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Volumn 48, Issue 3, 2008, Pages 632-638

Genes of folate biosynthesis in wheat

Author keywords

Differential expression; Folate biosynthesis; Gene isolation; Wheat

Indexed keywords

TRITICUM AESTIVUM;

EID: 54849424322     PISSN: 07335210     EISSN: 10959963     Source Type: Journal    
DOI: 10.1016/j.jcs.2008.02.007     Document Type: Article
Times cited : (14)

References (41)
  • 1
    • 0025954883 scopus 로고
    • Compartmentation of folate-mediated one-carbon metabolism in eukaryotes
    • Appling D. Compartmentation of folate-mediated one-carbon metabolism in eukaryotes. The FASEB Journal 5 (1991) 2645-2651
    • (1991) The FASEB Journal , vol.5 , pp. 2645-2651
    • Appling, D.1
  • 5
    • 0003989173 scopus 로고
    • Chemistry and Biochemistry of Pterins
    • John Wiley & Sons, New York
    • Blakely R., and Benkovic S. Chemistry and Biochemistry of Pterins. Folates and Pterins Vol. 2 (1984), John Wiley & Sons, New York
    • (1984) Folates and Pterins , vol.2
    • Blakely, R.1    Benkovic, S.2
  • 6
    • 0030299046 scopus 로고    scopus 로고
    • Folate, vitamin B12, and neuropsychiatric disorders
    • Bottiglieri T. Folate, vitamin B12, and neuropsychiatric disorders. Nutrition Reviews 54 (1996) 382-390
    • (1996) Nutrition Reviews , vol.54 , pp. 382-390
    • Bottiglieri, T.1
  • 7
    • 0031597388 scopus 로고    scopus 로고
    • Folate, vitamin B12, and serum total homocysteine levels in confirmed Alzheimer disease
    • Clarke R., Smith A., Jobst K., Refsum H., Sutton L., and Ueland P. Folate, vitamin B12, and serum total homocysteine levels in confirmed Alzheimer disease. Archives of Neurology 5 (1998) 1449-1455
    • (1998) Archives of Neurology , vol.5 , pp. 1449-1455
    • Clarke, R.1    Smith, A.2    Jobst, K.3    Refsum, H.4    Sutton, L.5    Ueland, P.6
  • 8
    • 0001292710 scopus 로고
    • Folate biochemistry and the metabolism of one-carbon units
    • Davies D. (Ed), Academic Press, San Diego, CA
    • Cossins E. Folate biochemistry and the metabolism of one-carbon units. In: Davies D. (Ed). The Biochemistry of Plants (1987), Academic Press, San Diego, CA 317-353
    • (1987) The Biochemistry of Plants , pp. 317-353
    • Cossins, E.1
  • 12
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • Emanuelsson O., Nielsen H., Brunak S., and von Heijne G. Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. Journal of Molecular Biology 300 (2000) 1005-1016
    • (2000) Journal of Molecular Biology , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    von Heijne, G.4
  • 13
    • 0033047207 scopus 로고    scopus 로고
    • Aleurone flour is a rich source of bioavailable folate in humans
    • Fenech M., Noakes M., Clifton P., and Topping D. Aleurone flour is a rich source of bioavailable folate in humans. The Journal of Nutrition 129 (1999) 1114-1119
    • (1999) The Journal of Nutrition , vol.129 , pp. 1114-1119
    • Fenech, M.1    Noakes, M.2    Clifton, P.3    Topping, D.4
  • 14
    • 0029070171 scopus 로고
    • Omega loops: no regular secondary structures significant in protein function and stability
    • Fetrow J. Omega loops: no regular secondary structures significant in protein function and stability. The FASEB Journal 9 (1995) 708-717
    • (1995) The FASEB Journal , vol.9 , pp. 708-717
    • Fetrow, J.1
  • 17
    • 0037452534 scopus 로고    scopus 로고
    • Catalytic roles of arginine residues 82 and 92 of Escherichia coli 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase: site directed mutagenesis and biochemical studies
    • Li Y., Wu Y., Blaszczyk J., Ji X., and Yan H. Catalytic roles of arginine residues 82 and 92 of Escherichia coli 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase: site directed mutagenesis and biochemical studies. Biochemistry 42 (2003) 1581-1588
    • (2003) Biochemistry , vol.42 , pp. 1581-1588
    • Li, Y.1    Wu, Y.2    Blaszczyk, J.3    Ji, X.4    Yan, H.5
  • 18
    • 0030277195 scopus 로고    scopus 로고
    • Folate: effects on carcinogenesis and the potential for cancer chemoprevention
    • Mason J., and Levesque T. Folate: effects on carcinogenesis and the potential for cancer chemoprevention. Oncology 10 (1996) 1727-1736
    • (1996) Oncology , vol.10 , pp. 1727-1736
    • Mason, J.1    Levesque, T.2
  • 19
    • 0000083882 scopus 로고
    • Pteroylpolyglutamates: biosynthesis, degradation and function
    • Chemistry and Biochemistry of Pterins. Blakley R., and Benkovic S. (Eds), John Wiley & Sons, New York
    • McGuire J., and Coward J. Pteroylpolyglutamates: biosynthesis, degradation and function. In: Blakley R., and Benkovic S. (Eds). Chemistry and Biochemistry of Pterins. Folates and Pterins Vol. 2 (1984), John Wiley & Sons, New York 135-190
    • (1984) Folates and Pterins , vol.2 , pp. 135-190
    • McGuire, J.1    Coward, J.2
  • 21
    • 49449115136 scopus 로고    scopus 로고
    • GTP Cyclohydrolase 1 expression and folate accumulation in the developing wheat seed
    • 10.1016/j.jcs.2007.11.008
    • McIntosh S., Brushett D., and Henry R. GTP Cyclohydrolase 1 expression and folate accumulation in the developing wheat seed. Journal of Cereal Science (2008) 10.1016/j.jcs.2007.11.008
    • (2008) Journal of Cereal Science
    • McIntosh, S.1    Brushett, D.2    Henry, R.3
  • 22
    • 0027525606 scopus 로고
    • Characterization of composite aminodeoxyisochorismate synthase and aminodeoxyisochorismate lyase activities of anthranilate synthase
    • Morollo A., and Bauerle R. Characterization of composite aminodeoxyisochorismate synthase and aminodeoxyisochorismate lyase activities of anthranilate synthase. Proceedings of the National Academy of Sciences of the USA 90 (1993) 9983-9987
    • (1993) Proceedings of the National Academy of Sciences of the USA , vol.90 , pp. 9983-9987
    • Morollo, A.1    Bauerle, R.2
  • 24
    • 0014847992 scopus 로고
    • The biosynthesis of folic acid compounds in plants. IV. Purification and properties of the dihydropteroate-synthesizing enzyme from pea seedlings
    • Okinaka O., and Iwai K. The biosynthesis of folic acid compounds in plants. IV. Purification and properties of the dihydropteroate-synthesizing enzyme from pea seedlings. The Journal of Vitaminology 16 (1970) 201-209
    • (1970) The Journal of Vitaminology , vol.16 , pp. 201-209
    • Okinaka, O.1    Iwai, K.2
  • 25
    • 0035910001 scopus 로고    scopus 로고
    • Tetrahydrofolate biosynthesis in plants: molecular and functional characterization of dihydrofolate synthetase and three isoforms of folylpolyglutamate synthetase in Arabidopsis thaliana
    • Ravanel S., Cherest H., Jabrin S., Grunwald D., Surdin-Kerjan Y., Douce R., and Rébeillé F. Tetrahydrofolate biosynthesis in plants: molecular and functional characterization of dihydrofolate synthetase and three isoforms of folylpolyglutamate synthetase in Arabidopsis thaliana. Proceedings of the National Academy of Sciences of the USA 98 (2001) 15360-15365
    • (2001) Proceedings of the National Academy of Sciences of the USA , vol.98 , pp. 15360-15365
    • Ravanel, S.1    Cherest, H.2    Jabrin, S.3    Grunwald, D.4    Surdin-Kerjan, Y.5    Douce, R.6    Rébeillé, F.7
  • 26
    • 0037733208 scopus 로고    scopus 로고
    • Folate biosynthesis in higher plants: purification and molecular cloning of a bifunctional 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase/7,8-dihydropteroate synthase localised in mitochondria
    • Rébeillé F., Macherel D., Mouillon J., Garin J., and Douce R. Folate biosynthesis in higher plants: purification and molecular cloning of a bifunctional 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase/7,8-dihydropteroate synthase localised in mitochondria. The EMBO Journal 3 (1997) 947-957
    • (1997) The EMBO Journal , vol.3 , pp. 947-957
    • Rébeillé, F.1    Macherel, D.2    Mouillon, J.3    Garin, J.4    Douce, R.5
  • 27
    • 0027174079 scopus 로고
    • p-Aminobenzoate synthesis in Escherichia coli: mutational analysis of three conserved amino acid residues of the amidotransferase PabA
    • Roux B., and Walsh C. p-Aminobenzoate synthesis in Escherichia coli: mutational analysis of three conserved amino acid residues of the amidotransferase PabA. Biochemistry 32 (1993) 3763-3768
    • (1993) Biochemistry , vol.32 , pp. 3763-3768
    • Roux, B.1    Walsh, C.2
  • 30
    • 0001226131 scopus 로고    scopus 로고
    • Folate and the prevention of disease
    • Pfleiderer W., and Rokos H. (Eds), Blackwell Science, Berlin
    • Scott J. Folate and the prevention of disease. In: Pfleiderer W., and Rokos H. (Eds). Chemistry and Biology of Pteridines and Folates (1997), Blackwell Science, Berlin 277-290
    • (1997) Chemistry and Biology of Pteridines and Folates , pp. 277-290
    • Scott, J.1
  • 33
    • 0024808080 scopus 로고
    • Folypolyglutamate synthesis and role in the regulation on one-carbon metabolism
    • Shane B. Folypolyglutamate synthesis and role in the regulation on one-carbon metabolism. Vitamins and Hormones 45 (1989) 263-335
    • (1989) Vitamins and Hormones , vol.45 , pp. 263-335
    • Shane, B.1
  • 35
    • 0025602271 scopus 로고
    • An apparent Bacillus subtilis folic acid biosynthetic operon containing pab, an amphibolic trpG gene, a third gene required for synthesis of para-aminobenzoic acid, and the dihydropteroate synthase gene
    • Slock J., Stahly D., Han C., Six E., and Crawford I. An apparent Bacillus subtilis folic acid biosynthetic operon containing pab, an amphibolic trpG gene, a third gene required for synthesis of para-aminobenzoic acid, and the dihydropteroate synthase gene. Journal of Bacteriology 172 (1992) 7211-7226
    • (1992) Journal of Bacteriology , vol.172 , pp. 7211-7226
    • Slock, J.1    Stahly, D.2    Han, C.3    Six, E.4    Crawford, I.5
  • 36
    • 0032499731 scopus 로고    scopus 로고
    • Structural homologies with ATP- and folate-binding enzymes in the crystal structure of folylpolyglutamate synthetase
    • Sun X., Bognar A., Baker E., and Smith C. Structural homologies with ATP- and folate-binding enzymes in the crystal structure of folylpolyglutamate synthetase. Proceedings of the National Academy of Sciences of the USA 95 (1998) 6647-6652
    • (1998) Proceedings of the National Academy of Sciences of the USA , vol.95 , pp. 6647-6652
    • Sun, X.1    Bognar, A.2    Baker, E.3    Smith, C.4
  • 37
    • 0026700594 scopus 로고
    • Cloning, sequence analysis, and overexpression of Escherichia coli folK, the gene coding for 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase
    • Talarico T., Ray P., Dev I., Merrill B., and Dallas W. Cloning, sequence analysis, and overexpression of Escherichia coli folK, the gene coding for 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase. Journal of Bacteriology 174 (1992) 5971-5977
    • (1992) Journal of Bacteriology , vol.174 , pp. 5971-5977
    • Talarico, T.1    Ray, P.2    Dev, I.3    Merrill, B.4    Dallas, W.5
  • 38
    • 0345608633 scopus 로고
    • Nutritional-physiological views in processing cereal products
    • Thomas B. Nutritional-physiological views in processing cereal products. Vegetables 15 (1968) 360
    • (1968) Vegetables , vol.15 , pp. 360
    • Thomas, B.1
  • 39
    • 0025266346 scopus 로고
    • Cloning and expression of the gene encoding Lactobacillus casei folylpoly-gamma-glutamate synthetase in Escherichia coli and determination of its primary structure
    • Toy J., and Bognar A. Cloning and expression of the gene encoding Lactobacillus casei folylpoly-gamma-glutamate synthetase in Escherichia coli and determination of its primary structure. Journal of Biological Chemistry 265 (1990) 2492-2499
    • (1990) Journal of Biological Chemistry , vol.265 , pp. 2492-2499
    • Toy, J.1    Bognar, A.2
  • 40
    • 0028809784 scopus 로고
    • Kinetic characterisation of 4-amino-deoxychorismate synthase from Escherichia coli
    • Viswanathan V., Green J., and Nichols B. Kinetic characterisation of 4-amino-deoxychorismate synthase from Escherichia coli. Journal of Bacteriology 177 (1995) 5918-5923
    • (1995) Journal of Bacteriology , vol.177 , pp. 5918-5923
    • Viswanathan, V.1    Green, J.2    Nichols, B.3
  • 41
    • 0035298434 scopus 로고    scopus 로고
    • GTP cyclohydrolase I feedback regulatory protein-dependent and -independent inhibitors of GTP cyclohydrolase I
    • Yoneyama T., Wilson L., and Hatakeyama K. GTP cyclohydrolase I feedback regulatory protein-dependent and -independent inhibitors of GTP cyclohydrolase I. Archives of Biochemistry and Biophysics 388 (2001) 67-73
    • (2001) Archives of Biochemistry and Biophysics , vol.388 , pp. 67-73
    • Yoneyama, T.1    Wilson, L.2    Hatakeyama, K.3


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