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Volumn 12, Issue 1, 1998, Pages 25-28

An expression system of rat calmodulin using T7 phage promoter in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLATION; CALMODULIN; CHROMATOGRAPHY; COMPLEMENTARY DNA; GENE EXPRESSION SYSTEM; ISOPROPYL BETA DEXTRO THIOGALACTOPYRANOSIDE; METHIONINE; METHYLATION; MUTANT PROTEIN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PHAGE PROMOTER; PHENYL SEPHAROSE; PROTEIN PROCESSING; RNA POLYMERASE; TRANSFORMATION; X RAY CRYSTALLOGRAPHY;

EID: 0032004888     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1997.0807     Document Type: Article
Times cited : (136)

References (23)
  • 1
    • 0029149085 scopus 로고
    • Molecular and structural basis of target recognition by calmodulin
    • Crivici A., Ikura M. Molecular and structural basis of target recognition by calmodulin. Annu. Rev. Biophys. Biomol. Struct. 24:1995;85-116.
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 85-116
    • Crivici, A.1    Ikura, M.2
  • 3
    • 0029058666 scopus 로고
    • Structural analysis of a novel interaction by calmodulin: High-affinity binding of a peptide in the absence of calcium
    • Urbauer J. L., Short J. H., Dow L. K., Wand A. J. Structural analysis of a novel interaction by calmodulin: High-affinity binding of a peptide in the absence of calcium. Biochemistry. 34:1995;8099-8109.
    • (1995) Biochemistry , vol.34 , pp. 8099-8109
    • Urbauer, J.L.1    Short, J.H.2    Dow, L.K.3    Wand, A.J.4
  • 5
    • 0023519975 scopus 로고
    • Molecular analysis of human and rat calmodulin complementary DNA clones: Evidence for additional active genes in these species
    • SenGupta B., Friedberg F., Detera-Wadleigh S. D. Molecular analysis of human and rat calmodulin complementary DNA clones: Evidence for additional active genes in these species. J. Biol. Chem. 262:1987;16663-16670.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16663-16670
    • Sengupta, B.1    Friedberg, F.2    Detera-Wadleigh, S.D.3
  • 7
    • 0019320688 scopus 로고
    • The complete amino acid sequence of the Ca2+-dependent modulator protein (calmodulin) of bovine brain
    • Watterson D. M., Sharief F., VanamanA T. C. The complete amino acid sequence of the Ca2+-dependent modulator protein (calmodulin) of bovine brain. J. Biol. Chem. 255:1980;962-975.
    • (1980) J. Biol. Chem. , vol.255 , pp. 962-975
    • Watterson, D.M.1    Sharief, F.2    Vanamana, T.C.3
  • 9
    • 0017904140 scopus 로고
    • Sequence homology of the Ca2+-dependent regulator of cyclic nucleotide phosphodiesterase from rat testis with other Ca2+-binding proteins
    • Dedman J. R., Jackson R. L., Schreiber W. E., Means A. R. Sequence homology of the Ca2+-dependent regulator of cyclic nucleotide phosphodiesterase from rat testis with other Ca2+-binding proteins. J. Biol. Chem. 253:1978;343-346.
    • (1978) J. Biol. Chem. , vol.253 , pp. 343-346
    • Dedman, J.R.1    Jackson, R.L.2    Schreiber, W.E.3    Means, A.R.4
  • 11
    • 0023156302 scopus 로고
    • Structure of a gene for rat calmodulin
    • Nojima H., Sokabe H. Structure of a gene for rat calmodulin. J. Mol. Biol. 193:1987;439-445.
    • (1987) J. Mol. Biol. , vol.193 , pp. 439-445
    • Nojima, H.1    Sokabe, H.2
  • 12
    • 0023114145 scopus 로고
    • Multiple calmodulin mRNA species are derived from two distinct genes
    • Nojima H., Kishi K., Sokabe H. Multiple calmodulin mRNA species are derived from two distinct genes. Mol. Cell. Biol. 7:1987;1873-1880.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 1873-1880
    • Nojima, H.1    Kishi, K.2    Sokabe, H.3
  • 13
    • 0024370325 scopus 로고
    • Structural organization of multiple rat calmodulin genes
    • Nojima H. Structural organization of multiple rat calmodulin genes. J. Mol. Biol. 208:1989;269-282.
    • (1989) J. Mol. Biol. , vol.208 , pp. 269-282
    • Nojima, H.1
  • 15
    • 0021886339 scopus 로고
    • Bacterial expression and characterization of proteins derived from the chicken calmodulin cDNA and a calmodulin processed gene
    • Putkey J. A., Slaughter G. R., Means A. R. Bacterial expression and characterization of proteins derived from the chicken calmodulin cDNA and a calmodulin processed gene. J. Biol. Chem. 260:1985;4704-4712.
    • (1985) J. Biol. Chem. , vol.260 , pp. 4704-4712
    • Putkey, J.A.1    Slaughter, G.R.2    Means, A.R.3
  • 16
    • 0022930606 scopus 로고
    • Efficient expression of heterologous genes inEscherichia coli:
    • Shatzman A. R., Rosenberg M. Efficient expression of heterologous genes inEscherichia coli: Ann. N.Y. Acad. Sci. 478:1986;233-248.
    • (1986) Ann. N.Y. Acad. Sci. , vol.478 , pp. 233-248
    • Shatzman, A.R.1    Rosenberg, M.2
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0020493109 scopus 로고
    • Ca2+-induced hydrophobic site on calmodulin: Application for purification of calmodulin by phenyl-Sepharose affinity chromatography
    • Gopalakrishna R., Anderson W. B. Ca2+-induced hydrophobic site on calmodulin: Application for purification of calmodulin by phenyl-Sepharose affinity chromatography. Biochem. Biophys. Res. Commun. 104:1982;830-836.
    • (1982) Biochem. Biophys. Res. Commun. , vol.104 , pp. 830-836
    • Gopalakrishna, R.1    Anderson, W.B.2
  • 19
    • 0028021757 scopus 로고
    • A mass spectrometric study on the in vivo posttranslational modification of GAP-43
    • Taniguchi H., Suzuki M., Manenti S., Titani K. A mass spectrometric study on the in vivo posttranslational modification of GAP-43. J. Biol. Chem. 269:1994;22481-22484.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22481-22484
    • Taniguchi, H.1    Suzuki, M.2    Manenti, S.3    Titani, K.4
  • 20
    • 0028334631 scopus 로고
    • Myristoylated alanine-rich C kinase substrate (MARCKS), a major protein kinase C substrate, is an in vivo substrate of proline-directed protein kinase(s): A mass spectroscopic analysis of the post-translational modifications
    • Taniguchi H., Manenti S., Suzuki M., Titani K. Myristoylated alanine-rich C kinase substrate (MARCKS), a major protein kinase C substrate, is an in vivo substrate of proline-directed protein kinase(s): A mass spectroscopic analysis of the post-translational modifications. J. Biol. Chem. 269:1994;18299-18302.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18299-18302
    • Taniguchi, H.1    Manenti, S.2    Suzuki, M.3    Titani, K.4
  • 21
    • 0029334151 scopus 로고
    • Secondary structure determination by NMR spectroscopy of an immunoglobulin-like domain from the giant muscle protein titin
    • Pfuhl M., Gautel M., Politou A. S., Joseph C., Pastore A. Secondary structure determination by NMR spectroscopy of an immunoglobulin-like domain from the giant muscle protein titin. J. Biomol. NMR. 6:1995;48-58.
    • (1995) J. Biomol. NMR , vol.6 , pp. 48-58
    • Pfuhl, M.1    Gautel, M.2    Politou, A.S.3    Joseph, C.4    Pastore, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.