메뉴 건너뛰기




Volumn 4, Issue 3, 2011, Pages 181-188

Expressed sequence tags from heat-shocked seagrass Zostera noltii (Hornemann) from its southern distribution range

Author keywords

Abiotic stress response; Climate change; EST library; High temperature stress

Indexed keywords

2' HYDROXYISOFLAVONE REDUCTASE; 2'-HYDROXYISOFLAVONE REDUCTASE; FLAVOPROTEIN; GLUTAMATE AMMONIA LIGASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; MICROSATELLITE DNA; OXIDOREDUCTASE; PEPTIDYLPROLYL ISOMERASE; TRANSCRIPTOME; VEGETABLE PROTEIN;

EID: 80051932338     PISSN: 18747787     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.margen.2011.04.003     Document Type: Article
Times cited : (27)

References (58)
  • 1
    • 27944470138 scopus 로고    scopus 로고
    • Heat-shock cognate 70 is required for the activation of heat-shock factor 1 in mammalian cells
    • Ahn S.G., Kim S.A., Yoon J.H., Vacratsis P. Heat-shock cognate 70 is required for the activation of heat-shock factor 1 in mammalian cells. Biochem. J. 2005, 392:145-152.
    • (2005) Biochem. J. , vol.392 , pp. 145-152
    • Ahn, S.G.1    Kim, S.A.2    Yoon, J.H.3    Vacratsis, P.4
  • 3
    • 37449004250 scopus 로고    scopus 로고
    • Crystal structure of the NADH: quinone oxidoreductase WrbA from Escherichia coli
    • Andrade S.L.A., Patridge E.V., Ferry J.G., Einsle O. Crystal structure of the NADH: quinone oxidoreductase WrbA from Escherichia coli. J. Bacteriol. 2007, 189:9101-9107.
    • (2007) J. Bacteriol. , vol.189 , pp. 9101-9107
    • Andrade, S.L.A.1    Patridge, E.V.2    Ferry, J.G.3    Einsle, O.4
  • 4
    • 0037059015 scopus 로고    scopus 로고
    • A subclass of plant heat shock cognate 70 chaperones carries a motif that facilitates trafficking through plasmodesmata
    • Aoki K., Kragler F., Xoconostle-Cazares B., Lucas W.J. A subclass of plant heat shock cognate 70 chaperones carries a motif that facilitates trafficking through plasmodesmata. Proc. Natl. Acad. Sci. USA 2002, 99:16342-16347.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 16342-16347
    • Aoki, K.1    Kragler, F.2    Xoconostle-Cazares, B.3    Lucas, W.J.4
  • 5
    • 34248176724 scopus 로고    scopus 로고
    • Heat shock genes-integrating cell survival and death
    • Arya R., Mallik M., Lakhotia S.C. Heat shock genes-integrating cell survival and death. J. Biosci. 2007, 32:595-610.
    • (2007) J. Biosci. , vol.32 , pp. 595-610
    • Arya, R.1    Mallik, M.2    Lakhotia, S.C.3
  • 6
    • 0030681260 scopus 로고    scopus 로고
    • The significance of digital gene expression profiles
    • Audic S., Claverie J.M. The significance of digital gene expression profiles. Genome Res. 1997, 7:986-995.
    • (1997) Genome Res. , vol.7 , pp. 986-995
    • Audic, S.1    Claverie, J.M.2
  • 7
    • 21244499405 scopus 로고    scopus 로고
    • GAPDH as a housekeeping gene: analysis of GAPDH mRNA expression in a panel of 72 human tissues
    • Barber R.D., Harmer D.W., Coleman R.A., Clark B.J. GAPDH as a housekeeping gene: analysis of GAPDH mRNA expression in a panel of 72 human tissues. Physiol. Genomics 2005, 21:389-395.
    • (2005) Physiol. Genomics , vol.21 , pp. 389-395
    • Barber, R.D.1    Harmer, D.W.2    Coleman, R.A.3    Clark, B.J.4
  • 8
    • 26444495615 scopus 로고    scopus 로고
    • Death versus survival: functional interaction between the apoptotic and stress-inducible heat shock protein pathways
    • Beere H.M. Death versus survival: functional interaction between the apoptotic and stress-inducible heat shock protein pathways. J. Clin. Investig. 2005, 115:2633-2639.
    • (2005) J. Clin. Investig. , vol.115 , pp. 2633-2639
    • Beere, H.M.1
  • 9
    • 33847051947 scopus 로고    scopus 로고
    • The molecular ecologist's guide to expressed sequence tags
    • Bouck A., Vision T. The molecular ecologist's guide to expressed sequence tags. Mol. Ecol. 2007, 16:907-924.
    • (2007) Mol. Ecol. , vol.16 , pp. 907-924
    • Bouck, A.1    Vision, T.2
  • 11
    • 33644825685 scopus 로고    scopus 로고
    • Photosynthetic responses of seven tropical seagrasses to elevated seawater temperature
    • Campbell S.J., McKenzie L.J., Kerville S.P. Photosynthetic responses of seven tropical seagrasses to elevated seawater temperature. J. Exp. Mar. Biol. Ecol. 2006, 330:455-468.
    • (2006) J. Exp. Mar. Biol. Ecol. , vol.330 , pp. 455-468
    • Campbell, S.J.1    McKenzie, L.J.2    Kerville, S.P.3
  • 12
    • 0031945665 scopus 로고    scopus 로고
    • Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function
    • Cheetham M.E., Caplan A.J. Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function. Cell Stress Chaperones 1998, 3:28-36.
    • (1998) Cell Stress Chaperones , vol.3 , pp. 28-36
    • Cheetham, M.E.1    Caplan, A.J.2
  • 13
    • 0036137277 scopus 로고    scopus 로고
    • DNA sequence quality trimming and vector removal
    • Chou H.H., Holmes M.H. DNA sequence quality trimming and vector removal. Bioinformatics 2001, 17:1093-1104.
    • (2001) Bioinformatics , vol.17 , pp. 1093-1104
    • Chou, H.H.1    Holmes, M.H.2
  • 14
    • 24644503098 scopus 로고    scopus 로고
    • Blast2GO: a universal tool for annotation, visualization and analysis in functional genomics research
    • Conesa A., Gotz S., Garcia-Gomez J.M., Terol J., Talon M., Robles M. Blast2GO: a universal tool for annotation, visualization and analysis in functional genomics research. Bioinformatics 2005, 21:3674-3676.
    • (2005) Bioinformatics , vol.21 , pp. 3674-3676
    • Conesa, A.1    Gotz, S.2    Garcia-Gomez, J.M.3    Terol, J.4    Talon, M.5    Robles, M.6
  • 15
    • 33744787347 scopus 로고    scopus 로고
    • High temperature effects on photosynthesis. PSII functionality and antioxidant activity of two Festuca arundinacea cultivars with different heat susceptibility
    • Cui L.J., Li J.L., Fan Y.M., Xu S., Zhang Z. High temperature effects on photosynthesis. PSII functionality and antioxidant activity of two Festuca arundinacea cultivars with different heat susceptibility. Botanical Studies 2006, 47:61-69.
    • (2006) Botanical Studies , vol.47 , pp. 61-69
    • Cui, L.J.1    Li, J.L.2    Fan, Y.M.3    Xu, S.4    Zhang, Z.5
  • 16
    • 0028353336 scopus 로고
    • Dnaj-like proteins-molecular chaperones and specific regulators of Hsp70
    • Cyr D.M., Langer T., Douglas M.G. Dnaj-like proteins-molecular chaperones and specific regulators of Hsp70. Trends Biochem. Sci. 1994, 19:176-181.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 176-181
    • Cyr, D.M.1    Langer, T.2    Douglas, M.G.3
  • 17
    • 10844250172 scopus 로고    scopus 로고
    • Insertion-sequence-mediated mutations isolated during adaptation to growth and starvation in Lactococcus lactis
    • de Visser J., Akkermans A.D.L., Hoekstra R.F., de Vos W.M. Insertion-sequence-mediated mutations isolated during adaptation to growth and starvation in Lactococcus lactis. Genetics 2004, 168:1145-1157.
    • (2004) Genetics , vol.168 , pp. 1145-1157
    • de Visser, J.1    Akkermans, A.D.L.2    Hoekstra, R.F.3    de Vos, W.M.4
  • 18
    • 33646758594 scopus 로고    scopus 로고
    • Biodiversity and the functioning of seagrass ecosystems
    • Duffy J.E. Biodiversity and the functioning of seagrass ecosystems. Mar. Ecol. Prog. Ser. 2006, 311:233-250.
    • (2006) Mar. Ecol. Prog. Ser. , vol.311 , pp. 233-250
    • Duffy, J.E.1
  • 19
    • 36849035794 scopus 로고    scopus 로고
    • MSATCOMMANDER: detection of microsatellite repeat arrays and automated, locus-specific primer design
    • Faircloth B.C. MSATCOMMANDER: detection of microsatellite repeat arrays and automated, locus-specific primer design. Molecular Ecology Resources 2008, 8:92-94.
    • (2008) Molecular Ecology Resources , vol.8 , pp. 92-94
    • Faircloth, B.C.1
  • 20
    • 0042477596 scopus 로고    scopus 로고
    • Assessment of the use of biomarkers in aquatic plants for the evaluation of environmental quality: application to seagrasses
    • Ferrat L., Pergent-Martini C., Romeo M. Assessment of the use of biomarkers in aquatic plants for the evaluation of environmental quality: application to seagrasses. Aquat. Toxicol. 2003, 65:187-204.
    • (2003) Aquat. Toxicol. , vol.65 , pp. 187-204
    • Ferrat, L.1    Pergent-Martini, C.2    Romeo, M.3
  • 22
    • 35748962910 scopus 로고    scopus 로고
    • The Hsp70 chaperone machines of Escherichia coli: a paradigm for the repartition of chaperone functions
    • Genevaux P., Georgopoulos C., Kelley W.L. The Hsp70 chaperone machines of Escherichia coli: a paradigm for the repartition of chaperone functions. Mol. Microbiol. 2007, 66:840-857.
    • (2007) Mol. Microbiol. , vol.66 , pp. 840-857
    • Genevaux, P.1    Georgopoulos, C.2    Kelley, W.L.3
  • 23
    • 0032926319 scopus 로고    scopus 로고
    • Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts
    • Gothel S.F., Marahiel M.A. Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts. Cell. Mol. Life Sci. 1999, 55:423-436.
    • (1999) Cell. Mol. Life Sci. , vol.55 , pp. 423-436
    • Gothel, S.F.1    Marahiel, M.A.2
  • 25
    • 67449132042 scopus 로고    scopus 로고
    • Identification and functional validation of a unique set of drought induced genes preferentially expressed in response to gradual water stress in peanut
    • Govind G., ThammeGowda H.V., Kalaiarasi P.J., Iyer D.R., Muthappa S.K., Nese S., Makarla U.K. Identification and functional validation of a unique set of drought induced genes preferentially expressed in response to gradual water stress in peanut. Mol. Genet. Genomics 2009, 281:591-605.
    • (2009) Mol. Genet. Genomics , vol.281 , pp. 591-605
    • Govind, G.1    ThammeGowda, H.V.2    Kalaiarasi, P.J.3    Iyer, D.R.4    Muthappa, S.K.5    Nese, S.6    Makarla, U.K.7
  • 26
    • 0029561598 scopus 로고
    • The glutathione S-Transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance
    • Hayes J.D., Pulford D.J. The glutathione S-Transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. Crit. Rev. Biochem. Mol. Biol. 1995, 30:445-600.
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 445-600
    • Hayes, J.D.1    Pulford, D.J.2
  • 29
    • 80051938551 scopus 로고    scopus 로고
    • IPCC, Climate Change 2007: The Physical Science Basis. Summary for Policymakers., (2007) 1-21.
    • IPCC, Climate Change 2007: The Physical Science Basis. Summary for Policymakers., (2007) 1-21.
  • 32
    • 27744523022 scopus 로고    scopus 로고
    • Plant responses to heat stress
    • Springer-Verlag, Berlin Heidelberg, H. Hirt, K. Shinozaki (Eds.)
    • Krishna P.S. Plant responses to heat stress. Plant Responses to Abiotic Stress 2004, 9-38. Springer-Verlag, Berlin Heidelberg. H. Hirt, K. Shinozaki (Eds.).
    • (2004) Plant Responses to Abiotic Stress , pp. 9-38
    • Krishna, P.S.1
  • 33
    • 0028890084 scopus 로고
    • Enzyme assembly after de-novo synthesis in rabbit reticulocyte lysate involves molecular chaperones and immunophilins
    • Kruse M., Brunke M., Escher A., Szalay A.A., Tropschug M., Zimmermann R. Enzyme assembly after de-novo synthesis in rabbit reticulocyte lysate involves molecular chaperones and immunophilins. J. Biol. Chem. 1995, 270:2588-2594.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2588-2594
    • Kruse, M.1    Brunke, M.2    Escher, A.3    Szalay, A.A.4    Tropschug, M.5    Zimmermann, R.6
  • 34
    • 11244271388 scopus 로고    scopus 로고
    • Control of glycolytic oscillations by temperature
    • Mair T., Warnke C., Tsuji K., Muller S.C. Control of glycolytic oscillations by temperature. Biophys. J. 2005, 88:639-646.
    • (2005) Biophys. J. , vol.88 , pp. 639-646
    • Mair, T.1    Warnke, C.2    Tsuji, K.3    Muller, S.C.4
  • 35
    • 57649210741 scopus 로고    scopus 로고
    • Temperature tolerance and survival of intertidal populations of the seagrass Zostera noltii (Hornemann) in Southern Europe (Ria Formosa, Portugal)
    • Massa S.I., Arnaud-Haond S., Pearson G.A., Serrao E.A. Temperature tolerance and survival of intertidal populations of the seagrass Zostera noltii (Hornemann) in Southern Europe (Ria Formosa, Portugal). Hydrobiologia 2009, 619:195-201.
    • (2009) Hydrobiologia , vol.619 , pp. 195-201
    • Massa, S.I.1    Arnaud-Haond, S.2    Pearson, G.A.3    Serrao, E.A.4
  • 36
    • 70349560275 scopus 로고    scopus 로고
    • UFO: a web server for ultra-fast functional profiling of whole genome protein sequences
    • Meinicke P. UFO: a web server for ultra-fast functional profiling of whole genome protein sequences. BMC Genomics 2009, 10.
    • (2009) BMC Genomics , vol.10
    • Meinicke, P.1
  • 37
    • 23144455729 scopus 로고    scopus 로고
    • OrfPredictor: predicting protein-coding regions in EST-derived sequences
    • Min X.J., Butler G., Storms R., Tsang A. OrfPredictor: predicting protein-coding regions in EST-derived sequences. Nucleic Acids Res. 2005, 33:W677-W680.
    • (2005) Nucleic Acids Res. , vol.33
    • Min, X.J.1    Butler, G.2    Storms, R.3    Tsang, A.4
  • 38
    • 0029196224 scopus 로고
    • A Cdna-encoding a metallothionein I-like protein from coffee leaves (Coffea-Arabica)
    • Moisyadi S., Stiles J.I. A Cdna-encoding a metallothionein I-like protein from coffee leaves (Coffea-Arabica). Plant Physiol. 1995, 107:295-296.
    • (1995) Plant Physiol. , vol.107 , pp. 295-296
    • Moisyadi, S.1    Stiles, J.I.2
  • 39
    • 0024469206 scopus 로고
    • Isolation and characterization of Sti1, a stress-inducible gene from saccharomyces-cerevisiae
    • Nicolet C.M., Craig E.A. Isolation and characterization of Sti1, a stress-inducible gene from saccharomyces-cerevisiae. Mol. Cell. Biol. 1989, 9:3638-3646.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 3638-3646
    • Nicolet, C.M.1    Craig, E.A.2
  • 40
    • 34447269976 scopus 로고    scopus 로고
    • Reticulon-like proteins in Arabidopsis thaliana: structural organization and ER localization
    • Nziengui H., Bouhidel K., Pillon D., Der C., Marty F., Schoefs B. Reticulon-like proteins in Arabidopsis thaliana: structural organization and ER localization. FEBS Lett. 2007, 581:3356-3362.
    • (2007) FEBS Lett. , vol.581 , pp. 3356-3362
    • Nziengui, H.1    Bouhidel, K.2    Pillon, D.3    Der, C.4    Marty, F.5    Schoefs, B.6
  • 44
    • 0032192028 scopus 로고    scopus 로고
    • Photosynthetic response of laboratory-cultured Halophila ovalis to thermal stress
    • Ralph P.J. Photosynthetic response of laboratory-cultured Halophila ovalis to thermal stress. Mar. Ecol. Prog. Ser. 1998, 171:123-130.
    • (1998) Mar. Ecol. Prog. Ser. , vol.171 , pp. 123-130
    • Ralph, P.J.1
  • 45
    • 0032704506 scopus 로고    scopus 로고
    • Photosynthetic response of Halophila ovalis (R-Br.) Hook. f. to combined environmental stress
    • Ralph P.J. Photosynthetic response of Halophila ovalis (R-Br.) Hook. f. to combined environmental stress. Aquat. Bot. 1999, 65:83-96.
    • (1999) Aquat. Bot. , vol.65 , pp. 83-96
    • Ralph, P.J.1
  • 48
    • 0037440150 scopus 로고    scopus 로고
    • IDEG6: a web tool for detection of differentially expressed genes in multiple tag sampling experiments
    • Romualdi C., Bortoluzzi S., D'Alessi F., Danieli G.A. IDEG6: a web tool for detection of differentially expressed genes in multiple tag sampling experiments. Physiol. Genomics 2003, 12:159-162.
    • (2003) Physiol. Genomics , vol.12 , pp. 159-162
    • Romualdi, C.1    Bortoluzzi, S.2    D'Alessi, F.3    Danieli, G.A.4
  • 49
    • 0025330639 scopus 로고
    • Heat-shock proteins
    • Schlesinger M.J. Heat-shock proteins. J. Biol. Chem. 1990, 265:12111-12114.
    • (1990) J. Biol. Chem. , vol.265 , pp. 12111-12114
    • Schlesinger, M.J.1
  • 50
    • 0029364576 scopus 로고
    • Protein-folding-prolyl isomerases join the fold
    • Schmid F.X. Protein-folding-prolyl isomerases join the fold. Curr. Biol. 1995, 5:993-994.
    • (1995) Curr. Biol. , vol.5 , pp. 993-994
    • Schmid, F.X.1
  • 52
    • 0028993937 scopus 로고
    • Comparative-study on populations of Zostera-Marina L (Eelgrass)-in-situ nitrogen enrichment and light manipulation
    • Vanlent F., Verschuure J.M., Vanveghel M.L.J. Comparative-study on populations of Zostera-Marina L (Eelgrass)-in-situ nitrogen enrichment and light manipulation. J. Exp. Mar. Biol. Ecol. 1995, 185:55-76.
    • (1995) J. Exp. Mar. Biol. Ecol. , vol.185 , pp. 55-76
    • Vanlent, F.1    Verschuure, J.M.2    Vanveghel, M.L.J.3
  • 53
    • 0742324902 scopus 로고    scopus 로고
    • Horseradish peroxidase: a modern view of a classic enzyme
    • Veitch N.C. Horseradish peroxidase: a modern view of a classic enzyme. Phytochemistry 2004, 65:249-259.
    • (2004) Phytochemistry , vol.65 , pp. 249-259
    • Veitch, N.C.1
  • 55
    • 0032482983 scopus 로고    scopus 로고
    • Evolutionary conserved light regulation of Calvin cycle activity by NADPH-mediated reversible phosphoribulokinase/CP12/glyceraldehyde-3-phosphate dehydrogenase complex dissociation
    • Wedel N., Soll J. Evolutionary conserved light regulation of Calvin cycle activity by NADPH-mediated reversible phosphoribulokinase/CP12/glyceraldehyde-3-phosphate dehydrogenase complex dissociation. Proc. Natl. Acad. Sci. USA 1998, 95:9699-9704.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9699-9704
    • Wedel, N.1    Soll, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.