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Volumn 10, Issue 4-5, 1999, Pages 339-342

Sequence of the gene encoding hsp90e from Cryptosporidium parvum

Author keywords

Apicomplexa; coccidia; Cryptosporidium parvum; hsp90

Indexed keywords

AMINO ACID SEQUENCE; CDNA LIBRARY; GENOME LIBRARY; HEAT SHOCK; MOLECULAR SIZE; NUCLEOTIDE SEQUENCE; OPEN READING FRAME; RESTRICTION MAPPING; SEQUENCE HOMOLOGY;

EID: 0033491332     PISSN: 19401736     EISSN: 19401744     Source Type: Journal    
DOI: 10.3109/10425179909033961     Document Type: Article
Times cited : (6)

References (18)
  • 1
    • 0029737509 scopus 로고
    • Mutant conformation of p53 translated in vitro and in vivo requires functional hsp90
    • Blagosklonny M. V., Toretsky J., Bohen S. and Neckers L. (1988). Mutant conformation of p53 translated in vitro and in vivo requires functional hsp90. Proc. Natl. Acad. Sci. 93, 8379-8383.
    • (1988) Proc. Natl. Acad. Sci. , vol.93 , pp. 8379-8383
    • Blagosklonny, M.V.1    Toretsky, J.2    Bohen, S.3    Neckers, L.4
  • 2
    • 0030605255 scopus 로고    scopus 로고
    • Sequence of the parasitic protozoan, Cryptosporidium parvum, putative protein disulfide isomerase-encoding DNA
    • DOI 10.1016/S0378-1119(96)00460-X, PII S037811199600460X
    • Blunt D. S., Montelone B. A., Upton S. J. and Khramtsov N. V. (1996). Sequence of the parasitic protozoan, Cryptosporidium parvum, putative protein disulfide isomerase-encoding DNA. Gene 181, 221-223. (Pubitemid 26418274)
    • (1996) Gene , vol.181 , Issue.1-2 , pp. 221-223
    • Blunt, D.S.1    Montelone, B.A.2    Upton, S.J.3    Khramtsov, N.V.4
  • 3
    • 0027300506 scopus 로고
    • Heat shock proteins: Molecular chaperones of protein biogenesis
    • Craig E. A., Gambill B. D. and Nelson R. J. (1993). Heat shock proteins: molecular chaperones of protein biogenesis. Microbiol. Rev. 57, 402-414. (Pubitemid 23170099)
    • (1993) Microbiological Reviews , vol.57 , Issue.2 , pp. 402-414
    • Craig, E.A.1    Gambill, B.D.2    Nelson, R.J.3
  • 4
    • 0030808079 scopus 로고    scopus 로고
    • Geldanamycin, a heat shock protein 90-binding benzoquinone ansamycin, inhibits steroid-dependent translocation of the glucocorticoid receptor from the cytoplasm to the nucleus
    • DOI 10.1021/bi970648x
    • Czar M. J., Galigiana M. D., Silverstein A. M. and Pratt W. B. (1997). Geldanamycin, a heat shock protein-binding benzoquinone ansamycin, inhibits steroid-dependent translocation of the glucocorticoid receptor from the cytoplasm to the nucleus, Biochemistry 36, 7776-7785. (Pubitemid 27287189)
    • (1997) Biochemistry , vol.36 , Issue.25 , pp. 7776-7785
    • Czar, M.J.1    Galigniana, M.D.2    Silverstein, A.M.3    Pratt, W.B.4
  • 5
    • 0028785298 scopus 로고
    • Phylogenic analysis of the 90 kD heat shock family of protein sequences and an examination of the relationship among animals, plants, and fungi species
    • Gupta R. S. (1995). Phylogenic analysis of the 90 kD heat shock family of protein sequences and an examination of the relationship among animals, plants, and fungi species. Mol. Biol. Evol. 12, 1063-1073.
    • (1995) Mol. Biol. Evol. , vol.12 , pp. 1063-1073
    • Gupta, R.S.1
  • 6
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • DOI 10.1038/381571a0
    • Hartl F. U. (1996). Molecular chaperones in cellular protein function. Nature 381, 571-580. (Pubitemid 26177472)
    • (1996) Nature , vol.381 , Issue.6583 , pp. 571-580
    • Hartl, F.U.1
  • 7
    • 0028023828 scopus 로고
    • Association of Hsp90 with cellular Src-family kinases in a cell-free system correlates with altered kinase structure and function
    • DOI 10.1021/bi00196a008
    • Hartson S. D. and Marts R. L. (1994). Association of hsp90 with cellular src-family kinases in a cell free system correlates with altered kinase structure and function. Biochemistry 33, 8912-8920. (Pubitemid 24257999)
    • (1994) Biochemistry , vol.33 , Issue.30 , pp. 8912-8920
    • Hartson, S.D.1    Matts, R.L.2
  • 8
    • 0029796733 scopus 로고    scopus 로고
    • Hsp90-mediated folding of the lymphoid cell kinase p561ck
    • Hartson S. D., Barrett D. J., Burn P. and Matts R. L. (1996). Hsp90-mediated folding of the lymphoid cell kinase p561ck. Biochemistry 35, 3451-13459.
    • (1996) Biochemistry , vol.35 , pp. 3451-13459
    • Hartson, S.D.1    Barrett, D.J.2    Burn, P.3    Matts, R.L.4
  • 9
    • 0024364170 scopus 로고
    • Sequence and regulation of a gene encoding a human 89-kilodalton heat shock protein
    • Hickey E., Brandon S. E., Smale G., Lloyd D. and Weber L. A. (1989). Sequence and regulation of a gene encoding a human 89-kilodalton heat shock protein. Mol. Cell. Biol. 9, 2615-2626. (Pubitemid 19148137)
    • (1989) Molecular and Cellular Biology , vol.9 , Issue.6 , pp. 2615-2626
    • Hickey, E.1    Brandon, S.E.2    Smale, G.3    Lloyd, D.4    Weber, L.A.5
  • 10
    • 0028940309 scopus 로고
    • Transient interaction of hsp90 with early unfolding intermediates of citrate synthase
    • Jakob U., Lilie H, Meyer I. and Buchner J. (1995). Transient interaction of hsp90 with early unfolding intermediates of citrate synthase. J. Biol. Chem. 270, 7288-7294.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7288-7294
    • Jakob, U.1    Lilie, H.2    Meyer, I.3    Buchner, J.4
  • 11
    • 0029328623 scopus 로고
    • Cloning and analysis of a Cryptosporidium parvum gene encoding a protein with homology to cytoplasmic form hsp70
    • Khramtsov N. V., Tilley M., Blunt D. S., Montelone B. A. and Upton S. J. (1995). Cloning and analysis of a Cryptosporidium parvum gene encoding a protein with homology to cytoplasmic form hsp70. J. Euk. Microbiol. 42, 416-422.
    • (1995) J. Euk. Microbiol. , vol.42 , pp. 416-422
    • Khramtsov, N.V.1    Tilley, M.2    Blunt, D.S.3    Montelone, B.A.4    Upton, S.J.5
  • 12
    • 0029037110 scopus 로고
    • Mutational analysis of the hsp90 function: Interactions with a steroid receptor and a protein kinase
    • Nathan D. F. and Lindquist S. (1995) Mutational analysis of the hsp90 function: interactions with a steroid receptor and a protein kinase. Mol. Cell. Biol. 15, 3917-3925.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3917-3925
    • Nathan, D.F.1    Lindquist, S.2
  • 13
    • 0023988955 scopus 로고
    • Evidence that luminal ER proteins are sorted from secreted proteins in a post-ER compartment
    • Pelham H. R. (1988). Evidence that luminal ER proteins are sorted from secreted proteins in a post-ER compartment. EMBO J. 7, 913-918.
    • (1988) EMBO J. , vol.7 , pp. 913-918
    • Pelham, H.R.1
  • 14
    • 0030810984 scopus 로고    scopus 로고
    • The function of steroid hormone receptors is inhibited by the hsp90- specific compound geldanamycin
    • DOI 10.1074/jbc.272.30.18694
    • Segnitz B. and Gehring U. (1997). The function of steroid hormone receptors is inhibited by the hsp90-specific compound geldanamycin. J. Biol. Chem. 272, 18694-18701. (Pubitemid 27318213)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.30 , pp. 18694-18701
    • Segnitz, B.1    Gehring, U.2
  • 16
    • 0030448228 scopus 로고    scopus 로고
    • Cooperative action of Hsp70, Hsp90, and DnaJ proteins in protein renaturation
    • DOI 10.1021/bi961825h
    • Schumacher R. J., Hansen W. J., Freeman B. C., Alnemri E., Litwack G. and Toft D. O. (1996). Cooperative action of hsp 70, hsp90, and DnaJ proteins in protein renaturation. Biochemistry 35, 14889-14898. (Pubitemid 26423824)
    • (1996) Biochemistry , vol.35 , Issue.47 , pp. 14889-14898
    • Schumacher, R.J.1    Hansen, W.J.2    Freeman, B.C.3    Alnemri, E.4    Litwack, G.5    Toft, D.O.6
  • 18
    • 0030046766 scopus 로고    scopus 로고
    • Assessment of glucocorticoid receptor-heat shock protein 90 interactions in vivo during nucleocytoplasmic trafficking
    • DOI 10.1210/me.10.1.3
    • Yang J. and DeFranco D. B. (1996) Assessment of glucocorticoid receptor-heat shock protein 90 interactions in vivo during nucleocytoplasmic trafficking. Mol. Endocrinol. 10, 3-13. (Pubitemid 26023769)
    • (1996) Molecular Endocrinology , vol.10 , Issue.1 , pp. 3-13
    • Yang, J.1    DeFranco, D.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.