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Volumn 24, Issue 3, 2012, Pages 1217-1229

A previously unknown Oxalyl-CoA synthetase is important for oxalate catabolism in Arabidopsis

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EID: 84860153593     PISSN: 10404651     EISSN: 1532298X     Source Type: Journal    
DOI: 10.1105/tpc.112.096032     Document Type: Article
Times cited : (66)

References (66)
  • 1
    • 0017334302 scopus 로고
    • Occurrence of oxalyl-CoA synthetase in Indian pulses
    • Adsule, R.N., and Barat, G.K. (1977). Occurrence of oxalyl-CoA synthetase in Indian pulses. Experientia 33: 416-417
    • (1977) Experientia , vol.33 , pp. 416-417
    • Adsule, R.N.1    Barat, G.K.2
  • 2
    • 0000608572 scopus 로고
    • Changes in the ascorbate system during seed development of Vicia faba L
    • Arrigoni, O., De Gara, L., Tommasi, F., and Liso, R. (1992). Changes in the ascorbate system during seed development of Vicia faba L. Plant Physiol. 99: 235-238
    • (1992) Plant Physiol , vol.99 , pp. 235-238
    • Arrigoni, O.1    de Gara, L.2    Tommasi, F.3    Liso, R.4
  • 3
    • 0000970148 scopus 로고
    • Simultaneous production and synergistic action of oxalic acid and polygalacturonase during pathogenesis by Sclerotium rolfsii
    • Bateman, D.F., and Beer, S.V. (1965). Simultaneous production and synergistic action of oxalic acid and polygalacturonase during pathogenesis by Sclerotium rolfsii. Phytopathology 55: 204-211
    • (1965) Phytopathology , vol.55 , pp. 204-211
    • Bateman, D.F.1    Beer, S.V.2
  • 4
    • 34248182280 scopus 로고    scopus 로고
    • The acyltransferase GPAT5 is required for the synthesis of suberin in seed coat and root of Arabidopsis
    • Beisson, F., Li, Y., Bonaventure, G., Pollard, M., and Ohlrogge, J.B. (2007). The acyltransferase GPAT5 is required for the synthesis of suberin in seed coat and root of Arabidopsis. Plant Cell 19: 351-368
    • (2007) Plant Cell , vol.19 , pp. 351-368
    • Beisson, F.1    Li, Y.2    Bonaventure, G.3    Pollard, M.4    Ohlrogge, J.B.5
  • 5
    • 29244469942 scopus 로고    scopus 로고
    • Structural basis for activation of the thiamin diphosphatedependent enzyme oxalyl-CoA decarboxylase by adenosine diphosphate
    • Berthold, C.L., Moussatche, P., Richards, N.G., and Lindqvist, Y. (2005). Structural basis for activation of the thiamin diphosphatedependent enzyme oxalyl-CoA decarboxylase by adenosine diphosphate. J. Biol. Chem. 280: 41645-41654.
    • (2005) J. Biol. Chem. , vol.280 , pp. 41645-41654
    • Berthold, C.L.1    Moussatche, P.2    Richards, N.G.3    Lindqvist, Y.4
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of proteindye binding
    • Bradford, M.M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of proteindye binding. Anal. Biochem. 72: 248-254
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0000947909 scopus 로고
    • Biogenesis of oxalate in plant tissues
    • Chang, C.C., and Beevers, H. (1968). Biogenesis of oxalate in plant tissues. Plant Physiol. 43: 1821-1828
    • (1968) Plant Physiol , vol.43 , pp. 1821-1828
    • Chang, C.C.1    Beevers, H.2
  • 9
    • 79960887002 scopus 로고    scopus 로고
    • Malonyl-CoA synthetase, encoded by ACYL ACTIVATING ENZYME13, is essential for growth and development of Arabidopsis
    • Chen, H., Kim, H.U., Weng, H., and Browse, J. (2011). Malonyl-CoA synthetase, encoded by ACYL ACTIVATING ENZYME13, is essential for growth and development of Arabidopsis. Plant Cell 23: 2247-2262
    • (2011) Plant Cell , vol.23 , pp. 2247-2262
    • Chen, H.1    Kim, H.U.2    Weng, H.3    Browse, J.4
  • 10
    • 70349759315 scopus 로고    scopus 로고
    • Germins: A diverse protein family important for crop improvement
    • Davidson, R.M., Reeves, P.A., Manosalva, P.M., and Leach, J.E. (2009). Germins: A diverse protein family important for crop improvement. Plant Sci. 177: 499-510
    • (2009) Plant Sci , vol.177 , pp. 499-510
    • Davidson, R.M.1    Reeves, P.A.2    Manosalva, P.M.3    Leach, J.E.4
  • 11
    • 17544394802 scopus 로고    scopus 로고
    • Influence of the testa on seed dormancy, germination, and longevity in Arabidopsis
    • Debeaujon, I., Léon-Kloosterziel, K.M., and Koornneef, M. (2000). Influence of the testa on seed dormancy, germination, and longevity in Arabidopsis. Plant Physiol. 122: 403-414
    • (2000) Plant Physiol , vol.122 , pp. 403-414
    • Debeaujon, I.1    Léon-Kloosterziel, K.M.2    Koornneef, M.3
  • 12
    • 0035721829 scopus 로고    scopus 로고
    • Soybean plants expressing an active oligomeric oxalate oxidase from the wheat gf-2.8 (germin) gene are resistant to the oxalate-secreting pathogen Sclerotina sclerotiorum
    • Donaldson, P.A., Anderson, T., Lane, B.G., Davidson, A.L., and Simmonds, D.H. (2001). Soybean plants expressing an active oligomeric oxalate oxidase from the wheat gf-2.8 (germin) gene are resistant to the oxalate-secreting pathogen Sclerotina sclerotiorum. Physiol. Mol. Plant Pathol. 59: 297-307
    • (2001) Physiol. Mol. Plant Pathol. , vol.59 , pp. 297-307
    • Donaldson, P.A.1    Anderson, T.2    Lane, B.G.3    Davidson, A.L.4    Simmonds, D.H.5
  • 13
    • 45049083213 scopus 로고    scopus 로고
    • Expressing a gene encoding wheat oxalate oxidase enhances resistance to Sclerotinia sclerotiorum in oilseed rape (Brassica napus)
    • Dong, X.B., Ji, R.Q., Guo, X.L., Foster, S.J., Chen, H., Dong, C.H., Liu, Y.Y., Hu, Q., and Liu, S.Y. (2008). Expressing a gene encoding wheat oxalate oxidase enhances resistance to Sclerotinia sclerotiorum in oilseed rape (Brassica napus). Planta 228: 331-340
    • (2008) Planta , vol.228 , pp. 331-340
    • Dong, X.B.1    Ji, R.Q.2    Guo, X.L.3    Foster, S.J.4    Chen, H.5    Dong, C.H.6    Liu, Y.Y.7    Hu, Q.8    Liu, S.Y.9
  • 15
    • 0036081355 scopus 로고    scopus 로고
    • Gene Expression Omnibus: NCBI gene expression and hybridization array data repository
    • Edgar, R., Domrachev, M., and Lash, A.E. (2002). Gene Expression Omnibus: NCBI gene expression and hybridization array data repository. Nucleic Acids Res. 30: 207-210
    • (2002) Nucleic Acids Res , vol.30 , pp. 207-210
    • Edgar, R.1    Domrachev, M.2    Lash, A.E.3
  • 16
    • 84980193373 scopus 로고
    • Metabolism of isolated cellular particles from photosynthetic tissues
    • Finkle, B.J., and Arnon, D.I. (1954). Metabolism of isolated cellular particles from photosynthetic tissues. Physiol. Plant. 7: 614-624
    • (1954) Physiol. Plant , vol.7 , pp. 614-624
    • Finkle, B.J.1    Arnon, D.I.2
  • 17
    • 20444368468 scopus 로고    scopus 로고
    • Calcium oxalate in plants: Formation and function
    • Franceschi, V.R., and Nakata, P.A. (2005). Calcium oxalate in plants: Formation and function. Annu. Rev. Plant Biol. 56: 41-71
    • (2005) Annu. Rev. Plant Biol. , vol.56 , pp. 41-71
    • Franceschi, V.R.1    Nakata, P.A.2
  • 18
    • 84860172746 scopus 로고
    • Zur biologischen oxydation der oxalsaure. II. Hoppe Seylers Z
    • Franke, W., Schumann, F., and Banerjee, B. (1943). Zur biologischen oxydation der oxalsaure. II. Hoppe Seylers Z. Physiol. Chem. 278: 24-42
    • (1943) Physiol. Chem. , vol.278 , pp. 24-42
    • Franke, W.1    Schumann, F.2    Banerjee, B.3
  • 19
    • 0014012999 scopus 로고
    • Oxalyl-coenzyme A synthetase from pea seeds
    • Giovanelli, J. (1966). Oxalyl-coenzyme A synthetase from pea seeds. Biochim. Biophys. Acta 118: 124-143
    • (1966) Biochim. Biophys. Acta. , vol.118 , pp. 124-143
    • Giovanelli, J.1
  • 20
    • 36949075560 scopus 로고
    • Adenosine triphosphate-and coenzyme A-dependent decarboxylation of oxalate by extracts of peas
    • Giovanelli, J., and Tobin, N.F. (1961). Adenosine triphosphate-and coenzyme A-dependent decarboxylation of oxalate by extracts of peas. Nature 190: 1006-1007
    • (1961) Nature , vol.190 , pp. 1006-1007
    • Giovanelli, J.1    Tobin, N.F.2
  • 21
    • 9744264568 scopus 로고
    • Enzymic decarboxylation of oxalate by extracts of plant tissue
    • Giovanelli, J., and Tobin, N.F. (1964). Enzymic decarboxylation of oxalate by extracts of plant tissue. Plant Physiol. 39: 139-145
    • (1964) Plant Physiol , vol.39 , pp. 139-145
    • Giovanelli, J.1    Tobin, N.F.2
  • 22
    • 2442507000 scopus 로고    scopus 로고
    • Affordable image analysis using NIH Image/ImageJ
    • Girish, V., and Vijayalakshmi, A. (2004). Affordable image analysis using NIH Image/ImageJ. Indian J. Cancer 41: 47.
    • (2004) Indian J. Cancer , vol.41 , pp. 47
    • Girish, V.1    Vijayalakshmi, A.2
  • 23
    • 0001467680 scopus 로고
    • Use of mutants to demonstrate the role of oxalic acid in pathogenicity of Sclerotinia sclerotiorum on Phaseolus vulgaris
    • Godoy, G., Steadman, J.R., Dickman, M.B., and Dam, R. (1990). Use of mutants to demonstrate the role of oxalic acid in pathogenicity of Sclerotinia sclerotiorum on Phaseolus vulgaris. Physiol. Mol. Plant Pathol. 37: 179-191
    • (1990) Physiol. Mol. Plant Pathol. , vol.37 , pp. 179-191
    • Godoy, G.1    Steadman, J.R.2    Dickman, M.B.3    Dam, R.4
  • 24
    • 11944261503 scopus 로고    scopus 로고
    • Vitamin C degradation in plant cells via enzymatic hydrolysis of 4-O-oxalyl-L-threonate
    • Green, M.A., and Fry, S.C. (2005). Vitamin C degradation in plant cells via enzymatic hydrolysis of 4-O-oxalyl-L-threonate. Nature 433: 83-87
    • (2005) Nature , vol.433 , pp. 83-87
    • Green, M.A.1    Fry, S.C.2
  • 25
    • 16544377400 scopus 로고    scopus 로고
    • Oxalate production by Sclerotinia sclerotiorum deregulates guard cells during infection
    • Guimarães, R.L., and Stotz, H.U. (2004). Oxalate production by Sclerotinia sclerotiorum deregulates guard cells during infection. Plant Physiol. 136: 3703-3711
    • (2004) Plant Physiol , vol.136 , pp. 3703-3711
    • Guimarães, R.L.1    Stotz, H.U.2
  • 26
    • 33644649331 scopus 로고    scopus 로고
    • Combining experimental and predicted datasets for determination of the subcellular location of proteins in Arabidopsis
    • Heazlewood, J.L., Tonti-Filippini, J., Verboom, R.E., and Millar, A.H. (2005). Combining experimental and predicted datasets for determination of the subcellular location of proteins in Arabidopsis. Plant Physiol. 139: 598-609
    • (2005) Plant Physiol , vol.139 , pp. 598-609
    • Heazlewood, J.L.1    Tonti-Filippini, J.2    Verboom, R.E.3    Millar, A.H.4
  • 27
    • 25644452138 scopus 로고    scopus 로고
    • Sclerotinia sclerotiorum: When "to be or not to be" a pathogen?
    • Hegedus, D.D., and Rimmer, S.R. (2005). Sclerotinia sclerotiorum: When "to be or not to be" a pathogen? FEMS Microbiol. Lett. 251: 177-184
    • (2005) FEMS Microbiol. Lett. , vol.251 , pp. 177-184
    • Hegedus, D.D.1    Rimmer, S.R.2
  • 28
    • 11844257472 scopus 로고    scopus 로고
    • The calcium conundrum. Both versatile nutrient and specific signal
    • Hirschi, K.D. (2004). The calcium conundrum. Both versatile nutrient and specific signal. Plant Physiol. 136: 2438-2442
    • (2004) Plant Physiol , vol.136 , pp. 2438-2442
    • Hirschi, K.D.1
  • 29
    • 71249083138 scopus 로고    scopus 로고
    • Chloroplast proteomics and the compartmentation of plastidial isoprenoid biosynthetic pathways
    • Joyard, J., Ferro, M., Masselon, C., Seigneurin-Berny, D., Salvi, D., Garin, J., and Rolland, N. (2009). Chloroplast proteomics and the compartmentation of plastidial isoprenoid biosynthetic pathways. Mol. Plant 2: 1154-1180
    • (2009) Mol. Plant , vol.2 , pp. 1154-1180
    • Joyard, J.1    Ferro, M.2    Masselon, C.3    Seigneurin-Berny, D.4    Salvi, D.5    Garin, J.6    Rolland, N.7
  • 30
    • 0033982936 scopus 로고    scopus 로고
    • KEGG: Kyoto encyclopedia of genes and genomes
    • Kanehisa, M., and Goto, S. (2000). KEGG: Kyoto encyclopedia of genes and genomes. Nucleic Acids Res. 28: 27-30
    • (2000) Nucleic Acids Res , vol.28 , pp. 27-30
    • Kanehisa, M.1    Goto, S.2
  • 31
    • 0036581417 scopus 로고    scopus 로고
    • GATEWAY vectors for Agrobacterium-mediated plant transformation
    • Karimi, M., Inzé, D., and 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    Inzé, D.2    Depicker, A.3
  • 32
    • 41649116914 scopus 로고    scopus 로고
    • Jasmonates meet fatty acids: Functional analysis of a new acyl-coenzyme A synthetase family from Arabidopsis thaliana
    • Kienow, L., Schneider, K., Bartsch, M., Stuible, H.-P., Weng, H., Miersch, O., Wasternack, C., and Kombrink, E. (2008). Jasmonates meet fatty acids: Functional analysis of a new acyl-coenzyme A synthetase family from Arabidopsis thaliana. J. Exp. Bot. 59: 403-419
    • (2008) J. Exp. Bot. , vol.59 , pp. 403-419
    • Kienow, L.1    Schneider, K.2    Bartsch, M.3    Stuible, H.-P.4    Weng, H.5    Miersch, O.6    Wasternack, C.7    Kombrink, E.8
  • 33
    • 43549124368 scopus 로고    scopus 로고
    • Oxalic acid is an elicitor of plant programmed cell death during Sclerotinia sclerotiorum disease development
    • Kim, K.S., Min, J.-Y., and Dickman, M.B. (2008). Oxalic acid is an elicitor of plant programmed cell death during Sclerotinia sclerotiorum disease development. Mol. Plant Microbe Interact. 21: 605-612
    • (2008) Mol. Plant Microbe Interact. , vol.21 , pp. 605-612
    • Kim, K.S.1    Min, J.-Y.2    Dickman, M.B.3
  • 34
    • 77954162163 scopus 로고    scopus 로고
    • Oxalate exudation into the root-tip water free space confers protection from aluminum toxicity and allows aluminum accumulation in the symplast in buckwheat (Fagopyrum esculentum)
    • Klug, B., and Horst, W.J. (2010). Oxalate exudation into the root-tip water free space confers protection from aluminum toxicity and allows aluminum accumulation in the symplast in buckwheat (Fagopyrum esculentum). New Phytol. 187: 380-391
    • (2010) New Phytol , vol.187 , pp. 380-391
    • Klug, B.1    Horst, W.J.2
  • 35
    • 33845678408 scopus 로고    scopus 로고
    • Identification of a peroxisomal acyl-activating enzyme involved in the biosynthesis of jasmonic acid in Arabidopsis
    • Koo, A.J.K., Chung, H.S., Kobayashi, Y., and Howe, G.A. (2006). Identification of a peroxisomal acyl-activating enzyme involved in the biosynthesis of jasmonic acid in Arabidopsis. J. Biol. Chem. 281: 33511-33520.
    • (2006) J. Biol. Chem. , vol.281 , pp. 33511-33520
    • Koo, A.J.K.1    Chung, H.S.2    Kobayashi, Y.3    Howe, G.A.4
  • 36
    • 33745454546 scopus 로고    scopus 로고
    • Medicago truncatula mutants demonstrate the role of plant calcium oxalate crystals as an effective defense against chewing insects
    • Korth, K.L., Doege, S.J., Park, S.H., Goggin, F.L., Wang, Q., Gomez, S.K., Liu, G., Jia, L., and Nakata, P.A. (2006). Medicago truncatula mutants demonstrate the role of plant calcium oxalate crystals as an effective defense against chewing insects. Plant Physiol. 141: 188-195
    • (2006) Plant Physiol , vol.141 , pp. 188-195
    • Korth, K.L.1    Doege, S.J.2    Park, S.H.3    Goggin, F.L.4    Wang, Q.5    Gomez, S.K.6    Liu, G.7    Jia, L.8    Nakata, P.A.9
  • 37
    • 0027161641 scopus 로고
    • Germin, a protein marker of early plant development, is an oxalate oxidase
    • Lane, B.G., Dunwell, J.M., Ray, J.A., Schmitt, M.R., and Cuming, A.C. (1993). Germin, a protein marker of early plant development, is an oxalate oxidase. J. Biol. Chem. 268: 12239-12242.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12239-12242
    • Lane, B.G.1    Dunwell, J.M.2    Ray, J.A.3    Schmitt, M.R.4    Cuming, A.C.5
  • 38
    • 0036800777 scopus 로고    scopus 로고
    • Overexpression of formate dehydrogenase in Arabidopsis thaliana resulted in plants tolerant to high concentrations of formate
    • Li, R., Moore, M., Bonham-Smith, P.C., and King, J. (2002). Overexpression of formate dehydrogenase in Arabidopsis thaliana resulted in plants tolerant to high concentrations of formate. J. Plant Physiol. 159: 1069-1076
    • (2002) J. Plant Physiol. , vol.159 , pp. 1069-1076
    • Li, R.1    Moore, M.2    Bonham-Smith, P.C.3    King, J.4
  • 40
    • 58149500279 scopus 로고    scopus 로고
    • The CBL-CIPK network in plant calcium signaling
    • Luan, S. (2009). The CBL-CIPK network in plant calcium signaling. Trends Plant Sci. 14: 37-42
    • (2009) Trends Plant Sci , vol.14 , pp. 37-42
    • Luan, S.1
  • 41
    • 0001322523 scopus 로고
    • Pectolytic enzymes of Scerlotinia sclerotiorum and their localization in infected bean
    • Lumsden, R.D. (1976). Pectolytic enzymes of Scerlotinia sclerotiorum and their localization in infected bean. Can. J. Bot. 54: 2630-2641
    • (1976) Can. J. Bot. , vol.54 , pp. 2630-2641
    • Lumsden, R.D.1
  • 42
    • 85033243925 scopus 로고    scopus 로고
    • Detoxifying aluminium with buckwheat
    • Ma, J.F., Zheng, S.J., Matsumoto, H., and Hiradate, S. (1997). Detoxifying aluminium with buckwheat. Nature 390: 569-570
    • (1997) Nature , vol.390 , pp. 569-570
    • Ma, J.F.1    Zheng, S.J.2    Matsumoto, H.3    Hiradate, S.4
  • 43
    • 0000643236 scopus 로고
    • Biosynthesis of b-N-oxalyl-l-a,b-diaminopropionic acid, the Lathyrus sativus neurotoxin
    • Malathi, K., Padmanaban, G., and Sarma, P.S. (1970). Biosynthesis of b-N-oxalyl-l-a,b-diaminopropionic acid, the Lathyrus sativus neurotoxin. Phytochemistry 9: 1603-1610
    • (1970) Phytochemistry , vol.9 , pp. 1603-1610
    • Malathi, K.1    Padmanaban, G.2    Sarma, P.S.3
  • 45
    • 0033840196 scopus 로고    scopus 로고
    • Arabidopsis thaliana germin-like proteins: Common and specific features point to a variety of functions
    • Membré, N., Bernier, F., Staiger, D., and Berna, A. (2000). Arabidopsis thaliana germin-like proteins: Common and specific features point to a variety of functions. Planta 211: 345-354
    • (2000) Planta , vol.211 , pp. 345-354
    • Membré, N.1    Bernier, F.2    Staiger, D.3    Berna, A.4
  • 46
    • 84982358134 scopus 로고
    • A revised medium for rapid growth and bio assays with tobacco tissue cultures
    • Murashige, T., and Skoog, F. (1962). A revised medium for rapid growth and bio assays with tobacco tissue cultures. Physiol. Plant. 15: 473-497
    • (1962) Physiol. Plant. , vol.15 , pp. 473-497
    • Murashige, T.1    Skoog, F.2
  • 48
    • 0037680190 scopus 로고    scopus 로고
    • Advances in our understanding of calcium oxalate crystal formation and function in plants
    • Nakata, P.A. (2003). Advances in our understanding of calcium oxalate crystal formation and function in plants. Plant Sci. 164: 901-909
    • (2003) Plant Sci , vol.164 , pp. 901-909
    • Nakata, P.A.1
  • 49
    • 0037906402 scopus 로고    scopus 로고
    • Calcium oxalate crystal formation is not essential for growth of Medicago truncatula
    • Nakata, P.A., and McConn, M.M. (2003). Calcium oxalate crystal formation is not essential for growth of Medicago truncatula. Plant Physiol. Biochem. 41: 325-329
    • (2003) Plant Physiol. Biochem. , vol.41 , pp. 325-329
    • Nakata, P.A.1    McConn, M.M.2
  • 50
    • 58149197587 scopus 로고    scopus 로고
    • ATTED-II provides coexpressed gene networks for Arabidopsis
    • (Database issue)
    • Obayashi, T., Hayashi, S., Saeki, M., Ohta, H., and Kinoshita, K. (2009). ATTED-II provides coexpressed gene networks for Arabidopsis. Nucleic Acids Res. 37(Database issue): D987-D991.
    • (2009) Nucleic Acids Res , vol.37
    • Obayashi, T.1    Hayashi, S.2    Saeki, M.3    Ohta, H.4    Kinoshita, K.5
  • 51
    • 0000889768 scopus 로고
    • Oxidation of glyoxylic acid to oxalic acid by glycolic acid oxidase
    • Richardson, K.E., and Tolbert, N.E. (1961). Oxidation of glyoxylic acid to oxalic acid by glycolic acid oxidase. J. Biol. Chem. 236: 1280-1284
    • (1961) J. Biol. Chem. , vol.236 , pp. 1280-1284
    • Richardson, K.E.1    Tolbert, N.E.2
  • 53
    • 79953236571 scopus 로고    scopus 로고
    • Genome-level and biochemical diversity of the acyl-activating enzyme superfamily in plants
    • Shockey, J., and Browse, J. (2011). Genome-level and biochemical diversity of the acyl-activating enzyme superfamily in plants. Plant J. 66: 143-160
    • (2011) Plant J , vol.66 , pp. 143-160
    • Shockey, J.1    Browse, J.2
  • 54
    • 0038796765 scopus 로고    scopus 로고
    • Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases
    • Shockey, J.M., Fulda, M.S., and Browse, J. (2003). Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 132: 1065-1076
    • (2003) Plant Physiol , vol.132 , pp. 1065-1076
    • Shockey, J.M.1    Fulda, M.S.2    Browse, J.3
  • 55
    • 0037008203 scopus 로고    scopus 로고
    • Arabidopsis contains nine long-chain acyl-coenzyme a synthetase genes that participate in fatty acid and glycerolipid metabolism
    • Shockey, J.M., Fulda, M.S., and Browse, J.A. (2002). Arabidopsis contains nine long-chain acyl-coenzyme a synthetase genes that participate in fatty acid and glycerolipid metabolism. Plant Physiol. 129: 1710-1722
    • (2002) Plant Physiol , vol.129 , pp. 1710-1722
    • Shockey, J.M.1    Fulda, M.S.2    Browse, J.A.3
  • 56
    • 34248653184 scopus 로고    scopus 로고
    • Rapid, transient expression of fluorescent fusion proteins in tobacco plants and generation of stably transformed plants
    • Sparkes, I.A., Runions, J., Kearns, A., and Hawes, C. (2006). Rapid, transient expression of fluorescent fusion proteins in tobacco plants and generation of stably transformed plants. Nat. Protoc. 1: 2019-2025
    • (2006) Nat. Protoc. , vol.1 , pp. 2019-2025
    • Sparkes, I.A.1    Runions, J.2    Kearns, A.3    Hawes, C.4
  • 57
    • 0344833432 scopus 로고
    • An oxalic acid oxidase in the leaves of Bougainvillea spectabilis
    • Srivastava, S.K., and Krishnan, P.S. (1962). An oxalic acid oxidase in the leaves of Bougainvillea spectabilis. Biochem. J. 85: 33-38
    • (1962) Biochem. J. , vol.85 , pp. 33-38
    • Srivastava, S.K.1    Krishnan, P.S.2
  • 61
    • 22044437388 scopus 로고    scopus 로고
    • The Botany Array Resource: E-Northerns, expression angling, and promoter analyses
    • Toufighi, K., Brady, S.M., Austin, R., Ly, E., and Provart, N.J. (2005). The Botany Array Resource: E-Northerns, expression angling, and promoter analyses. Plant J. 43: 153-163
    • (2005) Plant J , vol.43 , pp. 153-163
    • Toufighi, K.1    Brady, S.M.2    Austin, R.3    Ly, E.4    Provart, N.J.5
  • 62
    • 0028156657 scopus 로고
    • Acetylene reduction by symbiosomes and free bacteroids from broad bean (Vicia faba L.) nodules (role of oxalate)
    • Trinchant, J.C., Guerin, V., and Rigaud, J. (1994). Acetylene reduction by symbiosomes and free bacteroids from broad bean (Vicia faba L.) nodules (role of oxalate). Plant Physiol. 105: 555-561
    • (1994) Plant Physiol , vol.105 , pp. 555-561
    • Trinchant, J.C.1    Guerin, V.2    Rigaud, J.3
  • 63
    • 0037342553 scopus 로고    scopus 로고
    • An enhanced transient expression system in plants based on suppression of gene silencing by the p19 protein of tomato bushy stunt virus
    • Voinnet, O., Rivas, S., Mestre, P., and Baulcombe, D. (2003). An enhanced transient expression system in plants based on suppression of gene silencing by the p19 protein of tomato bushy stunt virus. Plant J. 33: 949-956
    • (2003) Plant J , vol.33 , pp. 949-956
    • Voinnet, O.1    Rivas, S.2    Mestre, P.3    Baulcombe, D.4
  • 64
    • 0034144394 scopus 로고    scopus 로고
    • Differentiation of mucilage secretory cells of the Arabidopsis seed coat
    • Western, T.L., Skinner, D.J., and Haughn, G.W. (2000). Differentiation of mucilage secretory cells of the Arabidopsis seed coat. Plant Physiol. 122: 345-356
    • (2000) Plant Physiol , vol.122 , pp. 345-356
    • Western, T.L.1    Skinner, D.J.2    Haughn, G.W.3
  • 66
    • 0023546276 scopus 로고
    • Studies on the anaerobic degradation of benzoic acid and 2-aminobenzoic acid by a denitrifying Pseudomonas strain
    • Ziegler, K., Braun, K., Bockler, A., and Fuchs, G. (1987). Studies on the anaerobic degradation of benzoic acid and 2-aminobenzoic acid by a denitrifying Pseudomonas strain. Arch. Microbiol. 149: 62-69.
    • (1987) Arch. Microbiol. , vol.149 , pp. 62-69
    • Ziegler, K.1    Braun, K.2    Bockler, A.3    Fuchs, G.4


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