메뉴 건너뛰기




Volumn 274, Issue 10, 2007, Pages 2523-2539

Characterization and expression analysis of the aspartic protease gene family of Cynara cardunculus L.

Author keywords

Aspartic proteases; Cardosin; Leader intron; Pistil; Promoter

Indexed keywords

ASPARTIC PROTEINASE; BETA GLUCURONIDASE; CARDOSIN A; CARDOSIN B; CARDOSIN C; CARDOSIN D; CYPROSIN B; UNCLASSIFIED DRUG; VEGETABLE PROTEIN;

EID: 34247586701     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2007.05787.x     Document Type: Article
Times cited : (27)

References (62)
  • 1
    • 3543023301 scopus 로고    scopus 로고
    • A novel aspartic proteinase is targeted to the secretory pathway and to the vacuole in the moss Physcomitrella patens
    • Schaaf A, Reski R Decker EL (2004) A novel aspartic proteinase is targeted to the secretory pathway and to the vacuole in the moss Physcomitrella patens. Eur J Cell Biol 83, 145 152.
    • (2004) Eur J Cell Biol , vol.83 , pp. 145-152
    • Schaaf, A.1    Reski, R.2    Decker, E.L.3
  • 2
    • 2942512921 scopus 로고    scopus 로고
    • Structure and function of plant aspartic proteinases
    • Simões I Faro C (2004) Structure and function of plant aspartic proteinases. Eur J Biochem 271, 2067 2075.
    • (2004) Eur J Biochem , vol.271 , pp. 2067-2075
    • Simões, I.1    Faro, C.2
  • 4
    • 0033600810 scopus 로고    scopus 로고
    • Crystal structure of cardosin A, a glycosylated and Arg-Gly-Asp- containing aspartic proteinase from the flowers of Cynara cardunculus L
    • Frazão C, Bento I, Costa J, Soares CM, Veríssimo P, Faro C, Pires E, Cooper J Carrondo MA (1999) Crystal structure of cardosin A, a glycosylated and Arg-Gly-Asp-containing aspartic proteinase from the flowers of Cynara cardunculus L. J Biol Chem 274, 27694 27701.
    • (1999) J Biol Chem , vol.274 , pp. 27694-27701
    • Frazão, C.1    Bento, I.2    Costa, J.3    Soares, C.M.4    Veríssimo, P.5    Faro, C.6    Pires, E.7    Cooper, J.8    Carrondo, M.A.9
  • 6
    • 0031257393 scopus 로고    scopus 로고
    • Cardosin A, an abundant aspartic proteinase, accumulates in protein storage vacuoles in the stigmatic papillae of Cynara cardunculus L
    • Ramalho-Santos M, Pissarra J, Veríssimo P, Pereira S, Salema R, Pires E Faro CJ (1997) Cardosin A, an abundant aspartic proteinase, accumulates in protein storage vacuoles in the stigmatic papillae of Cynara cardunculus L. Planta 203, 204 212.
    • (1997) Planta , vol.203 , pp. 204-212
    • Ramalho-Santos, M.1    Pissarra, J.2    Veríssimo, P.3    Pereira, S.4    Salema, R.5    Pires, E.6    Faro, C.J.7
  • 7
    • 28044444773 scopus 로고    scopus 로고
    • Molecular analysis of the interaction between cardosin a and phospholipase Dα
    • Simões I, Mueller EC, Otto A, Bur D, Cheung AY, Faro C Pires E (2005) Molecular analysis of the interaction between cardosin A and phospholipase Dα. FEBS J 272, 5786 5798.
    • (2005) FEBS J , vol.272 , pp. 5786-5798
    • Simões, I.1    Mueller, E.C.2    Otto, A.3    Bur, D.4    Cheung, A.Y.5    Faro, C.6    Pires, E.7
  • 8
    • 0030060726 scopus 로고    scopus 로고
    • Purification, characterization and partial amino acid sequencing of two new aspartic proteinases from fresh flowers of Cynara cardunculus L
    • Veríssimo P, Faro C, Moir AJG, Lin YZ, Tang J Pires E (1996) Purification, characterization and partial amino acid sequencing of two new aspartic proteinases from fresh flowers of Cynara cardunculus L. Eur J Biochem 235, 762 768.
    • (1996) Eur J Biochem , vol.235 , pp. 762-768
    • Veríssimo, P.1    Faro, C.2    Moir, A.J.G.3    Lin, Y.Z.4    Tang, J.5    Pires, E.6
  • 9
    • 0034982756 scopus 로고    scopus 로고
    • Molecular cloning and characterization of cDNA encoding cardosin B, an aspartic proteinase accumulating extracellularly in the transmitting tissue of Cynara cardunculus L
    • Vieira M, Pissarra J, Veríssimo P, Castanheira P, Costa Y, Pires E Faro C (2001) Molecular cloning and characterization of cDNA encoding cardosin B, an aspartic proteinase accumulating extracellularly in the transmitting tissue of Cynara cardunculus L. Plant Mol Biol 45, 529 539.
    • (2001) Plant Mol Biol , vol.45 , pp. 529-539
    • Vieira, M.1    Pissarra, J.2    Veríssimo, P.3    Castanheira, P.4    Costa, Y.5    Pires, E.6    Faro, C.7
  • 10
    • 0031894720 scopus 로고    scopus 로고
    • Molecular cloning of aspartic proteinases from flowers of Cynara cardunculus subsp. flavescens cv. cardoon and Centaurea calcitrapa
    • Brodelius PE, Cordeiro M, Mercke P, Domingos A, Clemente A Pais MS (1998) Molecular cloning of aspartic proteinases from flowers of Cynara cardunculus subsp. flavescens cv. cardoon and Centaurea calcitrapa. Aspartic Proteinases 436, 435 439.
    • (1998) Aspartic Proteinases , vol.436 , pp. 435-439
    • Brodelius, P.E.1    Cordeiro, M.2    Mercke, P.3    Domingos, A.4    Clemente, A.5    Pais, M.S.6
  • 11
    • 0028387411 scopus 로고
    • Isolation and characterization of a cDNA from flowers of Cynara cardunculus encoding cyprosin (an aspartic proteinase) and its use to study the organ-specific expression of cyprosin
    • Cordeiro MC, Xue ZT, Pietrzak M, Pais MS Brodelius PE (1994) Isolation and characterization of a cDNA from flowers of Cynara cardunculus encoding cyprosin (an aspartic proteinase) and its use to study the organ-specific expression of cyprosin. Plant Mol Biol 24, 733 741.
    • (1994) Plant Mol Biol , vol.24 , pp. 733-741
    • Cordeiro, M.C.1    Xue, Z.T.2    Pietrzak, M.3    Pais, M.S.4    Brodelius, P.E.5
  • 12
    • 0035896365 scopus 로고    scopus 로고
    • Aspartic protease in leaves of common bean (Phaseolus vulgaris L.) and cowpea (Vigna unguiculata L. Walp): Enzymatic activity, gene expression and relation to drought susceptibility
    • Cruz de Carvalho MH, d'Arcy-Lameta A, Roy-Macauley H, Gareil M, El Maarouf H, Pham-Thi AT Zuily-Fodil Y (2001) Aspartic protease in leaves of common bean (Phaseolus vulgaris L.) and cowpea (Vigna unguiculata L. Walp): enzymatic activity, gene expression and relation to drought susceptibility. FEBS Lett 492, 242 246.
    • (2001) FEBS Lett , vol.492 , pp. 242-246
    • Cruz De Carvalho, M.H.1    D'Arcy-Lameta, A.2    Roy-Macauley, H.3    Gareil, M.4    El Maarouf, H.5    Pham-Thi, A.T.6    Zuily-Fodil, Y.7
  • 13
    • 0032856481 scopus 로고    scopus 로고
    • Purification and properties of an aspartic protease from potato tuber that is inhibited by a basic chitinase
    • Guevara MG, Oliva CR, Machinandiarena M Daleo GR (1999) Purification and properties of an aspartic protease from potato tuber that is inhibited by a basic chitinase. Physiol Plant 106, 164 169.
    • (1999) Physiol Plant , vol.106 , pp. 164-169
    • Guevara, M.G.1    Oliva, C.R.2    MacHinandiarena, M.3    Daleo, G.R.4
  • 14
    • 28444471988 scopus 로고    scopus 로고
    • Molecular cloning of a potato leaf cDNA encoding an aspartic protease (StAsp) and its expression after P. infestans infection
    • Guevara MG, Almeida C, Mendieta JR, Faro CJ, Veríssimo P, Pires EV Daleo GR (2005) Molecular cloning of a potato leaf cDNA encoding an aspartic protease (StAsp) and its expression after P. infestans infection. Plant Physiol Biochem 43, 882 889.
    • (2005) Plant Physiol Biochem , vol.43 , pp. 882-889
    • Guevara, M.G.1    Almeida, C.2    Mendieta, J.R.3    Faro, C.J.4    Veríssimo, P.5    Pires, E.V.6    Daleo, G.R.7
  • 15
    • 0030220455 scopus 로고    scopus 로고
    • Molecular cloning of a tomato leaf cDNA encoding an aspartic protease, a systemic wound response protein
    • Schaller A Ryan CA (1996) Molecular cloning of a tomato leaf cDNA encoding an aspartic protease, a systemic wound response protein. Plant Mol Biol 31, 1073 1077.
    • (1996) Plant Mol Biol , vol.31 , pp. 1073-1077
    • Schaller, A.1    Ryan, C.A.2
  • 16
    • 0029101380 scopus 로고
    • Rice aspartic proteinase, oryzasin, expressed during seed ripening and germination, has a gene organization distinct from those of animal and microbial aspartic proteinases
    • Asakura T, Watanabe H, Abe K Arai S (1995) Rice aspartic proteinase, oryzasin, expressed during seed ripening and germination, has a gene organization distinct from those of animal and microbial aspartic proteinases. Eur J Biochem 232, 77 83.
    • (1995) Eur J Biochem , vol.232 , pp. 77-83
    • Asakura, T.1    Watanabe, H.2    Abe, K.3    Arai, S.4
  • 18
    • 21144449190 scopus 로고    scopus 로고
    • Comparative transcriptome analysis reveals significant differences in gene expression and signalling pathways between developmental and dark/starvation-induced senescence in Arabidopsis
    • Buchanan-Wollaston V, Page T, Harrison E, Breeze E, Lim PO, Nam HG, Lin JF, Wu SH, Swidzinski J, Ishizaki K et al. (2005) Comparative transcriptome analysis reveals significant differences in gene expression and signalling pathways between developmental and dark/starvation-induced senescence in Arabidopsis. Plant J 42, 567 585.
    • (2005) Plant J , vol.42 , pp. 567-585
    • Buchanan-Wollaston, V.1    Page, T.2    Harrison, E.3    Breeze, E.4    Lim, P.O.5    Nam, H.G.6    Lin, J.F.7    Wu, S.H.8    Swidzinski, J.9    Ishizaki, K.10
  • 19
    • 4344561914 scopus 로고    scopus 로고
    • Isolation and characterization of an aspartic proteinase gene from cowpea (Vigna unguiculata L. Walp.)
    • Cruz de Carvalho MH, Pham-Thi AT, Gareil M, d'Arcy-Lameta A Fodil YZ (2004) Isolation and characterization of an aspartic proteinase gene from cowpea (Vigna unguiculata L. Walp.). J Plant Physiol 161, 971 976.
    • (2004) J Plant Physiol , vol.161 , pp. 971-976
    • Cruz De Carvalho, M.H.1    Pham-Thi, A.T.2    Gareil, M.3    D'Arcy-Lameta, A.4    Fodil, Y.Z.5
  • 20
    • 0035112482 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of postharvest senescence in broccoli
    • Page T, Griffiths G Buchanan-Wollaston V (2001) Molecular and biochemical characterization of postharvest senescence in broccoli. Plant Physiol 125, 718 727.
    • (2001) Plant Physiol , vol.125 , pp. 718-727
    • Page, T.1    Griffiths, G.2    Buchanan-Wollaston, V.3
  • 23
    • 0031460023 scopus 로고    scopus 로고
    • Context sequences of translation initiation codon in plants
    • Joshi CP, Zhou H, Huang X Chiang VL (1997) Context sequences of translation initiation codon in plants. Plant Mol Biol 35, 993 1001.
    • (1997) Plant Mol Biol , vol.35 , pp. 993-1001
    • Joshi, C.P.1    Zhou, H.2    Huang, X.3    Chiang, V.L.4
  • 24
    • 0023664776 scopus 로고
    • An inspection of the domain between putative TATA box and translation start site in 79 plant genes
    • Joshi CP (1987) An inspection of the domain between putative TATA box and translation start site in 79 plant genes. Nucleic Acids Res 15, 6643 6653.
    • (1987) Nucleic Acids Res , vol.15 , pp. 6643-6653
    • Joshi, C.P.1
  • 25
    • 0022820961 scopus 로고
    • Nonmuscle and muscle tropomyosin isoforms are expressed from a single gene by alternative RNA splicing and polyadenylation
    • Helfman DM, Cheley S, Kuismanen E, Finn LA Yamawaki-Kataoka Y (1986) Nonmuscle and muscle tropomyosin isoforms are expressed from a single gene by alternative RNA splicing and polyadenylation. Mol Cell Biol 6, 3582 3595.
    • (1986) Mol Cell Biol , vol.6 , pp. 3582-3595
    • Helfman, D.M.1    Cheley, S.2    Kuismanen, E.3    Finn, L.A.4    Yamawaki-Kataoka, Y.5
  • 26
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: Integrated software for molecular evolutionary genetics analysis and sequence alignment
    • Kumar S, Tamura K Nei M (2004) MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment. Brief Bioinform 5, 150 163.
    • (2004) Brief Bioinform , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 27
    • 0000979455 scopus 로고    scopus 로고
    • Oryzasin as an aspartic proteinase occurring in rice seeds: Purification, characterization, and application to milk clotting
    • Asakura T, Watanabe H, Abe K Arai S (1997) Oryzasin as an aspartic proteinase occurring in rice seeds: purification, characterization, and application to milk clotting. J Agric Food Chem 45, 1070 1075.
    • (1997) J Agric Food Chem , vol.45 , pp. 1070-1075
    • Asakura, T.1    Watanabe, H.2    Abe, K.3    Arai, S.4
  • 28
    • 0031105906 scopus 로고    scopus 로고
    • Leaf senescence in Brassica napus: Cloning of senescence related genes by subtractive hybridisation
    • Buchanan-Wollaston V Ainsworth C (1997) Leaf senescence in Brassica napus: cloning of senescence related genes by subtractive hybridisation. Plant Mol Biol 33, 821 834.
    • (1997) Plant Mol Biol , vol.33 , pp. 821-834
    • Buchanan-Wollaston, V.1    Ainsworth, C.2
  • 29
    • 0036380769 scopus 로고    scopus 로고
    • The three typical aspartic proteinase genes of Arabidopsis thaliana are differentially expressed
    • Chen X, Pfeil JE Gal S (2002) The three typical aspartic proteinase genes of Arabidopsis thaliana are differentially expressed. Eur J Biochem 269, 4675 4684.
    • (2002) Eur J Biochem , vol.269 , pp. 4675-4684
    • Chen, X.1    Pfeil, J.E.2    Gal, S.3
  • 31
    • 0032126745 scopus 로고    scopus 로고
    • Phytepsin, a barley vacuolar aspartic proteinase, is highly expressed during autolysis of developing tracheary elements and sieve cells
    • Runeberg-Roos P Saarma M (1998) Phytepsin, a barley vacuolar aspartic proteinase, is highly expressed during autolysis of developing tracheary elements and sieve cells. Plant J 15, 139 145.
    • (1998) Plant J , vol.15 , pp. 139-145
    • Runeberg-Roos, P.1    Saarma, M.2
  • 32
    • 1942487289 scopus 로고    scopus 로고
    • Characterization of the genes for two soybean aspartic proteinases and analysis of their different tissue-dependent expression
    • Terauchi K, Asakura T, Nishizawa NK, Matsumoto I Abe K (2004) Characterization of the genes for two soybean aspartic proteinases and analysis of their different tissue-dependent expression. Planta 218, 947 957.
    • (2004) Planta , vol.218 , pp. 947-957
    • Terauchi, K.1    Asakura, T.2    Nishizawa, N.K.3    Matsumoto, I.4    Abe, K.5
  • 33
    • 0031944728 scopus 로고    scopus 로고
    • Substrate specificity and molecular modelling of aspartic proteinases (Cyprosins) from flowers of Cynara cardunculus subsp. flavescens cv. cardoon
    • Cordeiro MC, Lowther T, Dunn BM, Guruprasad K, Blundell T, Pais MS Brodelius PE (1998) Substrate specificity and molecular modelling of aspartic proteinases (Cyprosins) from flowers of Cynara cardunculus subsp. flavescens cv. cardoon. Aspartic Proteinases 436, 473 479.
    • (1998) Aspartic Proteinases , vol.436 , pp. 473-479
    • Cordeiro, M.C.1    Lowther, T.2    Dunn, B.M.3    Guruprasad, K.4    Blundell, T.5    Pais, M.S.6    Brodelius, P.E.7
  • 34
    • 0030295188 scopus 로고    scopus 로고
    • Intron sequences are involved in the plastid- and light-dependent expression of the spinach PsaD gene
    • Bolle C, Herrmann RG Oelmuller R (1996) Intron sequences are involved in the plastid- and light-dependent expression of the spinach PsaD gene. Plant J 10, 919 924.
    • (1996) Plant J , vol.10 , pp. 919-924
    • Bolle, C.1    Herrmann, R.G.2    Oelmuller, R.3
  • 35
    • 33749020281 scopus 로고    scopus 로고
    • Intron-regulated expression of SUVH3, an Arabidopsis Su (var) 3-9 homologue
    • Casas-Mollano JA, Lao NT Kavanagh TA (2006) Intron-regulated expression of SUVH3, an Arabidopsis Su (var) 3-9 homologue. J Exp Bot 57, 3301 3311.
    • (2006) J Exp Bot , vol.57 , pp. 3301-3311
    • Casas-Mollano, J.A.1    Lao, N.T.2    Kavanagh, T.A.3
  • 37
    • 23944469660 scopus 로고    scopus 로고
    • The leader intron of Arabidopsis thaliana genes encoding cytochrome c oxidase subunit 5c promotes high-level expression by increasing transcript abundance and translation efficiency
    • Curi GC, Chan RL Gonzalez DH (2005) The leader intron of Arabidopsis thaliana genes encoding cytochrome c oxidase subunit 5c promotes high-level expression by increasing transcript abundance and translation efficiency. J Exp Bot 56, 2563 2571.
    • (2005) J Exp Bot , vol.56 , pp. 2563-2571
    • Curi, G.C.1    Chan, R.L.2    Gonzalez, D.H.3
  • 38
    • 10344233719 scopus 로고    scopus 로고
    • The effect of intron location on intron-mediated enhancement of gene expression in Arabidopsis
    • Rose AB (2004) The effect of intron location on intron-mediated enhancement of gene expression in Arabidopsis. Plant J 40, 744 751.
    • (2004) Plant J , vol.40 , pp. 744-751
    • Rose, A.B.1
  • 39
    • 0033928910 scopus 로고    scopus 로고
    • Tissue-preferential expression of a rice alpha-tubulin gene, OsTubA1, mediated by the first intron
    • Jeon JS, Lee S, Jung KH, Jun SH, Kim C An G (2000) Tissue-preferential expression of a rice alpha-tubulin gene, OsTubA1, mediated by the first intron. Plant Physiol 123, 1005 1014.
    • (2000) Plant Physiol , vol.123 , pp. 1005-1014
    • Jeon, J.S.1    Lee, S.2    Jung, K.H.3    Jun, S.H.4    Kim, C.5    An, G.6
  • 40
    • 0027645823 scopus 로고
    • Distinct cis-acting elements direct pistil-specific and pollen-specific activity of the brassica-S locus glycoprotein gene promoter
    • Dzelzkalns VA, Thorsness MK, Dwyer KG, Baxter JS, Balent MA, Nasrallah ME Nasrallah JB (1993) Distinct cis-acting elements direct pistil-specific and pollen-specific activity of the brassica-S locus glycoprotein gene promoter. Plant Cell 5, 855 863.
    • (1993) Plant Cell , vol.5 , pp. 855-863
    • Dzelzkalns, V.A.1    Thorsness, M.K.2    Dwyer, K.G.3    Baxter, J.S.4    Balent, M.A.5    Nasrallah, M.E.6    Nasrallah, J.B.7
  • 41
    • 0031594306 scopus 로고    scopus 로고
    • Multiple elements of the S-2-RNase promoter from potato (Solanum tuberosum L.) are required for cell type-specific expression in transgenic potato and tobacco
    • Ficker M, Kirch HH, Eijlander R, Jacobsen E Thompson RD (1998) Multiple elements of the S-2-RNase promoter from potato (Solanum tuberosum L.) are required for cell type-specific expression in transgenic potato and tobacco. Mol Gen Genet 257, 132 142.
    • (1998) Mol Gen Genet , vol.257 , pp. 132-142
    • Ficker, M.1    Kirch, H.H.2    Eijlander, R.3    Jacobsen, E.4    Thompson, R.D.5
  • 42
    • 0036792343 scopus 로고    scopus 로고
    • A pistil-specific thaumatin/PR5-like protein gene of Japanese pear (Pyrus serotina): Sequence and promoter activity of the 5′ region in transgenic tobacco
    • Sassa H, Ushijima K Hirano H (2002) A pistil-specific thaumatin/PR5-like protein gene of Japanese pear (Pyrus serotina): sequence and promoter activity of the 5′ region in transgenic tobacco. Plant Mol Biol 50, 371 377.
    • (2002) Plant Mol Biol , vol.50 , pp. 371-377
    • Sassa, H.1    Ushijima, K.2    Hirano, H.3
  • 44
    • 0033565640 scopus 로고    scopus 로고
    • Crystal structure of plant aspartic proteinase prophytepsin: Inactivation and vacuolar targeting
    • Kervinen J, Tobin GJ, Costa J, Waugh DS, Wlodawer A Zdanov A (1999) Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting. EMBO J 18, 3947 3955.
    • (1999) EMBO J , vol.18 , pp. 3947-3955
    • Kervinen, J.1    Tobin, G.J.2    Costa, J.3    Waugh, D.S.4    Wlodawer, A.5    Zdanov, A.6
  • 45
    • 28444442762 scopus 로고    scopus 로고
    • Immunolocalization of the saposin-like insert of plant aspartic proteinases exhibiting saposin C activity. Expression in young flower tissues and in barley seeds
    • Brodelius M, Hiraiwa M, Marttila S, Al Karadaghi S, Picaud S Brodelius P (2005) Immunolocalization of the saposin-like insert of plant aspartic proteinases exhibiting saposin C activity. Expression in young flower tissues and in barley seeds. Physiol Plant 125, 405 418.
    • (2005) Physiol Plant , vol.125 , pp. 405-418
    • Brodelius, M.1    Hiraiwa, M.2    Marttila, S.3    Al Karadaghi, S.4    Picaud, S.5    Brodelius, P.6
  • 47
    • 0024720641 scopus 로고
    • Regulation of beta-glucuronidase expression in transgenic tobacco plants by an A/T-rich, cis-acting sequence found upstream of a French bean beta-phaseolin gene
    • Bustos MM, Guiltinan MJ, Jordano J, Begum D, Kalkan FA Hall TC (1989) Regulation of beta-glucuronidase expression in transgenic tobacco plants by an A/T-rich, cis-acting sequence found upstream of a French bean beta-phaseolin gene. Plant Cell 1, 839 853.
    • (1989) Plant Cell , vol.1 , pp. 839-853
    • Bustos, M.M.1    Guiltinan, M.J.2    Jordano, J.3    Begum, D.4    Kalkan, F.A.5    Hall, T.C.6
  • 48
    • 0026917018 scopus 로고
    • AT-rich promoter elements of soybean heat shock gene Gmhsp17.5E bind two distinct sets of nuclear proteins in vitro
    • Czarnecka E, Ingersoll JC Gurley WB (1992) AT-rich promoter elements of soybean heat shock gene Gmhsp17.5E bind two distinct sets of nuclear proteins in vitro. Plant Mol Biol 19, 985 1000.
    • (1992) Plant Mol Biol , vol.19 , pp. 985-1000
    • Czarnecka, E.1    Ingersoll, J.C.2    Gurley, W.B.3
  • 49
    • 0032125918 scopus 로고    scopus 로고
    • A/T-rich sequences act as quantitative enhancers of gene expression in transgenic tobacco and potato plants
    • Sandhu JS, Webster CI Gray JC (1998) A/T-rich sequences act as quantitative enhancers of gene expression in transgenic tobacco and potato plants. Plant Mol Biol 37, 885 896.
    • (1998) Plant Mol Biol , vol.37 , pp. 885-896
    • Sandhu, J.S.1    Webster, C.I.2    Gray, J.C.3
  • 53
    • 0025655858 scopus 로고
    • Intron-mediated enhancement of heterologous gene expression in maize
    • Mascarenhas D, Mettler IJ, Pierce DA Lowe HW (1990) Intron-mediated enhancement of heterologous gene expression in maize. Plant Mol Biol 15, 913 920.
    • (1990) Plant Mol Biol , vol.15 , pp. 913-920
    • Mascarenhas, D.1    Mettler, I.J.2    Pierce, D.A.3    Lowe, H.W.4
  • 54
    • 0030452647 scopus 로고    scopus 로고
    • Functional analysis of a Brassica oleracea SLR1 gene promoter
    • Hackett RM, Cadwallader G Franklin FC (1996) Functional analysis of a Brassica oleracea SLR1 gene promoter. Plant Physiol 112, 1601 1607.
    • (1996) Plant Physiol , vol.112 , pp. 1601-1607
    • Hackett, R.M.1    Cadwallader, G.2    Franklin, F.C.3
  • 57
    • 0036581417 scopus 로고    scopus 로고
    • GATEWAY vectors for Agrobacterium-mediated plant transformation
    • Karimi M, Inze D Depicker A (2002) GATEWAY vectors for Agrobacterium-mediated plant transformation. Trends Plant Sci 7, 193 195.
    • (2002) Trends Plant Sci , vol.7 , pp. 193-195
    • Karimi, M.1    Inze, D.2    Depicker, A.3
  • 58
  • 59
    • 0036000015 scopus 로고    scopus 로고
    • Tissue localization of a submergence-induced 1-aminocyclopropane-1- carboxylic acid synthase in rice
    • Zhou Z, de Almeida EJ, Rouan D, Michiels F, Van Montagu M Van Der SD (2002) Tissue localization of a submergence-induced 1-aminocyclopropane-1- carboxylic acid synthase in rice. Plant Physiol 129, 72 84.
    • (2002) Plant Physiol , vol.129 , pp. 72-84
    • Zhou, Z.1    De Almeida, E.J.2    Rouan, D.3    Michiels, F.4    Van Montagu, M.5    Van Der, S.D.6
  • 60
    • 69949124194 scopus 로고
    • Efficient transformation of Agrobacterium spp. by high voltage electroporation
    • Wen-Jun S Forde BG (1989) Efficient transformation of Agrobacterium spp. by high voltage electroporation. Nucleic Acids Res 17, 8385.
    • (1989) Nucleic Acids Res , vol.17 , pp. 8385
    • Wen-Jun, S.1    Forde, B.G.2
  • 61
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: A simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana
    • Clough SJ Bent AF (1998) Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J 16, 735 743.
    • (1998) Plant J , vol.16 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 62
    • 0342444416 scopus 로고
    • GUS fusions: Beta-glucuronidase as a sensitive and versatile gene fusion marker in higher plants
    • Jefferson RA, Kavanagh TA Bevan MW (1987) GUS fusions: beta-glucuronidase as a sensitive and versatile gene fusion marker in higher plants. EMBO J 6, 3901 3907.
    • (1987) EMBO J , vol.6 , pp. 3901-3907
    • Jefferson, R.A.1    Kavanagh, T.A.2    Bevan, M.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.