메뉴 건너뛰기




Volumn 159, Issue 4, 2011, Pages 244-251

Expression analysis and response of Penaeus monodon 14-3-3 genes to salinity stress

Author keywords

14 3 3; ATPase; Osmoregulation; Penaeus monodon; Salinity stress; Shrimp

Indexed keywords

MESSENGER RNA; PROTEIN 14 3 3; PROTEIN 14 3 3A; PROTEIN 14 3 3B; UNCLASSIFIED DRUG;

EID: 79958776919     PISSN: 10964959     EISSN: 18791107     Source Type: Journal    
DOI: 10.1016/j.cbpb.2011.05.004     Document Type: Article
Times cited : (28)

References (60)
  • 1
    • 33646926129 scopus 로고    scopus 로고
    • 14-3-3 proteins: a historic overview
    • Aitken A. 14-3-3 proteins: a historic overview. Semin. Cancer Biol. 2006, 16:162-172.
    • (2006) Semin. Cancer Biol. , vol.16 , pp. 162-172
    • Aitken, A.1
  • 3
    • 2942615094 scopus 로고    scopus 로고
    • Over-expression of ascorbate peroxidase in tobacco chloroplasts enhances the tolerance to salt stress and water deficit
    • Badawi G.H., Kawano N., Yamauchi Y., Shimada E., Sasaki R., Kubo A., Tanaka K. Over-expression of ascorbate peroxidase in tobacco chloroplasts enhances the tolerance to salt stress and water deficit. Physiol. Plant. 2004, 121:231-238.
    • (2004) Physiol. Plant. , vol.121 , pp. 231-238
    • Badawi, G.H.1    Kawano, N.2    Yamauchi, Y.3    Shimada, E.4    Sasaki, R.5    Kubo, A.6    Tanaka, K.7
  • 4
    • 0032033440 scopus 로고    scopus 로고
    • The 14-3-3 proteins associate with the plant plasma membrane H+-ATPase to generate a fusicoccin binding complex and a fusicoccin responsive system
    • Baunsgaard L., Fuglsang A.T., Jahn T., Korthout H.A., de Boer A.H., Palmgren M.G. The 14-3-3 proteins associate with the plant plasma membrane H+-ATPase to generate a fusicoccin binding complex and a fusicoccin responsive system. Plant J. 1998, 13:661-671.
    • (1998) Plant J. , vol.13 , pp. 661-671
    • Baunsgaard, L.1    Fuglsang, A.T.2    Jahn, T.3    Korthout, H.A.4    de Boer, A.H.5    Palmgren, M.G.6
  • 5
    • 41149160836 scopus 로고    scopus 로고
    • Sodium uptake in different life stages of crustaceans: the water flea Daphnia magna Strauss
    • Bianchini A., Wood C.M. Sodium uptake in different life stages of crustaceans: the water flea Daphnia magna Strauss. J. Exp. Biol. 2008, 211:539-547.
    • (2008) J. Exp. Biol. , vol.211 , pp. 539-547
    • Bianchini, A.1    Wood, C.M.2
  • 6
    • 0025179951 scopus 로고
    • Carbonic anhydrase in branchial tissues of osmoregulating shore crabs, Carcinus maenas
    • Böttcher K., Siebers D., Becker W. Carbonic anhydrase in branchial tissues of osmoregulating shore crabs, Carcinus maenas. J. Exp. Zool. 1990, 255:251-261.
    • (1990) J. Exp. Zool. , vol.255 , pp. 251-261
    • Böttcher, K.1    Siebers, D.2    Becker, W.3
  • 8
    • 0002991670 scopus 로고
    • The effect of salinity on the osmotic, sodium and chloride concentrations in the hemolymph of euryhaline shrimp of the genus Penaeus
    • Castille F.L., Lawrence A.L. The effect of salinity on the osmotic, sodium and chloride concentrations in the hemolymph of euryhaline shrimp of the genus Penaeus. Comp. Biochem. Physiol. A 1981, 68:75-80.
    • (1981) Comp. Biochem. Physiol. A , vol.68 , pp. 75-80
    • Castille, F.L.1    Lawrence, A.L.2
  • 9
    • 57549102034 scopus 로고    scopus 로고
    • Problems in Penaeus monodon culture in low salinity areas
    • Chanratchakool P. Problems in Penaeus monodon culture in low salinity areas. Aquaculture Asia 2003, 8:54-56.
    • (2003) Aquaculture Asia , vol.8 , pp. 54-56
    • Chanratchakool, P.1
  • 10
    • 33744935760 scopus 로고    scopus 로고
    • The rice 14-3-3 gene family and its involvement in responses to biotic and abiotic stress
    • Chen F., Li Q., Sun L., He Z. The rice 14-3-3 gene family and its involvement in responses to biotic and abiotic stress. DNA Res. 2006, 13:53-63.
    • (2006) DNA Res. , vol.13 , pp. 53-63
    • Chen, F.1    Li, Q.2    Sun, L.3    He, Z.4
  • 11
    • 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
  • 12
    • 47049118219 scopus 로고    scopus 로고
    • Phosphorylation-dependent binding of 14-3-3 proteins controls TRESK regulation
    • Czirjak G., Vuity D., Enyedi P. Phosphorylation-dependent binding of 14-3-3 proteins controls TRESK regulation. J. Biol. Chem. 2008, 283:15672-15680.
    • (2008) J. Biol. Chem. , vol.283 , pp. 15672-15680
    • Czirjak, G.1    Vuity, D.2    Enyedi, P.3
  • 13
    • 2942552470 scopus 로고    scopus 로고
    • Unlocking the code of 14-3-3
    • Dougherty M.K., Morrison D.K. Unlocking the code of 14-3-3. J. Cell Sci. 2004, 117:1875-1884.
    • (2004) J. Cell Sci. , vol.117 , pp. 1875-1884
    • Dougherty, M.K.1    Morrison, D.K.2
  • 14
    • 18144428731 scopus 로고    scopus 로고
    • The 14-3-3 protein translates the NA+, K+-ATPase alpha1-subunit phosphorylation signal into binding and activation of phosphoinositide 3-kinase during endocytosis
    • Efendiev R., Chen Z., Krmar R.T., Uhles S., Katz A.I., Pedemonte C.H., Bertorello A.M. The 14-3-3 protein translates the NA+, K+-ATPase alpha1-subunit phosphorylation signal into binding and activation of phosphoinositide 3-kinase during endocytosis. J. Biol. Chem. 2005, 280:16272-16277.
    • (2005) J. Biol. Chem. , vol.280 , pp. 16272-16277
    • Efendiev, R.1    Chen, Z.2    Krmar, R.T.3    Uhles, S.4    Katz, A.I.5    Pedemonte, C.H.6    Bertorello, A.M.7
  • 15
    • 79958832290 scopus 로고
    • PHYLIP: phylogeny inference Package. Version 3.5C. Seattle: University of Washington.
    • Felsenstein, J., 1993. PHYLIP: phylogeny inference Package. Version 3.5C. Seattle: University of Washington.
    • (1993)
    • Felsenstein, J.1
  • 16
    • 0000634839 scopus 로고
    • Osmotic and chloride regulation in the hemolymph of the tiger prawn, Penaeus monodon, during molting in various salinities
    • Ferraris R.P., Parado-Estepa F.D., de Jesus E.G., Ladja J.M. Osmotic and chloride regulation in the hemolymph of the tiger prawn, Penaeus monodon, during molting in various salinities. Mar. Biol. 1987, 95:377-385.
    • (1987) Mar. Biol. , vol.95 , pp. 377-385
    • Ferraris, R.P.1    Parado-Estepa, F.D.2    de Jesus, E.G.3    Ladja, J.M.4
  • 17
    • 35748944835 scopus 로고    scopus 로고
    • Osmotic stress sensing and signaling in fishes
    • Fiol D.F., Kultz D. Osmotic stress sensing and signaling in fishes. FEBS J. 2007, 274:5790-5798.
    • (2007) FEBS J. , vol.274 , pp. 5790-5798
    • Fiol, D.F.1    Kultz, D.2
  • 18
    • 52949121466 scopus 로고    scopus 로고
    • Structure-function relationships of ion transport in crustacean gills and antennal glands
    • Freire C.A., Onken H., McNamara J.C. Structure-function relationships of ion transport in crustacean gills and antennal glands. Comp. Biochem. Physiol. B 2008, 151:272-304.
    • (2008) Comp. Biochem. Physiol. B , vol.151 , pp. 272-304
    • Freire, C.A.1    Onken, H.2    McNamara, J.C.3
  • 19
    • 0033876921 scopus 로고    scopus 로고
    • Characterization of (Na+, K+)-ATPase in gill microsomes of the freshwater shrimp Macrobrachium olfersii
    • Furriel R.P., McNamara J.C., Leone F.A. Characterization of (Na+, K+)-ATPase in gill microsomes of the freshwater shrimp Macrobrachium olfersii. Comp. Biochem. Physiol. B 2000, 126:303-315.
    • (2000) Comp. Biochem. Physiol. B , vol.126 , pp. 303-315
    • Furriel, R.P.1    McNamara, J.C.2    Leone, F.A.3
  • 20
    • 33646898172 scopus 로고    scopus 로고
    • Structural determinants of 14-3-3 binding specificities and regulation of subcellular localization of 14-3-3-ligand complexes: a comparison of the X-ray crystal structures of all human 14-3-3 isoforms
    • Gardino A.K., Smerdon S.J., Yaffe M.B. Structural determinants of 14-3-3 binding specificities and regulation of subcellular localization of 14-3-3-ligand complexes: a comparison of the X-ray crystal structures of all human 14-3-3 isoforms. Semin. Cancer Biol. 2006, 16:173-182.
    • (2006) Semin. Cancer Biol. , vol.16 , pp. 173-182
    • Gardino, A.K.1    Smerdon, S.J.2    Yaffe, M.B.3
  • 21
    • 0000023978 scopus 로고
    • The role of carbonic anhydrase in blood ion and acid-base regulation
    • Henry R.P. The role of carbonic anhydrase in blood ion and acid-base regulation. Am. Zool. 1984, 24:241-253.
    • (1984) Am. Zool. , vol.24 , pp. 241-253
    • Henry, R.P.1
  • 22
    • 0035338532 scopus 로고    scopus 로고
    • Early carbonic anhydrase induction in the gills of the blue crab, Callinectes sapidus, during low salinity acclimation is independent of ornithine decarboxylase activity
    • Henry R.P., Watts S.A. Early carbonic anhydrase induction in the gills of the blue crab, Callinectes sapidus, during low salinity acclimation is independent of ornithine decarboxylase activity. J. Exp. Zool. 2001, 289:350-358.
    • (2001) J. Exp. Zool. , vol.289 , pp. 350-358
    • Henry, R.P.1    Watts, S.A.2
  • 23
    • 77953133969 scopus 로고    scopus 로고
    • Na/K-ATPase activity and osmo-ionic regulation in adult whiteleg shrimp Litopenaeus vannamei exposed to low salinities
    • Huong D.T.T., Jasmani S., Jayasankar V., Wilder M. Na/K-ATPase activity and osmo-ionic regulation in adult whiteleg shrimp Litopenaeus vannamei exposed to low salinities. Aquaculture Asia 2010, 304:88-94.
    • (2010) Aquaculture Asia , vol.304 , pp. 88-94
    • Huong, D.T.T.1    Jasmani, S.2    Jayasankar, V.3    Wilder, M.4
  • 24
    • 34347390485 scopus 로고    scopus 로고
    • Gill-specific transcriptional regulation of Na+/K+-ATPase alpha-subunit in the euryhaline shore crab Pachygrapsus marmoratus: sequence variants and promoter structure
    • Jayasundara N., Towle D.W., Weihrauch D., Spanings-Pierrot C. Gill-specific transcriptional regulation of Na+/K+-ATPase alpha-subunit in the euryhaline shore crab Pachygrapsus marmoratus: sequence variants and promoter structure. J. Exp. Biol. 2007, 210:2070-2081.
    • (2007) J. Exp. Biol. , vol.210 , pp. 2070-2081
    • Jayasundara, N.1    Towle, D.W.2    Weihrauch, D.3    Spanings-Pierrot, C.4
  • 25
    • 0036840274 scopus 로고    scopus 로고
    • Salt-stress-induced ABA accumulation is more sensitively triggered in roots than in shoots
    • Jia W., Wang Y., Zhang S., Zhang J. Salt-stress-induced ABA accumulation is more sensitively triggered in roots than in shoots. J. Exp. Bot. 2002, 53:2201-2206.
    • (2002) J. Exp. Bot. , vol.53 , pp. 2201-2206
    • Jia, W.1    Wang, Y.2    Zhang, S.3    Zhang, J.4
  • 26
    • 0037090803 scopus 로고    scopus 로고
    • 14-3-3 amplifies and prolongs adrenergic stimulation of HERG K+ channel activity
    • Kagan A., Melman Y.F., Krumerman A., McDonald T.V. 14-3-3 amplifies and prolongs adrenergic stimulation of HERG K+ channel activity. EMBO J. 2002, 21:1889-1898.
    • (2002) EMBO J. , vol.21 , pp. 1889-1898
    • Kagan, A.1    Melman, Y.F.2    Krumerman, A.3    McDonald, T.V.4
  • 27
    • 2342628035 scopus 로고    scopus 로고
    • The mechanism of sodium chloride uptake in hyperregulating aquatic animals
    • Kirschner L.B. The mechanism of sodium chloride uptake in hyperregulating aquatic animals. J. Exp. Biol. 2004, 207:1439-1452.
    • (2004) J. Exp. Biol. , vol.207 , pp. 1439-1452
    • Kirschner, L.B.1
  • 28
    • 0346783283 scopus 로고    scopus 로고
    • Teleost Fh14-3-3a protein protects Xenopus oocytes from hyperosmolality
    • Kohn A., Chakravarty D., Kultz D. Teleost Fh14-3-3a protein protects Xenopus oocytes from hyperosmolality. J. Exp. Zool. Part A 2003, 299:103-109.
    • (2003) J. Exp. Zool. Part A , vol.299 , pp. 103-109
    • Kohn, A.1    Chakravarty, D.2    Kultz, D.3
  • 29
    • 0035746265 scopus 로고    scopus 로고
    • A novel 14-3-3 gene is osmoregulated in gill epithelium of the euryhaline teleost Fundulus heteroclitus
    • Kültz D., Chakravarty D., Adilakshmi T. A novel 14-3-3 gene is osmoregulated in gill epithelium of the euryhaline teleost Fundulus heteroclitus. J. Exp. Biol. 2001, 204:2975-2985.
    • (2001) J. Exp. Biol. , vol.204 , pp. 2975-2985
    • Kültz, D.1    Chakravarty, D.2    Adilakshmi, T.3
  • 30
    • 0034607266 scopus 로고    scopus 로고
    • Gill Na,K-ATPase in the spiny lobster Palinurus elephas and other marine osmoconformers. Adaptiveness of enzymes from osmoconformity to hyperregulation
    • Lucu C., Devescovi M., Skaramuca B., Kozul V.V. Gill Na,K-ATPase in the spiny lobster Palinurus elephas and other marine osmoconformers. Adaptiveness of enzymes from osmoconformity to hyperregulation. J. Exp. Mar. Bio. Ecol. 2000, 246:163-178.
    • (2000) J. Exp. Mar. Bio. Ecol. , vol.246 , pp. 163-178
    • Lucu, C.1    Devescovi, M.2    Skaramuca, B.3    Kozul, V.V.4
  • 31
    • 0038020133 scopus 로고    scopus 로고
    • Na++K+-ATPase in gills of aquatic crustacea
    • Lucu C., Towle D.W. Na++K+-ATPase in gills of aquatic crustacea. Comp. Biochem. Physiol. A 2003, 135:195-214.
    • (2003) Comp. Biochem. Physiol. A , vol.135 , pp. 195-214
    • Lucu, C.1    Towle, D.W.2
  • 32
    • 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
  • 33
    • 0001603801 scopus 로고
    • Osmotic and ionic regulation. In: Mantel, L.H. (Ed.), The Biology of Crustacea. Internal Anatomy and Physiological Regulation. Academic Press, New York
    • Mantel, L.H., Farmer, L.L., 1983. Osmotic and ionic regulation. In: Mantel, L.H. (Ed.), The Biology of Crustacea. Internal Anatomy and Physiological Regulation, vol. 5. Academic Press, New York, pp. 53-161.
    • (1983) , vol.5 , pp. 53-161
    • Mantel, L.H.1    Farmer, L.L.2
  • 34
    • 24344460521 scopus 로고    scopus 로고
    • 14-3-3 proteins-an update
    • Mhawech P. 14-3-3 proteins-an update. Cell Res. 2005, 15:228-236.
    • (2005) Cell Res. , vol.15 , pp. 228-236
    • Mhawech, P.1
  • 35
    • 0034193428 scopus 로고    scopus 로고
    • The plant plasma membrane H+-ATPase: structure, function and regulation
    • Morsomme P., Boutry M. The plant plasma membrane H+-ATPase: structure, function and regulation. Biochim. Biophys. Acta 2000, 1465:1-16.
    • (2000) Biochim. Biophys. Acta , vol.1465 , pp. 1-16
    • Morsomme, P.1    Boutry, M.2
  • 37
    • 0030203863 scopus 로고    scopus 로고
    • TreeView: an application to display phylogenetic trees on personal computers
    • Page R.D. TreeView: an application to display phylogenetic trees on personal computers. Comput. Appl. Biosci. 1996, 12:357-358.
    • (1996) Comput. Appl. Biosci. , vol.12 , pp. 357-358
    • Page, R.D.1
  • 38
    • 33746869267 scopus 로고    scopus 로고
    • Effects of salinity and pH on immune parameters of the white shrimp Litopenaeus vannamei
    • Pan L.Q., Jiang L.X., Miao J.J. Effects of salinity and pH on immune parameters of the white shrimp Litopenaeus vannamei. J. Shellfish. Res. 2005, 24:1223-1227.
    • (2005) J. Shellfish. Res. , vol.24 , pp. 1223-1227
    • Pan, L.Q.1    Jiang, L.X.2    Miao, J.J.3
  • 39
    • 36649006233 scopus 로고    scopus 로고
    • Effects of salinity and pH on ion-transport enzyme activities, survival and growth of Litopenaeus vannamei postlarvae
    • Pan L.Q., Zhang L.J., Liu H.Y. Effects of salinity and pH on ion-transport enzyme activities, survival and growth of Litopenaeus vannamei postlarvae. Aquaculture Asia 2007, 273:711-720.
    • (2007) Aquaculture Asia , vol.273 , pp. 711-720
    • Pan, L.Q.1    Zhang, L.J.2    Liu, H.Y.3
  • 40
    • 0029108476 scopus 로고
    • Osmotic regulation in crustaceans
    • Péqueux A. Osmotic regulation in crustaceans. J. Crustacean Biol. 1995, 15:1-60.
    • (1995) J. Crustacean Biol. , vol.15 , pp. 1-60
    • Péqueux, A.1
  • 42
    • 0034093470 scopus 로고    scopus 로고
    • Active osmoregulatory ion uptake across the pleopods of the isopod Idotea baltica (Pallas): Electrophysiological measurements on isolated split endo- and exopodites mounted in a micro-using chamber
    • Postel U., Becker W., Brandt A., Luck-Kopp S., Riestenpatt S., Weihrauch D., Siebers D. Active osmoregulatory ion uptake across the pleopods of the isopod Idotea baltica (Pallas): Electrophysiological measurements on isolated split endo- and exopodites mounted in a micro-using chamber. J. Exp. Biol. 2000, 203:1141-1152.
    • (2000) J. Exp. Biol. , vol.203 , pp. 1141-1152
    • Postel, U.1    Becker, W.2    Brandt, A.3    Luck-Kopp, S.4    Riestenpatt, S.5    Weihrauch, D.6    Siebers, D.7
  • 43
    • 0028025943 scopus 로고
    • Cyclic AMP stimulation of electrogenic uptake of Na+ and Cl- across the gill epithelium of the Chinese crab Eriocheir sinensis
    • Riestenpatt S., Zeiske W., Onken H. Cyclic AMP stimulation of electrogenic uptake of Na+ and Cl- across the gill epithelium of the Chinese crab Eriocheir sinensis. J. Exp. Biol. 1994, 188:159-174.
    • (1994) J. Exp. Biol. , vol.188 , pp. 159-174
    • Riestenpatt, S.1    Zeiske, W.2    Onken, H.3
  • 45
    • 0032076829 scopus 로고    scopus 로고
    • 14-3-3 proteins are part of an abscisic acid-VIVIPAROUS1 (VP1) response complex in the Em promoter and interact with VP1 and EmBP1
    • Schultz T.F., Medina J., Hill A., Quatrano R.S. 14-3-3 proteins are part of an abscisic acid-VIVIPAROUS1 (VP1) response complex in the Em promoter and interact with VP1 and EmBP1. Plant Cell 1998, 10:837-847.
    • (1998) Plant Cell , vol.10 , pp. 837-847
    • Schultz, T.F.1    Medina, J.2    Hill, A.3    Quatrano, R.S.4
  • 46
    • 77955056499 scopus 로고    scopus 로고
    • Effect of salinity on survival, growth, food consumption and haemolymph osmolality of the pink shrimp Farfantepenaeus subtilis (Pérez-Farfante, 1967)
    • Silva E., Calazans N., Soares M., Soares R., Peixoto S. Effect of salinity on survival, growth, food consumption and haemolymph osmolality of the pink shrimp Farfantepenaeus subtilis (Pérez-Farfante, 1967). Aquaculture 2010, 306:352-356.
    • (2010) Aquaculture , vol.306 , pp. 352-356
    • Silva, E.1    Calazans, N.2    Soares, M.3    Soares, R.4    Peixoto, S.5
  • 50
    • 33947385842 scopus 로고    scopus 로고
    • V-type H+-ATPase and Na+, K+-ATPase in the gills of 13 euryhaline crabs during salinity acclimation
    • Tsai J.R., Lin H.C. V-type H+-ATPase and Na+, K+-ATPase in the gills of 13 euryhaline crabs during salinity acclimation. J. Exp. Biol. 2007, 210:620-627.
    • (2007) J. Exp. Biol. , vol.210 , pp. 620-627
    • Tsai, J.R.1    Lin, H.C.2
  • 51
    • 2342441988 scopus 로고    scopus 로고
    • Isoform-specific differences in rapid nucleocytoplasmic shuttling cause distinct subcellular distributions of 14-3-3 sigma and 14-3-3 zeta
    • van Hemert M.J., Niemantsverdriet M., Schmidt T., Backendorf C., Spaink H.P. Isoform-specific differences in rapid nucleocytoplasmic shuttling cause distinct subcellular distributions of 14-3-3 sigma and 14-3-3 zeta. J. Cell Sci. 2004, 117:1411-1420.
    • (2004) J. Cell Sci. , vol.117 , pp. 1411-1420
    • van Hemert, M.J.1    Niemantsverdriet, M.2    Schmidt, T.3    Backendorf, C.4    Spaink, H.P.5
  • 52
    • 2942572321 scopus 로고    scopus 로고
    • Molecular mechanisms and regulation of K+ transport in higher plants
    • Véry A.A., Sentenac H. Molecular mechanisms and regulation of K+ transport in higher plants. Annu. Rev. Plant Biol. 2003, 54:575-603.
    • (2003) Annu. Rev. Plant Biol. , vol.54 , pp. 575-603
    • Véry, A.A.1    Sentenac, H.2
  • 53
    • 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., 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.5    Lo, C.F.6
  • 54
    • 44149122571 scopus 로고    scopus 로고
    • Proteomic analysis of the response to high-salinity stress in Physcomitrella patens
    • Wang X., Yang P., Gao Q., Liu X., Kuang T., Shen S., He Y. Proteomic analysis of the response to high-salinity stress in Physcomitrella patens. Planta 2008, 228:167-177.
    • (2008) Planta , vol.228 , pp. 167-177
    • Wang, X.1    Yang, P.2    Gao, Q.3    Liu, X.4    Kuang, T.5    Shen, S.6    He, Y.7
  • 55
    • 76149097508 scopus 로고    scopus 로고
    • Identification of a functional splice variant of 14-3-3E1 in rainbow trout
    • Wanna W., Rexroad C.E., Yao J. Identification of a functional splice variant of 14-3-3E1 in rainbow trout. Mar. Biotechnol (NY). 2010, 12:70-80.
    • (2010) Mar. Biotechnol (NY). , vol.12 , pp. 70-80
    • Wanna, W.1    Rexroad, C.E.2    Yao, J.3
  • 56
    • 13144306138 scopus 로고    scopus 로고
    • Ion-motive ATPases and active, transbranchial NaCl uptake in the red freshwater crab, Dilocarcinus pagei (Decapoda, Trichodactylidae)
    • Weihrauch D., McNamara J.C., Towle D.W., Onken H. Ion-motive ATPases and active, transbranchial NaCl uptake in the red freshwater crab, Dilocarcinus pagei (Decapoda, Trichodactylidae). J. Exp. Biol. 2004, 207:4623-4631.
    • (2004) J. Exp. Biol. , vol.207 , pp. 4623-4631
    • Weihrauch, D.1    McNamara, J.C.2    Towle, D.W.3    Onken, H.4
  • 57
    • 0000042195 scopus 로고
    • Prawn biology and culture.
    • Wickins, J.,1976. Prawn biology and culture. Oceanogr. Mar. Biol. Ann. 14, 435-507.
    • (1976) Oceanogr. Mar. Biol. Ann. , vol.14 , pp. 435-507
    • Wickins, J.1
  • 58
    • 33750461583 scopus 로고    scopus 로고
    • Expression profiling of the 14-3-3 gene family in response to salt stress and potassium and iron deficiencies in young tomato (Solanum lycopersicum) roots: analysis by real-time RT-PCR
    • Xu W.F., Shi W.M. Expression profiling of the 14-3-3 gene family in response to salt stress and potassium and iron deficiencies in young tomato (Solanum lycopersicum) roots: analysis by real-time RT-PCR. Ann. Bot. 2006, 98:965-974.
    • (2006) Ann. Bot. , vol.98 , pp. 965-974
    • Xu, W.F.1    Shi, W.M.2
  • 59
    • 38349100547 scopus 로고    scopus 로고
    • Mechanisms of salt tolerance in transgenic Arabidopsis thaliana constitutively overexpressing the tomato 14-3-3 protein TFT7
    • Xu W.F., Shi W.M. Mechanisms of salt tolerance in transgenic Arabidopsis thaliana constitutively overexpressing the tomato 14-3-3 protein TFT7. Plant Soil 2007, 301:17-28.
    • (2007) Plant Soil , vol.301 , pp. 17-28
    • Xu, W.F.1    Shi, W.M.2
  • 60
    • 0031214265 scopus 로고    scopus 로고
    • Cloning and expression of an Arabidopsis gene encoding a putative peroxisomal ascorbate peroxidase
    • Zhang H., Wang J., Nickel U., Allen R.D., Goodman H.M. Cloning and expression of an Arabidopsis gene encoding a putative peroxisomal ascorbate peroxidase. Plant Mol. Biol. 1997, 34:967-971.
    • (1997) Plant Mol. Biol. , vol.34 , pp. 967-971
    • Zhang, H.1    Wang, J.2    Nickel, U.3    Allen, R.D.4    Goodman, H.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.