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Volumn 41, Issue 6, 1999, Pages 801-814

The eEF1A gene family is differentially expressed in maize endosperm

Author keywords

eEF1A; Endosperm; Gene family; Maize; opaque2

Indexed keywords

CDNA LIBRARY; COMPLEMENTARY DNA; DNA SCREENING; ENDOSPERM; GENETIC TRANSCRIPTION; MAIZE; MUTANT; PLANT GENETICS; WILD RELATIVE;

EID: 0033233408     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1006391207980     Document Type: Article
Times cited : (39)

References (49)
  • 1
    • 0026227753 scopus 로고
    • Two genes encoding the soybean translation elongation factor EF-1α are transcribed in seedling leaves
    • Aguilar, F., Montandon, P. and Stutz, C. 1991. Two genes encoding the soybean translation elongation factor EF-1α are transcribed in seedling leaves. Plant Mol. Biol. 17: 351-360.
    • (1991) Plant Mol. Biol. , vol.17 , pp. 351-360
    • Aguilar, F.1    Montandon, P.2    Stutz, C.3
  • 2
    • 0024745067 scopus 로고
    • The gene family encoding the Arabidopsis thaliana translation elongation factor EF-1α: Molecular cloning, characterization and expression
    • Axelos, M., Bardet, C., Liboz, T., LeVan Thai, A., Curie, C. and Lescure, B. 1989. The gene family encoding the Arabidopsis thaliana translation elongation factor EF-1α: molecular cloning, characterization and expression. Mol. Gen. Genet. 219: 106-112.
    • (1989) Mol. Gen. Genet. , vol.219 , pp. 106-112
    • Axelos, M.1    Bardet, C.2    Liboz, T.3    LeVan Thai, A.4    Curie, C.5    Lescure, B.6
  • 3
    • 0029411667 scopus 로고
    • Molecular cloning, characterization and expression of an elongation factor1 alpha gene in maize
    • Berberich, T., Sugawara, K., Harada, M. and Kusano, T. 1995. Molecular cloning, characterization and expression of an elongation factor1 alpha gene in maize. Plant Mol. Biol. 29: 611-615.
    • (1995) Plant Mol. Biol. , vol.29 , pp. 611-615
    • Berberich, T.1    Sugawara, K.2    Harada, M.3    Kusano, T.4
  • 4
    • 0030266994 scopus 로고    scopus 로고
    • The plant translational apparatus
    • Browning, K. 1996. The plant translational apparatus. Plant Mol. Biol. 32: 107-144.
    • (1996) Plant Mol. Biol. , vol.32 , pp. 107-144
    • Browning, K.1
  • 5
    • 0342923729 scopus 로고    scopus 로고
    • Screening corn (Zea mays) cDNA library with yeast sterol methyltransferase gene results in the isolation of a full length cDNA encoding elongation factor 1-alpha
    • Cao, H., Tong, Y. and Nes, W.D. 1997. Screening corn (Zea mays) cDNA library with yeast sterol methyltransferase gene results in the isolation of a full length cDNA encoding elongation factor 1-alpha. Plant Physiol. 113: 1463.
    • (1997) Plant Physiol. , vol.113 , pp. 1463
    • Cao, H.1    Tong, Y.2    Nes, W.D.3
  • 6
    • 0031588970 scopus 로고    scopus 로고
    • Site-direct mutants of post-translationally modified sites of yeast eEF1a using a shuttle vector containing a chromogenic switch
    • Cavallius, J., Popkie, A.P. and Merrick, W.C. 1997. Site-direct mutants of post-translationally modified sites of yeast eEF1A using a shuttle vector containing a chromogenic switch. Biochim. Biophys. Acta 1350: 345-358.
    • (1997) Biochim. Biophys. Acta , vol.1350 , pp. 345-358
    • Cavallius, J.1    Popkie, A.P.2    Merrick, W.C.3
  • 7
    • 0030463901 scopus 로고    scopus 로고
    • EF-1α is associated with a cytoskeletal network surrounding protein bodies in maize endosperm cells
    • Clore, A.M., Dannenhoffer, J.M. and Larkins, B.A. 1996. EF-1α is associated with a cytoskeletal network surrounding protein bodies in maize endosperm cells. Plant Cell 8: 2003-2014.
    • (1996) Plant Cell , vol.8 , pp. 2003-2014
    • Clore, A.M.1    Dannenhoffer, J.M.2    Larkins, B.A.3
  • 8
    • 0028670656 scopus 로고
    • Elongation factor 1α is a component of the subcortical actin bundles of characcean algae
    • Collings, D.A, Wasteneys, G.O., Miyazaki, M. and Williamson, M. 1994. Elongation factor 1α is a component of the subcortical actin bundles of characcean algae. Cell Biol. Int. 18: 1019-1024.
    • (1994) Cell Biol. Int. , vol.18 , pp. 1019-1024
    • Collings, D.A.1    Wasteneys, G.O.2    Miyazaki, M.3    Williamson, M.4
  • 9
    • 0025367870 scopus 로고
    • Three genes under different development control encode elongation factor 1-α in Xenopus laevis
    • Dje, M.K., Mazabraud, A., Viel, A., Maire, M.L., Denis, H., Crawford, E. and Brown, D.D. 1990. Three genes under different development control encode elongation factor 1-α in Xenopus laevis. Nucl. Acids Res. 18: 3489-3493.
    • (1990) Nucl. Acids Res. , vol.18 , pp. 3489-3493
    • Dje, M.K.1    Mazabraud, A.2    Viel, A.3    Maire, M.L.4    Denis, H.5    Crawford, E.6    Brown, D.D.7
  • 10
    • 0027951751 scopus 로고
    • Beyond translation: Elongation factor-1α and the cytoskeleton
    • Durso, N.A. and Cyr, R.J. 1994. Beyond translation: elongation factor-1α and the cytoskeleton. Protoplasma 180: 99-105.
    • (1994) Protoplasma , vol.180 , pp. 99-105
    • Durso, N.A.1    Cyr, R.J.2
  • 11
    • 0029020353 scopus 로고
    • pH regulation of the F-actin binding properties of Dictyostelium elongation factor 1-α
    • Edmonds, B.T., Murry, J. and Condeelis, J. 1995. pH regulation of the F-actin binding properties of Dictyostelium elongation factor 1-α. J. Biol. Chem. 270: 15222-15230.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15222-15230
    • Edmonds, B.T.1    Murry, J.2    Condeelis, J.3
  • 12
    • 0032562710 scopus 로고    scopus 로고
    • The effect of F-actin on the binding and hydrolysis of guanine nucleotide by Dictyostelium elongation factor 1A
    • Edmonds, B.T., Bell, A., Wyckoff, J., Condeelis, J. and Leyh, T.S. 1998. The effect of F-actin on the binding and hydrolysis of guanine nucleotide by Dictyostelium elongation factor 1A. J. Biol. Chem. 273: 10288-10295.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10288-10295
    • Edmonds, B.T.1    Bell, A.2    Wyckoff, J.3    Condeelis, J.4    Leyh, T.S.5
  • 13
    • 0021952340 scopus 로고
    • Regulation of protein synthesis factor EF-1α in Mucor racemosus
    • Fonzi, W.A., Katayama, C., Leathers, T. and Sypherd, P.S. 1985. Regulation of protein synthesis factor EF-1α in Mucor racemosus. Mol. Cell Biol. 5: 1100-1103.
    • (1985) Mol. Cell Biol. , vol.5 , pp. 1100-1103
    • Fonzi, W.A.1    Katayama, C.2    Leathers, T.3    Sypherd, P.S.4
  • 14
    • 0027692816 scopus 로고
    • The origin of the lysine-containing proteins in opaque2 maize endosperm
    • Habben, J.E., Kirleis, A.W. and Larkins, B.A.. 1993. The origin of the lysine-containing proteins in opaque2 maize endosperm. Plant Mol. Biol. 23: 825-838.
    • (1993) Plant Mol. Biol. , vol.23 , pp. 825-838
    • Habben, J.E.1    Kirleis, A.W.2    Larkins, B.A.3
  • 15
    • 0028981203 scopus 로고
    • Elongation factor 1α concentration is highly correlated with the lysine content of maize endosperm
    • Habben, J.E., Moro, G.L., Hunter, B.G., Hamaker, B.R. and Larkins, B.A. 1995. Elongation factor 1α concentration is highly correlated with the lysine content of maize endosperm. Proc. Natl. Acad. Sci. USA 92: 8640-8644.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8640-8644
    • Habben, J.E.1    Moro, G.L.2    Hunter, B.G.3    Hamaker, B.R.4    Larkins, B.A.5
  • 16
    • 0024451475 scopus 로고
    • Anchoring of peptide elongation factor EF-1α by phosphatidylinositol at the endoplasmic reticulum membrane
    • Hayashi, Y., Urade, R., Utsumi, S. and Kito, M. 1989. Anchoring of peptide elongation factor EF-1α by phosphatidylinositol at the endoplasmic reticulum membrane. J. Biochem. 106: 560-563.
    • (1989) J. Biochem. , vol.106 , pp. 560-563
    • Hayashi, Y.1    Urade, R.2    Utsumi, S.3    Kito, M.4
  • 18
    • 0016817277 scopus 로고
    • Identification of two copies of the gene for the elongation factor EF-Tu in E. coli
    • Jaskunas, S.R., Lindahl, L. and Nomura, M. 1975. Identification of two copies of the gene for the elongation factor EF-Tu in E. coli. Nature 257: 458-462.
    • (1975) Nature , vol.257 , pp. 458-462
    • Jaskunas, S.R.1    Lindahl, L.2    Nomura, M.3
  • 19
    • 0027933535 scopus 로고
    • Protein translation elongation factor-1α from Trypanosoma brucei binds calmodulin
    • Kaur, K.J. and Ruben, L. 1994. Protein translation elongation factor-1α from Trypanosoma brucei binds calmodulin. J. Biol. Chem. 269: 23045-23050.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23045-23050
    • Kaur, K.J.1    Ruben, L.2
  • 20
    • 0031906640 scopus 로고    scopus 로고
    • Isolation, characterization and mRNA expression of four cDNAs encoding translation elongation factor 1A from rice (Oryza sativa L.)
    • Kidou S. and Ejiri, S. 1998. Isolation, characterization and mRNA expression of four cDNAs encoding translation elongation factor 1A from rice (Oryza sativa L.). Plant Mol. Biol. 36: 137-148.
    • (1998) Plant Mol. Biol. , vol.36 , pp. 137-148
    • Kidou, S.1    Ejiri, S.2
  • 21
    • 0025137913 scopus 로고
    • The predicted amino acid sequence of a centrosphere protein in dividing sea urchin eggs is similar to elongation factor (EF-1α)
    • Kuriyama, R., Savereide, P., Lefebvre, P. and Dasgupta, S. 1990. The predicted amino acid sequence of a centrosphere protein in dividing sea urchin eggs is similar to elongation factor (EF-1α). J. Cell Sci. 95: 231-236.
    • (1990) J. Cell Sci. , vol.95 , pp. 231-236
    • Kuriyama, R.1    Savereide, P.2    Lefebvre, P.3    Dasgupta, S.4
  • 22
    • 0000430975 scopus 로고
    • Synthesis and deposition of zein in protein bodies of maize endosperm
    • Larkins, B.A. and Hurkman, W.J. 1978. Synthesis and deposition of zein in protein bodies of maize endosperm. Plant Physiol. 62: 256-263.
    • (1978) Plant Physiol. , vol.62 , pp. 256-263
    • Larkins, B.A.1    Hurkman, W.J.2
  • 23
    • 0027359613 scopus 로고
    • Differential expression of S1 and elongation factor-1 alpha during rat development
    • Lee, S., Wolfraim, L.A. and Wang, E 1993. Differential expression of S1 and elongation factor-1 alpha during rat development. J. Biol. Chem. 268: 24453-24459.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24453-24459
    • Lee, S.1    Wolfraim, L.A.2    Wang, E.3
  • 24
    • 0022670484 scopus 로고
    • Three genes for elongation factor EF-1α in Mucor racemosus
    • Linz, J.E., Katayama, C. and Sypherd, P.S. 1986. Three genes for elongation factor EF-1α in Mucor racemosus. Mol. Cell Biol. 6: 593-600.
    • (1986) Mol. Cell Biol. , vol.6 , pp. 593-600
    • Linz, J.E.1    Katayama, C.2    Sypherd, P.S.3
  • 25
    • 0029828821 scopus 로고    scopus 로고
    • F-actin sequesters elongation factor 1α from interaction with aminoacyl-tRNA in a pH-dependent reaction
    • Liu, G, Tang, J., Edmonds, B.T., Murray, J., Levin, S. and Condeelis, J. 1996. F-actin sequesters elongation factor 1α from interaction with aminoacyl-tRNA in a pH-dependent reaction. J. Cell Biol. 135: 953-963.
    • (1996) J. Cell Biol. , vol.135 , pp. 953-963
    • Liu, G.1    Tang, J.2    Edmonds, B.T.3    Murray, J.4    Levin, S.5    Condeelis, J.6
  • 26
    • 0030249704 scopus 로고    scopus 로고
    • Assignment of human elongation factor 1 genes: EEF1A maps to chromosome 6q14 and EF!A2 to 20q13.3
    • Lund, A., Knudsen, S.M., Vissing, H., Clark, B. and Tommerups, N. 1996. Assignment of human elongation factor 1 genes: EEF1A maps to chromosome 6q14 and EF!A2 to 20q13.3. Genomics 36: 359-361.
    • (1996) Genomics , vol.36 , pp. 359-361
    • Lund, A.1    Knudsen, S.M.2    Vissing, H.3    Clark, B.4    Tommerups, N.5
  • 27
    • 0028057371 scopus 로고
    • Production of hybridization probes by the PCR utilizing digoxigenin-modified nucleotides
    • P. Isaac (Ed.), Humana Press, Totowa, NJ
    • McCreery, T. and Helentjaris, T. 1994a. Production of hybridization probes by the PCR utilizing digoxigenin-modified nucleotides. In: P. Isaac (Ed.), Protocols for Nucleic Acid Analysis by Non-Radioactive Techniques, Humana Press, Totowa, NJ, pp. 107-112.
    • (1994) Protocols for Nucleic Acid Analysis by Non-Radioactive Techniques , pp. 107-112
    • McCreery, T.1    Helentjaris, T.2
  • 28
    • 0343687844 scopus 로고
    • Hybridization of digoxigenin labeled probes to Southern blots and detection by chemiluminescence
    • P. Isaac (Ed.), Humana Press, Totowa, NJ
    • McCreery, T. and Helentjaris, T. 1994b. Hybridization of digoxigenin labeled probes to Southern blots and detection by chemiluminescence. In: P. Isaac (Ed.), Protocols for Nucleic Acid Analysis by Non-Radioactive Techniques, Humana Press, Totowa, NJ, pp. 112-117.
    • (1994) Protocols for Nucleic Acid Analysis by Non-Radioactive Techniques , pp. 112-117
    • McCreery, T.1    Helentjaris, T.2
  • 29
    • 0026742870 scopus 로고
    • Sequence of a cDNA encoding the alpha-subunit of wheat translation elongation factor 1
    • Metz, A.M., Timmer, R.T., Allen, M.L. and Browning, K.S. 1992. Sequence of a cDNA encoding the alpha-subunit of wheat translation elongation factor 1. Gene 120: 315-316.
    • (1992) Gene , vol.120 , pp. 315-316
    • Metz, A.M.1    Timmer, R.T.2    Allen, M.L.3    Browning, K.S.4
  • 30
    • 0030484609 scopus 로고    scopus 로고
    • Characterization of the variability for lysine content in normal and opaque2 maize endosperm
    • Moro, G.L., Habben, J.E., Hamaker, B.R. and Larkins, B.A. 1996. Characterization of the variability for lysine content in normal and opaque2 maize endosperm. Crop Sci. 36: 1651-1659.
    • (1996) Crop Sci. , vol.36 , pp. 1651-1659
    • Moro, G.L.1    Habben, J.E.2    Hamaker, B.R.3    Larkins, B.A.4
  • 31
    • 0023710643 scopus 로고
    • Mammalian valyl-tRNA synthetase forms a complex with the first elongation factor
    • Motorin, Yu.A., Wolfson, A.D., Orlovsky, A.F. and Gladilin, K.L. 1988. Mammalian valyl-tRNA synthetase forms a complex with the first elongation factor. FEBS Lett. 238: 262-264.
    • (1988) FEBS Lett. , vol.238 , pp. 262-264
    • Motorin, Yu.A.1    Wolfson, A.D.2    Orlovsky, A.F.3    Gladilin, K.L.4
  • 32
    • 0021473991 scopus 로고
    • Polypeptide chain elongation factor 1α (EF-1α) from yeast: Nucleotide sequence of one of the two genes for EF-1α from Saccharomyces cerevisiae
    • Nagata, S., Nagashima, K., Tsunetsugu-Yokota, Y., Fujimura, K., Miyazaki, M. and Kaziro, Y. 1984. Polypeptide chain elongation factor 1α (EF-1α) from yeast: nucleotide sequence of one of the two genes for EF-1α from Saccharomyces cerevisiae. EMBO J. 3: 1825-1830.
    • (1984) EMBO J. , vol.3 , pp. 1825-1830
    • Nagata, S.1    Nagashima, K.2    Tsunetsugu-Yokota, Y.3    Fujimura, K.4    Miyazaki, M.5    Kaziro, Y.6
  • 33
    • 0025248661 scopus 로고
    • The mitotic apparatus-associated 51-kDa protein from sea urchin eggs is a GTP-binding protein and is immunologically related to yeast polypeptide elongation factor 1 alpha
    • Ohta, K., Toriyama, M., Miyazaki, M., Murofushi, H., Hosoda, S., Endo, S. and Sakai, H. 1990. The mitotic apparatus-associated 51-kDa protein from sea urchin eggs is a GTP-binding protein and is immunologically related to yeast polypeptide elongation factor 1 alpha. J Biol. Chem. 265: 3240-3247.
    • (1990) J Biol. Chem. , vol.265 , pp. 3240-3247
    • Ohta, K.1    Toriyama, M.2    Miyazaki, M.3    Murofushi, H.4    Hosoda, S.5    Endo, S.6    Sakai, H.7
  • 34
    • 0030203863 scopus 로고    scopus 로고
    • Tree View: An application to display phylogenetic trees on personal computers
    • Page, R.D. 1996. Tree View: an application to display phylogenetic trees on personal computers. Comput. Appl. Biosci. 12: 357-358.
    • (1996) Comput. Appl. Biosci. , vol.12 , pp. 357-358
    • Page, R.D.1
  • 36
    • 0032114345 scopus 로고    scopus 로고
    • Phosphoglycerylethanolamine posttranslational modification of plant eukaryotic elongation factor 1″
    • Ransom W.D., Lao, P.C., Gage, D.A. and Boss, W.F. 1998. Phosphoglycerylethanolamine posttranslational modification of plant eukaryotic elongation factor 1″. Plant Physiol. 117: 949-960.
    • (1998) Plant Physiol. , vol.117 , pp. 949-960
    • Ransom, W.D.1    Lao, P.C.2    Gage, D.A.3    Boss, W.F.4
  • 38
    • 0023665290 scopus 로고
    • Sequence and identification of the nucleotide binding site for the elongation factor Tu from Thermus thermophilus HB8
    • Seidler, L., Peter, M., Meissner, F. and Sprinzl, M. 1987. Sequence and identification of the nucleotide binding site for the elongation factor Tu from Thermus thermophilus HB8. Nucl. Acids Res. 15: 9263-9277.
    • (1987) Nucl. Acids Res. , vol.15 , pp. 9263-9277
    • Seidler, L.1    Peter, M.2    Meissner, F.3    Sprinzl, M.4
  • 40
    • 0031277439 scopus 로고    scopus 로고
    • Characterization of maize elongation factor 1A and its relationship to protein quality in the endosperm
    • Sun, Y., Carneiro, N., Clore, A.M., Moro, G.L., Habben, J.E. and Larkins, B.A. 1997. Characterization of maize elongation factor 1A and its relationship to protein quality in the endosperm. Plant Physiol. 115: 1101-1107.
    • (1997) Plant Physiol. , vol.115 , pp. 1101-1107
    • Sun, Y.1    Carneiro, N.2    Clore, A.M.3    Moro, G.L.4    Habben, J.E.5    Larkins, B.A.6
  • 41
    • 0024544872 scopus 로고
    • End-label fingerprintings show that an N-terminal segment of depactin participates in interaction with actin
    • Sutoh, K. and Mabuchi, I. 1989. End-label fingerprintings show that an N-terminal segment of depactin participates in interaction with actin. Biochemistry 28: 102-106.
    • (1989) Biochemistry , vol.28 , pp. 102-106
    • Sutoh, K.1    Mabuchi, I.2
  • 42
    • 0002121649 scopus 로고
    • Isolation of plant DNA and RNA
    • Taylor, B. and Powell, A. 1982. Isolation of plant DNA and RNA. Focus 4: 4-6.
    • (1982) Focus , vol.4 , pp. 4-6
    • Taylor, B.1    Powell, A.2
  • 43
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G. and Gibson, T.J. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acids Res. 22: 4673-4680.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 44
    • 0021435556 scopus 로고
    • The primary structure of elongation factor EF-1 alpha from the brine shrimp Artemia
    • van Hemert, F.J., Amons, R., Pluijms, W.J., van Ormondt, H. and Moller, W. 1984. The primary structure of elongation factor EF-1 alpha from the brine shrimp Artemia. EMBO J. 3: 1109-1113.
    • (1984) EMBO J. , vol.3 , pp. 1109-1113
    • Van Hemert, F.J.1    Amons, R.2    Pluijms, W.J.3    Van Ormondt, H.4    Moller, W.5
  • 45
    • 0025744934 scopus 로고
    • Phosphorylation of elongation factor 1 (EF-1) and valyl-tRNA synthetase by protein kinase C and stimulation of EF-1 activity
    • Venema, R.C., Peters, H.I. and Traugh, J.A. 1991. Phosphorylation of elongation factor 1 (EF-1) and valyl-tRNA synthetase by protein kinase C and stimulation of EF-1 activity. J. Biol. Chem. 266: 12574-12580.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12574-12580
    • Venema, R.C.1    Peters, H.I.2    Traugh, J.A.3
  • 46
    • 0024414072 scopus 로고
    • Murine elongation factor 1 alpha (EF-1 alpha) is posttranslationally modified by novel amide-linked ethanolamine-phosphoglycerol moieties. Addition of ethanolamine-phosphoglycerol to specific glutamic acid residues on EF-1 alpha
    • Whiteheart S.W., Shenbagamurthi, P., Chen, L., Cotter, R.J. and Hart, G.W. 1989. Murine elongation factor 1 alpha (EF-1 alpha) is posttranslationally modified by novel amide-linked ethanolamine-phosphoglycerol moieties. Addition of ethanolamine-phosphoglycerol to specific glutamic acid residues on EF-1 alpha. J. Biol. Chem. 264: 14334-14341.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14334-14341
    • Whiteheart, S.W.1    Shenbagamurthi, P.2    Chen, L.3    Cotter, R.J.4    Hart, G.W.5
  • 47
    • 0025000290 scopus 로고
    • Identification of an actin-binding protein from Dictyostelium as elongation factor 1α
    • Yang, F., Demma, M., Warren, V., Dharmawardhane, S. and Condeelis, J. 1990. Identification of an actin-binding protein from Dictyostelium as elongation factor 1α. Nature 347: 494-496.
    • (1990) Nature , vol.347 , pp. 494-496
    • Yang, F.1    Demma, M.2    Warren, V.3    Dharmawardhane, S.4    Condeelis, J.5
  • 48
    • 0027463634 scopus 로고
    • Purification and characterization of a phosphatidylinositol 4-kinase activator in carrot cells
    • Yang, W., Burkhart, W., Cavallius, J., Merrick, W.C. and Boss, W.F. 1993. Purification and characterization of a phosphatidylinositol 4-kinase activator in carrot cells. J. Biol. Chem. 265: 392-398.
    • (1993) J. Biol. Chem. , vol.265 , pp. 392-398
    • Yang, W.1    Burkhart, W.2    Cavallius, J.3    Merrick, W.C.4    Boss, W.F.5


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