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Volumn 80, Issue , 2013, Pages 196-206

Comparative proteomic identification of the hemocyte response to cold stress in white shrimp, Litopenaeus vannamei

Author keywords

Cold stress; Flow cytometry; Hemocyte; Litopenaeus vannamei; MALDI TOF TOF MS; Two dimensional electrophoresis

Indexed keywords

CALCIUM; CYSTATHIONINE GAMMA LYASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GLYOXALASE; HEMOCYANIN; HEMOCYTE TRANSGLUTAMINASE; MESSENGER RNA; ONCOPROTEIN; ONCOPROTEIN NM23; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; TRANSKETOLASE; UNCLASSIFIED DRUG; ANILINE DERIVATIVE; FLUO 3; PROTEOME; XANTHENE DERIVATIVE;

EID: 84874417591     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2012.12.017     Document Type: Article
Times cited : (70)

References (59)
  • 1
    • 0031435262 scopus 로고    scopus 로고
    • The effects of salinity and temperature on the growth and survival rates of juvenile white shrimp, Penaeus vannamei, Boone, 1931
    • Ponce-Palafox J., Martinez-Palacios C.A., Ross L.G. The effects of salinity and temperature on the growth and survival rates of juvenile white shrimp, Penaeus vannamei, Boone, 1931. Aquaculture 1997, 157:107-115.
    • (1997) Aquaculture , vol.157 , pp. 107-115
    • Ponce-Palafox, J.1    Martinez-Palacios, C.A.2    Ross, L.G.3
  • 2
    • 0029504301 scopus 로고
    • Temperature effects on growth, feeding rate and feed conversion of the Pacific white shrimp (Penaeus vannamei)
    • Wyban J., Walsh W.A., Godin D.M. Temperature effects on growth, feeding rate and feed conversion of the Pacific white shrimp (Penaeus vannamei). Aquaculture 1995, 138:267-279.
    • (1995) Aquaculture , vol.138 , pp. 267-279
    • Wyban, J.1    Walsh, W.A.2    Godin, D.M.3
  • 3
    • 79955481185 scopus 로고    scopus 로고
    • Oxidative stress, DNA damage and osmolality in the Pacific white shrimp, Litopenaeus vannamei exposed to acute low temperature stress
    • Qiu J., Wang W.N., Wang L.J., Liu Y.F., Wang A.L. Oxidative stress, DNA damage and osmolality in the Pacific white shrimp, Litopenaeus vannamei exposed to acute low temperature stress. Comp Biochem Physiol C 2011, 154:36-41.
    • (2011) Comp Biochem Physiol C , vol.154 , pp. 36-41
    • Qiu, J.1    Wang, W.N.2    Wang, L.J.3    Liu, Y.F.4    Wang, A.L.5
  • 4
    • 1842376847 scopus 로고    scopus 로고
    • Participation of a sialic acid-specific lectin from freshwater prawn Macrobrachium rosenbergii hemocytes in the recognition of non-self cells
    • Vazquez L., Maldonado G., Agundis C., Perez A., Cooper E.L., Zenteno E. Participation of a sialic acid-specific lectin from freshwater prawn Macrobrachium rosenbergii hemocytes in the recognition of non-self cells. J Exp Zool 1997, 279:265-272.
    • (1997) J Exp Zool , vol.279 , pp. 265-272
    • Vazquez, L.1    Maldonado, G.2    Agundis, C.3    Perez, A.4    Cooper, E.L.5    Zenteno, E.6
  • 5
    • 50149111579 scopus 로고    scopus 로고
    • Regulation of phagocytosis against bacterium by Rab GTPase in shrimp Marsupenaeus japonicus
    • Zong R.R., Wu W.L., Xu J.Y., Zhang X.B. Regulation of phagocytosis against bacterium by Rab GTPase in shrimp Marsupenaeus japonicus. Fish Shellfish Immunol 2008, 25:258-263.
    • (2008) Fish Shellfish Immunol , vol.25 , pp. 258-263
    • Zong, R.R.1    Wu, W.L.2    Xu, J.Y.3    Zhang, X.B.4
  • 6
    • 44749089658 scopus 로고    scopus 로고
    • Characterization of a prophenoloxidase from hemocytes of the shrimp Litopenaeus vannamei that is down-regulated by white spot syndrome virus
    • Ai H.S., Huang Y.C., Li S.D., Weng S.P., Yu X.Q., He J.G. Characterization of a prophenoloxidase from hemocytes of the shrimp Litopenaeus vannamei that is down-regulated by white spot syndrome virus. Fish Shellfish Immunol 2008, 25:28-39.
    • (2008) Fish Shellfish Immunol , vol.25 , pp. 28-39
    • Ai, H.S.1    Huang, Y.C.2    Li, S.D.3    Weng, S.P.4    Yu, X.Q.5    He, J.G.6
  • 7
    • 0033044218 scopus 로고    scopus 로고
    • Molecular cloning and characterization of prophenoloxidase in the black tiger shrimp, Penaeus monodon
    • Sritunyalucksana K., Cerenius L., Soderhall K. Molecular cloning and characterization of prophenoloxidase in the black tiger shrimp, Penaeus monodon. Dev Comp Immunol 1999, 23:179-186.
    • (1999) Dev Comp Immunol , vol.23 , pp. 179-186
    • Sritunyalucksana, K.1    Cerenius, L.2    Soderhall, K.3
  • 8
    • 0345863449 scopus 로고    scopus 로고
    • Molecular cloning and characterization of tiger shrimp (Penaeus monodon) transglutaminase
    • Huang C.C., Sritunyalucksana K., Soderhall K., Song Y.L. Molecular cloning and characterization of tiger shrimp (Penaeus monodon) transglutaminase. Dev Comp Immunol 2004, 28:279-294.
    • (2004) Dev Comp Immunol , vol.28 , pp. 279-294
    • Huang, C.C.1    Sritunyalucksana, K.2    Soderhall, K.3    Song, Y.L.4
  • 9
    • 2442485800 scopus 로고    scopus 로고
    • CDNA sequence encoding an 11.5-kDa antibacterial peptide of the shrimp Penaeus monodon
    • Chen J.Y., Pan C.Y., Kuo C.M. cDNA sequence encoding an 11.5-kDa antibacterial peptide of the shrimp Penaeus monodon. Fish Shellfish Immunol 2004, 16:659-664.
    • (2004) Fish Shellfish Immunol , vol.16 , pp. 659-664
    • Chen, J.Y.1    Pan, C.Y.2    Kuo, C.M.3
  • 11
    • 34548209154 scopus 로고    scopus 로고
    • Immune condition of Chlamys farreri in response to acute temperature challenge
    • Chen M.Y., Yang H.S., Delaporte M., Zhao S.J. Immune condition of Chlamys farreri in response to acute temperature challenge. Aquaculture 2007, 271:479-487.
    • (2007) Aquaculture , vol.271 , pp. 479-487
    • Chen, M.Y.1    Yang, H.S.2    Delaporte, M.3    Zhao, S.J.4
  • 12
    • 70249130067 scopus 로고    scopus 로고
    • Oxidative stress, DNA damage and antioxidant enzyme gene expression in the Pacific white shrimp, Litopenaeus vannamei when exposed to acute pH stress
    • Wang W.-N., Zhou J., Wang P., Tian T.-T., Zheng Y., Liu Y., et al. Oxidative stress, DNA damage and antioxidant enzyme gene expression in the Pacific white shrimp, Litopenaeus vannamei when exposed to acute pH stress. Comp Biochem Physiol C 2009, 150:428-435.
    • (2009) Comp Biochem Physiol C , vol.150 , pp. 428-435
    • Wang, W.-N.1    Zhou, J.2    Wang, P.3    Tian, T.-T.4    Zheng, Y.5    Liu, Y.6
  • 13
    • 76049083966 scopus 로고    scopus 로고
    • Reactive oxygen species, cellular redox systems, and apoptosis
    • Circu M.L., Aw T.Y. Reactive oxygen species, cellular redox systems, and apoptosis. Free Radic Biol Med 2010, 48:749-762.
    • (2010) Free Radic Biol Med , vol.48 , pp. 749-762
    • Circu, M.L.1    Aw, T.Y.2
  • 15
    • 0034178688 scopus 로고    scopus 로고
    • Effects of pH, temperature and salinity on immune parameters of the freshwater prawn Macrobrachium rosenbergii
    • Cheng W., Chen J.C. Effects of pH, temperature and salinity on immune parameters of the freshwater prawn Macrobrachium rosenbergii. Fish Shellfish Immunol 2000, 10:387-391.
    • (2000) Fish Shellfish Immunol , vol.10 , pp. 387-391
    • Cheng, W.1    Chen, J.C.2
  • 16
    • 0032210441 scopus 로고    scopus 로고
    • Effect of hypoxic stress on the immune response and the resistance to vibriosis of the shrimp Penaeus stylirostris
    • Le Moullac G., Soyez C., Saulnier D., Ansquer D., Avarre J.C., Levy P. Effect of hypoxic stress on the immune response and the resistance to vibriosis of the shrimp Penaeus stylirostris. Fish Shellfish Immunol 1998, 8:621-629.
    • (1998) Fish Shellfish Immunol , vol.8 , pp. 621-629
    • Le Moullac, G.1    Soyez, C.2    Saulnier, D.3    Ansquer, D.4    Avarre, J.C.5    Levy, P.6
  • 17
    • 60549110465 scopus 로고    scopus 로고
    • Contributions of functional genomics and proteomics to the study of immune responses in the Pacific white leg shrimp Litopenaeus vannamei
    • Robalino J., Carnegie R.B., O'Leary N., Ouvry-Patat S.A., de la Vega E., Prior S., et al. Contributions of functional genomics and proteomics to the study of immune responses in the Pacific white leg shrimp Litopenaeus vannamei. Vet Immunol Immunopathol 2009, 128:110-118.
    • (2009) Vet Immunol Immunopathol , vol.128 , pp. 110-118
    • Robalino, J.1    Carnegie, R.B.2    O'Leary, N.3    Ouvry-Patat, S.A.4    de la Vega, E.5    Prior, S.6
  • 18
    • 77954541265 scopus 로고    scopus 로고
    • Comparative proteomic profiles of the hepatopancreas in Fenneropenaeus chinensis response to white spot syndrome virus
    • Chai Y.M., Yu S.S., Zhao X.F., Zhu Q.A., Wang J.X. Comparative proteomic profiles of the hepatopancreas in Fenneropenaeus chinensis response to white spot syndrome virus. Fish Shellfish Immunol 2010, 29:480-486.
    • (2010) Fish Shellfish Immunol , vol.29 , pp. 480-486
    • Chai, Y.M.1    Yu, S.S.2    Zhao, X.F.3    Zhu, Q.A.4    Wang, J.X.5
  • 19
    • 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
  • 20
    • 35348964100 scopus 로고    scopus 로고
    • Proteomic analysis of differentially expressed proteins in Penaeus vannamei hemocytes upon Taura syndrome virus infection
    • Chongsatja P.O., Bourchookarn A., Lo C.F., Thongboonkerd V., Krittanai C. Proteomic analysis of differentially expressed proteins in Penaeus vannamei hemocytes upon Taura syndrome virus infection. Proteomics 2007, 7:3592-3601.
    • (2007) Proteomics , vol.7 , pp. 3592-3601
    • Chongsatja, P.O.1    Bourchookarn, A.2    Lo, C.F.3    Thongboonkerd, V.4    Krittanai, C.5
  • 21
    • 70449587007 scopus 로고    scopus 로고
    • Morphologic, physiological and immunological changes of haemocytes from Litopenaeus vannamei treated by lipopolysaccharide
    • Xian J.-A., Wang A.-L., Tian J.-X., Huang J.-W., Ye C.-X., Wang W.-N., et al. Morphologic, physiological and immunological changes of haemocytes from Litopenaeus vannamei treated by lipopolysaccharide. Aquaculture 2009, 298:139-145.
    • (2009) Aquaculture , vol.298 , pp. 139-145
    • Xian, J.-A.1    Wang, A.-L.2    Tian, J.-X.3    Huang, J.-W.4    Ye, C.-X.5    Wang, W.-N.6
  • 23
    • 0032585497 scopus 로고    scopus 로고
    • Annexin V binding assay as a tool to measure apoptosis in differentiated neuronal cells
    • Schutte B., Nuydens R., Geerts H., Ramaekers F. Annexin V binding assay as a tool to measure apoptosis in differentiated neuronal cells. J Neurosci Methods 1998, 86:63-69.
    • (1998) J Neurosci Methods , vol.86 , pp. 63-69
    • Schutte, B.1    Nuydens, R.2    Geerts, H.3    Ramaekers, F.4
  • 24
    • 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
  • 25
    • 0033662168 scopus 로고    scopus 로고
    • A modified silver staining protocol for visualization of proteins compatible with matrix-assisted laser desorption/ionization and electrospray ionization-mass spectrometry
    • Yan J.X., Wait R., Berkelman T., Harry R.A., Westbrook J.A., Wheeler C.H., et al. A modified silver staining protocol for visualization of proteins compatible with matrix-assisted laser desorption/ionization and electrospray ionization-mass spectrometry. Electrophoresis 2000, 21:3666-3672.
    • (2000) Electrophoresis , vol.21 , pp. 3666-3672
    • Yan, J.X.1    Wait, R.2    Berkelman, T.3    Harry, R.A.4    Westbrook, J.A.5    Wheeler, C.H.6
  • 27
    • 84987589406 scopus 로고
    • The influence of haemocyte number on the resistance of the freshwater crayfish, Pacifastacus leniusculus Dana, to the parasitic fungus Aphanomyces astaci
    • Persson M., Cerenius L., SÖDerhÄLl K. The influence of haemocyte number on the resistance of the freshwater crayfish, Pacifastacus leniusculus Dana, to the parasitic fungus Aphanomyces astaci. J Fish Dis 1987, 10:471-477.
    • (1987) J Fish Dis , vol.10 , pp. 471-477
    • Persson, M.1    Cerenius, L.2    SÖDerhÄLl, K.3
  • 28
    • 0001326407 scopus 로고
    • Identification of defence effectors in the haemolymph of Crustaceans with particular reference to the shrimp Penaeus japonicus (Bate): prospects and applications
    • Bachère E., Mialhe E., Rodriguez J. Identification of defence effectors in the haemolymph of Crustaceans with particular reference to the shrimp Penaeus japonicus (Bate): prospects and applications. Fish Shellfish Immunol 1995, 5:597-612.
    • (1995) Fish Shellfish Immunol , vol.5 , pp. 597-612
    • Bachère, E.1    Mialhe, E.2    Rodriguez, J.3
  • 29
    • 33745360009 scopus 로고    scopus 로고
    • Cytochrome c oxydase subunit I gene is up-regulated by cadmium in freshwater and marine bivalves
    • Achard-Joris M., Gonzalez P., Marie V., Baudrimont M., Bourdineaud J.-P. Cytochrome c oxydase subunit I gene is up-regulated by cadmium in freshwater and marine bivalves. Biometals 2006, 19:237-244.
    • (2006) Biometals , vol.19 , pp. 237-244
    • Achard-Joris, M.1    Gonzalez, P.2    Marie, V.3    Baudrimont, M.4    Bourdineaud, J.-P.5
  • 30
    • 0036478970 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species in cell death signaling
    • Fleury C., Mignotte B., Vayssière J.-L. Mitochondrial reactive oxygen species in cell death signaling. Biochimie 2002, 84:131-141.
    • (2002) Biochimie , vol.84 , pp. 131-141
    • Fleury, C.1    Mignotte, B.2    Vayssière, J.-L.3
  • 32
    • 0030603967 scopus 로고    scopus 로고
    • In vivo detoxification of cyanide by cystathionase γ-lyase
    • Porter D.W., Nealley E.W., Baskin S.I. In vivo detoxification of cyanide by cystathionase γ-lyase. Biochem Pharmacol 1996, 52:941-944.
    • (1996) Biochem Pharmacol , vol.52 , pp. 941-944
    • Porter, D.W.1    Nealley, E.W.2    Baskin, S.I.3
  • 33
    • 33846308476 scopus 로고    scopus 로고
    • Inhibition of cystathionine-γ-lyase leads to loss of glutathione and aggravation of mitochondrial dysfunction mediated by excitatory amino acid in the CNS
    • Diwakar L., Ravindranath V. Inhibition of cystathionine-γ-lyase leads to loss of glutathione and aggravation of mitochondrial dysfunction mediated by excitatory amino acid in the CNS. Neurochem Int 2007, 50:418-426.
    • (2007) Neurochem Int , vol.50 , pp. 418-426
    • Diwakar, L.1    Ravindranath, V.2
  • 34
    • 84862668692 scopus 로고    scopus 로고
    • Phenylephrine protects cardiomyocytes from starvation-induced apoptosis by increasing glyceraldehyde-3-phosphate dehydrogenase (GAPDH) activity
    • Yao L.L., Wang Y.G., Liu X.J., Zhou Y., Li N., Liu J., et al. Phenylephrine protects cardiomyocytes from starvation-induced apoptosis by increasing glyceraldehyde-3-phosphate dehydrogenase (GAPDH) activity. J Cell Physiol 2012, 227:3518-3527.
    • (2012) J Cell Physiol , vol.227 , pp. 3518-3527
    • Yao, L.L.1    Wang, Y.G.2    Liu, X.J.3    Zhou, Y.4    Li, N.5    Liu, J.6
  • 35
    • 84863112816 scopus 로고    scopus 로고
    • Cytosolic glyceraldehyde-3-phosphate dehydrogenases interact with phospholipase ddelta to transduce hydrogen peroxide signals in the Arabidopsis response to stress
    • Guo L., Devaiah S.P., Narasimhan R., Pan X., Zhang Y., Zhang W., et al. Cytosolic glyceraldehyde-3-phosphate dehydrogenases interact with phospholipase ddelta to transduce hydrogen peroxide signals in the Arabidopsis response to stress. Plant Cell 2012, 24:2200-2212.
    • (2012) Plant Cell , vol.24 , pp. 2200-2212
    • Guo, L.1    Devaiah, S.P.2    Narasimhan, R.3    Pan, X.4    Zhang, Y.5    Zhang, W.6
  • 36
    • 0027973979 scopus 로고
    • The gene encoding glyoxalase I from Pseudomonas putida: cloning, overexpression, and sequence comparisons with human glyoxalase I
    • Lu T., Creighton D.J., Antoine M., Fenselau C., Lovett P.S. The gene encoding glyoxalase I from Pseudomonas putida: cloning, overexpression, and sequence comparisons with human glyoxalase I. Gene 1994, 150:93-96.
    • (1994) Gene , vol.150 , pp. 93-96
    • Lu, T.1    Creighton, D.J.2    Antoine, M.3    Fenselau, C.4    Lovett, P.S.5
  • 38
    • 78651410794 scopus 로고    scopus 로고
    • Overexpression of glyoxalase-I reduces hyperglycemia-induced levels of advanced glycation end products and oxidative stress in diabetic rats
    • Brouwers O., Niessen P.M., Ferreira I., Miyata T., Scheffer P.G., Teerlink T., et al. Overexpression of glyoxalase-I reduces hyperglycemia-induced levels of advanced glycation end products and oxidative stress in diabetic rats. J Biol Chem 2011, 286:1374-1380.
    • (2011) J Biol Chem , vol.286 , pp. 1374-1380
    • Brouwers, O.1    Niessen, P.M.2    Ferreira, I.3    Miyata, T.4    Scheffer, P.G.5    Teerlink, T.6
  • 39
    • 82855177408 scopus 로고    scopus 로고
    • Increased glyoxalase I levels inhibit accumulation of oxidative stress and an advanced glycation end product in mouse mesangial cells cultured in high glucose
    • Kim K.M., Kim Y.S., Jung D.H., Lee J., Kim J.S. Increased glyoxalase I levels inhibit accumulation of oxidative stress and an advanced glycation end product in mouse mesangial cells cultured in high glucose. Exp Cell Res 2012, 318:152-159.
    • (2012) Exp Cell Res , vol.318 , pp. 152-159
    • Kim, K.M.1    Kim, Y.S.2    Jung, D.H.3    Lee, J.4    Kim, J.S.5
  • 40
    • 0029966429 scopus 로고    scopus 로고
    • Mussel glyoxalase I as a possible marker for ecotoxicological studies: purification and preliminary characterization
    • Regoli F., Saccucci F., Principato G. Mussel glyoxalase I as a possible marker for ecotoxicological studies: purification and preliminary characterization. Comp Biochem Physiol C Pharmacol Toxicol Endocrinol 1996, 113:313-317.
    • (1996) Comp Biochem Physiol C Pharmacol Toxicol Endocrinol , vol.113 , pp. 313-317
    • Regoli, F.1    Saccucci, F.2    Principato, G.3
  • 42
    • 8644285662 scopus 로고    scopus 로고
    • Nm23-M2/NDP kinase B induces endogenous c-myc and nm23-M1/NDP kinase A overexpression in BAF3 cells. Both NDP kinases protect the cells from oxidative stress-induced death
    • Arnaud-Dabernat S., Masse K., Smani M., Peuchant E., Landry M., Bourbon P.M., et al. Nm23-M2/NDP kinase B induces endogenous c-myc and nm23-M1/NDP kinase A overexpression in BAF3 cells. Both NDP kinases protect the cells from oxidative stress-induced death. Exp Cell Res 2004, 301:293-304.
    • (2004) Exp Cell Res , vol.301 , pp. 293-304
    • Arnaud-Dabernat, S.1    Masse, K.2    Smani, M.3    Peuchant, E.4    Landry, M.5    Bourbon, P.M.6
  • 43
    • 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
  • 46
    • 0019170917 scopus 로고
    • Partial purification and characterization of an actin depolymerizing factor from brain
    • Bamburg J.R., Harris H.E., Weeds A.G. Partial purification and characterization of an actin depolymerizing factor from brain. FEBS Lett 1980, 121:178-182.
    • (1980) FEBS Lett , vol.121 , pp. 178-182
    • Bamburg, J.R.1    Harris, H.E.2    Weeds, A.G.3
  • 47
    • 0030897031 scopus 로고    scopus 로고
    • Structure of 20S proteasome from yeast at 2.4angstrom resolution
    • Groll M., Ditzel L., Lowe J., Stock D., Bochtler M., Bartunik H.D., et al. Structure of 20S proteasome from yeast at 2.4angstrom resolution. Nature 1997, 386:463-471.
    • (1997) Nature , vol.386 , pp. 463-471
    • Groll, M.1    Ditzel, L.2    Lowe, J.3    Stock, D.4    Bochtler, M.5    Bartunik, H.D.6
  • 49
    • 78650709082 scopus 로고    scopus 로고
    • A cDNA microarray approach for analyzing transcriptional changes in Penaeus monodon after infection by pathogens
    • Pongsomboon S., Tang S., Boonda S., Aoki T., Hirono I., Tassanakajon A. A cDNA microarray approach for analyzing transcriptional changes in Penaeus monodon after infection by pathogens. Fish Shellfish Immunol 2011, 30:439-446.
    • (2011) Fish Shellfish Immunol , vol.30 , pp. 439-446
    • Pongsomboon, S.1    Tang, S.2    Boonda, S.3    Aoki, T.4    Hirono, I.5    Tassanakajon, A.6
  • 50
    • 33645789521 scopus 로고    scopus 로고
    • Affinity proteomic approach for identification of an IgA-like protein in Litopenaeus vannamei and study on its agglutination characterization
    • Zhang Y.L., Wang S.Y., Xu A.L., Chen J., Lin B.K., Peng X.X. Affinity proteomic approach for identification of an IgA-like protein in Litopenaeus vannamei and study on its agglutination characterization. J Proteome Res 2006, 5:815-821.
    • (2006) J Proteome Res , vol.5 , pp. 815-821
    • Zhang, Y.L.1    Wang, S.Y.2    Xu, A.L.3    Chen, J.4    Lin, B.K.5    Peng, X.X.6
  • 51
  • 52
    • 0035861645 scopus 로고    scopus 로고
    • Crustacean immunity - Antifungal peptides are generated from the C terminus of shrimp hemocyanin in response to microbial challenge
    • Destoumieux-Garzon D., Saulnier D., Garnier J., Jouffrey C., Bulet P., Bachere E. Crustacean immunity - Antifungal peptides are generated from the C terminus of shrimp hemocyanin in response to microbial challenge. J Biol Chem 2001, 276:47070-47077.
    • (2001) J Biol Chem , vol.276 , pp. 47070-47077
    • Destoumieux-Garzon, D.1    Saulnier, D.2    Garnier, J.3    Jouffrey, C.4    Bulet, P.5    Bachere, E.6
  • 53
    • 66749123017 scopus 로고    scopus 로고
    • C-terminal hemocyanin from hemocytes of Penaeus vannamei interacts with ERK1/2 and undergoes serine phosphorylation
    • Havanapan P.O., Kanlaya R., Bourchookarn A., Krittanai C., Thongboonkerd V. C-terminal hemocyanin from hemocytes of Penaeus vannamei interacts with ERK1/2 and undergoes serine phosphorylation. J Proteome Res 2009, 8:2476-2483.
    • (2009) J Proteome Res , vol.8 , pp. 2476-2483
    • Havanapan, P.O.1    Kanlaya, R.2    Bourchookarn, A.3    Krittanai, C.4    Thongboonkerd, V.5
  • 54
    • 81255157706 scopus 로고    scopus 로고
    • Identification and cloning of a transglutaminase from giant freshwater prawn, Macrobrachium rosenbergii, and its transcription during pathogen infection and moulting
    • Liu C.H., Chang C.C., Chiu Y.C., Cheng W., Yeh M.S. Identification and cloning of a transglutaminase from giant freshwater prawn, Macrobrachium rosenbergii, and its transcription during pathogen infection and moulting. Fish Shellfish Immunol 2011, 31:871-880.
    • (2011) Fish Shellfish Immunol , vol.31 , pp. 871-880
    • Liu, C.H.1    Chang, C.C.2    Chiu, Y.C.3    Cheng, W.4    Yeh, M.S.5
  • 55
    • 0037380557 scopus 로고    scopus 로고
    • Haemolymph parameters of Pacific white shrimp (Litopenaeus vannamei) infected with Taura syndrome virus
    • Song Y.L., Yu C.I., Lien T.W., Huang C.C., Lin M.N. Haemolymph parameters of Pacific white shrimp (Litopenaeus vannamei) infected with Taura syndrome virus. Fish Shellfish Immunol 2003, 14:317-331.
    • (2003) Fish Shellfish Immunol , vol.14 , pp. 317-331
    • Song, Y.L.1    Yu, C.I.2    Lien, T.W.3    Huang, C.C.4    Lin, M.N.5
  • 56
    • 70350770824 scopus 로고    scopus 로고
    • CDNA cloning, identification, tissue localisation, and transcription profile of a transglutaminase from white shrimp, Litopenaeus vannamei, after infection by Vibrio alginolyticus
    • Yeh M.S., Liu C.H., Hung C.W., Cheng W. cDNA cloning, identification, tissue localisation, and transcription profile of a transglutaminase from white shrimp, Litopenaeus vannamei, after infection by Vibrio alginolyticus. Fish Shellfish Immunol 2009, 27:748-756.
    • (2009) Fish Shellfish Immunol , vol.27 , pp. 748-756
    • Yeh, M.S.1    Liu, C.H.2    Hung, C.W.3    Cheng, W.4
  • 57
    • 0000922007 scopus 로고
    • Utilization of enzymes in organic chemistry: transketolase catalyzed synthesis of ketoses
    • Bolte J., Demuynck C., Samaki H. Utilization of enzymes in organic chemistry: transketolase catalyzed synthesis of ketoses. Tetrahedron Lett 1987, 28:5525-5528.
    • (1987) Tetrahedron Lett , vol.28 , pp. 5525-5528
    • Bolte, J.1    Demuynck, C.2    Samaki, H.3
  • 58
    • 0026664038 scopus 로고
    • Nucleotide and predicted amino acid sequence of a cDNA clone encoding part of human transketolase
    • Abedinia M., Layfield R., Jones S.M., Nixon P.F., Mattick J.S. Nucleotide and predicted amino acid sequence of a cDNA clone encoding part of human transketolase. Biochem Biophys Res Commun 1992, 183:1159-1166.
    • (1992) Biochem Biophys Res Commun , vol.183 , pp. 1159-1166
    • Abedinia, M.1    Layfield, R.2    Jones, S.M.3    Nixon, P.F.4    Mattick, J.S.5


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