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Volumn 37, Issue 7, 2007, Pages 763-776

Gene induction by desiccation stress in the entomopathogenic nematode Steinernema carpocapsae reveals parallels with drought tolerance mechanisms in plants

Author keywords

Anhydrobiosis; C type lectin; Desiccation tolerance; EST; Fatty acid desaturase; LEA; Nematode; Steinernema carpocapsae

Indexed keywords

LATE EMBRYOGENIC ABUNDANT PROTEIN; LECTIN; MEMBRANE PROTEIN; PROTEIN; REACTIVE OXYGEN METABOLITE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 34247482197     PISSN: 00207519     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijpara.2006.12.015     Document Type: Article
Times cited : (34)

References (86)
  • 1
    • 0344719188 scopus 로고    scopus 로고
    • Caenorhabditis elegans has scores of hedgehog-related genes: sequence and expression analysis
    • Aspöck G., Kagoshima H., Niklaus G., and Burglin T.R. Caenorhabditis elegans has scores of hedgehog-related genes: sequence and expression analysis. Genome Res. 9 (1999) 909-923
    • (1999) Genome Res. , vol.9 , pp. 909-923
    • Aspöck, G.1    Kagoshima, H.2    Niklaus, G.3    Burglin, T.R.4
  • 3
    • 0031922488 scopus 로고    scopus 로고
    • Isolation and characterization of genes expressed during early events of the dehydration process in the resurrection plant Craterostigma plantagineum
    • Bockel C., Salamini F., and Bartels D. Isolation and characterization of genes expressed during early events of the dehydration process in the resurrection plant Craterostigma plantagineum. J. Plant Physiol. 152 (1998) 158-166
    • (1998) J. Plant Physiol. , vol.152 , pp. 158-166
    • Bockel, C.1    Salamini, F.2    Bartels, D.3
  • 4
    • 0036139519 scopus 로고    scopus 로고
    • Differential expression of genes coding for ribosomal proteins in different human tissues
    • Bortoluzzi S., d'Alessi F., Romualdi C., and Danieli G.A. Differential expression of genes coding for ribosomal proteins in different human tissues. Bioinformatics 17 (2001) 1152-1157
    • (2001) Bioinformatics , vol.17 , pp. 1152-1157
    • Bortoluzzi, S.1    d'Alessi, F.2    Romualdi, C.3    Danieli, G.A.4
  • 5
    • 27244456225 scopus 로고    scopus 로고
    • Osmotic signaling in plants. Multiple pathways mediated by emerging kinase families
    • Boudsocq M., and Lauriere C. Osmotic signaling in plants. Multiple pathways mediated by emerging kinase families. Plant Physiol. 138 (2005) 1185-1194
    • (2005) Plant Physiol. , vol.138 , pp. 1185-1194
    • Boudsocq, M.1    Lauriere, C.2
  • 6
    • 0037034885 scopus 로고    scopus 로고
    • Anhydrobiosis - Plant desiccation gene found in a nematode
    • Browne J., Tunnacliffe A., and Burnell A. Anhydrobiosis - Plant desiccation gene found in a nematode. Nature 416 (2002) 38
    • (2002) Nature , vol.416 , pp. 38
    • Browne, J.1    Tunnacliffe, A.2    Burnell, A.3
  • 7
    • 4143088129 scopus 로고    scopus 로고
    • Dehydration-specific induction of hydrophilic protein genes in the anhydrobiotic nematode Aphelenchus avenae
    • Browne J.A., Dolan K.M., Tyson T., Goyal K., Tunnacliffe A., and Burnell A.M. Dehydration-specific induction of hydrophilic protein genes in the anhydrobiotic nematode Aphelenchus avenae. Eukaryot. Cell 3 (2004) 966-975
    • (2004) Eukaryot. Cell , vol.3 , pp. 966-975
    • Browne, J.A.1    Dolan, K.M.2    Tyson, T.3    Goyal, K.4    Tunnacliffe, A.5    Burnell, A.M.6
  • 8
    • 27544504430 scopus 로고    scopus 로고
    • Alternate metabolism during the dauer stage of the nematode Caenorhabditis elegans
    • Burnell A.M., Houthoofd K., O'Hanlon K., and Vanfleteren J.R. Alternate metabolism during the dauer stage of the nematode Caenorhabditis elegans. Exp. Gerontol. 40 (2005) 850-856
    • (2005) Exp. Gerontol. , vol.40 , pp. 850-856
    • Burnell, A.M.1    Houthoofd, K.2    O'Hanlon, K.3    Vanfleteren, J.R.4
  • 9
    • 0035819072 scopus 로고    scopus 로고
    • UNC-16, a JNK-signaling scaffold protein, regulates vesicle transport in C. elegans
    • Byrd D.T., Kawasaki M., Walcoff M., Hisamoto N., Matsumoto K., and Jin Y.S. UNC-16, a JNK-signaling scaffold protein, regulates vesicle transport in C. elegans. Neuron 32 (2001) 787-800
    • (2001) Neuron , vol.32 , pp. 787-800
    • Byrd, D.T.1    Kawasaki, M.2    Walcoff, M.3    Hisamoto, N.4    Matsumoto, K.5    Jin, Y.S.6
  • 10
    • 27644441980 scopus 로고    scopus 로고
    • Cross-stress tolerance and expression of stress-related proteins in osmotically desiccated entomopathogenic Steinernema feltiae IS-6
    • Chen S., Gollop N., and Glazer I. Cross-stress tolerance and expression of stress-related proteins in osmotically desiccated entomopathogenic Steinernema feltiae IS-6. Parasitology 131 (2005) 695-703
    • (2005) Parasitology , vol.131 , pp. 695-703
    • Chen, S.1    Gollop, N.2    Glazer, I.3
  • 12
    • 0035154353 scopus 로고    scopus 로고
    • The Caenorhabditis elegans odr-2 gene encodes a novel Ly-6-related protein required for olfaction
    • Chou J.H., Bargmann C.I., and Sengupta P. The Caenorhabditis elegans odr-2 gene encodes a novel Ly-6-related protein required for olfaction. Genetics 157 (2001) 211-224
    • (2001) Genetics , vol.157 , pp. 211-224
    • Chou, J.H.1    Bargmann, C.I.2    Sengupta, P.3
  • 13
    • 0031007034 scopus 로고    scopus 로고
    • Dehydrins: A commonality in the response of plants to dehydration and low temperature
    • Close T.J. Dehydrins: A commonality in the response of plants to dehydration and low temperature. Physiol. Plant 100 (1997) 291-296
    • (1997) Physiol. Plant , vol.100 , pp. 291-296
    • Close, T.J.1
  • 14
    • 0019972655 scopus 로고
    • Induction of anhydrobiosis - membrane changes during drying
    • Crowe J.H., and Crowe L.M. Induction of anhydrobiosis - membrane changes during drying. Cryobiology 19 (1982) 317-328
    • (1982) Cryobiology , vol.19 , pp. 317-328
    • Crowe, J.H.1    Crowe, L.M.2
  • 15
    • 0001773626 scopus 로고
    • Effects of dehydration on membranes and membrane stabilization at low water activities
    • Chapman D. (Ed), Academic Press, London
    • Crowe J.H., and Crowe L.M. Effects of dehydration on membranes and membrane stabilization at low water activities. In: Chapman D. (Ed). Biological Membranes 5 (1984), Academic Press, London 57-103
    • (1984) Biological Membranes , vol.5 , pp. 57-103
    • Crowe, J.H.1    Crowe, L.M.2
  • 16
    • 0348053809 scopus 로고
    • Preservation of membranes in anhydrobiotic organisms - the role of trehalose
    • Crowe J.H., Crowe L.M., and Chapman D. Preservation of membranes in anhydrobiotic organisms - the role of trehalose. Science 223 (1984) 701-703
    • (1984) Science , vol.223 , pp. 701-703
    • Crowe, J.H.1    Crowe, L.M.2    Chapman, D.3
  • 17
    • 0034644522 scopus 로고    scopus 로고
    • Signal transduction by the JNK group of MAP kinases
    • Davis R.J. Signal transduction by the JNK group of MAP kinases. Cell 103 (2000) 239-252
    • (2000) Cell , vol.103 , pp. 239-252
    • Davis, R.J.1
  • 18
    • 0036668632 scopus 로고    scopus 로고
    • Dealing with osmostress through MAP kinase activation
    • de Nadal E., Alepuz P.M., and Posas F. Dealing with osmostress through MAP kinase activation. EMBO Rep. 3 (2002) 735-740
    • (2002) EMBO Rep. , vol.3 , pp. 735-740
    • de Nadal, E.1    Alepuz, P.M.2    Posas, F.3
  • 19
    • 0034920428 scopus 로고    scopus 로고
    • Lectin-like proteins in model organisms: implications for evolution of carbohydrate-binding activity
    • Dodd R.B., and Drickamer K. Lectin-like proteins in model organisms: implications for evolution of carbohydrate-binding activity. Glycobiology 11 (2001) 71R-79R
    • (2001) Glycobiology , vol.11
    • Dodd, R.B.1    Drickamer, K.2
  • 20
    • 0033428909 scopus 로고    scopus 로고
    • C-type lectin-like domains in Caenorhabditis elegans: predictions from the complete genome sequence
    • Drickamer K., and Dodd R.B. C-type lectin-like domains in Caenorhabditis elegans: predictions from the complete genome sequence. Glycobiology 9 (1999) 1357-1369
    • (1999) Glycobiology , vol.9 , pp. 1357-1369
    • Drickamer, K.1    Dodd, R.B.2
  • 21
    • 0019874708 scopus 로고
    • Developmental biochemistry of cottonseed embryogenesis and germination - changing messenger ribonucleic-acid populations as shown by in vitro and in vivo protein-synthesis.14
    • Dure L., Greenway S.C., and Galau G.A. Developmental biochemistry of cottonseed embryogenesis and germination - changing messenger ribonucleic-acid populations as shown by in vitro and in vivo protein-synthesis.14. Biochemistry 20 (1981) 4162-4168
    • (1981) Biochemistry , vol.20 , pp. 4162-4168
    • Dure, L.1    Greenway, S.C.2    Galau, G.A.3
  • 23
    • 0035022351 scopus 로고    scopus 로고
    • Occurrence of a repeating 11-mer amino acid sequence motif in diverse organisms
    • Dure L. Occurrence of a repeating 11-mer amino acid sequence motif in diverse organisms. Protein Pept. Lett. 8 (2001) 115-122
    • (2001) Protein Pept. Lett. , vol.8 , pp. 115-122
    • Dure, L.1
  • 24
    • 0001364985 scopus 로고
    • A technique for the mass propagation of the DD-136 nematode
    • Dutky S., Thompson J., and Cantwell G. A technique for the mass propagation of the DD-136 nematode. J. Insect Pathol. 6 (1964) 417-422
    • (1964) J. Insect Pathol. , vol.6 , pp. 417-422
    • Dutky, S.1    Thompson, J.2    Cantwell, G.3
  • 25
    • 0034840604 scopus 로고    scopus 로고
    • Mass production of entomopathogenic nematodes for plant protection
    • Ehlers R.U. Mass production of entomopathogenic nematodes for plant protection. Appl. Microbiol. Biotechnol. 56 (2001) 623-633
    • (2001) Appl. Microbiol. Biotechnol. , vol.56 , pp. 623-633
    • Ehlers, R.U.1
  • 26
    • 0348230942 scopus 로고    scopus 로고
    • Glutaredoxins: Glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system
    • Fernandes A.P., and Holmgren A. Glutaredoxins: Glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system. Antiox. Redox Signal 6 (2004) 63-74
    • (2004) Antiox. Redox Signal , vol.6 , pp. 63-74
    • Fernandes, A.P.1    Holmgren, A.2
  • 27
    • 0141744887 scopus 로고    scopus 로고
    • Differential gene expression during desiccation stress in the insect-killing nematode Steinernema feltiae IS-6
    • Gal T.Z., Glazer I., and Koltai H. Differential gene expression during desiccation stress in the insect-killing nematode Steinernema feltiae IS-6. J. Parasitol. 89 (2003) 761-766
    • (2003) J. Parasitol. , vol.89 , pp. 761-766
    • Gal, T.Z.1    Glazer, I.2    Koltai, H.3
  • 28
    • 7644219570 scopus 로고    scopus 로고
    • An LEA group 3 family member is involved in survival of C. elegans during exposure to stress
    • Gal T.Z., Glazer I., and Koltai H. An LEA group 3 family member is involved in survival of C. elegans during exposure to stress. FEBS Lett. 577 (2004) 21-26
    • (2004) FEBS Lett. , vol.577 , pp. 21-26
    • Gal, T.Z.1    Glazer, I.2    Koltai, H.3
  • 29
    • 0034007384 scopus 로고    scopus 로고
    • Highly hydrophilic proteins in prokaryotes and eukaryotes are common during conditions of water deficit
    • Garay-Arroyo A., Colmenero-Flores J.M., Garciarrubio A., and Covarrubias A.A. Highly hydrophilic proteins in prokaryotes and eukaryotes are common during conditions of water deficit. J. Biol. Chem. 275 (2000) 5668-5674
    • (2000) J. Biol. Chem. , vol.275 , pp. 5668-5674
    • Garay-Arroyo, A.1    Colmenero-Flores, J.M.2    Garciarrubio, A.3    Covarrubias, A.A.4
  • 30
    • 0035831429 scopus 로고    scopus 로고
    • Solution structure of the N-terminal domain of the human TFIIH MAT1 subunit - new insights into the RING finger family
    • Gervais V., Busso D., Wasielewski E., Poterszman A., Egly J.M., Thierry J.C., and Kieffer B. Solution structure of the N-terminal domain of the human TFIIH MAT1 subunit - new insights into the RING finger family. J. Biol. Chem. 276 (2001) 7457-7464
    • (2001) J. Biol. Chem. , vol.276 , pp. 7457-7464
    • Gervais, V.1    Busso, D.2    Wasielewski, E.3    Poterszman, A.4    Egly, J.M.5    Thierry, J.C.6    Kieffer, B.7
  • 32
    • 0038305931 scopus 로고    scopus 로고
    • Transition from natively unfolded to folded state induced by desiccation in an anhydrobiotic nematode protein
    • Goyal K., Tisi L., Basran A., Browne J., Burnell A., Zurdo J., and Tunnacliffe A. Transition from natively unfolded to folded state induced by desiccation in an anhydrobiotic nematode protein. J. Biol. Chem. 278 (2003) 12977-12984
    • (2003) J. Biol. Chem. , vol.278 , pp. 12977-12984
    • Goyal, K.1    Tisi, L.2    Basran, A.3    Browne, J.4    Burnell, A.5    Zurdo, J.6    Tunnacliffe, A.7
  • 33
    • 17044405795 scopus 로고    scopus 로고
    • LEA proteins prevent protein aggregation due to water stress
    • Goyal K., Walton L.J., and Tunnacliffe A. LEA proteins prevent protein aggregation due to water stress. Biochem. J. 388 (2005) 151-157
    • (2005) Biochem. J. , vol.388 , pp. 151-157
    • Goyal, K.1    Walton, L.J.2    Tunnacliffe, A.3
  • 34
    • 0002535446 scopus 로고    scopus 로고
    • Formulation and application technology
    • Gaugler R. (Ed), CABI Publishing, Wallingford, UK
    • Grewal P.S. Formulation and application technology. In: Gaugler R. (Ed). Entomopathogenic Nematology (2002), CABI Publishing, Wallingford, UK 265-287
    • (2002) Entomopathogenic Nematology , pp. 265-287
    • Grewal, P.S.1
  • 35
    • 33744528415 scopus 로고    scopus 로고
    • Physiological, genetic, and molecular mechanisms of chemoreception, thermobiosis, and anhydrobiosis in entomopathogenic nematodes
    • Grewal P.S., Bornstein-Forst S., Burnell A.M., Glazer I., and Jagdale G.B. Physiological, genetic, and molecular mechanisms of chemoreception, thermobiosis, and anhydrobiosis in entomopathogenic nematodes. Biol. Control 38 (2006) 54-65
    • (2006) Biol. Control , vol.38 , pp. 54-65
    • Grewal, P.S.1    Bornstein-Forst, S.2    Burnell, A.M.3    Glazer, I.4    Jagdale, G.B.5
  • 36
    • 0028916402 scopus 로고
    • Thermal adaptation in biological-membranes - is homeoviscous adaptation the explanation?
    • Hazel J.R. Thermal adaptation in biological-membranes - is homeoviscous adaptation the explanation?. Annu. Rev. Physiol. 57 (1995) 19-42
    • (1995) Annu. Rev. Physiol. , vol.57 , pp. 19-42
    • Hazel, J.R.1
  • 38
    • 4043084803 scopus 로고    scopus 로고
    • Response of human cells to desiccation: comparison with hyperosmotic stress response
    • Huang Z.B., and Tunnacliffe A. Response of human cells to desiccation: comparison with hyperosmotic stress response. J. Physiol. Lond. 558 (2004) 181-191
    • (2004) J. Physiol. Lond. , vol.558 , pp. 181-191
    • Huang, Z.B.1    Tunnacliffe, A.2
  • 39
    • 0037075542 scopus 로고    scopus 로고
    • Novel modulation of neuronal nicotinic acetylcholine receptors by association with the endogenous prototoxin lynx1
    • Ibańez-Tallon I., Miwa J.M., Wang H.-L., Adams N.C., Crabtree G.W., Sine S.M., and Heintz N. Novel modulation of neuronal nicotinic acetylcholine receptors by association with the endogenous prototoxin lynx1. Neuron 33 (2002) 893-903
    • (2002) Neuron , vol.33 , pp. 893-903
    • Ibańez-Tallon, I.1    Miwa, J.M.2    Wang, H.-L.3    Adams, N.C.4    Crabtree, G.W.5    Sine, S.M.6    Heintz, N.7
  • 42
    • 33646558973 scopus 로고    scopus 로고
    • An EST catalogue from the resurrection plant Selaginella lepidophylla reveals abiotic stress-adaptive genes
    • Iturriaga G., Cushman M.A.F., and Cushman J.C. An EST catalogue from the resurrection plant Selaginella lepidophylla reveals abiotic stress-adaptive genes. Plant Sci. 170 (2006) 1173-1184
    • (2006) Plant Sci. , vol.170 , pp. 1173-1184
    • Iturriaga, G.1    Cushman, M.A.F.2    Cushman, J.C.3
  • 44
    • 0017301265 scopus 로고
    • Non-aging developmental variant of Caenorhabditis elegans
    • Klass M., and Hirsh D. Non-aging developmental variant of Caenorhabditis elegans. Nature 260 (1976) 523-525
    • (1976) Nature , vol.260 , pp. 523-525
    • Klass, M.1    Hirsh, D.2
  • 45
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., and Doolittle R. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157 (1982) 105-132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.2
  • 46
    • 12144264839 scopus 로고    scopus 로고
    • Transcriptional targets of DAF-16 insulin signaling pathway protect C. elegans from extreme hypertonic stress
    • Lamitina S.T., and Strange K. Transcriptional targets of DAF-16 insulin signaling pathway protect C. elegans from extreme hypertonic stress. Am. J. Physiol. 288 (2005) C467-C474
    • (2005) Am. J. Physiol. , vol.288
    • Lamitina, S.T.1    Strange, K.2
  • 47
    • 0033780607 scopus 로고    scopus 로고
    • Desiccation survival of entomopathogenic nematodes of the genus Heterorhabditis
    • Liu Q.Z., and Glazer I. Desiccation survival of entomopathogenic nematodes of the genus Heterorhabditis. Phytoparasitica 28 (2000) 331-340
    • (2000) Phytoparasitica , vol.28 , pp. 331-340
    • Liu, Q.Z.1    Glazer, I.2
  • 48
    • 0031659941 scopus 로고    scopus 로고
    • Structure and expression of fatty acid desaturases
    • Los D.A., and Murata N. Structure and expression of fatty acid desaturases. Biochim. Biophys. Acta 1394 (1998) 3-15
    • (1998) Biochim. Biophys. Acta , vol.1394 , pp. 3-15
    • Los, D.A.1    Murata, N.2
  • 49
    • 73849159982 scopus 로고
    • Structure of liquid-crystalline phases of lipid-water systems
    • Luzzati V., and Husson F. Structure of liquid-crystalline phases of lipid-water systems. J. Cell Biol. 12 (1962) 207-219
    • (1962) J. Cell Biol. , vol.12 , pp. 207-219
    • Luzzati, V.1    Husson, F.2
  • 50
    • 84908597142 scopus 로고
    • Anhydrobiosis in nematodes - carbohydrate and lipid-metabolism during dehydration
    • Madin K.A.C., and Crowe J.H. Anhydrobiosis in nematodes - carbohydrate and lipid-metabolism during dehydration. J. Exp. Zool. 193 (1975) 335-342
    • (1975) J. Exp. Zool. , vol.193 , pp. 335-342
    • Madin, K.A.C.1    Crowe, J.H.2
  • 51
    • 0029030017 scopus 로고
    • Localized Bicaudal-C RNA encodes a protein containing a KH domain, the RNA-binding motif of FMR1
    • Mahone M., Saffman E.E., and Lasko P.F. Localized Bicaudal-C RNA encodes a protein containing a KH domain, the RNA-binding motif of FMR1. EMBO J. 14 (1995) 2043-2055
    • (1995) EMBO J. , vol.14 , pp. 2043-2055
    • Mahone, M.1    Saffman, E.E.2    Lasko, P.F.3
  • 53
    • 33748911199 scopus 로고    scopus 로고
    • Ribosomal protein gene regulation: what about plants?
    • McIntosh K.B., and Bonham-Smith P.C. Ribosomal protein gene regulation: what about plants?. Can. J. Bot. 84 (2006) 342-362
    • (2006) Can. J. Bot. , vol.84 , pp. 342-362
    • McIntosh, K.B.1    Bonham-Smith, P.C.2
  • 54
    • 21444454736 scopus 로고    scopus 로고
    • Emerging MAP kinase pathways in plant stress signalling
    • Nakagami H., Pitzschke A., and Hirt H. Emerging MAP kinase pathways in plant stress signalling. Trends Plant Sci. 10 (2005) 339-346
    • (2005) Trends Plant Sci. , vol.10 , pp. 339-346
    • Nakagami, H.1    Pitzschke, A.2    Hirt, H.3
  • 55
    • 33645101851 scopus 로고    scopus 로고
    • Regulons involved in osmotic stress-responsive and cold stress-responsive gene expression in plants
    • Nakashima K., and Yamaguchi-Shinozaki K. Regulons involved in osmotic stress-responsive and cold stress-responsive gene expression in plants. Physiol. Plantarum 126 (2006) 62-71
    • (2006) Physiol. Plantarum , vol.126 , pp. 62-71
    • Nakashima, K.1    Yamaguchi-Shinozaki, K.2
  • 56
    • 0037129982 scopus 로고    scopus 로고
    • Characterization of a novel mammalian phosphatase having sequence similarity to Schizosaccharomyces pombe PHO2 and Saccharomyces cerevisiae PHO13
    • Ndubuisil M.I., Kwok B.H.B., Vervoort J., Koh B.D., Elofsson M., and Crews C.M. Characterization of a novel mammalian phosphatase having sequence similarity to Schizosaccharomyces pombe PHO2 and Saccharomyces cerevisiae PHO13. Biochemistry 41 (2002) 7841-7848
    • (2002) Biochemistry , vol.41 , pp. 7841-7848
    • Ndubuisil, M.I.1    Kwok, B.H.B.2    Vervoort, J.3    Koh, B.D.4    Elofsson, M.5    Crews, C.M.6
  • 57
    • 0031820692 scopus 로고    scopus 로고
    • The effect of day of emergence from the insect cadaver on the behavior and environmental tolerances of infective juveniles of the entomopathogenic nematode Heterorhabditis megidis (strain UK211)
    • O'Leary S.A., Stack C.M., Chubb M.A., and Burnell A.M. The effect of day of emergence from the insect cadaver on the behavior and environmental tolerances of infective juveniles of the entomopathogenic nematode Heterorhabditis megidis (strain UK211). J. Parasitol. 84 (1998) 665-672
    • (1998) J. Parasitol. , vol.84 , pp. 665-672
    • O'Leary, S.A.1    Stack, C.M.2    Chubb, M.A.3    Burnell, A.M.4
  • 58
    • 0034864423 scopus 로고    scopus 로고
    • Behavioural and physiological responses of infective juveniles of the entomopathogenic nematode Heterorhabditis to desiccation
    • O'Leary S.A., Power A.P., Stack C.M., and Burnell A.M. Behavioural and physiological responses of infective juveniles of the entomopathogenic nematode Heterorhabditis to desiccation. Biol. Control 46 (2001) 345-362
    • (2001) Biol. Control , vol.46 , pp. 345-362
    • O'Leary, S.A.1    Power, A.P.2    Stack, C.M.3    Burnell, A.M.4
  • 59
    • 0031450537 scopus 로고    scopus 로고
    • Desiccation survival and water contents of entomopathogenic nematodes, Steinernema spp. (Rhabditida: Steinernematidae)
    • Patel M.N., Perry R.N., and Wright D.J. Desiccation survival and water contents of entomopathogenic nematodes, Steinernema spp. (Rhabditida: Steinernematidae). Int. J. Parasitol. 27 (1997) 61-70
    • (1997) Int. J. Parasitol. , vol.27 , pp. 61-70
    • Patel, M.N.1    Perry, R.N.2    Wright, D.J.3
  • 60
    • 0034655983 scopus 로고    scopus 로고
    • Identification and characterization of an animal Delta(12) fatty acid desaturase gene by heterologous expression in Saccharomyces cerevisiae
    • Peyou-Ndi M.M., Watts J.L., and Browse J. Identification and characterization of an animal Delta(12) fatty acid desaturase gene by heterologous expression in Saccharomyces cerevisiae. Arch. Biochem. Biophys. 376 (2000) 399-408
    • (2000) Arch. Biochem. Biophys. , vol.376 , pp. 399-408
    • Peyou-Ndi, M.M.1    Watts, J.L.2    Browse, J.3
  • 61
    • 0036581160 scopus 로고    scopus 로고
    • Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR
    • Pfaffl M.W., Horgan G.W., and Dempfle L. Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR. Nucleic. Acids Res. 30 (2002) 36
    • (2002) Nucleic. Acids Res. , vol.30 , pp. 36
    • Pfaffl, M.W.1    Horgan, G.W.2    Dempfle, L.3
  • 62
    • 0027948550 scopus 로고
    • Desiccation tolerance of prokaryotes
    • Potts M. Desiccation tolerance of prokaryotes. Micrbiol Rev. 58 (1994) 755-805
    • (1994) Micrbiol Rev. , vol.58 , pp. 755-805
    • Potts, M.1
  • 63
    • 0001104583 scopus 로고    scopus 로고
    • Genetic and environmental regulation of dauer larva development
    • Riddle D.L., Blumenthal T., Meyer B.J., and Priess J.R. (Eds), Cold Spring Harbor Laboratory Press, New York
    • Riddle D.L., and Albert P.S. Genetic and environmental regulation of dauer larva development. In: Riddle D.L., Blumenthal T., Meyer B.J., and Priess J.R. (Eds). C. elegans II (1997), Cold Spring Harbor Laboratory Press, New York 739-768
    • (1997) C. elegans II , pp. 739-768
    • Riddle, D.L.1    Albert, P.S.2
  • 64
    • 0346997045 scopus 로고    scopus 로고
    • The fence and picket structure of the plasma membrane of live cells as revealed by single molecule techniques (Review)
    • Ritchie K., Iino R., Fujiwara T., Murase K., and Kusumi A. The fence and picket structure of the plasma membrane of live cells as revealed by single molecule techniques (Review). Mol. Membr. Biol. 20 (2003) 13-18
    • (2003) Mol. Membr. Biol. , vol.20 , pp. 13-18
    • Ritchie, K.1    Iino, R.2    Fujiwara, T.3    Murase, K.4    Kusumi, A.5
  • 66
    • 9144254513 scopus 로고    scopus 로고
    • Regulation of the osmoregulatory HOG MAPK cascade in yeast
    • Saito H., and Tatebayashi K. Regulation of the osmoregulatory HOG MAPK cascade in yeast. J. Biochem. 136 (2004) 267-272
    • (2004) J. Biochem. , vol.136 , pp. 267-272
    • Saito, H.1    Tatebayashi, K.2
  • 67
    • 33644513076 scopus 로고    scopus 로고
    • Control of Plutella xylostella using polymer-formulated Steinernema carpocapsae and Bacillus thuringiensis in cabbage fields
    • Schroer S., Yi X.L., and Ehlers R.U. Control of Plutella xylostella using polymer-formulated Steinernema carpocapsae and Bacillus thuringiensis in cabbage fields. Nematology 7 (2005) 37-44
    • (2005) Nematology , vol.7 , pp. 37-44
    • Schroer, S.1    Yi, X.L.2    Ehlers, R.U.3
  • 68
    • 0041976072 scopus 로고    scopus 로고
    • Comparison of beneficial traits among strains of the entomopathogenic nematode, Steinernema carpocapsae, for control of Curculio caryae (Coleoptera: Curculionidae)
    • Shapiro-Ilan D.I., Stuart R., and McCoy C.W. Comparison of beneficial traits among strains of the entomopathogenic nematode, Steinernema carpocapsae, for control of Curculio caryae (Coleoptera: Curculionidae). Biol. Control 28 (2003) 129-136
    • (2003) Biol. Control , vol.28 , pp. 129-136
    • Shapiro-Ilan, D.I.1    Stuart, R.2    McCoy, C.W.3
  • 69
    • 0032852479 scopus 로고    scopus 로고
    • CREB: A stimulus-induced transcription factor activated by a diverse array of extracellular signals
    • Shaywitz A.J., and Greenberg M.E. CREB: A stimulus-induced transcription factor activated by a diverse array of extracellular signals. Annu. Rev. Biochem. 68 (1999) 821-861
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 821-861
    • Shaywitz, A.J.1    Greenberg, M.E.2
  • 70
  • 71
    • 0029187038 scopus 로고
    • Entomopathogenic nematodes for the biological control of insects
    • Smart G.C. Entomopathogenic nematodes for the biological control of insects. J. Nematol. 27 (1995) 529-534
    • (1995) J. Nematol. , vol.27 , pp. 529-534
    • Smart, G.C.1
  • 72
    • 0037227141 scopus 로고    scopus 로고
    • Exogenous reference RNA for normalization of real-time quantitative PCR
    • Smith R.D., Brown B., Ikonomi P., and Schecter A.N. Exogenous reference RNA for normalization of real-time quantitative PCR. Biotechniques 34 (2003) 88-91
    • (2003) Biotechniques , vol.34 , pp. 88-91
    • Smith, R.D.1    Brown, B.2    Ikonomi, P.3    Schecter, A.N.4
  • 73
    • 0033003716 scopus 로고    scopus 로고
    • Desiccation survival of the entomopathogenic nematode Steinernema feltiae: induction of anhydrobiosis
    • Solomon A., Paperna I., and Glazer I. Desiccation survival of the entomopathogenic nematode Steinernema feltiae: induction of anhydrobiosis. Nematology 1 (1999) 61-68
    • (1999) Nematology , vol.1 , pp. 61-68
    • Solomon, A.1    Paperna, I.2    Glazer, I.3
  • 74
    • 0033814380 scopus 로고    scopus 로고
    • Desiccation stress of entomopathogenic nematodes induces the accumulation of a novel heat-stable protein
    • Solomon A., Salomon R., Paperna I., and Glazer I. Desiccation stress of entomopathogenic nematodes induces the accumulation of a novel heat-stable protein. Parasitology 121 (2000) 409-416
    • (2000) Parasitology , vol.121 , pp. 409-416
    • Solomon, A.1    Salomon, R.2    Paperna, I.3    Glazer, I.4
  • 75
    • 0030606605 scopus 로고    scopus 로고
    • Cloning, sequencing and mapping of a manganese superoxide dismutase gene of the nematode Caenorhabditis elegans
    • Suzuki N.I.K., Yasuda K., and Ishii N. Cloning, sequencing and mapping of a manganese superoxide dismutase gene of the nematode Caenorhabditis elegans. DNA Res. 3 (1996) 171-174
    • (1996) DNA Res. , vol.3 , pp. 171-174
    • Suzuki, N.I.K.1    Yasuda, K.2    Ishii, N.3
  • 76
    • 2942755628 scopus 로고    scopus 로고
    • Isolation of a new member of group 3 late embryogenesis abundant protein gene from a halotorelant green alga by a functional expression screening with cyanobacterial cells
    • Tanaka S., Ikeda K., and Miyasaka H. Isolation of a new member of group 3 late embryogenesis abundant protein gene from a halotorelant green alga by a functional expression screening with cyanobacterial cells. FEMS Microbiol. Lett. 236 (2004) 41-45
    • (2004) FEMS Microbiol. Lett. , vol.236 , pp. 41-45
    • Tanaka, S.1    Ikeda, K.2    Miyasaka, H.3
  • 77
    • 0032054379 scopus 로고    scopus 로고
    • A specific alkaline phosphatase from Saccharomyces cerevisiae with protein phosphatase activity
    • Tuleva B., Vasileva-Tonkova E., and Galabova D. A specific alkaline phosphatase from Saccharomyces cerevisiae with protein phosphatase activity. FEMS Microbiol Lett. 161 (1998) 139-144
    • (1998) FEMS Microbiol Lett. , vol.161 , pp. 139-144
    • Tuleva, B.1    Vasileva-Tonkova, E.2    Galabova, D.3
  • 78
    • 24144463133 scopus 로고    scopus 로고
    • A putative LEA protein, but no trehalose, is present in anhydrobiotic bdelloid rotifers
    • Tunnacliffe A., Lapinski J., and McGee B. A putative LEA protein, but no trehalose, is present in anhydrobiotic bdelloid rotifers. Hydrobiologia 546 (2005) 315-321
    • (2005) Hydrobiologia , vol.546 , pp. 315-321
    • Tunnacliffe, A.1    Lapinski, J.2    McGee, B.3
  • 81
    • 0034669882 scopus 로고    scopus 로고
    • Why are natively unfolded" proteins unstructured under physiologic conditions?
    • Uversky V.N., Gillespie J.R., and Fink A.L. Why are natively unfolded" proteins unstructured under physiologic conditions?. Proteins. 41 (2000) 415-427
    • (2000) Proteins. , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 82
    • 0037136552 scopus 로고    scopus 로고
    • A regulatory cytoplasmic poly(A) polymerase in Caenorhabditis elegans
    • Wang L.T., Eckmann C.R., Kadyk L.C., Wickens M., and Kimble J. A regulatory cytoplasmic poly(A) polymerase in Caenorhabditis elegans. Nature 419 (2002) 312-316
    • (2002) Nature , vol.419 , pp. 312-316
    • Wang, L.T.1    Eckmann, C.R.2    Kadyk, L.C.3    Wickens, M.4    Kimble, J.5
  • 83
    • 2942549269 scopus 로고    scopus 로고
    • LEAping to conclusions: a computational reanalysis of late embryogenesis abundant proteins and their possible roles
    • Wise M.J. LEAping to conclusions: a computational reanalysis of late embryogenesis abundant proteins and their possible roles. BMC Bioinformatics. 4 (2003) 52
    • (2003) BMC Bioinformatics. , vol.4 , pp. 52
    • Wise, M.J.1
  • 84
    • 0742323272 scopus 로고    scopus 로고
    • POPP the question: what do LEA proteins do?
    • Wise M.J., and Tunnacliffe A. POPP the question: what do LEA proteins do?. Trends Plant Sci. 9 (2004) 13-17
    • (2004) Trends Plant Sci. , vol.9 , pp. 13-17
    • Wise, M.J.1    Tunnacliffe, A.2
  • 85
    • 13744261322 scopus 로고    scopus 로고
    • Organization of cis-acting regulatory elements in osmotic- and cold-stress-responsive promoters
    • Yamaguchi-Shinozaki K., and Shinozaki K. Organization of cis-acting regulatory elements in osmotic- and cold-stress-responsive promoters. Trends Plant Sci. 10 (2005) 88-94
    • (2005) Trends Plant Sci. , vol.10 , pp. 88-94
    • Yamaguchi-Shinozaki, K.1    Shinozaki, K.2
  • 86
    • 29144452851 scopus 로고    scopus 로고
    • The C-type lectin-like domain superfamily
    • Zelensky A.N., and Gready J.E. The C-type lectin-like domain superfamily. FEBS J. 272 (2005) 6179-6217
    • (2005) FEBS J. , vol.272 , pp. 6179-6217
    • Zelensky, A.N.1    Gready, J.E.2


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