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Volumn 41, Issue 4, 2000, Pages 399-407

Possible involvement of phosphoinositide-Ca2+ signaling in the regulation of α-amylase expression and germination of rice seed (Oryza satira L.)

Author keywords

Ca2+; Gibberellin; Inositol 1,4,5 trisphosphate; Neomycin; Rice seed; Amylase isoform I 1

Indexed keywords

ABSCISIC ACID; ALEURONE; AMYLASE; CALCIUM; ENZYME INDUCTION; GERMINATION; GIBBERELLIC ACID; INOSITOL 1,4,5 TRISPHOSPHATE; NEOMYCIN; SIGNAL TRANSDUCTION;

EID: 0034115517     PISSN: 00320781     EISSN: None     Source Type: Journal    
DOI: 10.1093/pcp/41.4.399     Document Type: Article
Times cited : (60)

References (48)
  • 1
    • 0025129252 scopus 로고
    • 2+ channels in isolated red beet root vacuole membrane by inositol 1,4,5-trisphosphate
    • 2+ channels in isolated red beet root vacuole membrane by inositol 1,4,5-trisphosphate. Nature 343: 567-570.
    • (1990) Nature , vol.343 , pp. 567-570
    • Alexandre, J.1    Lassalles, J.P.2    Kado, R.T.3
  • 2
    • 0027397544 scopus 로고
    • Inositol trisphosphate and calcium signalling
    • Berridge, M.J. (1993) Inositol trisphosphate and calcium signalling. Nature 361: 315-325.
    • (1993) Nature , vol.361 , pp. 315-325
    • Berridge, M.J.1
  • 3
    • 0030879977 scopus 로고    scopus 로고
    • Hormonal signalling in cereal aleurone
    • Bethke, P.V., Schuurink, R. and Jones, R.L. (1997) Hormonal signalling in cereal aleurone. J. Exp. Bot. 48: 1337-1356.
    • (1997) J. Exp. Bot. , vol.48 , pp. 1337-1356
    • Bethke, P.V.1    Schuurink, R.2    Jones, R.L.3
  • 4
    • 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
  • 5
    • 0028855262 scopus 로고
    • Calcium regulation in plant cells and its role in signaling
    • Bush, D.S. (1995) Calcium regulation in plant cells and its role in signaling. Annu. Rev. Plant Physiol. Plant Mol. Biol. 46: 95-122.
    • (1995) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.46 , pp. 95-122
    • Bush, D.S.1
  • 6
    • 0006203382 scopus 로고    scopus 로고
    • Effects of gibberellic acid and environmental factors on cytosolic calcium in wheat aleurone cells
    • Bush, D.S. (1996) Effects of gibberellic acid and environmental factors on cytosolic calcium in wheat aleurone cells. Planta 199: 88-89.
    • (1996) Planta , vol.199 , pp. 88-89
    • Bush, D.S.1
  • 7
    • 0024971705 scopus 로고
    • The calcium requirement for stability and enzymatic activity of two isoforms of barley aleurone a-amylase
    • Bush, D.S., Sticher, L., Huystee, R., Wagner, D. and Jones, R.L. (1989) The calcium requirement for stability and enzymatic activity of two isoforms of barley aleurone a-amylase. J. Biol. Chem. 264: 19392-19398.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19392-19398
    • Bush, D.S.1    Sticher, L.2    Huystee, R.3    Wagner, D.4    Jones, R.L.5
  • 8
    • 0010537002 scopus 로고
    • Neomycin inhibits the phosphatidylinositol monophosphate and phosphatidylinositol bisphosphate stimulation of plasma membrane ATPase activity
    • Chen, Q. and Boss, W.F. (1991) Neomycin inhibits the phosphatidylinositol monophosphate and phosphatidylinositol bisphosphate stimulation of plasma membrane ATPase activity. Plant Physiol. 96: 340-343.
    • (1991) Plant Physiol. , vol.96 , pp. 340-343
    • Chen, Q.1    Boss, W.F.2
  • 9
    • 0031105943 scopus 로고    scopus 로고
    • 2+ in the gibberellin-dependent signaling pathway in aleurone cells
    • 2+ in the gibberellin-dependent signaling pathway in aleurone cells. Plant J. 11: 363-371.
    • (1997) Plant J. , vol.11 , pp. 363-371
    • Chen, X.1    Chang, M.2    Wang, B.3    Wu, R.4
  • 10
    • 0028119153 scopus 로고
    • Why do plants have phosphoinositides?
    • Coté, G.G. and Crain, R.C. (1994) Why do plants have phosphoinositides? BioEssays 16: 39-46.
    • (1994) BioEssays , vol.16 , pp. 39-46
    • Coté, G.G.1    Crain, R.C.2
  • 11
    • 0029832826 scopus 로고    scopus 로고
    • Growth of pollen tubes of Papaver rhoeas is regulated by a slow-moving calcium wave propagated by inositol 1,4,5-trisphosphate
    • Franklin-Tong, V.E., Drøbak, B.K., Allan, A.C., Watkins, P.A.C. and Trewavas, A.J. (1996) Growth of pollen tubes of Papaver rhoeas is regulated by a slow-moving calcium wave propagated by inositol 1,4,5-trisphosphate. Plant Cell 8: 1305-1321.
    • (1996) Plant Cell , vol.8 , pp. 1305-1321
    • Franklin-Tong, V.E.1    Drøbak, B.K.2    Allan, A.C.3    Watkins, P.A.C.4    Trewavas, A.J.5
  • 12
    • 0026534659 scopus 로고
    • Gibberellic acid and abscisic acid coordinately regulate cytoplasmic calcium and secretory activity in barley aleurone protoplasts
    • Gilroy, S. and Jones, R.L. (1992) Gibberellic acid and abscisic acid coordinately regulate cytoplasmic calcium and secretory activity in barley aleurone protoplasts. Proc. Natl. Acad. Sci. USA 89: 3591-3595.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3591-3595
    • Gilroy, S.1    Jones, R.L.2
  • 13
    • 0029061510 scopus 로고
    • A gene encoding a phosphatidylinositol-specific phospholipase C is induced by dehydration and salt stress in Arabidopsis thaliana
    • Hirayama, T., Ohto, C., Mizoguchi, T. and Shinozaki, K. (1995) A gene encoding a phosphatidylinositol-specific phospholipase C is induced by dehydration and salt stress in Arabidopsis thaliana. Proc. Natl. Acad. Sci. USA 92: 3903-3907.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3903-3907
    • Hirayama, T.1    Ohto, C.2    Mizoguchi, T.3    Shinozaki, K.4
  • 14
    • 0029105103 scopus 로고
    • Developmental and hormonal regulation of rice a-amylase (RAmy1A)-gusA fusion genes in transgenic rice seeds
    • Itoh, K., Yamaguchi, J., Huang, N., Rodriguez, R. L., Akazawa, T. and Shimamoto, K. (1995). Developmental and hormonal regulation of rice a-amylase (RAmy1A)-gusA fusion genes in transgenic rice seeds. Plant Physiol. 107: 25-31.
    • (1995) Plant Physiol. , vol.107 , pp. 25-31
    • Itoh, K.1    Yamaguchi, J.2    Huang, N.3    Rodriguez, R.L.4    Akazawa, T.5    Shimamoto, K.6
  • 15
    • 51249176890 scopus 로고
    • Assaying chimeric genes in plants: The GUS gene fusion system
    • Jefferson, R.A. (1987) Assaying chimeric genes in plants: The GUS gene fusion system. Plant Mol. Biol. Rep. 5: 387-405.
    • (1987) Plant Mol. Biol. Rep. , vol.5 , pp. 387-405
    • Jefferson, R.A.1
  • 16
    • 0031794835 scopus 로고    scopus 로고
    • Heterotrimeric G proteins are implicated in gibberellin induction of a-amylase gene expression in wild oat aleurone
    • Jones, H.D., Smith, S.J., Desikan, R., Plakidou-Dymock, S., Lovegrove, A. and Hooley, R. (1998) Heterotrimeric G proteins are implicated in gibberellin induction of a-amylase gene expression in wild oat aleurone. Plant Cell 10: 245-253.
    • (1998) Plant Cell , vol.10 , pp. 245-253
    • Jones, H.D.1    Smith, S.J.2    Desikan, R.3    Plakidou-Dymock, S.4    Lovegrove, A.5    Hooley, R.6
  • 17
    • 0028229326 scopus 로고    scopus 로고
    • Molecular structure of a barley a-amylase-inhibitor complex: Implications for starch binding and catalysis
    • Kadziola, A., Søgaard, M., Svensson, B. and Haser, R. (1998) Molecular structure of a barley a-amylase-inhibitor complex: Implications for starch binding and catalysis. J. Mol. Biol. 239: 104-121.
    • (1998) J. Mol. Biol. , vol.239 , pp. 104-121
    • Kadziola, A.1    Søgaard, M.2    Svensson, B.3    Haser, R.4
  • 18
    • 0032125543 scopus 로고    scopus 로고
    • Effects of (+)-8′,8′,8′-trifluoro-abscisic acid on a-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′-trifluoro-abscisic acid on a-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
  • 19
    • 0030040679 scopus 로고    scopus 로고
    • Inositol trisphosphate may mediate closure of potassium channels by light and darkness in Samanea saman motor cells
    • Kim, H.Y., Coté, G.G. and Crain, R.C. (1996) Inositol trisphosphate may mediate closure of potassium channels by light and darkness in Samanea saman motor cells. Planta 198: 279-287.
    • (1996) Planta , vol.198 , pp. 279-287
    • Kim, H.Y.1    Coté, G.G.2    Crain, R.C.3
  • 20
    • 0031788164 scopus 로고    scopus 로고
    • Molecular and enzymatic characterization of three phosphoinositide-specific phospholipase C isoforms from potato
    • Kopka, J., Pical, C., Gray, J.E. and Müller-Röber, B. (1998) Molecular and enzymatic characterization of three phosphoinositide-specific phospholipase C isoforms from potato. Plant Physiol. 116: 239-250.
    • (1998) Plant Physiol. , vol.116 , pp. 239-250
    • Kopka, J.1    Pical, C.2    Gray, J.E.3    Müller-Röber, B.4
  • 21
    • 0030087964 scopus 로고    scopus 로고
    • Okadaic acid, a protein phosphatase inhibitor, blocks calcium changes, gene expression, and cell death induced by gibberellin in wheat aleurone cells
    • Kuo, A., Cappelluti, S., Cervantes-Cervantes, M., Rodriguez, M. and Bush, D.S. (1996). Okadaic acid, a protein phosphatase inhibitor, blocks calcium changes, gene expression, and cell death induced by gibberellin in wheat aleurone cells. Plant Cell 8: 259-269.
    • (1996) Plant Cell , vol.8 , pp. 259-269
    • Kuo, A.1    Cappelluti, S.2    Cervantes-Cervantes, M.3    Rodriguez, M.4    Bush, D.S.5
  • 22
    • 0027358804 scopus 로고
    • Phospholipase C activation during elicitation of the oxidative burst in cultured plant cells
    • Legendre, L., Yueh, Y.G., Crain, R., Haddock, N., Heinstein, P.F. and Low, P.S. (1993) Phospholipase C activation during elicitation of the oxidative burst in cultured plant cells. J. Biol. Chem. 268: 24559-24563.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24559-24563
    • Legendre, L.1    Yueh, Y.G.2    Crain, R.3    Haddock, N.4    Heinstein, P.F.5    Low, P.S.6
  • 23
    • 0028114185 scopus 로고
    • Protein phosphatase inhibitors enhance the expression of an a-amylase gene, aAmy3, in cultured rice cells
    • Lue, M.-Y. and Lee, H.-T. (1994) Protein phosphatase inhibitors enhance the expression of an a-amylase gene, aAmy3, in cultured rice cells. Biochem. Biophys. Res. Commun. 205: 807-816.
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 807-816
    • Lue, M.-Y.1    Lee, H.-T.2
  • 24
    • 0000046879 scopus 로고
    • Speed of germination-aid in selection and evaluation for seedling emergence and vigor
    • Maguire, J.D. (1962) Speed of germination-aid in selection and evaluation for seedling emergence and vigor. Crop Sci. 2: 176-177.
    • (1962) Crop Sci. , vol.2 , pp. 176-177
    • Maguire, J.D.1
  • 26
    • 0030744750 scopus 로고    scopus 로고
    • The a-amylase multigene family
    • Mitsui, T. and Itoh, K. (1997) The a-amylase multigene family. Trends Plant Sci. 2: 255-261.
    • (1997) Trends Plant Sci. , vol.2 , pp. 255-261
    • Mitsui, T.1    Itoh, K.2
  • 28
    • 0032849188 scopus 로고    scopus 로고
    • Sucrose-controlled transport and turnover of a-amylase in rice (Oryza sativa L.) cells
    • Mitsui, T., Loboda, T., Kamimura, I., Hori, H., Itoh, K. and Mitsunaga, S. (1999b) Sucrose-controlled transport and turnover of a-amylase in rice (Oryza sativa L.) cells. Plant Cell Physiol. 40: 884-893.
    • (1999) Plant Cell Physiol. , vol.40 , pp. 884-893
    • Mitsui, T.1    Loboda, T.2    Kamimura, I.3    Hori, H.4    Itoh, K.5    Mitsunaga, S.6
  • 29
    • 0030113407 scopus 로고    scopus 로고
    • Physicochemical and serological characterization of rice a-amylase isoforms and identification of their corresponding genes
    • Mitsui, T., Yamaguchi, J. and Akazawa, T. (1996) Physicochemical and serological characterization of rice a-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
  • 30
    • 0027965954 scopus 로고
    • Leupeptin and E-64, inhibitors of cysteine proteinase, prevent gentamicin-induced lysosomal phospholipidosis in cultured rat fibroblasts
    • Montenez, J.-P., Kishore, B.K., Maldague, P. and Tulkens, P.M. (1994) Leupeptin and E-64, inhibitors of cysteine proteinase, prevent gentamicin-induced lysosomal phospholipidosis in cultured rat fibroblasts. Toxicol. Lett. 73: 201-208.
    • (1994) Toxicol. Lett. , vol.73 , pp. 201-208
    • Montenez, J.-P.1    Kishore, B.K.2    Maldague, P.3    Tulkens, P.M.4
  • 31
    • 0031200791 scopus 로고    scopus 로고
    • 2+ release across nonvacuolar membranes in cauliflower
    • 2+ release across nonvacuolar membranes in cauliflower. Plant Physiol. 114: 1511-1521.
    • (1997) Plant Physiol. , vol.114 , pp. 1511-1521
    • Muir, S.R.1    Sanders, D.2
  • 32
    • 0342421409 scopus 로고
    • Phosphoinositides in barley aleurone layers and gibberellic acid-induced changes in metabolism
    • Murthy, P.P.N., Renders, J.M. and Kerane, L.M. (1989) Phosphoinositides in barley aleurone layers and gibberellic acid-induced changes in metabolism. Plant Physiol. 91: 1266-1269.
    • (1989) Plant Physiol. , vol.91 , pp. 1266-1269
    • Murthy, P.P.N.1    Renders, J.M.2    Kerane, L.M.3
  • 33
    • 0018115154 scopus 로고
    • Purification of a-amylase and β-amylase from endosperm tissues of germinating rice seeds
    • Okamoto, K. and Akazawa, T. (1978) Purification of a-amylase and β-amylase from endosperm tissues of germinating rice seeds. Agric. Biol. Chem. 42: 1379-1384.
    • (1978) Agric. Biol. Chem. , vol.42 , pp. 1379-1384
    • Okamoto, K.1    Akazawa, T.2
  • 34
    • 0000987533 scopus 로고    scopus 로고
    • cGMP is required for gibberellic acid-induced gene expression in barley aleurone
    • Penson, S.P., Schuurink, R.C., Fath, A., Gubler, F., Jacobsen, J.V. and Jones, R.L. (1996) cGMP is required for gibberellic acid-induced gene expression in barley aleurone. Plant Cell 8: 2325-2333.
    • (1996) Plant Cell , vol.8 , pp. 2325-2333
    • Penson, S.P.1    Schuurink, R.C.2    Fath, A.3    Gubler, F.4    Jacobsen, J.V.5    Jones, R.L.6
  • 35
    • 0031412147 scopus 로고    scopus 로고
    • Sugar repression of a gibberellin-dependent signaling pathway in barley embryos
    • Perata, P., Matsukura, C., Vernieri, P. and Yamaguchi, J. (1997) Sugar repression of a gibberellin-dependent signaling pathway in barley embryos. Plant Cell 9: 2197-2208.
    • (1997) Plant Cell , vol.9 , pp. 2197-2208
    • Perata, P.1    Matsukura, C.2    Vernieri, P.3    Yamaguchi, J.4
  • 36
    • 0031769611 scopus 로고    scopus 로고
    • Tansley review no. 100. Gibberellins: Regulating genes and germination
    • Ritchie, S. and Gilroy, S. (1998a) Tansley review No. 100. Gibberellins: regulating genes and germination. New Phytol. 140: 363-383.
    • (1998) New Phytol. , vol.140 , pp. 363-383
    • Ritchie, S.1    Gilroy, S.2
  • 37
    • 0001176645 scopus 로고    scopus 로고
    • Calcium-dependent protein phosphorylation may mediate the gibberellic acid response in barley aleurone
    • Ritchie, S. and Gilroy, S. (1998b) Calcium-dependent protein phosphorylation may mediate the gibberellic acid response in barley aleurone. Plant Physiol. 116: 765-776.
    • (1998) Plant Physiol. , vol.116 , pp. 765-776
    • Ritchie, S.1    Gilroy, S.2
  • 38
    • 0032478336 scopus 로고    scopus 로고
    • Abscisic acid signal transduction in the barley aleurone is mediated by phospholipase D activity
    • Ritchie, S. and Gilroy, S. (1998c) Abscisic acid signal transduction in the barley aleurone is mediated by phospholipase D activity. Proc. Natl. Acad. Sci. USA 95: 2697-2702.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2697-2702
    • Ritchie, S.1    Gilroy, S.2
  • 39
    • 0030060649 scopus 로고    scopus 로고
    • Identification and preliminary characterisation of a calcium-dependent high-affinity binding site for inositol trisphosphate from Chenopodium rubrum
    • Scanlon, C.H., Martinec, J., Machácková, I., Rolph, C.E. and Lumsden, P.J. (1996) Identification and preliminary characterisation of a calcium-dependent high-affinity binding site for inositol trisphosphate from Chenopodium rubrum. Plant Physiol. 110: 867-874.
    • (1996) Plant Physiol. , vol.110 , pp. 867-874
    • Scanlon, C.H.1    Martinec, J.2    Machácková, I.3    Rolph, C.E.4    Lumsden, P.J.5
  • 40
    • 0000665321 scopus 로고    scopus 로고
    • Modulation of calmodulin mRNA and protein levels in barley aleurone
    • Schuurink, R.C., Chan, P.V. and Jones, R.L. (1996) Modulation of calmodulin mRNA and protein levels in barley aleurone. Plant Physiol. 111: 371-380.
    • (1996) Plant Physiol. , vol.111 , pp. 371-380
    • Schuurink, R.C.1    Chan, P.V.2    Jones, R.L.3
  • 41
    • 0029360601 scopus 로고
    • Characterization of a plasma membrane-associated phosphoinositol-specific phospholipase C from soybean
    • Shi, J., Gonzales, R.A. and Bhattacharyya, M.K. (1995) Characterization of a plasma membrane-associated phosphoinositol-specific phospholipase C from soybean. Plant J. 8: 381-390.
    • (1995) Plant J. , vol.8 , pp. 381-390
    • Shi, J.1    Gonzales, R.A.2    Bhattacharyya, M.K.3
  • 42
    • 0029959880 scopus 로고    scopus 로고
    • Carbohydrate starvation stimulates differential expression of rice a-amylase genes that is modulated through complicated transcriptional and posttranscriptional processes
    • Sheu, J.-J., Yu, T.-S., Tong, W.-F. and Yu, S.-M. (1996) Carbohydrate starvation stimulates differential expression of rice a-amylase genes that is modulated through complicated transcriptional and posttranscriptional processes. J. Biol. Chem. 271: 26998-27004.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26998-27004
    • Sheu, J.-J.1    Yu, T.-S.2    Tong, W.-F.3    Yu, S.-M.4
  • 43
    • 0031891965 scopus 로고    scopus 로고
    • Temporal and spatial experssion of the a-amylase gene during seed germination in rice and barley
    • Sugimoto, N., Taketa, G., Nagato, Y. and Yamaguchi, J. (1998) Temporal and spatial experssion of the a-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    Taketa, G.2    Nagato, Y.3    Yamaguchi, J.4
  • 44
    • 0029141325 scopus 로고
    • 8′,8′-difluoro- and 8′,8′,8′-trifluoroabscisic acids as highly potent, long-lasting analogues of abscisic acid
    • Todoroki, Y., Hirai, N. and Koshimizu, K. (1995) 8′,8′-difluoro- and 8′,8′,8′-trifluoroabscisic acids as highly potent, long-lasting analogues of abscisic acid. Phytochemistry 38: 561-568.
    • (1995) Phytochemistry , vol.38 , pp. 561-568
    • Todoroki, Y.1    Hirai, N.2    Koshimizu, K.3
  • 45
    • 0000098309 scopus 로고
    • Properties of plasma membrane isolated from chilling-sensitive etiolated seedlings of Vigna radiata L
    • Yoshida, S., Kawata, T., Uemura, M. and Niki, T. (1986) Properties of plasma membrane isolated from chilling-sensitive etiolated seedlings of Vigna radiata L. Plant Physiol. 80: 152-160.
    • (1986) Plant Physiol. , vol.80 , pp. 152-160
    • Yoshida, S.1    Kawata, T.2    Uemura, M.3    Niki, T.4
  • 46
    • 0030790118 scopus 로고    scopus 로고
    • Structure and function of inositol 1,4,5-trisphosphate receptor
    • Yoshida, Y. and Imai, S. (1997) Structure and function of inositol 1,4,5-trisphosphate receptor. Jpn. J. Pharmacol. 74: 125-137.
    • (1997) Jpn. J. Pharmacol. , vol.74 , pp. 125-137
    • Yoshida, Y.1    Imai, S.2
  • 47
    • 0000792375 scopus 로고
    • Purification and characterization of membrane-bound inositol phospholipid-specific phospholipase C from suspension-cultured rice (Oryza sativa L.) cells: Identification of a regulatory factor
    • Yotsushima, K., Mitsui, T., Takaoka, T., Hayakawa, T. and Igaue, I. (1993) Purification and characterization of membrane-bound inositol phospholipid-specific phospholipase C from suspension-cultured rice (Oryza sativa L.) cells: identification of a regulatory factor. Plant Physiol. 102: 165-172.
    • (1993) Plant Physiol. , vol.102 , pp. 165-172
    • Yotsushima, K.1    Mitsui, T.2    Takaoka, T.3    Hayakawa, T.4    Igaue, I.5
  • 48
    • 0030589612 scopus 로고    scopus 로고
    • Structure views of phosphoinositide-specific phospholipase C: Signalling the way ahead
    • Williams, R.L. and Katan M. (1996) Structure views of phosphoinositide-specific phospholipase C: signalling the way ahead. Structure 4: 1387-1394.
    • (1996) Structure , vol.4 , pp. 1387-1394
    • Williams, R.L.1    Katan, M.2


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