novel genes, ALS2CR1, ALS2CR2, and ALS2CR3, in the juvenile amyotrophic lateral sclerosis (ALS2) critical region at chromosome 2q33eq34: candidate genes for ALS2. Genomics 2001, 71:200-213.
    • (2001) Genomics , vol.71 , pp. 200-213
    • Hadano, S.1    Yanagisawa, Y.2    Skaug, J.3    Fichter, K.4    Nasir, J.5    Martindale, D.6
  • 47
    • 0016205894 scopus 로고
    • Observations of the phagocytosis and elimination of carmine particles injected into the abdominal musculature of the white shrimp, Penaeus setiferus
    • Fontaine C.T., Lightner D.V. Observations of the phagocytosis and elimination of carmine particles injected into the abdominal musculature of the white shrimp, Penaeus setiferus. J Invertebr Pathol 1974, 24:141-148.
    • (1974) J Invertebr Pathol , vol.24 , pp. 141-148
    • Fontaine, C.T.1    Lightner, D.V.2
  • 48
    • 4644341946 scopus 로고    scopus 로고
    • Dietary administration of sodium alginate enhances the immune ability of white shrimp Litopenaeus vannamei and its resistance against Vibrio alginolyticus
    • Cheng W., Liu C.H., Kuo C.M., Chen J.C. Dietary administration of sodium alginate enhances the immune ability of white shrimp Litopenaeus vannamei and its resistance against Vibrio alginolyticus. Fish Shellfish Immunol 2005, 18:1-12.
    • (2005) Fish Shellfish Immunol , vol.18 , pp. 1-12
    • Cheng, W.1    Liu, C.H.2    Kuo, C.M.3    Chen, J.C.4
  • 49
    • 18144364736 scopus 로고    scopus 로고
    • Effects of dopamine on the immunity of white shrimp Litopenaeus vannamei
    • Cheng W., Chieu H.T., Tsai C.H., Chen J.C. Effects of dopamine on the immunity of white shrimp Litopenaeus vannamei. Fish Shellfish Immunol 2005, 19:375-385.
    • (2005) Fish Shellfish Immunol , vol.19 , pp. 375-385
    • Cheng, W.1    Chieu, H.T.2    Tsai, C.H.3    Chen, J.C.4
  • 50
    • 33745260957 scopus 로고    scopus 로고
    • Extended substrate recognition in caspase-3 revealed by high Resolution X-ray structure analysis
    • Ganesan R., Mitt P.R.E., Jelakovic S., Grütter M.G. Extended substrate recognition in caspase-3 revealed by high Resolution X-ray structure analysis. J Mol Biol 2006, 359:1378-1388.
    • (2006) J Mol Biol , vol.359 , pp. 1378-1388
    • Ganesan, R.1    Mitt, P.R.E.2    Jelakovic, S.3    Grütter, M.G.4
  • 52
    • 4344630346 scopus 로고    scopus 로고
    • Translation inhibition during the induction of apoptosis: RNA or protein degradation?
    • Bushell M., Stonely M., Sarnow P., Willis A.E. Translation inhibition during the induction of apoptosis: RNA or protein degradation?. Biochem Soc Trans 2004, 32:606-610.
    • (2004) Biochem Soc Trans , vol.32 , pp. 606-610
    • Bushell, M.1    Stonely, M.2    Sarnow, P.3    Willis, A.E.4
  • 53
    • 58049200617 scopus 로고    scopus 로고
    • Apoptosis: a review of pro-apoptotic and anti-apoptotic pathways and dysregulation in disease
    • O'Brien M.A., Kirby R. Apoptosis: a review of pro-apoptotic and anti-apoptotic pathways and dysregulation in disease. J Vet Emerg Crit Care 2008, 18:572-585.
    • (2008) J Vet Emerg Crit Care , vol.18 , pp. 572-585
    • O'Brien, M.A.1    Kirby, R.2
  • 54
    • 0032493870 scopus 로고    scopus 로고
    • Differential requirement for caspase 9 in apoptotic pathways in vivo
    • Hakem R., Hakem A., Duncan G.S., Henderson J.T., Woo M., Soengas M.S., et al. Differential requirement for caspase 9 in apoptotic pathways in vivo. Cell 1998, 94:339-352.
    • (1998) Cell , vol.94 , pp. 339-352
    • Hakem, R.1    Hakem, A.2    Duncan, G.S.3    Henderson, J.T.4    Woo, M.5    Soengas, M.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.