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Volumn 15, Issue 1, 1998, Pages 1-32

Cupins: A New Superfamily of Functionally Diverse Proteins that Include Germins and Plant Storage Proteins

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGY;

EID: 0031948520     PISSN: 02648725     EISSN: 20465556     Source Type: Journal    
DOI: 10.1080/02648725.1998.10647950     Document Type: Article
Times cited : (199)

References (204)
  • 3
    • 0028155477 scopus 로고
    • Trans formed hairy roots of Mesembryanthemum crystallinum: Gene expression patterns upon salt stress
    • Andolfatto, P., Bornhauser, A., Bohnert, H.J. and Thomas, J.C. (1994). Trans formed hairy roots of Mesembryanthemum crystallinum: gene expression patterns upon salt stress. Physiological Plant Physiology 90,708-714.
    • (1994) Physiological Plant Physiology , vol.90 , pp. 708-714
    • Andolfatto, P.1    Bornhauser, A.2    Bohnert, H.J.3    Thomas, J.C.4
  • 4
    • 0001561366 scopus 로고
    • The oxalic acid content of some common foods
    • Andrews, J.C. and Viser, E.T. (1951). The oxalic acid content of some common foods. Food Research 16, 306-312.
    • (1951) Food Research , vol.16 , pp. 306-312
    • Andrews, J.C.1    Viser, E.T.2
  • 7
    • 0024672742 scopus 로고
    • Purification and characterisation of oxalyl-coenzyme A decarboxylase from Oxalobacterformi genes
    • Baetz, A.L. and Allison, M.J. (1989). Purification and characterisation of oxalyl-coenzyme A decarboxylase from Oxalobacterformi genes. Journal of Bacteriology 171,2605-2608.
    • (1989) Journal of Bacteriology , vol.171 , pp. 2605-2608
    • Baetz, A.L.1    Allison, M.J.2
  • 9
    • 0038294198 scopus 로고
    • Determination of oxalate by luminol chemilumines-cence
    • Abstr. 0573
    • Baljon, C.M. and Thibert, R.J. (1994). Determination of oxalate by luminol chemilumines-cence. Clinical Chemistry 40, Abstr. 0573.
    • (1994) Clinical Chemistry , vol.40
    • Baljon, C.M.1    Thibert, R.J.2
  • 10
  • 12
    • 0029587196 scopus 로고
    • Seed storage proteins of spermatophytes share a common ancestor with desiccation proteins of fungi
    • Bäumlein, H., Braun, H., Kakhovskaya, La. and Shütov, A.D. (1995). Seed storage proteins of spermatophytes share a common ancestor with desiccation proteins of fungi. Journal of Molecular Evolution 41, 1070-1075.
    • (1995) Journal of Molecular Evolution , vol.41 , pp. 1070-1075
    • Bäumlein, H.1    Braun, H.2    Kakhovskaya, L.A.3    Shütov, A.D.4
  • 13
    • 0031058124 scopus 로고    scopus 로고
    • The 32-kilobase exp gene cluster of Rhizobium melioti directing the biosynthesis of galactoglucan: Genetic organisation and properties of the encoded gene products
    • Becker, A., Ruberg, S., Küster, H., Roxlau, A.A. and Keller, M. (1997). The 32-kilobase exp gene cluster of Rhizobium melioti directing the biosynthesis of galactoglucan: genetic organisation and properties of the encoded gene products. Journal of Bacteriology 179, 1375-1384.
    • (1997) Journal of Bacteriology , vol.179 , pp. 1375-1384
    • Becker, A.1    Ruberg, S.2    Küster, H.3    Roxlau, A.A.4    Keller, M.5
  • 14
    • 0026736632 scopus 로고
    • Analysis of a polyketide synthesis-encoding gene cluster of Streptomyces curacoi
    • Bergh, S. and Uhlen, M. (1992a). Analysis of a polyketide synthesis-encoding gene cluster of Streptomyces curacoi. Gene 117,131-136.
    • (1992) Gene , vol.117 , pp. 131-136
    • Bergh, S.1    Uhlen, M.2
  • 15
    • 0026811765 scopus 로고
    • Cloning, analysis, and heterologous expression of a polyketide synthase gene cluster of Streptomyces curacoi
    • Bergh, S. and Uhlfin, M. (1992b). Cloning, analysis, and heterologous expression of a polyketide synthase gene cluster of Streptomyces curacoi. Biotechnology and Applied Biochemistry 15, 80-89.
    • (1992) Biotechnology and Applied Biochemistry , vol.15 , pp. 80-89
    • Bergh, S.1    Uhlfin, M.2
  • 16
    • 0031081434 scopus 로고    scopus 로고
    • Regulated expression of a wheal germin gene in tobacco: Oxalate oxidase activity and apoplastic localization of the heterologous protein
    • Berna, A. and Bernier, F. (1997). Regulated expression of a wheal germin gene in tobacco: oxalate oxidase activity and apoplastic localization of the heterologous protein. Plant Molecular Biology 33,417-429.
    • (1997) Plant Molecular Biology , vol.33 , pp. 417-429
    • Berna, A.1    Bernier, F.2
  • 17
    • 0023461304 scopus 로고
    • Gene families encode the major encyslment-specific proteins of Physarum polycephulum plasmodia
    • Bernier, F., Lemieux, G. and Pallotta, D. (1987). Gene families encode the major encyslment-specific proteins of Physarum polycephulum plasmodia. Gene 59,265-277.
    • (1987) Gene , vol.59 , pp. 265-277
    • Bernier, F.1    Lemieux, G.2    Pallotta, D.3
  • 18
    • 0030821171 scopus 로고    scopus 로고
    • Dealing with database explosion: A cautionary note
    • Biiatia, U., Robison, K. and Gilbert, W. (1997). Dealing with database explosion: a cautionary note. Science 276,1724-1725.
    • (1997) Science , vol.276 , pp. 1724-1725
    • Biiatia, U.1    Robison, K.2    Gilbert, W.3
  • 19
    • 0024449599 scopus 로고
    • Analysis of the nucleotide sequence of the Streptomyces glaucescens tan I genes provides key information about the enzymology of polyketide antibiotic synthesis
    • Bibb, M.J., Biro, S., Motamedi, H., Collins, J.F. and Hutchinson, C.R. (1989). Analysis of the nucleotide sequence of the Streptomyces glaucescens tan I genes provides key information about the enzymology of polyketide antibiotic synthesis. EMBO Journal 8, 2727-2736.
    • (1989) EMBO Journal , vol.8 , pp. 2727-2736
    • Bibb, M.J.1    Biro, S.2    Motamedi, H.3    Collins, J.F.4    Hutchinson, C.R.5
  • 20
    • 0027317343 scopus 로고
    • Hybridization and DNA sequence analyses suggest an early evolutionary divergence of related biosynthetic gene sets encoding polyketide antibiotics and spore pigments in Streptomyces spp
    • Blanco, G., Brian, P., Pereda, A., Mendez, C., Salas, J.A. and Chater, K.F. (1993). Hybridization and DNA sequence analyses suggest an early evolutionary divergence of related biosynthetic gene sets encoding polyketide antibiotics and spore pigments in Streptomyces spp. Gene 130, 107-116.
    • (1993) Gene , vol.130 , pp. 107-116
    • Blanco, G.1    Brian, P.2    Pereda, A.3    Mendez, C.4    Salas, J.A.5    Chater, K.F.6
  • 22
    • 0029666134 scopus 로고    scopus 로고
    • A vicilin-like seed protein of cycads: Similarity to sucrose-binding proteins
    • Braun, H., Czhial, A., Shotov, A.D. and Baumlein, H. (1996). A vicilin-like seed protein of cycads: similarity to sucrose-binding proteins. Plant Molecular Biology 31, 35-44.
    • (1996) Plant Molecular Biology , vol.31 , pp. 35-44
    • Braun, H.1    Czhial, A.2    Shotov, A.D.3    Baumlein, H.4
  • 23
    • 0028146327 scopus 로고
    • Mapping the auxin-binding site of auxin-binding protein 1
    • Brown, J.C. and Jones, A.M. (1994). Mapping the auxin-binding site of auxin-binding protein 1. Journal of Biological Chemistry 269, 21136-21140.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 21136-21140
    • Brown, J.C.1    Jones, A.M.2
  • 25
    • 0024060207 scopus 로고
    • Characterisation of a polyubiquiiirj gene from Arahidopsis thaliana
    • Burke, T.J., Callis, J. and Vjerstra, R.D. (1988). Characterisation of a polyubiquiiirj gene from Arahidopsis thaliana. Molecular and General Genetics 213. 435-443.
    • (1988) Molecular and General Genetics , vol.213 , pp. 435-443
    • Burke, T.J.1    Callis, J.2    Vjerstra, R.D.3
  • 27
    • 0016636923 scopus 로고
    • Oxalate and formate in Alcaligenes and Pseudomonas species
    • Chandra, T.S. and Shethna, Y.I. (1975). Oxalate and formate in Alcaligenes and Pseudomonas species. Antonie Van teewenhoek 41, 465-477.
    • (1975) Antonie Van Teewenhoek , vol.41 , pp. 465-477
    • Chandra, T.S.1    Shethna, Y.I.2
  • 28
    • 0014028953 scopus 로고
    • Purification and properties of oxalic acid oxidase
    • Chiriboga, J. (1966). Purification and properties of oxalic acid oxidase. Archive of Biochem-istry and Biophysics 116, 516-523.
    • (1966) Archive of Biochem-Istry and Biophysics , vol.116 , pp. 516-523
    • Chiriboga, J.1
  • 29
    • 0030473529 scopus 로고    scopus 로고
    • Molecular cloning and expression of the hot pepper ERahpi gene encoding auxin-binding protein
    • Choi, S.Y. (1996). Molecular cloning and expression of the hot pepper ERahpi gene encoding auxin-binding protein. Plant Molecular Biology 32, 995-997.
    • (1996) Plant Molecular Biology , vol.32 , pp. 995-997
    • Choi, S.Y.1
  • 31
    • 0025770551 scopus 로고
    • Analysis of an Erwinia chrysanthemi gene cluster involved in pectin degradation
    • Condemine, C. and Robert-Baudouy, J. (1991). Analysis of an Erwinia chrysanthemi gene cluster involved in pectin degradation. Molecular Microbiology 5, 1191-2202.
    • (1991) Molecular Microbiology , vol.5 , pp. 1191-2202
    • Condemine, C.1    Robert-Baudouy, J.2
  • 32
    • 0029955989 scopus 로고    scopus 로고
    • Assimilation of oxalate, acetate, and CO2 by Oxalobacter formigenex
    • Cornick, N.A. and Aluson, M.J. (1996). Assimilation of oxalate, acetate, and CO2 by Oxalobacter formigenex. Canadian Journal of Microbiology 42, 1081-1086.
    • (1996) Canadian Journal of Microbiology , vol.42 , pp. 1081-1086
    • Cornick, N.A.1    Aluson, M.J.2
  • 34
    • 0025129406 scopus 로고
    • Spore col our inStreptomyces coelicolor A 3 (2) involves the developmental regulated synthesis of a compound biosynthetically related to polyketide antibiotics
    • Davis, N.K. and Chater, K.F. (1993). Spore col our inStreptomyces coelicolor A 3 (2) involves the developmental regulated synthesis of a compound biosynthetically related to polyketide antibiotics. Molecular Microbiology 4, 1679-1691.
    • (1993) Molecular Microbiology , vol.4 , pp. 1679-1691
    • Davis, N.K.1    Chater, K.F.2
  • 38
    • 0001418061 scopus 로고
    • Arahidopsis thaliana as a model for studying Sderotinia sclerotiorum pathogenesis
    • Dickman, M.B. and Mitra, A. (1992). Arahidopsis thaliana as a model for studying Sderotinia sclerotiorum pathogenesis. Physiological and Molecular Plant Pathology 41, 255-263.
    • (1992) Physiological and Molecular Plant Pathology , vol.41 , pp. 255-263
    • Dickman, M.B.1    Mitra, A.2
  • 39
    • 0029294599 scopus 로고
    • Three glycosylated polypeptides secreted by several embryogenic cell lines of pine show highly specific serological affinity to antibodies directed against the wheat germin apoprotein monomer
    • Domon, J-M., Dumas, B., Lain£, E., Meyer, Y., David, A. and David, H. (1995). Three glycosylated polypeptides secreted by several embryogenic cell lines of pine show highly specific serological affinity to antibodies directed against the wheat germin apoprotein monomer. Plant Physiology 108, 141-148.
    • (1995) Plant Physiology , vol.108 , pp. 141-148
    • Domon, J.-M.1    Dumas, B.2    Lain£, E.3    Meyer, Y.4    David, A.5    David, H.6
  • 42
    • 0029109382 scopus 로고
    • Tissue-specific expression of germin-like oxalate oxidase during development and fungal infection of barley seedlings
    • Dumas, B., Freynisset, G. and Pallet, K. (1995). Tissue-specific expression of germin-like oxalate oxidase during development and fungal infection of barley seedlings. Plant Physiology 107. 1091-1096.
    • (1995) Plant Physiology , vol.107 , pp. 1091-1096
    • Dumas, B.1    Freynisset, G.2    Pallet, K.3
  • 44
    • 0031888149 scopus 로고    scopus 로고
    • Microbial ancestorsofseedstorageproteinsxonservation of motifs in a functionally diverse superfamily of enzymes
    • Dunwell, J.M. and Gane, P.J. (1998). Microbial ancestorsofseedstorageproteinsxonservation of motifs in a functionally diverse superfamily of enzymes. Journal of Molecular Evolution (in press).
    • (1998) Journal of Molecular Evolution
    • Dunwell, J.M.1    Gane, P.J.2
  • 45
    • 0029660710 scopus 로고    scopus 로고
    • Oxalate production by fungi: Its role in pathogenicity and ecology in the soil environment
    • Dutton, M.V. and Evans, C.S. (1996). Oxalate production by fungi: its role in pathogenicity and ecology in the soil environment. Canadian Journal of Microbiology 42, 881-895.
    • (1996) Canadian Journal of Microbiology , vol.42 , pp. 881-895
    • Dutton, M.V.1    Evans, C.S.2
  • 46
    • 0027464948 scopus 로고
    • Oxalate production by Basidiomycetes, including the white-rot species Coriolus versicolor and Phanerochaete chrysosporium
    • Dutton, M.V., Evans, C.S., Atkey, P.T. and Wood, D.A. (1993). Oxalate production by Basidiomycetes, including the white-rot species Coriolus versicolor and Phanerochaete chrysosporium. Applied Microbiology and Biotechnology 39, 5-10.
    • (1993) Applied Microbiology and Biotechnology , vol.39 , pp. 5-10
    • Dutton, M.V.1    Evans, C.S.2    Atkey, P.T.3    Wood, D.A.4
  • 47
    • 0028056037 scopus 로고
    • Modelling the auxin-binding site of auxin-binding protein I of maize
    • Edgerton, M.D., Tropsha, A. and Jones, A.M. (1994). Modelling the auxin-binding site of auxin-binding protein I of maize. Phytochemistry 35, 1111-1123.
    • (1994) Phytochemistry , vol.35 , pp. 1111-1123
    • Edgerton, M.D.1    Tropsha, A.2    Jones, A.M.3
  • 50
    • 0000057177 scopus 로고    scopus 로고
    • An antibody raised to a maize auxin-binding protein has inhibitory effects on cell division of tobacco protoplasts
    • Fellner, M., Ephritikhine, G., Barbier-Brygoo, H. and Guern, J. (1996). An antibody raised to a maize auxin-binding protein has inhibitory effects on cell division of tobacco protoplasts. Plant Physiology and Biochemistry 34. 133-138.
    • (1996) Plant Physiology and Biochemistry , vol.34 , pp. 133-138
    • Fellner, M.1    Ephritikhine, G.2    Barbier-Brygoo, H.3    Guern, J.4
  • 53
    • 7144232355 scopus 로고    scopus 로고
    • Modelling based on the structure of viciiins predicts a histidine cluster in the active site of oxalate oxidase
    • Gane, P.J., Dunwell, J.M. and Warwickor, J. (1997). Modelling based on the structure of viciiins predicts a histidine cluster in the active site of oxalate oxidase. Journal of Molecular Evolution (in press).
    • (1997) Journal of Molecular Evolution
    • Gane, P.J.1    Dunwell, J.M.2    Warwickor, J.3
  • 55
    • 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. Physiological and Molecular Pathology 37, 179-191.
    • (1990) Physiological and Molecular Pathology , vol.37 , pp. 179-191
    • Godoy, G.1    Steadman, J.R.2    Dickman, M.B.3    Dam, R.4
  • 57
    • 0027022498 scopus 로고
    • A 62-kD sucrose binding protein isexprcssed and localized in tissues actively engaged in sucrosc transport
    • Grimes, H.D., Overvoorde, P.J., Ripp, K., Franceschi, V.R. and Hitt, W.D. (1992). A 62-kD sucrose binding protein isexprcssed and localized in tissues actively engaged in sucrosc transport. The Plant Cell 4, 1561-1574.
    • (1992) The Plant Cell , vol.4 , pp. 1561-1574
    • Grimes, H.D.1    Overvoorde, P.J.2    Ripp, K.3    Franceschi, V.R.4    Hitt, W.D.5
  • 58
    • 0021668860 scopus 로고
    • Signal resistance of a soluble protein to enzyme hydrolysis. An unorthodox approach to the isolation and purification of germin, a rare growth-related protein
    • Grzelczak, Z.F. and Lane, B.G. (1984). Signal resistance of a soluble protein to enzyme hydrolysis. An unorthodox approach to the isolation and purification of germin, a rare growth-related protein. Canadian Journal of Biochemistry and Cell Biology 62, 1351-1353.
    • (1984) Canadian Journal of Biochemistry and Cell Biology , vol.62 , pp. 1351-1353
    • Grzelczak, Z.F.1    Lane, B.G.2
  • 59
    • 0000269056 scopus 로고
    • Germin. Compartmentation of the protein, its translatable mRNA and its biosynthesis among roots, slems, and leaves of wheat seedlings
    • Grzelczak, Z.F., Rahman, S., Kennedy, T.D. and Lane, B.G. (1985). Germin. Compartmentation of the protein, its translatable mRNA and its biosynthesis among roots, slems, and leaves of wheat seedlings. Canadian Journal of Biochemistry and Cell Bioloev 63, 1003-1013.
    • (1985) Canadian Journal of Biochemistry and Cell Bioloev , vol.63 , pp. 1003-1013
    • Grzelczak, Z.F.1    Rahman, S.2    Kennedy, T.D.3    Lane, B.G.4
  • 60
    • 0037618701 scopus 로고
    • The rapid enzymatic determination of oxalate in wort and beer
    • Haas, G.J and Flefschman, A.I. (1961). The rapid enzymatic determination of oxalate in wort and beer. Journal of Food and Agriculture 9. 451-452.
    • (1961) Journal of Food and Agriculture , vol.9 , pp. 451-452
    • Haas, G.J.1    Flefschman, A.I.2
  • 61
    • 0028364942 scopus 로고
    • Contribution of genes from the capsule gene complex (Cps) to lipooligosaccharide biosynthesis and serum resistance in Neisseria meningitidis
    • Hammerschmidt, S., Birkholz, C., Zahringer, U., Robertson, B.D., Van Putten, J., Fueling, O. and Frosch, M. (1994). Contribution of genes from the capsule gene complex (cps) to lipooligosaccharide biosynthesis and serum resistance in Neisseria meningitidis. Molecular Microbiology II, 885-896.
    • (1994) Molecular Microbiology , vol.11 , pp. 885-896
    • Hammerschmidt, S.1    Birkholz, C.2    Zahringer, U.3    Robertson, B.D.4    Van Putten, J.5    Fueling, O.6    Frosch, M.7
  • 62
    • 0028139813 scopus 로고
    • Enzymatic assay of oxalate in urine by flow injection analysis using immobilized oxalate oxidase and chemilumines-cence detection
    • Hansen, E.H., Winthor, S.K. and Gundstrup, M. (1994). Enzymatic assay of oxalate in urine by flow injection analysis using immobilized oxalate oxidase and chemilumines-cence detection. Analytical Letters 27, 1239-1253.
    • (1994) Analytical Letters , vol.27 , pp. 1239-1253
    • Hansen, E.H.1    Winthor, S.K.2    Gundstrup, M.3
  • 63
    • 0025825803 scopus 로고
    • Cloning an Escherichia coli gene encoding a protein remarkably similar to mammalian aldehyde dehydrogenases
    • Heim, R. and Strehler, E.E. (1991). Cloning an Escherichia coli gene encoding a protein remarkably similar to mammalian aldehyde dehydrogenases. Gene 99. 15-23.
    • (1991) Gene , vol.99 , pp. 15-23
    • Heim, R.1    Strehler, E.E.2
  • 64
    • 0028534823 scopus 로고
    • Circadian oscillationsofatranscriptencodingagermm-likeprotein that is associated with cell walls in young leaves of the long-day plant Sinapis alba L
    • Heinrzen, C., Fischer, R., Melzer, S., Kappeler, S., Apel, K. and Stafger, D. (1994). Circadian oscillationsofatranscriptencodingagermm-likeprotein that is associated with cell walls in young leaves of the long-day plant Sinapis alba L. Plant Physiology 106,905-915.
    • (1994) Plant Physiology , vol.106 , pp. 905-915
    • Heinrzen, C.1    Fischer, R.2    Melzer, S.3    Kappeler, S.4    Apel, K.5    Stafger, D.6
  • 65
    • 0026410103 scopus 로고
    • Automated assembly of protein blocks for database searching
    • Henjkoff, S. and Henikoff, J.G. (1991). Automated assembly of protein blocks for database searching. Nucleic Acids Research 19, 6565-6572.
    • (1991) Nucleic Acids Research , vol.19 , pp. 6565-6572
    • Henjkoff, S.1    Henikoff, J.G.2
  • 68
    • 0031580201 scopus 로고    scopus 로고
    • Crystal structure of a decameric complex of human serum amyloid P component with bound dAMP
    • Hohenester, E., Hutchinson, W.L., Pepys, M.B. and Wood, S.P. (1997). Crystal structure of a decameric complex of human serum amyloid P component with bound dAMP. Journal of Molecular Biology 269, 570-578.
    • (1997) Journal of Molecular Biology , vol.269 , pp. 570-578
    • Hohenester, E.1    Hutchinson, W.L.2    Pepys, M.B.3    Wood, S.P.4
  • 71
    • 0001281332 scopus 로고
    • A comparison of the effect of salt on polypeptides and translatable mRNAs of a salt-tolerant and a salt-sensitive cultivar of barley
    • Hurkman, W J., Fornarl C.S. and Tanaka, C.K. (1989). A comparison of the effect of salt on polypeptides and translatable mRNAs of a salt-tolerant and a salt-sensitive cultivar of barley. Plant Physiology 90, 1444-1456.
    • (1989) Plant Physiology , vol.90 , pp. 1444-1456
    • Hurkman, W.J.1    Fornarl, C.S.2    Tanaka, C.K.3
  • 72
    • 0028369213 scopus 로고
    • Nucleotide sequence of a transcript encoding a germ in-like protein that is present in salt-stressed barley (Hordeum vulgare) roots
    • Hurkman, W.J., Lane, B.G. and Tanaka, C.K. (1994). Nucleotide sequence of a transcript encoding a germ in-like protein that is present in salt-stressed barley (Hordeum vulgare) roots. Plant Physiology 104. 803-804.
    • (1994) Plant Physiology , vol.104 , pp. 803-804
    • Hurkman, W.J.1    Lane, B.G.2    Tanaka, C.K.3
  • 73
    • 0001635395 scopus 로고
    • Germin-like polypeptides increase in barley roots during salt stress
    • Hurkman, W.J., Tao, H.P. and Tanaka, C.K. (1991). Germin-like polypeptides increase in barley roots during salt stress. Plant Physiology 97, 366-374.
    • (1991) Plant Physiology , vol.97 , pp. 366-374
    • Hurkman, W.J.1    Tao, H.P.2    Tanaka, C.K.3
  • 74
    • 0030046304 scopus 로고    scopus 로고
    • Effect of salt stress on germin gene expression in barley roots
    • Hurkman, W.J. and Tanaka, C.K. (1996a), Effect of salt stress on germin gene expression in barley roots. Plant Physiology 110. 971-977.
    • (1996) Plant Physiology , vol.110 , pp. 971-977
    • Hurkman, W.J.1    Tanaka, C.K.2
  • 75
    • 0000527312 scopus 로고    scopus 로고
    • Germin gene expression is induced in wheat leaves by powdery mildew infection
    • Hurkman, W.J. and Tanaka, C.K. (1996b). Germin gene expression is induced in wheat leaves by powdery mildew infection. Plant Physiology 111, 735-739.
    • (1996) Plant Physiology , vol.111 , pp. 735-739
    • Hurkman, W.J.1    Tanaka, C.K.2
  • 76
    • 0008918927 scopus 로고
    • Immune complex of banana oxalate oxidase: Use in quantitation of urinary oxalate
    • Inamdar, K.V., Tarachand, Ü., Devasagayam, T.Pa. and Raohavan, K.G. (1986). Immune complex of banana oxalate oxidase: use in quantitation of urinary oxalate. Analytical Letters 19, 1987-1999.
    • (1986) Analytical Letters , vol.19 , pp. 1987-1999
    • Inamdar, K.V.1    Tarachand, Ü.2    Devasagayam, T.3    Raohavan, K.G.4
  • 77
    • 0024319980 scopus 로고
    • Determination of urinaiy oxalate with disposable oxalate oxidase membrane strips
    • Inamdar, K.V., Tarachand, U. and Raghavan, K.G. (1989). Determination of urinaiy oxalate with disposable oxalate oxidase membrane strips. Analytical Letters 22,841-851.
    • (1989) Analytical Letters , vol.22 , pp. 841-851
    • Inamdar, K.V.1    Tarachand, U.2    Raghavan, K.G.3
  • 80
    • 0025980642 scopus 로고
    • Structure and sequence of the rfb (O antigen) gene cluster of Salmonella scrovar ryphimurium (strain LT2)
    • Jiang, X.M., Neal, B., Santiago, F., Lee, S.J., Romana, L.K. and Reeves, P.R. (1991). Structure and sequence of the rfb (O antigen) gene cluster of Salmonella scrovar ryphimurium (strain LT2). Molecular Microbiology 5, 695-713.
    • (1991) Molecular Microbiology , vol.5 , pp. 695-713
    • Jiang, X.M.1    Neal, B.2    Santiago, F.3    Lee, S.J.4    Romana, L.K.5    Reeves, P.R.6
  • 84
    • 0027138815 scopus 로고
    • A 3.9-kb DNA region of Xanthomonas campestris pwcampestris that is necessary for lipopolysaccharide production encodes a set of enzymes involved in the synthes is of dTDP-rhamnose
    • Koplin, R., Wang, G., Hotte, B., Priefer, U.B. and Puiiler, A. (1993). A 3.9-kb DNA region of Xanthomonas campestris pw.campestris that is necessary for lipopolysaccharide production encodes a set of enzymes involved in the synthes is of dTDP-rhamnose. Journal of Bacteriology 175,7782-7792.
    • (1993) Journal of Bacteriology , vol.175 , pp. 7782-7792
    • Koplin, R.1    Wang, G.2    Hotte, B.3    Priefer, U.B.4    Puiiler, A.5
  • 85
    • 0031569895 scopus 로고    scopus 로고
    • Oxalate oxidase from barley roots: Purification to homogeneity and study of some molecular, catalytic, and binding properties
    • Kotsira, V.P. and Clonis, Y.D. (1997). Oxalate oxidase from barley roots: purification to homogeneity and study of some molecular, catalytic, and binding properties. Archives of Biochemistry and Biophysics 340, 239-249.
    • (1997) Archives of Biochemistry and Biophysics , vol.340 , pp. 239-249
    • Kotsira, V.P.1    Clonis, Y.D.2
  • 86
    • 85004331379 scopus 로고
    • Purification and characterization of oxalate oxidase from Pseudomonas sp. OX-53
    • Koyama, H. (1988). Purification and characterization of oxalate oxidase from Pseudomonas sp. OX-53. Agricultural and Biological Chemistry 52,743-748.
    • (1988) Agricultural and Biological Chemistry , vol.52 , pp. 743-748
    • Koyama, H.1
  • 87
    • 0027379978 scopus 로고
    • Nucleotide sequence analysis of five putative Streptomyces griseus genes, one of which complements an early function in daunorubicin biosynthesis that is linked to a putative gene cluster involved in TDP-daunosamine formation
    • Krugel, H., Schumann, G., Hanel, F. and Fiedler, G. (1993). Nucleotide sequence analysis of five putative Streptomyces griseus genes, one of which complements an early function in daunorubicin biosynthesis that is linked to a putative gene cluster involved in TDP-daunosamine formation. Molecular and General Genetics 241, 193-202.
    • (1993) Molecular and General Genetics , vol.241 , pp. 193-202
    • Krugel, H.1    Schumann, G.2    Hanel, F.3    Fiedler, G.4
  • 88
    • 84920301801 scopus 로고
    • Partial purification, some properties and possible physiological role of an oxalate oxidase from grain sorghum leaves
    • Kuchhal, N.K., Satypal and Pundir, C.S. (1993). Partial purification, some properties and possible physiological role of an oxalate oxidase from grain sorghum leaves. Indian Journal of Plant Physiology 36, 159-162.
    • (1993) Indian Journal of Plant Physiology , vol.36 , pp. 159-162
    • Kuchhal, N.K.1    Satypal And Pundir, C.S.2
  • 89
    • 0029901748 scopus 로고    scopus 로고
    • Generation of a proton motive force by the anaerobic oxalate-degrading bacterium Oxalobacter formigenes
    • Kühner, C.H., Hartman, P. A. and Allison, M.J. (1996). Generation of a proton motive force by the anaerobic oxalate-degrading bacterium Oxalobacter formigenes. Applied and Environmental Microbiology 62, 2494-2500.
    • (1996) Applied and Environmental Microbiology , vol.62 , pp. 2494-2500
    • Kühner, C.H.1    Hartman, P.A.2    Allison, M.J.3
  • 91
    • 0029072158 scopus 로고
    • Biomimetic dye-ligands for oxalate recognizing enzymes. Studies with oxalate oxidase and oxalate decarboxylase
    • Labrou, N.E. and Clonis, Y.D. (1995). Biomimetic dye-ligands for oxalate recognizing enzymes. Studies with oxalate oxidase and oxalate decarboxylase. Journal of Biotechnology 40, 59-70.
    • (1995) Journal of Biotechnology , vol.40 , pp. 59-70
    • Labrou, N.E.1    Clonis, Y.D.2
  • 92
    • 2642676086 scopus 로고
    • The molecular-genetic analysis of Triticum tauschii, the D genome donor to hexaploid wheat
    • Lagudah, E.S., Apels, R. and Brown, A.D.H. (1991). The molecular-genetic analysis of Triticum tauschii, the D genome donor to hexaploid wheat. Genome 36,913-918.
    • (1991) Genome , vol.36 , pp. 913-918
    • Lagudah, E.S.1    Apels, R.2    Brown, A.D.H.3
  • 93
    • 0019161355 scopus 로고
    • Spectrophotometric determination of urinary oxalate with oxalate oxidase prepared from moss
    • Laker, M.F., Hofman, A.F. and Meeuse, B.J. (1980). Spectrophotometric determination of urinary oxalate with oxalate oxidase prepared from moss. Clinical Chemistry 26,827-830.
    • (1980) Clinical Chemistry , vol.26 , pp. 827-830
    • Laker, M.F.1    Hofman, A.F.2    Meeuse, B.J.3
  • 94
    • 0025719084 scopus 로고
    • Cellular desiccation andhydration: Developmentally regulatedproteins, and the maturation and germination of seed embryos
    • Lane, B.G. (1991). Cellular desiccation andhydration: developmentally regulatedproteins, and the maturation and germination of seed embryos. FASEB Journal 5, 2893-2901.
    • (1991) FASEB Journal , vol.5 , pp. 2893-2901
    • Lane, B.G.1
  • 95
    • 0028270214 scopus 로고
    • Oxalate, germin, and the extracellular matrix of higher plants
    • Lane, B.G. (1994). Oxalate, germin, and the extracellular matrix of higher plants. FASEB Journal 8,294-301.
    • (1994) FASEB Journal , vol.8 , pp. 294-301
    • Lane, B.G.1
  • 100
    • 0029124544 scopus 로고
    • Determination of urinary oxalate using banana oxalate oxidase: Comparison with immobilized enzyme
    • Lathika, K.M., Inamdar, K.V., Tarachand, U., Singh, B.B. and Raghavan, K.G. (1995a). Determination of urinary oxalate using banana oxalate oxidase: comparison with immobilized enzyme. Analytical tetters 28,425-442.
    • (1995) Analytical Tetters , vol.28 , pp. 425-442
    • Lathika, K.M.1    Inamdar, K.V.2    Tarachand, U.3    Singh, B.B.4    Raghavan, K.G.5
  • 101
    • 0029077469 scopus 로고
    • Oxalate depletion from leafy vegetables using alginate entrapped banana oxalate oxidase
    • Lathika, K.M., Sharma, S., Inambar, K.V. and Raghavan, K.G. (1995b). Oxalate depletion from leafy vegetables using alginate entrapped banana oxalate oxidase. Biotechnology Letters 17, 407-410.
    • (1995) Biotechnology Letters , vol.17 , pp. 407-410
    • Lathika, K.M.1    Sharma, S.2    Inambar, K.V.3    Raghavan, K.G.4
  • 102
    • 0028361114 scopus 로고
    • Structure of phaseolin at 2.2 A resolution: Implications for a common viciiin/legumin structure and the genetic engineering of seed storage proteins
    • Lawrence, M.C., Izard, T., Beuchat, M., Blagrove, R.J. and Colman, P.M. (1994). Structure of phaseolin at 2.2 A resolution: Implications for a common viciiin/legumin structure and the genetic engineering of seed storage proteins. Journal of Molecular Biology 238, 748-776.
    • (1994) Journal of Molecular Biology , vol.238 , pp. 748-776
    • Lawrence, M.C.1    Izard, T.2    Beuchat, M.3    Blagrove, R.J.4    Colman, P.M.5
  • 103
    • 0030152386 scopus 로고    scopus 로고
    • Characterization of a strawberry gene for auxin-binding protein, and its expression in insect cells
    • Lazarus, C.M. and Macdonald, H. (1996). Characterization of a strawberry gene for auxin-binding protein, and its expression in insect cells. Plant Molecular Biology 31,267-277.
    • (1996) Plant Molecular Biology , vol.31 , pp. 267-277
    • Lazarus, C.M.1    Macdonald, H.2
  • 104
    • 0031106179 scopus 로고    scopus 로고
    • Characterization of two cDNAs encoding auxin-binding proteins inNicotiana tabacum
    • Leblanc, N., Roux, C., Pradjer, J.M. and Perrot-Rechenmann, C. (1997). Characterization of two cDNAs encoding auxin-binding proteins inNicotiana tabacum. Plant Molecular Biology 33,679-689.
    • (1997) Plant Molecular Biology , vol.33 , pp. 679-689
    • Leblanc, N.1    Roux, C.2    Pradjer, J.M.3    Perrot-Rechenmann, C.4
  • 106
    • 0030045016 scopus 로고    scopus 로고
    • Cloning, purification, and properties of a phosphotyrosine protein from Streptomyces coelicolor A3(2)
    • Li, Y. and Strohl, W.R. (1996). Cloning, purification, and properties of a phosphotyrosine protein from Streptomyces coelicolor A3(2). Journal of Bacteriology 178, 136-142.
    • (1996) Journal of Bacteriology , vol.178 , pp. 136-142
    • Li, Y.1    Strohl, W.R.2
  • 109
    • 0025756826 scopus 로고
    • Cloning and expression of the oxalyl-CoA decarboxylase gene from the bacterium, Oxalobacterformigenes: Prospects for gene therapy to control Ca-oxalate kidney stone formation
    • Lung, H-Y., Cornelius, J.G. and Peck, A.B. (1991). Cloning and expression of the oxalyl-CoA decarboxylase gene from the bacterium, Oxalobacterformigenes: Prospects for gene therapy to control Ca-oxalate kidney stone formation. American Journal of Kidney Diseases 17, 381-385.
    • (1991) American Journal of Kidney Diseases , vol.17 , pp. 381-385
    • Lung, H.-Y.1    Cornelius, J.G.2    Peck, A.B.3
  • 110
    • 0028355157 scopus 로고
    • Molecular cloning, DNA sequence, and gene expression of the oxalyl-coenzyme A decarboxylase gene, oxc, from the bacterium Oxalobacterformigenes
    • Lung, H-Y., Baetz, A.L. and Peck, A.B. (1994). Molecular cloning, DNA sequence, and gene expression of the oxalyl-coenzyme A decarboxylase gene, oxc, from the bacterium Oxalobacterformigenes. Journal of Bacteriology 176,2468-2472.
    • (1994) Journal of Bacteriology , vol.176 , pp. 2468-2472
    • Lung, H.-Y.1    Baetz, A.L.2    Peck, A.B.3
  • 111
    • 0030900410 scopus 로고    scopus 로고
    • The rate of phaseolin assembly is controlled by the glucosylation state of its N-linked oligosaccharide chains
    • Lupatelu, F., Pedrazzjni, E., Boluni, R., Vitale, A. and Ceriotti, A. (1997). The rate of phaseolin assembly is controlled by the glucosylation state of its N-linked oligosaccharide chains. The Plant Cell 9,597-609.
    • (1997) The Plant Cell , vol.9 , pp. 597-609
    • Lupatelu, F.1    Pedrazzjni, E.2    Boluni, R.3    Vitale, A.4    Ceriotti, A.5
  • 112
    • 0028232084 scopus 로고
    • Characterisation of the dTDP-rhamnose biosynthetic genes encoded in the rfb locus of Shigella flexneri
    • Macpherson, D.F., Manning, P.A. and Morona, R. (1994). Characterisation of the dTDP-rhamnose biosynthetic genes encoded in the rfb locus of Shigella flexneri. Molecular Microbiology 11,281-292.
    • (1994) Molecular Microbiology , vol.11 , pp. 281-292
    • Macpherson, D.F.1    Manning, P.A.2    Morona, R.3
  • 114
    • 0000564054 scopus 로고
    • Oxalic acid, cell wall degrading enzymes and their significance in the virulence of two Sclerotinia sclerotiorum isolates on sunflower
    • Marciano, P., Di Lenna, P. and Macro, P. (1983). Oxalic acid, cell wall degrading enzymes and their significance in the virulence of two Sclerotinia sclerotiorum isolates on sunflower. Plant Pathology 22, 339-345.
    • (1983) Plant Pathology , vol.22 , pp. 339-345
    • Marciano, P.1    Di Lenna, P.2    Macro, P.3
  • 115
    • 0029560547 scopus 로고
    • Genetic analysis of the dTDP-rhamnose biosynthesis region of Escherichia coli VW 187 (07:K I) rfb geneclustcr: Identification of functional homologs of ifbB and rfbA in the rff cluster and correct location of rffe gene
    • Marolda, C.L. and Valvano, M.A. (1995). Genetic analysis of the dTDP-rhamnose biosynthesis region of Escherichia coli VW 187 (07:K I) rfb geneclustcr: identification of functional homologs of ifbB and rfbA in the rff cluster and correct location of rffe gene. Journal of Bacteriology 177, 5539-5546.
    • (1995) Journal of Bacteriology , vol.177 , pp. 5539-5546
    • Marolda, C.L.1    Valvano, M.A.2
  • 116
    • 0000915734 scopus 로고
    • Sclerotinia and Phomopsis-two devastating sunflower pathogens
    • Masirevic, S. and Gulya, T.J. (1992). Sclerotinia and Phomopsis-two devastating sunflower pathogens. Field Crops Research 30, 271-300.
    • (1992) Field Crops Research , vol.30 , pp. 271-300
    • Masirevic, S.1    Gulya, T.J.2
  • 117
    • 0028075334 scopus 로고
    • Identification of amino acid residues involved in the activity of phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase. A bifunctional enzyme in the alginate biosynthetic pathway of Pseudomonas aeruginosa
    • May, T.B., Shinabarger, D., Boyd, A. and Chakrabarty, A.M. (1994). Identification of amino acid residues involved in the activity of phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase. A bifunctional enzyme in the alginate biosynthetic pathway of Pseudomonas aeruginosa. Journal of Biological Chemistry 269, 4872-4877.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 4872-4877
    • May, T.B.1    Shinabarger, D.2    Boyd, A.3    Chakrabarty, A.M.4
  • 118
    • 0001193081 scopus 로고
    • Germin: Physicochemical properties of the glycoprotein which s ignals the onset of growth in the germinating wheal embryo
    • Mccubbin, W.C., Cyril, M.K., Kennedy, T.D. and Lane, B.G. (1987). Germin: physicochemical properties of the glycoprotein which s ignals the onset of growth in the germinating wheal embryo. Biochemistry and Cell Biology 65, 1039-1048.
    • (1987) Biochemistry and Cell Biology , vol.65 , pp. 1039-1048
    • McCubbin, W.C.1    Cyril, M.K.2    Kennedy, T.D.3    Lane, B.G.4
  • 119
    • 0008074058 scopus 로고
    • An inhibitor of oxalic acid oxidase in beet extracts
    • Meeuse, B.J.D. and Campbell, J.M. (1959). An inhibitor of oxalic acid oxidase in beet extracts. Plant Physiology 34, 583-586.
    • (1959) Plant Physiology , vol.34 , pp. 583-586
    • Meeuse, B.J.D.1    Campbell, J.M.2
  • 120
    • 0026352583 scopus 로고
    • Oxalate decarboxylase from Collyhia velutipes. Purification, characterisation and cloning
    • Mehta, A. and Daita, A. (1991). Oxalate decarboxylase from Collyhia velutipes. Purification, characterisation and cloning. Journal of Biological Chemistry, 2(5), 23548-23553.
    • (1991) Journal of Biological Chemistry , vol.2 , Issue.5 , pp. 23548-23553
    • Mehta, A.1    Daita, A.2
  • 121
    • 0029188962 scopus 로고
    • Oxalate decarboxylase in the brown-rot wood decay fungus Postia placenta
    • Micales, J.A. (1995). Oxalate decarboxylase in the brown-rot wood decay fungus Postia placenta. Material Organismen 29, 177-186.
    • (1995) Material Organismen , vol.29 , pp. 177-186
    • Micales, J.A.1
  • 122
    • 0000318696 scopus 로고
    • Nucleotide sequence of a root-specific transcript encoding a germin-like protein from the halophyte Mesemhryanthetmm crystallinum
    • Mlchalowskl, C.B. and Bohnert, H.J. (1992). Nucleotide sequence of a root-specific transcript encoding a germin-like protein from the halophyte Mesemhryanthetmm crystallinum. Plant Physiology 100, 537-538.
    • (1992) Plant Physiology , vol.100 , pp. 537-538
    • Mlchalowskl, C.B.1    Bohnert, H.J.2
  • 124
    • 0031053420 scopus 로고    scopus 로고
    • Identification and characterisation of the dTDP-rhamnose biosynthesis and transfer genes of the lipopolysaccharide-related rfh locus in Leptospira interrogans serovar Copenhagen i
    • Mitci Hson, M., Bulach, D.M., Vinh, T., Rajakumar, K., Faine, S. and Adler, B. (1997). Identification and characterisation of the dTDP-rhamnose biosynthesis and transfer genes of the lipopolysaccharide-related rfh locus in Leptospira interrogans serovar Copenhagen i. Journal of Bacteriology 179, 1262-1267.
    • (1997) Journal of Bacteriology , vol.179 , pp. 1262-1267
    • Mitci Hson, M.1    Bulach, D.M.2    Vinh, T.3    Rajakumar, K.4    Faine, S.5    Adler, B.6
  • 126
    • 0027372804 scopus 로고
    • Can homologous proteins evolve different enzymatic activities?
    • Murzin, A.G. (1993). Can homologous proteins evolve different enzymatic activities? Trends in Biochemical Science 18,403-405.
    • (1993) Trends in Biochemical Science , vol.18 , pp. 403-405
    • Murzin, A.G.1
  • 127
    • 0029178046 scopus 로고
    • Towards an understanding of ABPI
    • Napier, R.M. (1995). Towards an understanding of ABPI. Journal of Experimental Botanv 46, 1787-1795.
    • (1995) Journal of Experimental Botanv , vol.46 , pp. 1787-1795
    • Napier, R.M.1
  • 128
    • 0029140360 scopus 로고
    • Auxin action and auxin-binding proteins
    • Napier, R.M. and Venis, M.A. (1995). Auxin action and auxin-binding proteins. New Phytologist 129, 167-201.
    • (1995) New Phytologist , vol.129 , pp. 167-201
    • Napier, R.M.1    Venis, M.A.2
  • 131
    • 0002094024 scopus 로고
    • Role of oxalic acid in the Sclerotinia wilt of sunflower
    • Noyes, R.D. and Hancock, J.G. (1981). Role of oxalic acid in the Sclerotinia wilt of sunflower. Physiological Plant Pathology 18, 123-132.
    • (1981) Physiological Plant Pathology , vol.18 , pp. 123-132
    • Noyes, R.D.1    Hancock, J.G.2
  • 132
    • 0020501622 scopus 로고
    • Quantification of urinary oxalate with oxalate oxidase from beet stems
    • Obzansky, D.M. and Richardson, K.E. (1983). Quantification of urinary oxalate with oxalate oxidase from beet stems. Clinical Chemistry 29, 1815-1819.
    • (1983) Clinical Chemistry , vol.29 , pp. 1815-1819
    • Obzansky, D.M.1    Richardson, K.E.2
  • 134
    • 0042127880 scopus 로고
    • Sequence analysis of ß-xylosidase gene from Bacillus stearothermophilus
    • Oh, H. and Choi, Y. (1994). Sequence analysis of ß-xylosidase gene from Bacillus stearothermophilus. Korean Journal ofApplied Microbiology and Biotechnology, 22, 134-142.
    • (1994) Korean Journal Ofapplied Microbiology and Biotechnology , vol.22 , pp. 134-142
    • Oh, H.1    Choi, Y.2
  • 135
    • 0000066602 scopus 로고
    • Purification and properties of an aux in-binding protein from the shoot apex of peach tree
    • Ohmiya, A., Kikuchi, M., Sakai, S. and Hayashi, T. (1993). Purification and properties of an aux in-binding protein from the shoot apex of peach tree. Plant Cell Physiology 34,177-183.
    • (1993) Plant Cell Physiology , vol.34 , pp. 177-183
    • Ohmiya, A.1    Kikuchi, M.2    Sakai, S.3    Hayashi, T.4
  • 136
    • 7144236793 scopus 로고
    • Absorption of calcium and oxalic acid in higher green plants
    • Olsen, C. (1939). Absorption of calcium and oxalic acid in higher green plants. Comptes Rendus de Travaux Laboratoire Carlsberg 23, 101-124.
    • (1939) Comptes Rendus De Travaux Laboratoire Carlsberg , vol.23 , pp. 101-124
    • Olsen, C.1
  • 138
    • 38249006702 scopus 로고
    • Changes in polypeptides in Pharbitis cotyledons during the first flower-inductive period
    • Ono, M., Sage-Ono, K., Yasui, M., Okasaki, M. and Harada, H. (1993). Changes in polypeptides in Pharbitis cotyledons during the first flower-inductive period. Plant Science 89. 135-145.
    • (1993) Plant Science , vol.89 , pp. 135-145
    • Ono, M.1    Sage-Ono, K.2    Yasui, M.3    Okasaki, M.4    Harada, H.5
  • 139
    • 0030248929 scopus 로고    scopus 로고
    • Transient increase in the level of mRNA for a germin-Iike protein in leaves of the short-day plant Pharbitis nil during the photoperiodic induction of flowering
    • Ono, M., Sage-Ono, K., Inode, M., Kamada, H. and Harada, H. (1996). Transient increase in the level of mRNA for a germin-Iike protein in leaves of the short-day plant Pharbitis nil during the photoperiodic induction of flowering. Plant Cell Physiology 37, 855-861.
    • (1996) Plant Cell Physiology , vol.37 , pp. 855-861
    • Ono, M.1    Sage-Ono, K.2    Inode, M.3    Kamada, H.4    Harada, H.5
  • 140
    • 85024003443 scopus 로고
    • Decomposition of oxalic acid by plants (In Russian). Bulletin of the Academy of Science, Petrograd, 937-948
    • Palladin, V.I. and Lovchinovskaya, E.I. (1916). Decomposition of oxalic acid by plants (in Russian). Bulletin of the Academy of Science, Petrograd, 937-948. Abstract in Chemical Abstract (1917) 11, 48.
    • (1916) Abstract in Chemical Abstract (1917) , vol.11 , pp. 48
    • Palladin, V.I.1    Lovchinovskaya, E.I.2
  • 141
    • 0026812337 scopus 로고
    • Molecular analysis of an auxin binding protein gene located on chromosome 4 of Arahidopsis
    • Palme, K., Hesse, T., Campos, N., Garbers, C. and Yanofsky, M.F. (1992). Molecular analysis of an auxin binding protein gene located on chromosome 4 of Arahidopsis. The Plant Cell 4. 193-201.
    • (1992) The Plant Cell , vol.4 , pp. 193-201
    • Palme, K.1    Hesse, T.2    Campos, N.3    Garbers, C.4    Yanofsky, M.F.5
  • 142
    • 7144234264 scopus 로고
    • The importance of oxygen in the nutrient substrate for planls-organic acid
    • Pepkowrrz, L.P., Gilbert, S.G. and Siuve, J.W. (1941). The importance of oxygen in the nutrient substrate for planls-organic acid. Soil Science 58, 295-303.
    • (1941) Soil Science , vol.58 , pp. 295-303
    • Pepkowrrz, L.P.1    Gilbert, S.G.2    Siuve, J.W.3
  • 146
    • 0026332251 scopus 로고
    • Genetics of streptomycin production in Streptomyces griseus: Molecular structure and putative function of genes strELMB2N
    • Pissowotzki, K., Mansourl K. and Piepersberg, W. (1991). Genetics of streptomycin production in Streptomyces griseus: molecular structure and putative function of genes strELMB2N. Molecular and General Genetics 231, 113-123.
    • (1991) Molecular and General Genetics , vol.231 , pp. 113-123
    • Pissowotzki, K.1    Mansourl, K.2    Piepersberg, W.3
  • 147
    • 0042903727 scopus 로고
    • Statocytes of the wheat haulm
    • Prankerd, T.L. (1920). Statocytes of the wheat haulm. Botanical Gazette 70, 148-152.
    • (1920) Botanical Gazette , vol.70 , pp. 148-152
    • Prankerd, T.L.1
  • 149
    • 0029838899 scopus 로고    scopus 로고
    • In vivo and in vitro folding of a recombinant metalloenzyme. Phosphomannose isomerase
    • Proudfoot, A.E., Goffin, L., Payton, M.A., Wells, T.N. and Bernard, A.R. (1996). In vivo and in vitro folding of a recombinant metalloenzyme. phosphomannose isomerase. Biochemical Journal 318. 437-442.
    • (1996) Biochemical Journal , vol.318 , pp. 437-442
    • Proudfoot, A.E.1    Goffin, L.2    Payton, M.A.3    Wells, T.N.4    Bernard, A.R.5
  • 150
    • 0008243555 scopus 로고
    • Purification and properties of an oxalate oxidase from Sorghum leaves
    • Pundir, C.S. (1991). Purification and properties of an oxalate oxidase from Sorghum leaves. Phytochemistry 30, 1065-1067.
    • (1991) Phytochemistry , vol.30 , pp. 1065-1067
    • Pundir, C.S.1
  • 151
    • 0000871154 scopus 로고
    • Detection of an oxalate oxidase in grain sorghum roots
    • Pundir, C.S. and Kuchhal, N.K. (1989). Detection of an oxalate oxidase in grain sorghum roots. Phytochemistry 28, 2909-2912.
    • (1989) Phytochemistry , vol.28 , pp. 2909-2912
    • Pundir, C.S.1    Kuchhal, N.K.2
  • 152
    • 0001544217 scopus 로고
    • Occurrence of an oxalate oxidase in Sorghum leaves
    • Pundir, C.S. and Nath, R. (1984). Occurrence of an oxalate oxidase in Sorghum leaves. Phytochemistry 23, 1871-1874.
    • (1984) Phytochemistry , vol.23 , pp. 1871-1874
    • Pundir, C.S.1    Nath, R.2
  • 153
    • 0022525914 scopus 로고
    • Degradation of oxalate in rats implanted with immobilized oxalate oxidase
    • Raghavan, K.G. and Tarachand, U. (1986). Degradation of oxalate in rats implanted with immobilized oxalate oxidase. FEBS Letters 195, 101-105.
    • (1986) FEBS Letters , vol.195 , pp. 101-105
    • Raghavan, K.G.1    Tarachand, U.2
  • 154
    • 0031021970 scopus 로고    scopus 로고
    • Biotechnology and the red seaweed polysaccharide industry: Status, needs and prospects
    • Renn, D. (1997). Biotechnology and the red seaweed polysaccharide industry: status, needs and prospects. Trends in Biotechnology 15, 9-14.
    • (1997) Trends in Biotechnology , vol.15 , pp. 9-14
    • Renn, D.1
  • 155
    • 84920298143 scopus 로고
    • The identification of cryptic rhamnose biosynthesis genes in Neisseria gonorrhoea and their relationship to lipopoiy-saccharide biosynthesis
    • Robertson, Bd., Frosch, M. and Van Putten, J.P. (1994). The identification of cryptic rhamnose biosynthesis genes in Neisseria gonorrhoea and their relationship to lipopoiy-saccharide biosynthesis. Molecular Microbiology 11, 281-292.
    • (1994) Molecular Microbiology , vol.11 , pp. 281-292
    • Robertson, B.D.1    Frosch, M.2    Van Putten, J.P.3
  • 156
    • 0027143263 scopus 로고
    • Oxalic acid effects in exudates of Sderotinia trifolium and S. Sclerotiorum and potential uses in selection
    • Rowe, D.E. (1993). Oxalic acid effects in exudates of Sderotinia trifolium and S. sclerotiorum and potential uses in selection. Crop Science 33, 1146-1149.
    • (1993) Crop Science , vol.33 , pp. 1146-1149
    • Rowe, D.E.1
  • 158
    • 0000070363 scopus 로고
    • On a treadmill: Breeding sunflowers for resistance to disease
    • Sackston, W.E. (1992). On a treadmill: breeding sunflowers for resistance to disease. Annual Review of Phytopathology 30, 529-551.
    • (1992) Annual Review of Phytopathology , vol.30 , pp. 529-551
    • Sackston, W.E.1
  • 159
    • 0028593895 scopus 로고
    • Comparison of performance and analytical applications of two immobilized oxalate sensors
    • Sakaamini, M.A. and Vallon, J.J. (1994). Comparison of performance and analytical applications of two immobilized oxalate sensors. Analytica Chimica Acta 299, 75-79.
    • (1994) Analytica Chimica Acta , vol.299 , pp. 75-79
    • Sakaamini, M.A.1    Vallon, J.J.2
  • 160
    • 0029879888 scopus 로고    scopus 로고
    • Cloning of type 8 capsule genes and analysis of gene clusters of di fferent capsular polysaccharides in Staphylococcus aureus
    • Sau, S. and Lee, C.Y. (1996). Cloning of type 8 capsule genes and analysis of gene clusters of di fferent capsular polysaccharides in Staphylococcus aureus. Journal ofBacteriology 178, 2118-2126.
    • (1996) Journal Ofbacteriology , vol.178 , pp. 2118-2126
    • Sau, S.1    Lee, C.Y.2
  • 161
    • 0027665030 scopus 로고
    • Molecular analysis of three maize 22kDa auxin-binding protein genes-transient expression and regulatory regions
    • Schwob, E., Choi, S-Y., Simmons, C., Migliaccio, F., Ilag, L., Hesse, T., Palme, K. and Soll, D. (1993). Molecular analysis of three maize 22kDa auxin-binding protein genes-transient expression and regulatory regions. The Plant Journal 4,423-432.
    • (1993) The Plant Journal , vol.4 , pp. 423-432
    • Schwob, E.1    Choi, S.-Y.2    Simmons, C.3    Migliaccio, F.4    Ilag, L.5    Hesse, T.6    Palme, K.7    Soll, D.8
  • 163
    • 0000007203 scopus 로고
    • Oxalic acid decarboxylase, a new enzyme from the mycelia of wood destroying fungi
    • Shimazono, H. (1955). Oxalic acid decarboxylase, a new enzyme from the mycelia of wood destroying fungi. Journal of Biochemistry 42, 321-340.
    • (1955) Journal of Biochemistry , vol.42 , pp. 321-340
    • Shimazono, H.1
  • 164
    • 0002018028 scopus 로고
    • Decarboxylation of oxalic acid during ripening of banana fruit (Musa sapientum L)
    • Shimokawa, K., Ubda, Y. and Kasai, Z. (1972). Decarboxylation of oxalic acid during ripening of banana fruit (Musa sapientum L). Agricultural and Biological Chemistry 36. 2021-2024.
    • (1972) Agricultural and Biological Chemistry , vol.36 , pp. 2021-2024
    • Shimokawa, K.1    Ubda, Y.2    Kasai, Z.3
  • 165
    • 0027611632 scopus 로고
    • Structure of the gene for an auxin-binding protein and a gene for 7SL RNA from Arabidopsis thaliana
    • Shimomura, S., Liu, W., Inohara, N., Watanabe, S. and Futai, M. (1993). Structure of the gene for an auxin-binding protein and a gene for 7SL RNA from Arabidopsis thaliana. Plant Cell Physiology 34,633-637.
    • (1993) Plant Cell Physiology , vol.34 , pp. 633-637
    • Shimomura, S.1    Liu, W.2    Inohara, N.3    Watanabe, S.4    Futai, M.5
  • 166
    • 0030995329 scopus 로고    scopus 로고
    • DNA sequencing and expression of the formyl coenzyme A transferase gene, frc, from O.Xalobacter formigenes
    • Sfdhu, H., Ogden, S.D., Lung, H.Y., Luttge, B.G., Baetz, A.L. and Peck, A.B. (1997). DNA sequencing and expression of the formyl coenzyme A transferase gene, frc, from O.xalobacter formigenes. Journal of Microbiology 179, 3378-3381.
    • (1997) Journal of Microbiology , vol.179 , pp. 3378-3381
    • Sfdhu, H.1    Ogden, S.D.2    Lung, H.Y.3    Luttge, B.G.4    Baetz, A.L.5    Peck, A.B.6
  • 167
    • 0022432415 scopus 로고
    • Nucleotide sequences from phaseolin cDNA clones: The major storage proteins from Phaseolus vulgaris arc encoded by two unique gene families
    • Slightom, J.L., Drong, R.F., Klassey, R.C. and Hoffman, L.M. (1985). Nucleotide sequences from phaseolin cDNA clones: The major storage proteins from Phaseolus vulgaris arc encoded by two unique gene families. Nucleic Acids Research 13,6483-6498.
    • (1985) Nucleic Acids Research , vol.13 , pp. 6483-6498
    • Slightom, J.L.1    Drong, R.F.2    Klassey, R.C.3    Hoffman, L.M.4
  • 168
    • 0027213769 scopus 로고
    • The ancestral lnep replication system consisted of contiguous oriV and trfA segments as deduced from a comparison of the nucleotide sequences of diverse IncP plasmids
    • Smith, C.A., Pinkney, M., Guiney, D.G. and Thomas, C.M. (1993). The ancestral lnep replication system consisted of contiguous oriV and trfA segments as deduced from a comparison of the nucleotide sequences of diverse IncP plasmids. Journal of General Microbiology 139, 1761-1766.
    • (1993) Journal of General Microbiology , vol.139 , pp. 1761-1766
    • Smith, C.A.1    Pinkney, M.2    Guiney, D.G.3    Thomas, C.M.4
  • 169
    • 0031047005 scopus 로고    scopus 로고
    • Identification of an Fe(IH)-dihydroxyphenylalanine site in recombinant phosphomannose isomerase from Candida albicans
    • Smith, J.J., Thomson, Aj., Proudfoot, A.E. and Wells, T.N. (1997). Identification of an Fe(IH)-dihydroxyphenylalanine site in recombinant phosphomannose isomerase from Candida albicans. European Journal of Biochemistry 244, 325-333.
    • (1997) European Journal of Biochemistry , vol.244 , pp. 325-333
    • Smith, J.J.1    Thomson, A.J.2    Proudfoot, A.E.3    Wells, T.N.4
  • 170
    • 0000837688 scopus 로고
    • Mechanism of water stress-induced xylem embolism
    • Sperry, J.S. and Tyree, M.T. (1988). Mechanism of water stress-induced xylem embolism. Plant Physiology 88, 581-587.
    • (1988) Plant Physiology , vol.88 , pp. 581-587
    • Sperry, J.S.1    Tyree, M.T.2
  • 171
    • 0028774537 scopus 로고
    • Comparative analyses of pentraxins: Implications for protomer assembly and ligand binding
    • Srinavasan, N., White, H.E., Emsley, J., Wood, S.P., Pepys, M.B. and Blundell, T.L. (1994). Comparative analyses of pentraxins: implications for protomer assembly and ligand binding. Structure 2, 1017-1027.
    • (1994) Structure , vol.2 , pp. 1017-1027
    • Srinavasan, N.1    White, H.E.2    Emsley, J.3    Wood, S.P.4    Pepys, M.B.5    Blundell, T.L.6
  • 172
    • 84920302788 scopus 로고
    • Die Rolle der Oxalsaure in der Pflanze. Enzymatische Abbau dcs Oxalations
    • Staehelin, M. (1919). Die Rolle der Oxalsaure in der Pflanze. Enzymatische Abbau dcs Oxalations. Biochemische Zeitung 96, 1-49.
    • (1919) Biochemische Zeitung , vol.96 , pp. 1-49
    • Staehelin, M.1
  • 176
    • 0028028945 scopus 로고
    • Purification and partial characterisation of a glycoprotein from pea (Pisum sativum) with receptor activity for rhicadhesin, an attachment protein of Rhizobiaceae
    • Swart, S., Logman, T.J.J., Smit, G., Lugtenberg, B.J. and Kijne, J.W. (1994). Purification and partial characterisation of a glycoprotein from pea (Pisum sativum) with receptor activity for rhicadhesin, an attachment protein of Rhizobiaceae. Plant Molecular Biology 24,171-183.
    • (1994) Plant Molecular Biology , vol.24 , pp. 171-183
    • Swart, S.1    Logman, T.J.J.2    Smit, G.3    Lugtenberg, B.J.4    Kijne, J.W.5
  • 177
    • 0008555970 scopus 로고
    • Introduction of genes for oxalate degrading enzymes into plants as a potential means of providing tolerance to Sclerotinta
    • Thompson, C., Dunwell, J.M., Johnstone, C.E., Lay, V., Ray, J., Watson, H. and Nisbet, A. (1995a). Introduction of genes for oxalate degrading enzymes into plants as a potential means of providing tolerance to Sclerotinta. IOBC wprs Bulletin 18,34-38.
    • (1995) IOBC Wprs Bulletin , vol.18 , pp. 34-38
    • Thompson, C.1    Dunwell, J.M.2    Johnstone, C.E.3    Lay, V.4    Ray, J.5    Watson, H.6    Nisbet, A.7
  • 179
    • 0030748530 scopus 로고    scopus 로고
    • Subceliular localization of H2O2 in plants. H2O3 accumulation in papillae and hypersensitive response during the powdery-mildew interaction
    • Thordahl-Christensen, H., Zhang, Z., Wei, Y. and Collinge, D.B. (1997). Subceliular localization of H2O2 in plants. H2O3 accumulation in papillae and hypersensitive response during the powdery-mildew interaction. The Plant Journal 11,1187-1194.
    • (1997) The Plant Journal , vol.11 , pp. 1187-1194
    • Thordahl-Christensen, H.1    Zhang, Z.2    Wei, Y.3    Collinge, D.B.4
  • 180
    • 0028133201 scopus 로고
    • Studies on the biosynthesis of 3.6-didcoxyhexoses: Molecular cloning and characterization of the asc (ascaryiose) region from Yersinia pseudotuberculosis serogroup VA
    • Thorson, J.S., Lo, S.F., Ploux, O., He, X. and Liu, H.W. (1994). Studies on the biosynthesis of 3.6-didcoxyhexoses: molecular cloning and characterization of the asc (ascaryiose) region from Yersinia pseudotuberculosis serogroup VA. Journal of Bacteriology 176, 5483-5493.
    • (1994) Journal of Bacteriology , vol.176 , pp. 5483-5493
    • Thorson, J.S.1    Lo, S.F.2    Ploux, O.3    He, X.4    Liu, H.W.5
  • 181
    • 0028156657 scopus 로고
    • Acetylene reduction by symbiosomes and free bacteroids from broad bean (Vida faba L.) nodules: Role of oxalate
    • Trinchant, J-C., Gudrln, V. and Rjgaud, J. (1994). Acetylene reduction by symbiosomes and free bacteroids from broad bean (Vida faba L.) nodules: role of oxalate. Plant Physiology 105, 555-561.
    • (1994) Plant Physiology , vol.105 , pp. 555-561
    • Trinchant, J.-C.1    Gudrln, V.2    Rjgaud, J.3
  • 182
    • 0030466556 scopus 로고    scopus 로고
    • Bacteroid oxalate oxidase and soluble oxalate in nodules of faba beans (Vida faba L.) submitted to water restricted conditions: Possible involvement in nitrogen fixation
    • Trinchant, J-C. and Rigaud, J. (1996). Bacteroid oxalate oxidase and soluble oxalate in nodules of faba beans (Vida faba L.) submitted to water restricted conditions: possible involvement in nitrogen fixation. Journal of Experimental Botany 47, 1865-1870.
    • (1996) Journal of Experimental Botany , vol.47 , pp. 1865-1870
    • Trinchant, J.-C.1    Rigaud, J.2
  • 183
    • 0029636421 scopus 로고
    • Altered physicochemical characteristics of polyethylene glycol linked beet stem oxalate oxidase
    • Varalakshmi, P., Lathika, K.M., Raghavan, K.G. and Singh’ B.B. (1995). Altered physicochemical characteristics of polyethylene glycol linked beet stem oxalate oxidase. Biotechnology and Bioengineering 46, 254-257.
    • (1995) Biotechnology and Bioengineering , vol.46 , pp. 254-257
    • Varalakshmi, P.1    Lathika, K.M.2    Raghavan, K.G.3    Singh’, B.B.4
  • 184
    • 0026556481 scopus 로고
    • Studies on oxalate oxidase from beet stems upon immobilisation on concanavalin A
    • Varalakshmi, P. and Richardson, K.E. (1992). Studies on oxalate oxidase from beet stems upon immobilisation on concanavalin A. Biochemical International 26. 153-162.
    • (1992) Biochemical International , vol.26 , pp. 153-162
    • Varalakshmi, P.1    Richardson, K.E.2
  • 186
    • 0029167492 scopus 로고
    • The binding protein associates with monomeric phaseolin
    • Vitale, A., Biel, L.A. and Ceriottj, A. (1995). The binding protein associates with monomeric phaseolin. Plant Physiology 107, 1411-1418.
    • (1995) Plant Physiology , vol.107 , pp. 1411-1418
    • Vitale, A.1    Biel, L.A.2    Ceriottj, A.3
  • 187
    • 2042498593 scopus 로고
    • Organic acid content of com plants as influenced by pH of substrate and form of nitrogen supplied
    • Wadleigh, C.H. and Shfve, J.W. (1939). Organic acid content of com plants as influenced by pH of substrate and form of nitrogen supplied. American Journal of Botany 26.244-248.
    • (1939) American Journal of Botany , vol.26 , pp. 244-248
    • Wadleigh, C.H.1    Shfve, J.W.2
  • 188
    • 0001518485 scopus 로고
    • Vacuolar deposition of ascorbate-derived oxalic acid in barley
    • Wagner, Gj. (1981). Vacuolar deposition of ascorbate-derived oxalic acid in barley. Plant Physiology 67, 591-593.
    • (1981) Plant Physiology , vol.67 , pp. 591-593
    • Wagner, G.1
  • 189
    • 0026593942 scopus 로고
    • Molecular analysis of a Salmonella cnterica group El rfb gene cluster: O antigen and the genetic basis for the major polymorphism
    • Wang, L., Romanna, L.K. and Reeves, P.R. (1992). Molecular analysis of a Salmonella cnterica group El rfb gene cluster: O antigen and the genetic basis for the major polymorphism. Genetics 130,429-443.
    • (1992) Genetics , vol.130 , pp. 429-443
    • Wang, L.1    Romanna, L.K.2    Reeves, P.R.3
  • 191
    • 0030948290 scopus 로고    scopus 로고
    • Oxidative burst: An early plant response to pathogen infection
    • Wojtaszek, P. (1997). Oxidative burst: an early plant response to pathogen infection. Biochemical Journal 322,681-692.
    • (1997) Biochemical Journal , vol.322 , pp. 681-692
    • Wojtaszek, P.1
  • 192
    • 0028835212 scopus 로고
    • BEAUTY: An enhanced BLAST-based search tool that integrates multiple biological information resources into sequence similarity search results
    • Worley, K.C., Wiese, B.A. and Smith, R.F. (1990). BEAUTY: an enhanced BLAST-based search tool that integrates multiple biological information resources into sequence similarity search results. Genome Research 5, 173-184.
    • (1990) Genome Research , vol.5 , pp. 173-184
    • Worley, K.C.1    Wiese, B.A.2    Smith, R.F.3
  • 193
    • 0142092127 scopus 로고
    • Organic acids in the ripening banana fruit
    • Wyman, H. and Palmer, J.K. (1964). Organic acids in the ripening banana fruit. Plant Physiology 39, 630-633.
    • (1964) Plant Physiology , vol.39 , pp. 630-633
    • Wyman, H.1    Palmer, J.K.2
  • 194
    • 0028318096 scopus 로고
    • Amperometric determination of oxalate in plasma and urine by liquid chromatography with immobilized oxalate oxidase
    • Yamato, S., Wakabayashi, H., Nakajima, M. and ShiMada, K. (1994). Amperometric determination of oxalate in plasma and urine by liquid chromatography with immobilized oxalate oxidase. Journal of Chromatography 656, 29-35.
    • (1994) Journal of Chromatography , vol.656 , pp. 29-35
    • Yamato, S.1    Wakabayashi, H.2    Nakajima, M.3    Shimada, K.4
  • 196
    • 0028303288 scopus 로고
    • Genetic analysis of the O-specific lipopolysaccharide biosynthesis region (Rfb) of Escherichia coli K-12 W3110: Identification of genes that confer group 6 specificity to Shigella flexneri serotypes Y and 4a
    • Yao, Z. and Valvano, M.A. (1994). Genetic analysis of the O-specific lipopolysaccharide biosynthesis region (rfb) of Escherichia coli K-12 W3110: identification of genes that confer group 6 specificity to Shigella flexneri serotypes Y and 4a. Journal of Bacteriology 176,4133-4143.
    • (1994) Journal of Bacteriology , vol.176 , pp. 4133-4143
    • Yao, Z.1    Valvano, M.A.2
  • 197
    • 0029811103 scopus 로고    scopus 로고
    • Gene for aspartate racemase from the sulfur-dependent hypcrthermophilic achaeum, Desulfurococcus strain SY
    • Yohda, M., Endo, I., Abe, Y., Ohta, T., Iida, T., Maruyama, T. and Kagawa, Y. (1996). Gene for aspartate racemase from the sulfur-dependent hypcrthermophilic achaeum, Desulfurococcus strain SY. Journal of Biological Chemistry 271, 22017-22021.
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 22017-22021
    • Yohda, M.1    Endo, I.2    Abe, Y.3    Ohta, T.4    Iida, T.5    Maruyama, T.6    Kagawa, Y.7
  • 198
    • 0029189180 scopus 로고
    • Cloning and sequencing of a 36-kb region of the Bacillus subtil is genome between the gnt and iol operons
    • Yoshida, K., Seki, S., Fujimura, M., Miwa, Y. and Fujita, Y. (1995). Cloning and sequencing of a 36-kb region of the Bacillus subtil is genome between the gnt and iol operons. DNA Research 2, 61-69.
    • (1995) DNA Research , vol.2 , pp. 61-69
    • Yoshida, K.1    Seki, S.2    Fujimura, M.3    Miwa, Y.4    Fujita, Y.5
  • 199
    • 0004475301 scopus 로고
    • Oxalic acid as a sucking inhibitor of the brown planthopper in rice (Delphacidae, Homoptera). Entomology
    • Yoshiiiara, T., Sogawa, K., Pathak, M.D., Juliano, B.O. and Sakamura, S. (1990). Oxalic acid as a sucking inhibitor of the brown planthopper in rice (Delphacidae, Homoptera). Entomology, Experimental and Applied 27, 149-155.
    • (1990) Experimental and Applied , vol.27 , pp. 149-155
    • Yoshiiiara, T.1    Sogawa, K.2    Pathak, M.D.3    Juliano, B.O.4    Sakamura, S.5
  • 200
    • 7144238851 scopus 로고
    • Enzymic oxidation of oxalic acid by higher plants.(in Russian)
    • Abstract in Chemical Abstracts (1929) 23, 29-91
    • Zaleski, W. and Kukharkova, A.M. (1928). Enzymic oxidation of oxalic acid by higher plants.(in Russian). Ukraine Khemical Zhurnal 3, 139-152. Abstract in Chemical Abstracts (1929) 23, 29-91.
    • (1928) Ukraine Khemical Zhurnal , vol.3 , pp. 139-152
    • Zaleski, W.1    Kukharkova, A.M.2
  • 201
    • 0001215821 scopus 로고
    • Über die fermentative Oxydation der Oxalsäure
    • Zaleski, W. and Reinhard, A. (1912). Über die fermentative Oxydation der Oxalsäure. Biochemische Zeitung 33, 449-455.
    • (1912) Biochemische Zeitung , vol.33 , pp. 449-455
    • Zaleski, W.1    Reinhard, A.2
  • 202
    • 0027281825 scopus 로고
    • Genetic organisation and sequence of the rfb gene cluster of Yersinia enterocolitica serotype 0:3: Similarities to the dTDP-L-rhamnose biosynthesis pathway of Salmonella and to the bacterial polysaccharide transport systems
    • Zhang, L., Al-Hendy, A., Toivanen, P. and Skurnik, M. (1993). Genetic organisation and sequence of the rfb gene cluster of Yersinia enterocolitica serotype 0:3: similarities to the dTDP-L-rhamnose biosynthesis pathway of Salmonella and to the bacterial polysaccharide transport systems. Molecular Microbiology 9, 309-321.
    • (1993) Molecular Microbiology , vol.9 , pp. 309-321
    • Zhang, L.1    Al-Hendy, A.2    Toivanen, P.3    Skurnik, M.4
  • 203
    • 0028854951 scopus 로고
    • Germin-like oxalate oxidase, a H2O2-producing enzyme, accumulates in barley attacked by the powdery mildew fungus
    • Zhang, Z., Collinge, D.B. and Thordahl-Christensen, H. (1995). Germin-like oxalate oxidase, a H2O2-producing enzyme, accumulates in barley attacked by the powdery mildew fungus. The Plant Journal 8, 139-145.
    • (1995) The Plant Journal , vol.8 , pp. 139-145
    • Zhang, Z.1    Collinge, D.B.2    Thordahl-Christensen, H.3
  • 204
    • 21444450761 scopus 로고    scopus 로고
    • Ethanol increases sensitivity of oxalate oxidase assaysand facilitates direct activity staining in SDS gels
    • Zhang, Z., Yang, J., Collinge, D.B. and Thordahl-Christensen, H. (1996). Ethanol increases sensitivity of oxalate oxidase assaysand facilitates direct activity staining in SDS gels. Plant Molecular Biology Reporter 14, 266-272.
    • (1996) Plant Molecular Biology Reporter , vol.14 , pp. 266-272
    • Zhang, Z.1    Yang, J.2    Collinge, D.B.3    Thordahl-Christensen, H.4


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