메뉴 건너뛰기




Volumn 14, Issue 2, 2004, Pages 417-421

Cloning, sequencing, and expression of cDNA encoding bovine prion protein

Author keywords

BSE; cDNA; Korean cattle; Prion protein

Indexed keywords

AMINO ACID; COMPLEMENTARY DNA; ISOPROPYL THIOGALACTOSIDE; ISOPROTEIN; NUCLEOTIDE; PRION PROTEIN; PROTEINASE; RECOMBINANT PROTEIN;

EID: 2442610729     PISSN: 10177825     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (5)

References (29)
  • 4
    • 0023860332 scopus 로고
    • Detection of prion protein mRNA in normal and scrapie-infected tissues and cell lines
    • Caughey, B., R. E. Race, and B. Chesebro. 1988. Detection of prion protein mRNA in normal and scrapie-infected tissues and cell lines. J. Gen. Virol. 69: 711-716.
    • (1988) J. Gen. Virol. , vol.69 , pp. 711-716
    • Caughey, B.1    Race, R.E.2    Chesebro, B.3
  • 6
    • 0032032312 scopus 로고    scopus 로고
    • Prion protein expression in human leukocyte differentiation
    • Dodelet, V. C. and N. R. Cashman. 1998. Prion protein expression in human leukocyte differentiation. Blood 91: 1556-1561.
    • (1998) Blood , vol.91 , pp. 1556-1561
    • Dodelet, V.C.1    Cashman, N.R.2
  • 7
    • 0031087229 scopus 로고    scopus 로고
    • Characterization of the bovine prion protein gene: The expression requires interaction between the promoter and intron
    • Inoue, S., M. Tanaka, M. Horiuchi, N. Ishiguro, and M. Shinagawa. 1997. Characterization of the bovine prion protein gene: The expression requires interaction between the promoter and intron. J. Vet. Med. Sci. 59: 175-183.
    • (1997) J. Vet. Med. Sci. , vol.59 , pp. 175-183
    • Inoue, S.1    Tanaka, M.2    Horiuchi, M.3    Ishiguro, N.4    Shinagawa, M.5
  • 8
    • 0032802332 scopus 로고    scopus 로고
    • Cellular biology of prion disease
    • Harris, D. A. 1999. Cellular biology of prion disease. Clin. Microbiol. Rev. 12: 429-444.
    • (1999) Clin. Microbiol. Rev. , vol.12 , pp. 429-444
    • Harris, D.A.1
  • 9
    • 0027252644 scopus 로고
    • Location of the mRNA for a chicken prion protein by in situ hybridization
    • Harris, D. A., P. Lele, and W. D. Snider. 1993. Location of the mRNA for a chicken prion protein by in situ hybridization. Proc. Natl. Acad. Sci. USA 90: 4309-4313.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4309-4313
    • Harris, D.A.1    Lele, P.2    Snider, W.D.3
  • 10
    • 0033570204 scopus 로고    scopus 로고
    • Prion protein interconversions and the transmissible spongiform encephalopathies
    • Horiuchi, M. and B. Caughey. 1999. Prion protein interconversions and the transmissible spongiform encephalopathies. Structure 7: R231-R240.
    • (1999) Structure , vol.7
    • Horiuchi, M.1    Caughey, B.2
  • 11
    • 0035091270 scopus 로고    scopus 로고
    • Effects of environmental factors on in vivo folding of Bacillus macerans cyclodextrin glycosyltransferase in recombinant Escherichia coli
    • Jin, H. H., N. S. Han, D. H. Kweon, Y. C. Park, and J. H. Seo. 2001. Effects of environmental factors on in vivo folding of Bacillus macerans cyclodextrin glycosyltransferase in recombinant Escherichia coli. J. Microbiol. Biotechnol. 11: 92-96.
    • (2001) J. Microbiol. Biotechnol. , vol.11 , pp. 92-96
    • Jin, H.H.1    Han, N.S.2    Kweon, D.H.3    Park, Y.C.4    Seo, J.H.5
  • 12
    • 0033757590 scopus 로고    scopus 로고
    • Refolding of Bacillus macernas cyclodextrin glucanotransferase expressed as inclusion bodies in recombinant Escherichia coli
    • Kim, C. I., M. D. Kim, Y. C. Park, N. S. Han, and J. H. Seo. 2000. Refolding of Bacillus macernas cyclodextrin glucanotransferase expressed as inclusion bodies in recombinant Escherichia coli. J. Microbiol. Biotechnol. 10: 632-637.
    • (2000) J. Microbiol. Biotechnol. , vol.10 , pp. 632-637
    • Kim, C.I.1    Kim, M.D.2    Park, Y.C.3    Han, N.S.4    Seo, J.H.5
  • 13
    • 0023001210 scopus 로고
    • Molecular cloning and complete sequence of prion protein cDNA from mouse brain infected with the scrapie agent
    • Locht, C., B. Chesebro, R. Race, and J. M. Keith. 1986. Molecular cloning and complete sequence of prion protein cDNA from mouse brain infected with the scrapie agent. Proc. Natl. Acad. Sci. USA 83: 6372-6376.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6372-6376
    • Locht, C.1    Chesebro, B.2    Race, R.3    Keith, J.M.4
  • 15
    • 0028902465 scopus 로고
    • Developmental expression of the prion protein gene in glial cells
    • Moster, M., R. J. Colello, U. Pott, and B. Oesch. 1995. Developmental expression of the prion protein gene in glial cells. Neuron 14: 509-517.
    • (1995) Neuron , vol.14 , pp. 509-517
    • Moster, M.1    Colello, R.J.2    Pott, U.3    Oesch, B.4
  • 17
    • 0036207353 scopus 로고    scopus 로고
    • Expression and purification of an ACE-inhibitory peptide multimer from synthetic DNA in Escherichia coli
    • Oh, K. S., Y. S. Park, and H. C. Sung. 2002. Expression and purification of an ACE-inhibitory peptide multimer from synthetic DNA in Escherichia coli. J. Microbiol. Biotechnol. 12: 59-64.
    • (2002) J. Microbiol. Biotechnol. , vol.12 , pp. 59-64
    • Oh, K.S.1    Park, Y.S.2    Sung, H.C.3
  • 20
    • 0029914594 scopus 로고    scopus 로고
    • Semipreparative chromatographic method to purify the normal cellular isoform of the prion protein in nondenatured form
    • Pergami, P., H. Jaffe, and J. Safar. 1996. Semipreparative chromatographic method to purify the normal cellular isoform of the prion protein in nondenatured form. Anal. Biochem. 236: 63-73.
    • (1996) Anal. Biochem. , vol.236 , pp. 63-73
    • Pergami, P.1    Jaffe, H.2    Safar, J.3
  • 21
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner, S. B. 1982. Novel proteinaceous infectious particles cause scrapie. Science 216: 136-144.
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 22
    • 0030822582 scopus 로고    scopus 로고
    • Prion disease and the BSE crisis
    • Prusiner, S. B. 1997. Prion disease and the BSE crisis. Science 278: 245-251.
    • (1997) Science , vol.278 , pp. 245-251
    • Prusiner, S.B.1
  • 26
    • 0032518430 scopus 로고    scopus 로고
    • Large-scale production, purification and refolding of the full-length cellular prion protein from Syrian golden hamster in E. coli using the glutathione S-transferase-fusion system
    • Volkel, D., W. Blankenfeldt, and D. Schomburg. 1998. Large-scale production, purification and refolding of the full-length cellular prion protein from Syrian golden hamster in E. coli using the glutathione S-transferase-fusion system. Eur. J. Biochem. 251: 462-471.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 462-471
    • Volkel, D.1    Blankenfeldt, W.2    Schomburg, D.3
  • 27
    • 0030600139 scopus 로고    scopus 로고
    • The ninth data lecture. Molecular biology of transmissible spongiform encephalopathies
    • Weissmann, C. 1996. The ninth data lecture. Molecular biology of transmissible spongiform encephalopathies. FEBS Lett. 389: 3-11.
    • (1996) FEBS Lett. , vol.389 , pp. 3-11
    • Weissmann, C.1
  • 28
    • 0030856847 scopus 로고    scopus 로고
    • Bovine spongiform encephalopathy and early onset variant Creutzfeldt-Jakob disease
    • Weissmann, C. and A. Aguzzi. 1997. Bovine spongiform encephalopathy and early onset variant Creutzfeldt-Jakob disease. Curr. Opin. Neurobiol. 7: 695-700.
    • (1997) Curr. Opin. Neurobiol. , vol.7 , pp. 695-700
    • Weissmann, C.1    Aguzzi, A.2
  • 29


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.