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Volumn 46, Issue 6, 2005, Pages 858-869

Involvement of α-amylase I-1 in starch degradation in rice chloroplasts

Author keywords

Amylase; Chloroplast; Glycoprotein; Golgi complex; Oryza sativa L.; Starch; Transgenic plant

Indexed keywords

ORYZA SATIVA;

EID: 24644497271     PISSN: 00320781     EISSN: 14719053     Source Type: Journal    
DOI: 10.1093/pcp/pci091     Document Type: Article
Times cited : (119)

References (62)
  • 1
    • 0033174657 scopus 로고    scopus 로고
    • Characterization of chimeric enzymes constructed between two distinct α-amylase cDNAs from cultured rice cells
    • Abe, R., Yoshida, K., Aoyagi, M., Kasahara, S., Ichishima, E. and Nakajima, T. (1999) Characterization of chimeric enzymes constructed between two distinct α-amylase cDNAs from cultured rice cells. Biosci. Biotechnol. Biochem. 63: 1329-1335.
    • (1999) Biosci. Biotechnol. Biochem. , vol.63 , pp. 1329-1335
    • Abe, R.1    Yoshida, K.2    Aoyagi, M.3    Kasahara, S.4    Ichishima, E.5    Nakajima, T.6
  • 2
    • 84940980492 scopus 로고
    • Recent progress in α-amylase biosynthesis
    • Edited by Preiss, J. Academic Press, New York
    • Akazawa, T., Mitsui, T. and Hayashi, M. (1988) Recent progress in α-amylase biosynthesis. In The Biochemistry of Plants. Volume 4. Edited by Preiss, J. pp. 465-492. Academic Press, New York.
    • (1988) The Biochemistry of Plants , vol.4 , pp. 465-492
    • Akazawa, T.1    Mitsui, T.2    Hayashi, M.3
  • 3
    • 0000779576 scopus 로고
    • Nucleotide sequence of the T-DNA region from the Agrobacterium tumefaciens octopine Ti plasmid pTi15955
    • Barker, R.F., Idler, K.B., Thompson, D.V. and Kemp, J.D. (1983) Nucleotide sequence of the T-DNA region from the Agrobacterium tumefaciens octopine Ti plasmid pTi15955. Plant Mol. Biol. 2: 335-350.
    • (1983) Plant Mol. Biol. , vol.2 , pp. 335-350
    • Barker, R.F.1    Idler, K.B.2    Thompson, D.V.3    Kemp, J.D.4
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0032584607 scopus 로고    scopus 로고
    • Identification of a glycoprotein from rat liver mitochondrial inner membrane and demonstration of its origin in the endoplasmic reticulum
    • Chandra, N.C., Spiro, M.J. and Spiro, R.G. (1998) Identification of a glycoprotein from rat liver mitochondrial inner membrane and demonstration of its origin in the endoplasmic reticulum. J. Biol. Chem. 273: 19715-19721.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19715-19721
    • Chandra, N.C.1    Spiro, M.J.2    Spiro, R.G.3
  • 7
    • 3543041300 scopus 로고    scopus 로고
    • Signal peptide-dependent targeting of a rice α-amylase and cargo proteins to plastids and extracellular compartments of plant cells
    • Chen, M.H., Huang, L.F., Li, H.M., Chen, Y.R. and Yu, S.M. (2004) Signal peptide-dependent targeting of a rice α-amylase and cargo proteins to plastids and extracellular compartments of plant cells. Plant Physiol. 135: 1-11.
    • (2004) Plant Physiol. , vol.135 , pp. 1-11
    • Chen, M.H.1    Huang, L.F.2    Li, H.M.3    Chen, Y.R.4    Yu, S.M.5
  • 8
    • 0028180895 scopus 로고
    • Expression of α-amylase, carbohydrate metabolism, and autophagy in cultured rice cells is coordinately regulated by sugar nutrient
    • Chen, M.H., Liu, L.F., Chen, Y.R., Wu, H.K. and Yu, S.M. (1994) Expression of α-amylase, carbohydrate metabolism, and autophagy in cultured rice cells is coordinately regulated by sugar nutrient. Plant J. 6: 625-636.
    • (1994) Plant J. , vol.6 , pp. 625-636
    • Chen, M.H.1    Liu, L.F.2    Chen, Y.R.3    Wu, H.K.4    Yu, S.M.5
  • 9
    • 0037649050 scopus 로고    scopus 로고
    • Complete sequence of the binary vector pBI121 and its application in cloning T-DNA insertion from transgenic plants
    • Chen, P.Y., Wang, C.K., Soong, S.C. and To, K.Y. (2003) Complete sequence of the binary vector pBI121 and its application in cloning T-DNA insertion from transgenic plants. Mol. Breeding 11: 287-293.
    • (2003) Mol. Breeding , vol.11 , pp. 287-293
    • Chen, P.Y.1    Wang, C.K.2    Soong, S.C.3    To, K.Y.4
  • 12
    • 0033906480 scopus 로고    scopus 로고
    • Agrobacterium-mediated transformation of monocot and dicot plants using the NCR promoter derived from soybean chlorotic mottle virus
    • Fukuoka, H., Ogawa, T., Mitsuhara, I., Iwai, T., Isuzugawa, K., et al. (2000) Agrobacterium-mediated transformation of monocot and dicot plants using the NCR promoter derived from soybean chlorotic mottle virus. Plant Cell Rep. 19: 815-820.
    • (2000) Plant Cell Rep. , vol.19 , pp. 815-820
    • Fukuoka, H.1    Ogawa, T.2    Mitsuhara, I.3    Iwai, T.4    Isuzugawa, K.5
  • 13
    • 0033179390 scopus 로고    scopus 로고
    • Isolation and characterization of the cDNA encoding a glycosylated accessory protein of pea chloroplast DNA polymerase
    • Gaikwad, A., Tewari, K.K., Kumar, D., Chen, W. and Mukherjee, S.K. (1999) Isolation and characterization of the cDNA encoding a glycosylated accessory protein of pea chloroplast DNA polymerase. Nucleic Acids Res. 27: 3120-3129.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 3120-3129
    • Gaikwad, A.1    Tewari, K.K.2    Kumar, D.3    Chen, W.4    Mukherjee, S.K.5
  • 14
    • 0028500170 scopus 로고
    • The small, versatile pPZP family of Agrobacterium binary vectors for plant transformation
    • Hajdukiewicz, P., Svab, Z. and Maliga, P. (1994) The small, versatile pPZP family of Agrobacterium binary vectors for plant transformation. Plant Mol. Biol. 25: 989-994.
    • (1994) Plant Mol. Biol. , vol.25 , pp. 989-994
    • Hajdukiewicz, P.1    Svab, Z.2    Maliga, P.3
  • 15
    • 0037062951 scopus 로고    scopus 로고
    • RNA interference
    • Hannon, G.J. (2002) RNA interference. Nature 418: 244-251.
    • (2002) Nature , vol.418 , pp. 244-251
    • Hannon, G.J.1
  • 16
    • 0025303628 scopus 로고
    • Structure and biosynthesis of the xylose-containing carbohydrate moiety of rice α-amylase
    • Hayashi, M., Turu, A., Mitsui, T., Takahashi, N., Hanzawa, H., Arata, Y. and Akazawa, T. (1990) Structure and biosynthesis of the xylose-containing carbohydrate moiety of rice α-amylase, Eur. J. Biochem. 191: 287-295.
    • (1990) Eur. J. Biochem. , vol.191 , pp. 287-295
    • Hayashi, M.1    Turu, A.2    Mitsui, T.3    Takahashi, N.4    Hanzawa, H.5    Arata, Y.6    Akazawa, T.7
  • 17
    • 0028483231 scopus 로고
    • Efficient transformation of rice (Oryza sativa L.) mediated by Agrobacterium and sequence analysis of the boundaries of the T-DNA
    • Hiei, Y., Ohta, S., Komari, T. and Kumashiro, T. (1994) Efficient transformation of rice (Oryza sativa L.) mediated by Agrobacterium and sequence analysis of the boundaries of the T-DNA. Plant J. 6: 271-282.
    • (1994) Plant J. , vol.6 , pp. 271-282
    • Hiei, Y.1    Ohta, S.2    Komari, T.3    Kumashiro, T.4
  • 18
    • 0022917028 scopus 로고
    • The hyper-virulence of Agrobacterium tumefaciens A281 is encoded in a region of pTiBo542 outside of T-DNA
    • Hood, E.E., Helmer, G.L., Fraley, R.T. and Chilton, M.D. (1986) The hyper-virulence of Agrobacterium tumefaciens A281 is encoded in a region of pTiBo542 outside of T-DNA. J. Bacteriol. 168: 1291-1301.
    • (1986) J. Bacteriol. , vol.168 , pp. 1291-1301
    • Hood, E.E.1    Helmer, G.L.2    Fraley, R.T.3    Chilton, M.D.4
  • 19
    • 0025429268 scopus 로고
    • Classification and characterization of the rice α-amylase multigene family
    • Huang, N., Sutliff, T.D., Litts, J.C. and Rodriguez, R.L. (1990) Classification and characterization of the rice α-amylase multigene family. Plant Mol. Biol. 14: 655-668.
    • (1990) Plant Mol. Biol. , vol.14 , pp. 655-668
    • Huang, N.1    Sutliff, T.D.2    Litts, J.C.3    Rodriguez, R.L.4
  • 20
    • 0026778658 scopus 로고
    • Classification and evolution of α-amylase genes in plants
    • Huang, N., Stebbins, G.L. and Rodriguez, R.L. (1992) Classification and evolution of α-amylase genes in plants. Proc. Natl Acad. Sci. USA 89: 7526-7530.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 7526-7530
    • Huang, N.1    Stebbins, G.L.2    Rodriguez, R.L.3
  • 21
    • 0035006891 scopus 로고    scopus 로고
    • slender rice, a constitutive response mutant, is caused by a null mutation of the SLR1 gene, an ortholog of the height-regulating gene GAI/RGA/RHT/D8
    • Ikeda, A., Ueguchi-Tanaka, M., Sonoda, Y., Kitano, H., Koshioka, M., Futsuhara, Y., Matsuoka, M. and Yamaguchi, J. (2001) slender rice, a constitutive response mutant, is caused by a null mutation of the SLR1 gene, an ortholog of the height-regulating gene GAI/RGA/RHT/D8. Plant Cell 13: 999-1010
    • (2001) Plant Cell , vol.13 , pp. 999-1010
    • Ikeda, A.1    Ueguchi-Tanaka, M.2    Sonoda, Y.3    Kitano, H.4    Koshioka, M.5    Futsuhara, Y.6    Matsuoka, M.7    Yamaguchi, J.8
  • 22
    • 0034703608 scopus 로고    scopus 로고
    • Protein translocation within chloroplast is similar in Euglena and higher plants
    • Inagaki, J., Fujita, Y., Hase, T. and Yamamoto, Y. (2000) Protein translocation within chloroplast is similar in Euglena and higher plants. Biochem. Biophys. Res. Commun. 277: 436-442.
    • (2000) Biochem. Biophys. Res. Commun. , vol.277 , pp. 436-442
    • Inagaki, J.1    Fujita, Y.2    Hase, T.3    Yamamoto, Y.4
  • 23
    • 0029041413 scopus 로고
    • Cosuppression, flower color patterns, and metastable gene expression states
    • Jorgensen, R.A. (1995) Cosuppression, flower color patterns, and metastable gene expression states. Science 268: 686-691.
    • (1995) Science , vol.268 , pp. 686-691
    • Jorgensen, R.A.1
  • 24
    • 10744232079 scopus 로고    scopus 로고
    • Loss-of-function mutations of the rice GAMYB gene impair α-amylase expression in aleurone and flower development
    • Kaneko, M., Inukai, Y., Ueguchi-Tanaka, M., Itoh, H., Izawa, T., et al. (2004) Loss-of-function mutations of the rice GAMYB gene impair α-amylase expression in aleurone and flower development. Plant Cell 16: 33-44.
    • (2004) Plant Cell , vol.16 , pp. 33-44
    • Kaneko, M.1    Inukai, Y.2    Ueguchi-Tanaka, M.3    Itoh, H.4    Izawa, T.5
  • 25
    • 0032125543 scopus 로고    scopus 로고
    • Effects of (+)-8′, 8′, 8′-trifluoroabscisic acid on α-amylase expression and sugar accumulation in rice cells
    • Kashem, M.A., Hori, H., Itoh, K., Hayakawa, T., Todoroki, Y., Hirai, N., Ohigashi, H. and Mitsui, T. (1998) Effects of (+)-8′, 8′, 8′-trifluoroabscisic acid on α-amylase expression and sugar accumulation in rice cells. Planta 205: 319-326.
    • (1998) Planta , vol.205 , pp. 319-326
    • Kashem, M.A.1    Hori, H.2    Itoh, K.3    Hayakawa, T.4    Todoroki, Y.5    Hirai, N.6    Ohigashi, H.7    Mitsui, T.8
  • 26
    • 0034115517 scopus 로고    scopus 로고
    • 2+ signaling in the regulation of α-amylase expression and germination of rice seed (Oryza sativa L.)
    • 2+ signaling in the regulation of α-amylase expression and germination of rice seed (Oryza sativa L.). Plant Cell Physiol. 41: 399-407.
    • (2000) Plant Cell Physiol. , vol.41 , pp. 399-407
    • Kashem, M.A.1    Itoh, K.2    Iwabuchi, S.3    Hori, H.4    Mitsui, T.5
  • 27
    • 0026477602 scopus 로고
    • Nucleotide sequence of a high-pI rice (Oryza sativa) α-amylase gene
    • Kim, J.-K. and Wu, R. (1992) Nucleotide sequence of a high-pI rice (Oryza sativa) α-amylase gene. Plant Mol. Biol. 18: 399-402.
    • (1992) Plant Mol. Biol. , vol.18 , pp. 399-402
    • Kim, J.-K.1    Wu, R.2
  • 28
    • 0001451455 scopus 로고
    • Purification, characterization and localization of rice UDP-glucose pyrophosphorylase
    • Kimura, S., Mitsui, T., Matsuoka, T. and Igaue, I. (1992) Purification, characterization and localization of rice UDP-glucose pyrophosphorylase. Plant Physiol. Biochem. 30: 683-693.
    • (1992) Plant Physiol. Biochem. , vol.30 , pp. 683-693
    • Kimura, S.1    Mitsui, T.2    Matsuoka, T.3    Igaue, I.4
  • 29
    • 0025271676 scopus 로고
    • Glycan research on barley, maize, oats, and sorghum grain α-amylases: Comparison with rice α-amylase
    • Lecommandeur, D., Sirou, Y. and Laurière, C. (1990) Glycan research on barley, maize, oats, and sorghum grain α-amylases: comparison with rice α-amylase. Arch. Biochem. Biophys. 278: 245-250.
    • (1990) Arch. Biochem. Biophys. , vol.278 , pp. 245-250
    • Lecommandeur, D.1    Sirou, Y.2    Laurière, C.3
  • 30
    • 0001489664 scopus 로고
    • Characterization and subcellular localization of debranching enzyme and endoamylase from the leaves of sugar beet
    • Li, B., Servaites, J.C. and Geiger, D.R. (1992) Characterization and subcellular localization of debranching enzyme and endoamylase from the leaves of sugar beet. Plant Physiol. 98: 1277-1284.
    • (1992) Plant Physiol. , vol.98 , pp. 1277-1284
    • Li, B.1    Servaites, J.C.2    Geiger, D.R.3
  • 31
    • 0036670303 scopus 로고    scopus 로고
    • Three novel MYB proteins with one DNA binding repeat mediate sugar and hormone regulation of α-amylase gene expression
    • Lu, C.A., Ho, Th.D., Ho, S.L. and Yu, S.M. (2002) Three novel MYB proteins with one DNA binding repeat mediate sugar and hormone regulation of α-amylase gene expression. Plant Cell 14: 1963-1980.
    • (2002) Plant Cell , vol.14 , pp. 1963-1980
    • Lu, C.A.1    Ho, T.D.2    Ho, S.L.3    Yu, S.M.4
  • 32
    • 0033829419 scopus 로고    scopus 로고
    • Sugar uptake and transport in rice embryo. Expression of companion cell-specific sucrose transporter (OsSUT1) induced by sugar and light
    • Matsukura, C., Saitoh, T., Hirose, T., Ohsugi, R., Perata, P. and Yamaguchi, J. (2000) Sugar uptake and transport in rice embryo. Expression of companion cell-specific sucrose transporter (OsSUT1) induced by sugar and light. Plant Physiol. 124: 85-93.
    • (2000) Plant Physiol. , vol.124 , pp. 85-93
    • Matsukura, C.1    Saitoh, T.2    Hirose, T.3    Ohsugi, R.4    Perata, P.5    Yamaguchi, J.6
  • 33
    • 0034843596 scopus 로고    scopus 로고
    • Separation of distinct compartments of Golgi complex by sucrose density gradient centrifugation
    • Mikami, S., Hori, H. and Mitsui, T. (2001) Separation of distinct compartments of Golgi complex by sucrose density gradient centrifugation. Plant Sci. 161: 665-675.
    • (2001) Plant Sci. , vol.161 , pp. 665-675
    • Mikami, S.1    Hori, H.2    Mitsui, T.3
  • 34
    • 0021871295 scopus 로고
    • Biosynthesis of rice seed α-amylase: Two pathways of amylase secretion by the scutellum
    • Mitsui, T., Akazawa, T., Christeller, J.T. and Tartakoff, A.M. (1985) Biosynthesis of rice seed α-amylase: two pathways of amylase secretion by the scutellum. Arch. Biochem. Biophys. 241: 315-328.
    • (1985) Arch. Biochem. Biophys. , vol.241 , pp. 315-328
    • Mitsui, T.1    Akazawa, T.2    Christeller, J.T.3    Tartakoff, A.M.4
  • 35
    • 0030744750 scopus 로고    scopus 로고
    • The α-amylase multigene family
    • Mitsui, T. and Itoh, K. (1997) The α-amylase multigene family. Trends Plant Sci. 2: 255-261.
    • (1997) Trends Plant Sci. , vol.2 , pp. 255-261
    • Mitsui, T.1    Itoh, K.2
  • 36
  • 37
    • 0030113407 scopus 로고    scopus 로고
    • Physicochemical and serological characterization of rice α-amylase isoforms and identification of their corresponding genes
    • Mitsui, T., Yamaguchi, J. and Akazawa, T. (1996) Physicochemical and serological characterization of rice α-amylase isoforms and identification of their corresponding genes. Plant Physiol. 110: 1395-1404.
    • (1996) Plant Physiol. , vol.110 , pp. 1395-1404
    • Mitsui, T.1    Yamaguchi, J.2    Akazawa, T.3
  • 38
    • 0020731281 scopus 로고
    • Biosynthesis of rice seed α-amylase: Proteolytic processing and glycosylation of precursor polypeptides by microsomes
    • Miyata, S. and Akazawa, T. (1983) Biosynthesis of rice seed α-amylase: proteolytic processing and glycosylation of precursor polypeptides by microsomes. J. Cell Biol. 96: 802-806.
    • (1983) J. Cell Biol. , vol.96 , pp. 802-806
    • Miyata, S.1    Akazawa, T.2
  • 39
    • 3142607550 scopus 로고    scopus 로고
    • Proteomic identification of α-amylase isoforms encoded by RAmy3B/3C from germinating rice seeds
    • Nanjo, Y., Asatsuma, S., Itoh, K., Hori, H. and Mitsui, T. (2004a) Proteomic identification of α-amylase isoforms encoded by RAmy3B/3C from germinating rice seeds. Biosci. Biotechnol. Biochem. 68: 112-118.
    • (2004) Biosci. Biotechnol. Biochem. , vol.68 , pp. 112-118
    • Nanjo, Y.1    Asatsuma, S.2    Itoh, K.3    Hori, H.4    Mitsui, T.5
  • 40
    • 3142640923 scopus 로고    scopus 로고
    • Posttranscriptional regulation of α-amylase II-4 expression by gibberellin in germinating rice seeds
    • Nanjo, Y., Asatsuma, S., Itoh, K., Hori, H., Mitsui, T. and Fujisawa, Y. (2004b) Posttranscriptional regulation of α-amylase II-4 expression by gibberellin in germinating rice seeds. Plant Physiol. Biochem. 42: 477-484.
    • (2004) Plant Physiol. Biochem. , vol.42 , pp. 477-484
    • Nanjo, Y.1    Asatsuma, S.2    Itoh, K.3    Hori, H.4    Mitsui, T.5    Fujisawa, Y.6
  • 41
    • 0016249580 scopus 로고
    • Studies on spinach ribulosebisphosphate carboxylase. Carboxylase and oxygenase reaction examined by immunochemical methods
    • Nishimura, M. and Akazawa, T. (1974) Studies on spinach ribulosebisphosphate carboxylase. Carboxylase and oxygenase reaction examined by immunochemical methods. Biochemistry 13: 2277-2281.
    • (1974) Biochemistry , vol.13 , pp. 2277-2281
    • Nishimura, M.1    Akazawa, T.2
  • 42
    • 0033136084 scopus 로고    scopus 로고
    • Non-invasive quantitative detection and application of non-toxic, S65T-type green fluorescent protein in living plants
    • Niwa, Y., Hirano, T., Yoshimoto, K., Shimizu, M. and Kobayashi, H. (1999) Non-invasive quantitative detection and application of non-toxic, S65T-type green fluorescent protein in living plants. Plant J. 18: 455-463.
    • (1999) Plant J. , vol.18 , pp. 455-463
    • Niwa, Y.1    Hirano, T.2    Yoshimoto, K.3    Shimizu, M.4    Kobayashi, H.5
  • 43
    • 0001004433 scopus 로고
    • Subcellular localization of the starch degradative and biosynthetic enzymes of spinach leaves
    • Okita, T.W., Greenberg, E., Kuhn, D.N. and Preiss, J. (1979) Subcellular localization of the starch degradative and biosynthetic enzymes of spinach leaves. Plant Physiol. 64: 187-192.
    • (1979) Plant Physiol. , vol.64 , pp. 187-192
    • Okita, T.W.1    Greenberg, E.2    Kuhn, D.N.3    Preiss, J.4
  • 44
    • 0025363754 scopus 로고
    • The alpha-amylase genes in Oryza sativa: Characterization of cDNA clones and mRNA expression during seed germination
    • O'Neill, S.D., Kumagai, M.H., Majumdar, A., Huang, N., Sutliff, T.D. and Rodriguez, R.L. (1990) The alpha-amylase genes in Oryza sativa: characterization of cDNA clones and mRNA expression during seed germination. Mol. Gen. Genet. 221: 235-244.
    • (1990) Mol. Gen. Genet. , vol.221 , pp. 235-244
    • O'Neill, S.D.1    Kumagai, M.H.2    Majumdar, A.3    Huang, N.4    Sutliff, T.D.5    Rodriguez, R.L.6
  • 45
    • 0036072544 scopus 로고    scopus 로고
    • Down regulation of a chloroplast-targeted beta-amylase leads to a starch-excess phenotype in leaves
    • Scheidig, A., Frohlich, A., Schulze, S., Lloyd, J.R. and Kossmann, J. (2002) Down regulation of a chloroplast-targeted beta-amylase leads to a starch-excess phenotype in leaves. Plant J. 30: 581-591.
    • (2002) Plant J. , vol.30 , pp. 581-591
    • Scheidig, A.1    Frohlich, A.2    Schulze, S.3    Lloyd, J.R.4    Kossmann, J.5
  • 46
    • 12744280061 scopus 로고    scopus 로고
    • Silencing in Arabidopsis T-DNA transformants: The predominant role of a gene-specific RNA sensing mechanism versus position effects
    • Schubert, D., Lechtenberg, B., Forsbach, A., Gils, M., Bahadur, S. and Schmidt, R. (2004) Silencing in Arabidopsis T-DNA transformants: the predominant role of a gene-specific RNA sensing mechanism versus position effects. Plant Cell, 16: 2561-2572.
    • (2004) Plant Cell , vol.16 , pp. 2561-2572
    • Schubert, D.1    Lechtenberg, B.2    Forsbach, A.3    Gils, M.4    Bahadur, S.5    Schmidt, R.6
  • 47
    • 0347976048 scopus 로고
    • Plant α-amylase
    • Edited by The Amylase Research Society of Japan Pergamon Press, Oxford
    • Shinke, R. (1988) Plant α-amylase. In Handbook of Amylases and Related Enzymes. Edited by The Amylase Research Society of Japan. pp. 26-32. Pergamon Press, Oxford.
    • (1988) Handbook of Amylases and Related Enzymes , pp. 26-32
    • Shinke, R.1
  • 48
    • 0345736279 scopus 로고    scopus 로고
    • Characterization of putative amylases from apple (Malus domestica) and Arabidopsis thaliana
    • Stanley, D., Fitzgerald, A.M., Farnden, K.J.F. and McRae, E.A. (2002) Characterization of putative amylases from apple (Malus domestica) and Arabidopsis thaliana. Biologia 57: 137-148.
    • (2002) Biologia , vol.57 , pp. 137-148
    • Stanley, D.1    Fitzgerald, A.M.2    Farnden, K.J.F.3    McRae, E.A.4
  • 49
    • 0000289670 scopus 로고
    • In-vitro degradation of starch granules isolated from spinach chloroplasts
    • Steup, M., Robenek, H. and Melkonian, M. (1983) In-vitro degradation of starch granules isolated from spinach chloroplasts. Planta 158: 428-436.
    • (1983) Planta , vol.158 , pp. 428-436
    • Steup, M.1    Robenek, H.2    Melkonian, M.3
  • 50
    • 0031891965 scopus 로고    scopus 로고
    • Temporal and spatial expression of the α-amylase gene during seed germination in rice and barley
    • Sugimoto, N., Takeda, G., Nagato, Y. and Yamaguchi, J. (1998) Temporal and spatial expression of the α-amylase gene during seed germination in rice and barley. Plant Cell Physiol. 39: 323-333.
    • (1998) Plant Cell Physiol. , vol.39 , pp. 323-333
    • Sugimoto, N.1    Takeda, G.2    Nagato, Y.3    Yamaguchi, J.4
  • 51
    • 0032955849 scopus 로고    scopus 로고
    • Topology of Euglena chloroplast protein precursors within endoplasmic reticulum to Golgi to chloroplast transport vesicles
    • Sulli, C., Fang, Z., Muchhal, U. and Schwartzbach, S.D. (1999) Topology of Euglena chloroplast protein precursors within endoplasmic reticulum to Golgi to chloroplast transport vesicles. J. Biol. Chem. 274: 457-463.
    • (1999) J. Biol. Chem. , vol.274 , pp. 457-463
    • Sulli, C.1    Fang, Z.2    Muchhal, U.3    Schwartzbach, S.D.4
  • 52
    • 0029030925 scopus 로고
    • The polyprotein precursor to the Euglena light-harvesting chlorophyll a/b-binding protein is transported to the Golgi apparatus prior to chloroplast import and polyprotein processing
    • Sulli, C. and Schwartzbach, S.D. (1995) The polyprotein precursor to the Euglena light-harvesting chlorophyll a/b-binding protein is transported to the Golgi apparatus prior to chloroplast import and polyprotein processing. J. Biol. Chem. 270: 13084-13090.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13084-13090
    • Sulli, C.1    Schwartzbach, S.D.2
  • 53
    • 3142671423 scopus 로고    scopus 로고
    • Proteomics of the rice cell: Systematic identification of the protein populations in subcellular compartments
    • Tanaka, N., Fujita, M., Handa, H., Murayama, S., Uemura, M., et al. (2004) Proteomics of the rice cell: systematic identification of the protein populations in subcellular compartments. Mol. Genet. Genomics. 271: 566-576.
    • (2004) Mol. Genet. Genomics , vol.271 , pp. 566-576
    • Tanaka, N.1    Fujita, M.2    Handa, H.3    Murayama, S.4    Uemura, M.5
  • 54
    • 0001129198 scopus 로고    scopus 로고
    • Kinetic parameters of two rice α-amylase isozymes for oligosaccharide degradation
    • Terashima, M., Hayashi, N., Thomas, B.R., Rodriguez, R.L. and Katoh, S. (1996) Kinetic parameters of two rice α-amylase isozymes for oligosaccharide degradation. Plant Sci. 116: 9-14.
    • (1996) Plant Sci. , vol.116 , pp. 9-14
    • Terashima, M.1    Hayashi, N.2    Thomas, B.R.3    Rodriguez, R.L.4    Katoh, S.5
  • 55
    • 0030990058 scopus 로고    scopus 로고
    • Functional roles of protein domains on rice α-amylase activity
    • Terashima, M., Hosono, M. and Katoh, S. (1997) Functional roles of protein domains on rice α-amylase activity. Appl. Microbiol. Biotechnol. 47: 364-367.
    • (1997) Appl. Microbiol. Biotechnol. , vol.47 , pp. 364-367
    • Terashima, M.1    Hosono, M.2    Katoh, S.3
  • 56
    • 0028080142 scopus 로고
    • The roles of the N-linked carbohydrate chain of rice α-amylase in the thermostability and enzyme kinetics
    • Terashima, M., Kubo, A., Suzawa, M., Itoh, Y. and Katoh, S. (1994) The roles of the N-linked carbohydrate chain of rice α-amylase in the thermostability and enzyme kinetics. Eur. J. Biochem. 226: 249-254.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 249-254
    • Terashima, M.1    Kubo, A.2    Suzawa, M.3    Itoh, Y.4    Katoh, S.5
  • 57
    • 0032415326 scopus 로고    scopus 로고
    • Analysis of embryo-specific α-amylase using isolated mature rice embryos
    • Yamaguchi, J. (1998) Analysis of embryo-specific α-amylase using isolated mature rice embryos. Breeding Sci. 48: 365-370.
    • (1998) Breeding Sci. , vol.48 , pp. 365-370
    • Yamaguchi, J.1
  • 58
    • 0030106249 scopus 로고    scopus 로고
    • Sugars act as signal molecules and osmotica to regulate the expression of α-amylase genes and metabolic activities in germinating cereal grains
    • Yu, S.-M., Lee, Y.-C., Fang, S.-C., Chan, M.-T., Hwa, S.-F. and Liu, L.-F. (1996) Sugars act as signal molecules and osmotica to regulate the expression of α-amylase genes and metabolic activities in germinating cereal grains. Plant Mol. Biol. 30: 1277-1289.
    • (1996) Plant Mol. Biol. , vol.30 , pp. 1277-1289
    • Yu, S.-M.1    Lee, Y.-C.2    Fang, S.-C.3    Chan, M.-T.4    Hwa, S.-F.5    Liu, L.-F.6
  • 59
    • 20144371205 scopus 로고    scopus 로고
    • α-Amylase is not required for breakdown of transitory starch in Arabidopsis leaves
    • Yu, T.-S., Zeeman, S.C., Thorneycroft, D., Fulton, D.C., Dunstan, H., et al. (2005) α-Amylase is not required for breakdown of transitory starch in Arabidopsis leaves. J. Biol. Chem. 280: 9773-9779.
    • (2005) J. Biol. Chem. , vol.280 , pp. 9773-9779
    • Yu, T.-S.1    Zeeman, S.C.2    Thorneycroft, D.3    Fulton, D.C.4    Dunstan, H.5
  • 60
    • 0032143523 scopus 로고    scopus 로고
    • A starch-accumulating mutant of Arabidopsis thaliana deficient in a chloroplastic starch-hydrolysing enzyme
    • Zeeman, S.C., Northrop, F., Smith, A.M. and ap Rees, T. (1998) A starch-accumulating mutant of Arabidopsis thaliana deficient in a chloroplastic starch-hydrolysing enzyme. Plant J. 15: 357-365.
    • (1998) Plant J. , vol.15 , pp. 357-365
    • Zeeman, S.C.1    Northrop, F.2    Smith, A.M.3    Ap Rees, T.4
  • 61
    • 3542995724 scopus 로고    scopus 로고
    • The breakdown of starch in leaves
    • Zeeman, S.C., Smith, S.M. and Smith, A.M. (2004) The breakdown of starch in leaves. New Phytol. 163: 247-261.
    • (2004) New Phytol. , vol.163 , pp. 247-261
    • Zeeman, S.C.1    Smith, S.M.2    Smith, A.M.3
  • 62
    • 0001272522 scopus 로고
    • Partial purification and characterization of the major endoamylase of mature pea leaves
    • Ziegler, P. (1988) Partial purification and characterization of the major endoamylase of mature pea leaves. Plant Physiol. 86: 659-666.
    • (1988) Plant Physiol. , vol.86 , pp. 659-666
    • Ziegler, P.1


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