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Volumn 99, Issue 1, 1999, Pages 11-19

Molecular cloning and nuclear localization of a histone deacetylase homologue in Plasmodium falciparum

Author keywords

Histone deacetylase; Nuclear protein; Plasmodium falciparum; Transcription regulation

Indexed keywords

COMPLEMENTARY DNA; HISTONE DEACETYLASE; MESSENGER RNA;

EID: 0033525720     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(98)00177-7     Document Type: Article
Times cited : (74)

References (23)
  • 1
    • 1842411320 scopus 로고    scopus 로고
    • X-ray structure of the nucleosome core particle at 2.8 A resolution
    • Luger K., Maeder A.W., Richmond R.K., Sargent D.F., Richmond T.J. X-ray structure of the nucleosome core particle at 2.8 A resolution. Nature. 389:1997;251-259.
    • (1997) Nature , vol.389 , pp. 251-259
    • Luger, K.1    Maeder, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 2
    • 0026441880 scopus 로고
    • Reversible histone modifications and chromosome cell cycle
    • Bradbury E.M. Reversible histone modifications and chromosome cell cycle. BioEssays. 14:1992;9-16.
    • (1992) BioEssays , vol.14 , pp. 9-16
    • Bradbury, E.M.1
  • 5
    • 0030961614 scopus 로고    scopus 로고
    • Histone acetyltransferases in control
    • Wade P.A., Wolffe A.P. Histone acetyltransferases in control. Curr. Biol. 7:1997;82-84.
    • (1997) Curr. Biol. , vol.7 , pp. 82-84
    • Wade, P.A.1    Wolffe, A.P.2
  • 6
    • 0030916336 scopus 로고    scopus 로고
    • What's up and down with histone deacetylation and transcription
    • Pazin M.J., Kadonaga J.T. What's up and down with histone deacetylation and transcription. Cell. 89:1997;325-328.
    • (1997) Cell , vol.89 , pp. 325-328
    • Pazin, M.J.1    Kadonaga, J.T.2
  • 7
    • 10544250252 scopus 로고    scopus 로고
    • Apicidine: A novel antiprotozoal agent that inhibits parasite histone deacetylase
    • Darkin-Rattray S.J., Gurnett A.M., Myers R.W. et al. Apicidine: a novel antiprotozoal agent that inhibits parasite histone deacetylase. Proc Natl Acad Sci USA. 93:1996;13143-13147.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13143-13147
    • Darkin-Rattray, S.J.1    Gurnett, A.M.2    Myers, R.W.3
  • 8
    • 0019276533 scopus 로고
    • Nucleosomal organization of chromatin in Plasmodium knowlesi
    • Wunderlich F., Falk H., Konig E. Nucleosomal organization of chromatin in Plasmodium knowlesi. J Parasitol. 66:1980;1063-1065.
    • (1980) J Parasitol , vol.66 , pp. 1063-1065
    • Wunderlich, F.1    Falk, H.2    Konig, E.3
  • 9
    • 0028299732 scopus 로고
    • Plasmodium falciparum chromatin: Nucleosomal orgnisation and histone-like protein
    • Cary C., Lamont D., Dalton J.P., Doerig C. Plasmodium falciparum chromatin: nucleosomal orgnisation and histone-like protein. Parasitol Res. 80:1994;255-258.
    • (1994) Parasitol Res , vol.80 , pp. 255-258
    • Cary, C.1    Lamont, D.2    Dalton, J.P.3    Doerig, C.4
  • 11
    • 0028908412 scopus 로고
    • Identification of Plasmodium falciparum histone 2B and histone 3 genes
    • Bennett B.J., Thompson J., Coppel R.L. Identification of Plasmodium falciparum histone 2B and histone 3 genes. Mol Biochem Parasitol. 70:1995;231-233.
    • (1995) Mol Biochem Parasitol , vol.70 , pp. 231-233
    • Bennett, B.J.1    Thompson, J.2    Coppel, R.L.3
  • 12
    • 0028983365 scopus 로고
    • The sequence of Plasmodium falciparum histone H3
    • Longhurst H.J., Holder A.A. The sequence of Plasmodium falciparum histone H3. Mol Biochem Parasitol. 69:1995;111-113.
    • (1995) Mol Biochem Parasitol , vol.69 , pp. 111-113
    • Longhurst, H.J.1    Holder, A.A.2
  • 13
    • 0029943490 scopus 로고    scopus 로고
    • Stage-specific expression of Plasmodium falciparum protein related to the eykaryotic mitogen-activated protein kinases
    • Lin D.T., Goldman N.D., Syin C. Stage-specific expression of Plasmodium falciparum protein related to the eykaryotic mitogen-activated protein kinases. Mol Biochem Parasitol. 78:1996;67-77.
    • (1996) Mol Biochem Parasitol , vol.78 , pp. 67-77
    • Lin, D.T.1    Goldman, N.D.2    Syin, C.3
  • 14
    • 0029932598 scopus 로고    scopus 로고
    • A mammalian histone deacetylase related to the yeast transcriptional regulator RPD3p
    • Taunton J., Hassig C.A., Schreiber S.L. A mammalian histone deacetylase related to the yeast transcriptional regulator RPD3p. Science. 272:1996;408-411.
    • (1996) Science , vol.272 , pp. 408-411
    • Taunton, J.1    Hassig, C.A.2    Schreiber, S.L.3
  • 16
    • 0025743647 scopus 로고
    • Induction and localization of Plasmodium falciparum stress proteins related to the heat shock protein 70 family
    • Kumar N., Koski G., Masakadu H., Aikawa M., Hong Z. Induction and localization of Plasmodium falciparum stress proteins related to the heat shock protein 70 family. Mol Biochem Parasitol. 48:1991;47-58.
    • (1991) Mol Biochem Parasitol , vol.48 , pp. 47-58
    • Kumar, N.1    Koski, G.2    Masakadu, H.3    Aikawa, M.4    Hong, Z.5
  • 17
    • 0025214509 scopus 로고
    • Immunoelectron microscopy of parasites
    • Aikawa M., Atkinson C.T. Immunoelectron microscopy of parasites. Adv Parasitol. 29:1990;151-214.
    • (1990) Adv Parasitol , vol.29 , pp. 151-214
    • Aikawa, M.1    Atkinson, C.T.2
  • 18
    • 0026060619 scopus 로고
    • RPD3 encodes a second factor required to achieve maximum positive and negative transcriptional states in Saccharomyces cerevisiae
    • Vidal M., Gaber R.F. RPD3 encodes a second factor required to achieve maximum positive and negative transcriptional states in Saccharomyces cerevisiae. Mol Cell Biol. 11:1991;6317-6327.
    • (1991) Mol Cell Biol , vol.11 , pp. 6317-6327
    • Vidal, M.1    Gaber, R.F.2
  • 19
    • 0023690466 scopus 로고
    • Molecular biology of malaria parasites
    • Webber J.L. Molecular biology of malaria parasites. Exp Parasitol. 66:1988;143-170.
    • (1988) Exp Parasitol , vol.66 , pp. 143-170
    • Webber, J.L.1
  • 20
    • 0030812917 scopus 로고    scopus 로고
    • Histone deacetylase, acetoin utilization proteins and acetylpolyamine amidohydrolases are members of an ancient protein superfamily
    • Leipe D.D., Landsman D. Histone deacetylase, acetoin utilization proteins and acetylpolyamine amidohydrolases are members of an ancient protein superfamily. Nucleic Acids Res. 25:1997;3693-3697.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3693-3697
    • Leipe, D.D.1    Landsman, D.2
  • 21
    • 0031434997 scopus 로고    scopus 로고
    • The origin and utility of histone deacetylases
    • Khochbin S., Wolffe A.P. The origin and utility of histone deacetylases. FEBS Letts. 419:1997;157-160.
    • (1997) FEBS Letts. , vol.419 , pp. 157-160
    • Khochbin, S.1    Wolffe, A.P.2
  • 22
    • 0032584224 scopus 로고    scopus 로고
    • A role for histone deacetylase activity in HDAC1-mediated transcriptional repression
    • Hassig C.A., Tong J.K., Fleischer T.C. et al. A role for histone deacetylase activity in HDAC1-mediated transcriptional repression. Proc Natl Acad Sci USA. 95:1998;3519-3524.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3519-3524
    • Hassig, C.A.1    Tong, J.K.2    Fleischer, T.C.3
  • 23
    • 0001756213 scopus 로고    scopus 로고
    • Second family of histone deacetylases
    • Aravind L., Koonin E.V. Second family of histone deacetylases. Science. 280:1998;1167a-1167.
    • (1998) Science , vol.280
    • Aravind, L.1    Koonin, E.V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.