메뉴 건너뛰기




Volumn 30, Issue 6, 2000, Pages 761-768

Anti-malarial effect of histone deacetylation inhibitors and mammalian tumour cytodifferentiating agents

Author keywords

Anti malarial; Histone deacetylation inhibitor; Plasmodium berghei; Plasmodium falciparum; SBHA

Indexed keywords

APICIDIN; CHLOROQUINE; ENZYME INHIBITOR; HISTONE DEACETYLASE; MEFLOQUINE; MW 2996; PYRIMETHAMINE; TRICHOSTATIN A; UNCLASSIFIED DRUG;

EID: 0034192770     PISSN: 00207519     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0020-7519(00)00043-6     Document Type: Article
Times cited : (111)

References (41)
  • 1
    • 10544250252 scopus 로고    scopus 로고
    • Apicidin: A novel antiprotozoal agent that inhibits parasite histone deacetylase
    • Darkin-Rattray S.J., Gurnett A.M., Myers R.W., et al. Apicidin: 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
  • 2
    • 0030915199 scopus 로고    scopus 로고
    • The histones of Plasmodium falciparum: Identification, purification and a possible role in the pathology of malaria
    • Longhurst H.J., Holder A.A. The histones of Plasmodium falciparum: identification, purification and a possible role in the pathology of malaria. Parasitology. 114:1997;413-419.
    • (1997) Parasitology , vol.114 , pp. 413-419
    • Longhurst, H.J.1    Holder, A.A.2
  • 4
    • 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
  • 5
    • 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
  • 6
    • 0027992581 scopus 로고
    • Chromatin structure determines the sites of chromosome breakages in Plasmodium falciparum
    • Lanzer M., Wetheimer S.P., de Bruin D., Ravetch J.V. Chromatin structure determines the sites of chromosome breakages in Plasmodium falciparum. Nucleic. Acids Res. 22:1994;3099-3103.
    • (1994) Nucleic. Acids Res. , vol.22 , pp. 3099-3103
    • Lanzer, M.1    Wetheimer, S.P.2    De Bruin, D.3    Ravetch, J.V.4
  • 7
    • 0028299732 scopus 로고
    • Plasmodium falciparum chromatin: Nucleosomal organisation and histone-like proteins
    • Cary C., Lamont D., Dalton J.P., Doerig C. Plasmodium falciparum chromatin: nucleosomal organisation and histone-like proteins. 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
  • 8
    • 0033525720 scopus 로고    scopus 로고
    • Molecular cloning and nuclear localization of a histone deacetylase homologue in Plasmodium falciparum
    • Joshi M.B., Lin D.T., Chiang P.H., Goldman N.D., et al. Molecular cloning and nuclear localization of a histone deacetylase homologue in Plasmodium falciparum. Mol. Biochem. Parasitol. 99:1999;11-19.
    • (1999) Mol. Biochem. Parasitol. , vol.99 , pp. 11-19
    • Joshi, M.B.1    Lin, D.T.2    Chiang, P.H.3    Goldman, N.D.4
  • 9
    • 0017767153 scopus 로고
    • N-Butyrate causes histone modification in HeLa and Friend erythroleukaemia cells
    • Riggs M.G., Whittaker R.G., Neumann J.R., Ingram V.M. n-Butyrate causes histone modification in HeLa and Friend erythroleukaemia cells. Nature. 268:1977;462-464.
    • (1977) Nature , vol.268 , pp. 462-464
    • Riggs, M.G.1    Whittaker, R.G.2    Neumann, J.R.3    Ingram, V.M.4
  • 10
    • 0024996768 scopus 로고
    • Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A
    • Yoshida M., Kijima M., Akita M., Beppu T. Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A. J. Biol. Chem. 28:1990;17174-17179.
    • (1990) J. Biol. Chem. , vol.28 , pp. 17174-17179
    • Yoshida, M.1    Kijima, M.2    Akita, M.3    Beppu, T.4
  • 11
    • 0016734084 scopus 로고
    • Butyric acid, a potent inducer of erythroid differentiation in cultured erythroleukemic cells
    • Leder A., Leder P. Butyric acid, a potent inducer of erythroid differentiation in cultured erythroleukemic cells. Cell. 5:1975;319-322.
    • (1975) Cell , vol.5 , pp. 319-322
    • Leder, A.1    Leder, P.2
  • 12
    • 0020025385 scopus 로고
    • Effects of sodium butyrate, a new pharmacological agent, on cells in culture
    • Kruh J. Effects of sodium butyrate, a new pharmacological agent, on cells in culture. Mol. Cell Biochem. 42:1982;65-82.
    • (1982) Mol. Cell Biochem. , vol.42 , pp. 65-82
    • Kruh, J.1
  • 13
    • 0023195737 scopus 로고
    • Effects of trichostatins on differentiation of murine erythroleukemia cells
    • Yoshida M., Nomura S., Beppu T. Effects of trichostatins on differentiation of murine erythroleukemia cells. Cancer Res. 47:1987;3688-3691.
    • (1987) Cancer Res. , vol.47 , pp. 3688-3691
    • Yoshida, M.1    Nomura, S.2    Beppu, T.3
  • 14
    • 0025954615 scopus 로고
    • Potent cytodifferentiating agents related to hexamethylenebisacetamide
    • Breslow R., Jursic B., Yan Z.F., et al. Potent cytodifferentiating agents related to hexamethylenebisacetamide. Proc. Natl. Acad. Sci. USA. 88:1991;5542-5546.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5542-5546
    • Breslow, R.1    Jursic, B.2    Yan, Z.F.3
  • 15
    • 0030786371 scopus 로고    scopus 로고
    • Tumor selectivity and transcriptional activation by azeleic bishydroxamic acid in human melanocytic cells
    • Parsons P.G., Hansen C., Fairlie D.P., et al. Tumor selectivity and transcriptional activation by azeleic bishydroxamic acid in human melanocytic cells. Biochem. Pharmacol. 53:1997;1719-1724.
    • (1997) Biochem. Pharmacol. , vol.53 , pp. 1719-1724
    • Parsons, P.G.1    Hansen, C.2    Fairlie, D.P.3
  • 16
    • 0032989027 scopus 로고    scopus 로고
    • Antitumour activity in vitro and in vivo of selective differentiating agents containing hydroxamate
    • in press
    • Qiu L, Kelso MJ, Hansen C, West ML, Fairlie DP, Parsons PG. Antitumour activity in vitro and in vivo of selective differentiating agents containing hydroxamate. Br J Cancer, in press.
    • Br J Cancer
    • Qiu, L.1    Kelso, M.J.2    Hansen, C.3    West, M.L.4    Fairlie, D.P.5    Parsons, P.G.6
  • 17
    • 0032539890 scopus 로고    scopus 로고
    • A class of hybrid polar inducers of transformed cell differentiation inhibits histone deacetylases
    • Richon V.M., Emiliani S., Verdin E., et al. A class of hybrid polar inducers of transformed cell differentiation inhibits histone deacetylases. Proc. Natl. Acad. Sci. USA. 95:1998;3003-3007.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3003-3007
    • Richon, V.M.1    Emiliani, S.2    Verdin, E.3
  • 18
    • 0023277005 scopus 로고
    • Genetic analysis of the human malaria parasite Plasmodium falciparum
    • Walliker D., Quakyi I.A., Wellems T.E., et al. Genetic analysis of the human malaria parasite Plasmodium falciparum. Science. 236:1987;1661-1666.
    • (1987) Science , vol.236 , pp. 1661-1666
    • Walliker, D.1    Quakyi, I.A.2    Wellems, T.E.3
  • 20
    • 13144250200 scopus 로고    scopus 로고
    • Molecular analysis of recrudescent parasites in a Plasmodium falciparum drug efficacy trial in Gabon
    • Ranford-Cartwright L.C., Taylor J., Umasunthar T., et al. Molecular analysis of recrudescent parasites in a Plasmodium falciparum drug efficacy trial in Gabon. Trans. R. Soc. Trop. Med. Hyg. 91:1997;719-724.
    • (1997) Trans. R. Soc. Trop. Med. Hyg. , vol.91 , pp. 719-724
    • Ranford-Cartwright, L.C.1    Taylor, J.2    Umasunthar, T.3
  • 21
  • 22
    • 0017311840 scopus 로고
    • Human malaria parasites in continuous culture
    • Trager W., Jensen J.B. Human malaria parasites in continuous culture. Science. 193:1976;673-675.
    • (1976) Science , vol.193 , pp. 673-675
    • Trager, W.1    Jensen, J.B.2
  • 25
    • 0027474443 scopus 로고
    • Derivation of highly mefloquine-resistant lines from Plasmodium falciparum in vitro
    • Peel S.A., Merritt S.C., Hendy J., Baric R.S. Derivation of highly mefloquine-resistant lines from Plasmodium falciparum in vitro. Am. J. Trop. Med. Hyg. 48:1993;385-397.
    • (1993) Am. J. Trop. Med. Hyg. , vol.48 , pp. 385-397
    • Peel, S.A.1    Merritt, S.C.2    Hendy, J.3    Baric, R.S.4
  • 26
    • 0025266610 scopus 로고
    • Alternative chromatin structure of CpG islands
    • Tazi J., Bird A. Alternative chromatin structure of CpG islands. Cell. 60:1990;909-920.
    • (1990) Cell , vol.60 , pp. 909-920
    • Tazi, J.1    Bird, A.2
  • 27
    • 0027183088 scopus 로고
    • The inactive X chromosome in female mammals is distinguished by a lack of histone H4 acetylation, a cytogenetic marker for gene expression
    • Jeppesen P., Turner B.M. The inactive X chromosome in female mammals is distinguished by a lack of histone H4 acetylation, a cytogenetic marker for gene expression. Cell. 74:1993;281-289.
    • (1993) Cell , vol.74 , pp. 281-289
    • Jeppesen, P.1    Turner, B.M.2
  • 28
    • 0029119093 scopus 로고
    • Histone H4 acetylation distinguishes coding regions of the human genome from heterochromatin in a differentiation-dependent but transcription-independent manner
    • O'Neill L.P., Turner B.M. Histone H4 acetylation distinguishes coding regions of the human genome from heterochromatin in a differentiation-dependent but transcription-independent manner. EMBO J. 14:1995;3946-3957.
    • (1995) EMBO J. , vol.14 , pp. 3946-3957
    • O'Neill, L.P.1    Turner, B.M.2
  • 30
    • 0030451463 scopus 로고    scopus 로고
    • Reduced levels of histone H3 acetylation on the inactive X chromosome in human females
    • Boggs B.A., Connors B., Sobel R.E., Chinault A.C., Allis C.D. Reduced levels of histone H3 acetylation on the inactive X chromosome in human females. Chromosoma. 105:1996;303-309.
    • (1996) Chromosoma , vol.105 , pp. 303-309
    • Boggs, B.A.1    Connors, B.2    Sobel, R.E.3    Chinault, A.C.4    Allis, C.D.5
  • 31
    • 0028106737 scopus 로고
    • Dependence of transcriptional repression on CpG methylation density
    • Hsieh C.-L. Dependence of transcriptional repression on CpG methylation density. Mol. Cell. Biol. 14:1994;5487-5494.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5487-5494
    • Hsieh, C.-L.1
  • 32
    • 0032482974 scopus 로고    scopus 로고
    • Trichostatin A causes selective loss of DNA methylation in Neurospora
    • Selker E.U. Trichostatin A causes selective loss of DNA methylation in Neurospora. Proc. Natl. Acad. Sci. USA. 95:1998;9430-9435.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9430-9435
    • Selker, E.U.1
  • 33
    • 0032574977 scopus 로고    scopus 로고
    • Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex
    • Nan X., Ng H.H., Johnson C.A., et al. Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex. Nature. 393:1998;386-389.
    • (1998) Nature , vol.393 , pp. 386-389
    • Nan, X.1    Ng, H.H.2    Johnson, C.A.3
  • 34
    • 0030799238 scopus 로고    scopus 로고
    • Epigenetic silencing of RNA polymerase I transcription: A role for DNA methylation and histone modification in nucleolar dominance
    • Chen Z.J., Pikaard C.S. Epigenetic silencing of RNA polymerase I transcription: a role for DNA methylation and histone modification in nucleolar dominance. Genes Dev. 11:1997;2124-2136.
    • (1997) Genes Dev. , vol.11 , pp. 2124-2136
    • Chen, Z.J.1    Pikaard, C.S.2
  • 35
    • 0017891669 scopus 로고
    • Antimalarial activity of S-isobutyl adenosine against Plasmodium falciparum in culture
    • Trager W., Robert-Gero M., Lederer E. Antimalarial activity of S-isobutyl adenosine against Plasmodium falciparum in culture. FEBS Lett. 85:1978;264-266.
    • (1978) FEBS Lett. , vol.85 , pp. 264-266
    • Trager, W.1    Robert-Gero, M.2    Lederer, E.3
  • 36
    • 0018935181 scopus 로고
    • Plasmodium falciparum: Antimalarial activity in culture of sinefungin and other methylation inhibitions
    • Trager W., Tershakovec M., Chiang P.K., Cantoni G.L. Plasmodium falciparum: Antimalarial activity in culture of sinefungin and other methylation inhibitions. Exp. Parasitol. 50:1980;83-89.
    • (1980) Exp. Parasitol. , vol.50 , pp. 83-89
    • Trager, W.1    Tershakovec, M.2    Chiang, P.K.3    Cantoni, G.L.4
  • 37
    • 0022658458 scopus 로고
    • Antimalarial activity of Neoplanocin A with perturbations in the metabolism of purines, polyamines and S-adenosylmethionine
    • Whaun J.M., Miura G.A., Brown N.D., Gordon R.K., Chiang P.K. Antimalarial activity of Neoplanocin A with perturbations in the metabolism of purines, polyamines and S-adenosylmethionine. J. Pharmacol. Exp. Ther. 236:1986;277-283.
    • (1986) J. Pharmacol. Exp. Ther. , vol.236 , pp. 277-283
    • Whaun, J.M.1    Miura, G.A.2    Brown, N.D.3    Gordon, R.K.4    Chiang, P.K.5
  • 38
    • 0021119651 scopus 로고
    • Effects of two methylioadenosine analogues, SIBA and deaza-SIBA, on P. falciparum-infected red cells
    • Whaun J.M., Brown N.D., Chiang P.K. Effects of two methylioadenosine analogues, SIBA and deaza-SIBA, on P. falciparum-infected red cells. Prog. Clin. Biol. Res. 155:1984;143-157.
    • (1984) Prog. Clin. Biol. Res. , vol.155 , pp. 143-157
    • Whaun, J.M.1    Brown, N.D.2    Chiang, P.K.3
  • 39
    • 0029145415 scopus 로고
    • Hypermodified bases in DNA
    • Gommers-Ampt J.H., Borst P. Hypermodified bases in DNA. FASEB J. 9:1995;1034-1042.
    • (1995) FASEB J. , vol.9 , pp. 1034-1042
    • Gommers-Ampt, J.H.1    Borst, P.2
  • 40
    • 0025729938 scopus 로고
    • A novel DNA nucleotide in Trypanosoma brucei only present in the mammalian phase of the life-cycle
    • Gommers-Ampt J., Lutgerink J., Borst P. A novel DNA nucleotide in Trypanosoma brucei only present in the mammalian phase of the life-cycle. Nucl. Acids Res. 19:1991;1745-1751.
    • (1991) Nucl. Acids Res. , vol.19 , pp. 1745-1751
    • Gommers-Ampt, J.1    Lutgerink, J.2    Borst, P.3
  • 41
    • 0027333558 scopus 로고
    • β-D-glucosyl-hydroxymethyluracil: A novel modified base present in the DNA of the parasitic protozoan T. brucei
    • Gommers-Ampt J.H., ven Leeuwen A.L., de Beer A.L., et al. β-D-glucosyl-hydroxymethyluracil: A novel modified base present in the DNA of the parasitic protozoan T. brucei. Cell. 75:1993;1129-1136.
    • (1993) Cell , vol.75 , pp. 1129-1136
    • Gommers-Ampt, J.H.1    Ven Leeuwen, A.L.2    De Beer, A.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.