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Volumn 17, Issue 1, 1999, Pages 49-56

Expression and purification of recombinant mouse fibrillarin

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ANIMAL MODEL; AUTOIMMUNITY; CARBOXY TERMINAL SEQUENCE; CHELATION; CHROMATOGRAPHY; DISULFIDE BOND; EPITOPE; ESCHERICHIA COLI; EXPRESSION VECTOR; FIBRILLARIN; MERCAPTOETHANOL; PROTEIN DENATURATION; PROTEIN EXPRESSION; PROTEIN HYDROLYSIS; PROTEIN PURIFICATION; RECOMBINANT PROTEIN; RIBOSOMAL RNA; RNA SPLICING; SCLERODERMA; SMALL NUCLEOLAR RIBONUCLEOPROTEIN;

EID: 0033213584     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1999.1099     Document Type: Article
Times cited : (18)

References (25)
  • 1
    • 0022405831 scopus 로고
    • Purification and partial characterization of a nucleolar scleroderma antigen rich in NG, NG-dimethylarginine
    • Lischwe M. A., Ochs R. L., Reddy R., Cook R. G., Yeoman L. C., Tan E. M., Reichlin M., Busch H. Purification and partial characterization of a nucleolar scleroderma antigen rich in NG, NG-dimethylarginine. J. Biol. Chem. 260:1985;14304-14310.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14304-14310
    • Lischwe, M.A.1    Ochs, R.L.2    Reddy, R.3    Cook, R.G.4    Yeoman, L.C.5    Tan, E.M.6    Reichlin, M.7    Busch, H.8
  • 2
    • 0022196373 scopus 로고
    • Fibrillarin: A new protein of the nucleolus identified by autoimmune sera
    • Ochs R. L., Lischwe M. A., Spohn W. H., Busch H. Fibrillarin: A new protein of the nucleolus identified by autoimmune sera. Biol. Cell. 54:1985;123-134.
    • (1985) Biol. Cell. , vol.54 , pp. 123-134
    • Ochs, R.L.1    Lischwe, M.A.2    Spohn, W.H.3    Busch, H.4
  • 3
    • 0027536869 scopus 로고
    • Temperature-sensitive mutations demonstrate roles for yeast fibrillarin in pre-rRNA processing, pre-rRNA methylation, and ribosome assembly
    • Tollervey D., Lehtonen H., Jansen R., Kern H., Hurt E. Temperature-sensitive mutations demonstrate roles for yeast fibrillarin in pre-rRNA processing, pre-rRNA methylation, and ribosome assembly. Cell. 72:1993;443-457.
    • (1993) Cell , vol.72 , pp. 443-457
    • Tollervey, D.1    Lehtonen, H.2    Jansen, R.3    Kern, H.4    Hurt, E.5
  • 4
    • 0027367190 scopus 로고
    • Molecular cloning and sequence analysis of U3 snoRNA-associated mouse fibrillarin
    • Turley S. J., Tan E. M., Pollard K. M. Molecular cloning and sequence analysis of U3 snoRNA-associated mouse fibrillarin. Biochim. Biophys. Acta. 1216:1993;119-122.
    • (1993) Biochim. Biophys. Acta , vol.1216 , pp. 119-122
    • Turley, S.J.1    Tan, E.M.2    Pollard, K.M.3
  • 5
    • 0031110061 scopus 로고    scopus 로고
    • The autoimmunity-induced xenobiotic mercury interacts with the autoantigen fibrillarin and modifies its molecular and antigenic properties
    • Pollard K. M., Lee D. K., Casiano C. A., Bluthner M., Johnston M. M., Tan E. M. The autoimmunity-induced xenobiotic mercury interacts with the autoantigen fibrillarin and modifies its molecular and antigenic properties. J. Immunol. 158:1997;3521-3528.
    • (1997) J. Immunol. , vol.158 , pp. 3521-3528
    • Pollard, K.M.1    Lee, D.K.2    Casiano, C.A.3    Bluthner, M.4    Johnston, M.M.5    Tan, E.M.6
  • 9
    • 0028833417 scopus 로고
    • Analysis of autoantibody response to fibrillarin in human disease and murine models of autoimmunity
    • Takeuchi K., Turley S. J., Tan E. M., Pollard K. M. Analysis of autoantibody response to fibrillarin in human disease and murine models of autoimmunity. J. Immunol. 154:1995;961-971.
    • (1995) J. Immunol. , vol.154 , pp. 961-971
    • Takeuchi, K.1    Turley, S.J.2    Tan, E.M.3    Pollard, K.M.4
  • 11
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier F. W., Moffatt B. A. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189:1986;113-130.
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 12
    • 0024558335 scopus 로고
    • One-step preparation of competent Escherichia coli: Transformation and storage of bacterial cells in the same solution
    • Chung C. T., Niemela S. L., Miller R. H. One-step preparation of competent Escherichia coli: Transformation and storage of bacterial cells in the same solution. Proc. Natl. Acad. Sci. USA. 86:1989;2172-2175.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 2172-2175
    • Chung, C.T.1    Niemela, S.L.2    Miller, R.H.3
  • 13
    • 0023659137 scopus 로고
    • New metal chelate absorbent selective for proteins and peptides containing neighbouring histidine residues
    • Hochuli E., Dobeli H., Schacher A. New metal chelate absorbent selective for proteins and peptides containing neighbouring histidine residues. J. Chromatogr. 411:1987;177-184.
    • (1987) J. Chromatogr. , vol.411 , pp. 177-184
    • Hochuli, E.1    Dobeli, H.2    Schacher, A.3
  • 15
    • 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. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 16
    • 0001536304 scopus 로고
    • Autoantibodies to ribonucleoprotein particles by immunoblotting
    • N. R. Rose, H. Friedman, & J. L. Fahey. Washington: Am. Soc. Microbiol.
    • Chan E. K. L., Pollard K. M. Autoantibodies to ribonucleoprotein particles by immunoblotting. Rose N. R., Friedman H., Fahey J. L. Manual of Clinical Laboratory Immunology. 1992;755-761 Am. Soc. Microbiol. Washington.
    • (1992) Manual of Clinical Laboratory Immunology , pp. 755-761
    • Chan, E.K.L.1    Pollard, K.M.2
  • 17
    • 0024429732 scopus 로고
    • Production of soluble recombinant proteins in bacteria
    • Schein C. H. Production of soluble recombinant proteins in bacteria. Biotechnology. 7:1989;1141-1149.
    • (1989) Biotechnology , vol.7 , pp. 1141-1149
    • Schein, C.H.1
  • 18
    • 0031076278 scopus 로고    scopus 로고
    • Purification and biochemical characterization of the 19-kDa signal recognition particle RNA-binding protein expressed as a hexahistidine-tagged polypeptide in Escherichia coli
    • Henry K. A., Zweib C., Fried H. Purification and biochemical characterization of the 19-kDa signal recognition particle RNA-binding protein expressed as a hexahistidine-tagged polypeptide in Escherichia coli. Protein Expression Purif. 9:1996;15-26.
    • (1996) Protein Expression Purif. , vol.9 , pp. 15-26
    • Henry, K.A.1    Zweib, C.2    Fried, H.3
  • 19
    • 0026031446 scopus 로고
    • Epitope tagging and protein surveillance
    • San Diego: Academic Press. p. 508-519
    • Kolodziej P. A., Young R. A. Epitope tagging and protein surveillance. Methods in Enzymology. 1991;Academic Press, San Diego. p. 508-519.
    • (1991) Methods in Enzymology
    • Kolodziej, P.A.1    Young, R.A.2
  • 21
    • 0028094123 scopus 로고
    • Immunoaffinity purification of FLAG epitope-tagged bacterial alkaline phosphatase using a novel monoclonal antibody and peptide elution
    • Brizzard B. L., Chubet R. G., Vizard D. L. Immunoaffinity purification of FLAG epitope-tagged bacterial alkaline phosphatase using a novel monoclonal antibody and peptide elution. Biotechniques. 16:1994;730-735.
    • (1994) Biotechniques , vol.16 , pp. 730-735
    • Brizzard, B.L.1    Chubet, R.G.2    Vizard, D.L.3
  • 23
    • 0031006770 scopus 로고    scopus 로고
    • Agglutination-inhibition assay for the detection of recombinant proteins tagged with peptide epitopes
    • Ross R., Kumpf K., Reske-Kunz A. B. Agglutination-inhibition assay for the detection of recombinant proteins tagged with peptide epitopes. Biotechniques. 22:1997;897-904.
    • (1997) Biotechniques , vol.22 , pp. 897-904
    • Ross, R.1    Kumpf, K.2    Reske-Kunz, A.B.3
  • 24
    • 0027369861 scopus 로고
    • Biochemical and spectroscopic probes of mercury(II) coordination environments in proteins
    • San Diego: Academic Press. p. 71-97
    • Utschig L. M., Wright J. G., O'Halloran T. V. Biochemical and spectroscopic probes of mercury(II) coordination environments in proteins. Methods of Enzymology. 1993;Academic Press, San Diego. p. 71-97.
    • (1993) Methods of Enzymology
    • Utschig, L.M.1    Wright, J.G.2    O'Halloran, T.V.3
  • 25
    • 0031930872 scopus 로고    scopus 로고
    • Use of recombinant pemphigus vulgaris antigen in development of ELISA and IB assays to detect pemphigus vulgaris autoantibodies
    • Bhol K., Tyagi S., Natarajan K., Nagarwalla N., Ahmed A. R. Use of recombinant pemphigus vulgaris antigen in development of ELISA and IB assays to detect pemphigus vulgaris autoantibodies. J. Eur. Acad. Dermatol. Venereol. 10:1998;28-35.
    • (1998) J. Eur. Acad. Dermatol. Venereol. , vol.10 , pp. 28-35
    • Bhol, K.1    Tyagi, S.2    Natarajan, K.3    Nagarwalla, N.4    Ahmed, A.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.