메뉴 건너뛰기




Volumn 30, Issue 4, 2010, Pages 585-602

Strategies in developing promising histone deacetylase inhibitors

Author keywords

Computational techniques; Histone deacetylase inhibitors; Natural products; Probes; Selectivity

Indexed keywords

APICIDIN; HC TOXIN; HISTONE DEACETYLASE; HISTONE DEACETYLASE INHIBITOR; INDOLE AMIDE DERIVATIVE; LARGAZOLE; MS 257; N (2 AMINOPHENYL) 4 [4 (3 PYRIDINYL) 2 PYRIMIDINYLAMINOMETHYL]BENZAMIDE; PSAMMAPLIN A; ROMIDEPSIN; TRAPOXIN; TRICHOSTATIN A; TUBACIN; UNCLASSIFIED DRUG; VORINOSTAT; BIOLOGICAL PRODUCT; MOLECULAR PROBE;

EID: 77955480670     PISSN: 01986325     EISSN: 10981128     Source Type: Journal    
DOI: 10.1002/med.20169     Document Type: Review
Times cited : (38)

References (107)
  • 1
    • 0030812917 scopus 로고    scopus 로고
    • Histone deacetylases, acetoin utilization proteins and acetylpolyamine amidohydrolases are members of an ancient protein superfamily
    • DOI 10.1093/nar/25.18.3693
    • Leipe DD, Landsman D. Histone deacetylases, acetoin utilization proteins and acetylpolyamine amidohydrolases are members of an ancient protein superfamily. Nucleic Acids Res 1997;25: 3693-3697. (Pubitemid 27390190)
    • (1997) Nucleic Acids Research , vol.25 , Issue.18 , pp. 3693-3697
    • Leipe, D.D.1    Landsman, D.2
  • 3
    • 1842578986 scopus 로고    scopus 로고
    • Molecular evolution of the histone deacetylase family: Functional implications of phylogenetic analysis
    • Gregoretti IV, Lee YM, Goodson HV. Molecular evolution of the histone deacetylase family: Functional implications of phylogenetic analysis. J Mol Biol 2004;338:17-31.
    • (2004) J Mol Biol , vol.338 , pp. 17-31
    • Gregoretti, I.V.1    Lee, Y.M.2    Goodson, H.V.3
  • 4
    • 30344477367 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
    • DOI 10.1038/nrc1779
    • Minucci S, Pelicci PG. Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer. Nat Rev Cancer 2006;6:38-51. (Pubitemid 43054973)
    • (2006) Nature Reviews Cancer , vol.6 , Issue.1 , pp. 38-51
    • Minucci, S.1    Pelicci, P.G.2
  • 6
  • 7
    • 0032814843 scopus 로고    scopus 로고
    • A general requirement for the Sin3-Rpd3 histone deacetylase complex in regulating silencing in Saccharomyces cerevisiae
    • Sun ZW, Hampsey M. A general requirement for the Sin3-Rpd3 histone deacetylase complex in regulating silencing in Saccharomyces cerevisiae. Genetics 1999;152:921-932. (Pubitemid 29330893)
    • (1999) Genetics , vol.152 , Issue.3 , pp. 921-932
    • Sun, Z.-W.1    Hampsey, M.2
  • 8
    • 33745835064 scopus 로고    scopus 로고
    • Dissecting the biological functions of Drosophila histone deacetylases by RNA interference and transcriptional profiling
    • DOI 10.1074/jbc.M511945200
    • Foglietti C, Filocamo G, de Rinaldis E, Lahm A, Cortese R, Steinkuhler C. Dissecting the biological functions of drosophila histone deacetylases by RNA interference and transcriptional profiling. J Biol Chem 2006;281:17968-17976. (Pubitemid 44035596)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.26 , pp. 17968-17976
    • Foglietti, C.1    Filocamo, G.2    Cundari, E.3    De Rinaldis, E.4    Lahm, A.5    Cortese, R.6    Steinkuhler, C.7
  • 10
    • 33750324764 scopus 로고    scopus 로고
    • Negative and positive regulation of gene expression by mouse histone deacetylase 1
    • Zupkovitz G, Tishler J, Posch M, Sadzak IS, Decker T, Seiser C. Negative and positive regulation of gene expression by mouse histone deacetylase 1. Mol Cell Biol 2006;26: 7913-7918.
    • (2006) Mol Cell Biol , vol.26 , pp. 7913-7918
    • Zupkovitz, G.1    Tishler, J.2    Posch, M.3    Sadzak, I.S.4    Decker, T.5    Seiser, C.6
  • 13
    • 26844518082 scopus 로고    scopus 로고
    • Intracellular trafficking of histone deacetylase 4 regulates neuronal cell death
    • DOI 10.1523/JNEUROSCI.1826-05.2005
    • Bolger TA, Yao TP. Intracellular trafficking of histone deacetylase 4 regulates neuronal cell death. J Neurosci 2005;25:9544-9553. (Pubitemid 41464769)
    • (2005) Journal of Neuroscience , vol.25 , Issue.41 , pp. 9544-9553
    • Bolger, T.A.1    Yao, T.-P.2
  • 14
    • 0037162697 scopus 로고    scopus 로고
    • Class II histone deacetylases act as signal-responsive repressors of cardiac hypertrophy
    • DOI 10.1016/S0092-8674(02)00861-9
    • Zhang CL, McKinsey TA, Chang S, Antos JA, Olson EN. Class II histone deacetylases act as signal-responsive repressors of cardiac hypertrophy. Cell 2002;110:479-488. (Pubitemid 35232291)
    • (2002) Cell , vol.110 , Issue.4 , pp. 479-488
    • Zhang, C.L.1    McKinsey, T.A.2    Chang, S.3    Antos, C.L.4    Hill, J.A.5    Olson, E.N.6
  • 15
    • 4544358659 scopus 로고    scopus 로고
    • Histone deacetylases 5 and 9 govern responsiveness of the heart to a subset of stress signals and play redundant roles in heart development
    • DOI 10.1128/MCB.24.19.8467-8476.2004
    • Chang S, McKinsey TA, Zhang CL, Richardson JA, Hill JA, Olson EN. Histone deacetylases 5 and 9 govern responsiveness of the heart to a subset of stress signals and play redundant roles in heart development. Mol Cell Biol 2004;24:8467-8476. (Pubitemid 39245069)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.19 , pp. 8467-8476
    • Chang, S.1    McKinsey, T.A.2    Zhang, C.L.3    Richardson, J.A.4    Hill, J.A.5    Olson, E.N.6
  • 16
    • 0037728615 scopus 로고    scopus 로고
    • HDAC7, a thymus-specific class II histone deacetylase, regulates Nur77 transcription and TCR-mediated apoptosis
    • DOI 10.1016/S1074-7613(03)00109-2
    • Dequiedt F, Kasler H, Fischle W, Kiermer V, Weinstein M, Herndier BG, Verdin E. HDAC7, a thymus-specific class ii histone deacetylase, regulates Nur77 transcription and TCR-mediated apoptosis. Immunity 2003;18:687-698. (Pubitemid 36588585)
    • (2003) Immunity , vol.18 , Issue.5 , pp. 687-698
    • Dequiedt, F.1    Kasler, H.2    Fischle, W.3    Kiermer, V.4    Weinstein, M.5    Herndier, B.G.6    Verdin, E.7
  • 17
    • 0037416151 scopus 로고    scopus 로고
    • HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo
    • DOI 10.1093/emboj/cdg115
    • Zhang Y, Li N, Caron C, Matthias G, Hess D, Khochbin S, Matthias P. HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo. EMBO J 2003;22:1168-1179. (Pubitemid 36313600)
    • (2003) EMBO Journal , vol.22 , Issue.5 , pp. 1168-1179
    • Zhang, Y.1    Li, N.2    Caron, C.3    Matthias, G.4    Hess, D.5    Khochbin, S.6    Matthias, P.7
  • 21
    • 0036898253 scopus 로고    scopus 로고
    • Acetylation inactivates the transcriptional repressor BCL6
    • DOI 10.1038/ng1018
    • Bereshchenko OR, Gu W, Dalla-Favera R. Acetylation inactivates the transcriptional repressor BCL6. Nat Genet 2002;32:606-613. (Pubitemid 35435172)
    • (2002) Nature Genetics , vol.32 , Issue.4 , pp. 606-613
    • Bereshchenko, O.R.1    Gu, W.2    Dalla-Favera, R.3
  • 22
    • 30544445468 scopus 로고    scopus 로고
    • Sirt1 inhibitor, Sirtinol, induces senescence-like growth arrest with attenuated RasÂ-MAPK signaling in human cancer cells
    • Ota H, Tokunaga E, Chang K, Hikasa M, Iijima K, Eto M, Kozaki K, Akishita M, Ouchi Y, Kaneki M. Sirt1 inhibitor, Sirtinol, induces senescence-like growth arrest with attenuated RasÂ-MAPK signaling in human cancer cells. Oncogene 2006;25:176-185.
    • (2006) Oncogene , vol.25 , pp. 176-185
    • Ota, H.1    Tokunaga, E.2    Chang, K.3    Hikasa, M.4    Iijima, K.5    Eto, M.6    Kozaki, K.7    Akishita, M.8    Ouchi, Y.9    Kaneki, M.10
  • 25
    • 50249091120 scopus 로고    scopus 로고
    • Chemical regulation of epigenetic modifications: Opportunities for new cancer therapy
    • Zheng YG, Wu J, Chen Z, Goodman M. Chemical regulation of epigenetic modifications: Opportunities for new cancer therapy. Med Res Rev 2008;28:645-687.
    • (2008) Med Res Rev , vol.28 , pp. 645-687
    • Zheng, Y.G.1    Wu, J.2    Chen, Z.3    Goodman, M.4
  • 26
    • 42049096372 scopus 로고    scopus 로고
    • Chemical origins of isoform selectivity in histone deacetylase inhibitors
    • DOI 10.2174/138161208783885353
    • Butler KV, Kozikowski AP. Chemical origins of isoform selectivity in histone deacetylase inhibitors. Curr Pharm Des 2008;14:505-528. (Pubitemid 351516876)
    • (2008) Current Pharmaceutical Design , vol.14 , Issue.6 , pp. 505-528
    • Butler, K.V.1    Kozikowski, A.P.2
  • 27
    • 42049103914 scopus 로고    scopus 로고
    • From natural products to small molecule ketone histone deacetylase inhibitors: Development of new class specific agents
    • DOI 10.2174/138161208783885317
    • Jones P, Steinkuhler C. From natural products to small molecule ketone histone deacetylase inhibitors: Development of new class specific agents. Curr Pharm Des 2008;14:545-561. (Pubitemid 351516878)
    • (2008) Current Pharmaceutical Design , vol.14 , Issue.6 , pp. 545-561
    • Jones, P.1    Steinkuhler, C.2
  • 30
    • 22844432021 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: A novel basis for antileukemia activity of histone deacetylase inhibitors
    • DOI 10.1074/jbc.C500186200
    • Bali P, Pranpat M, Bradner J, Balasis M, Fiskus W, Guo F, Rocha K, Kumaraswamy S, Boyapalle S, Atadja P, Seto E, Bhalla K. Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: A novel basis for antileukemia activity of histone deacetylase inhibitors. J Biol Chem 2005;280:26729-26734. (Pubitemid 41040705)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.29 , pp. 26729-26734
    • Bali, P.1    Pranpat, M.2    Bradner, J.3    Balasis, M.4    Fiskus, W.5    Guo, F.6    Rocha, K.7    Kumaraswamy, S.8    Boyapalle, S.9    Atadja, P.10    Seto, E.11    Bhalla, K.12
  • 35
    • 34047175919 scopus 로고    scopus 로고
    • Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation
    • DOI 10.1523/JNEUROSCI.0037-07.2007
    • Dompierre JP, Godin JD, Charrin BC, Cordelieres FP, King SJ, Humbert S, Saudou F. Histone deacetylase 6 inhibition compensates for the transport deficit in huntington's disease by increasing tubulin acetylation. J Neurosci 2007;27:3571-3583. (Pubitemid 46515140)
    • (2007) Journal of Neuroscience , vol.27 , Issue.13 , pp. 3571-3583
    • Dompierre, J.P.1    Godin, J.D.2    Charrin, B.C.3    Cordelieres, F.P.4    King, S.J.5    Humbert, S.6    Saudou, F.7
  • 36
    • 34347224016 scopus 로고    scopus 로고
    • Functional differences in epigenetic modulators - Superiority of mercaptoacetamide-based histone deacetylase inhibitors relative to hydroxamates in cortical neuron neuroprotection studies
    • DOI 10.1021/jm070178x
    • Kozikoeski AP, Chen Y, Gaysin A, Chen B, D'Annibale MA, Suto CM, Langley BC. Functional differences in epigenetic modulators-superiority of mercaptoacetamide-based histone deacetylase inhibitors relative to hydroxamates in cortical neuron neuroprotection studies. J Med Chem 2007;50:3054-3061. (Pubitemid 47001248)
    • (2007) Journal of Medicinal Chemistry , vol.50 , Issue.13 , pp. 3054-3061
    • Kozikowski, A.P.1    Chen, Y.2    Gaysin, A.3    Chen, B.4    D'Annibale, M.A.5    Suto, C.M.6    Langley, B.C.7
  • 37
    • 0038522853 scopus 로고    scopus 로고
    • Multidimensional chemical genetic analysis of diversity-oriented synthesis-derived deacetylase inhibitors using cell-based assays
    • Haggarty SJ, Koeller KM, Wong JC, Butcher RA, Schreiber SL. Multidimensional chemical genetic analysis of diversity-oriented synthesis-derived deacetylase inhibitors using cell-based assays. Chem Biol 2003;10:383-396.
    • (2003) Chem Biol , vol.10 , pp. 383-396
    • Haggarty, S.J.1    Koeller, K.M.2    Wong, J.C.3    Butcher, R.A.4    Schreiber, S.L.5
  • 38
    • 0344640906 scopus 로고    scopus 로고
    • Domain-selective smallmolecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation
    • Haggarty SJ, Koeller KM, Wong JC, Grozinger CM, Schreiber SL. Domain-selective smallmolecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation. Proc Natl Acad Sci USA 2003;100:4389-4394.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 4389-4394
    • Haggarty, S.J.1    Koeller, K.M.2    Wong, J.C.3    Grozinger, C.M.4    Schreiber, S.L.5
  • 39
    • 0035961036 scopus 로고    scopus 로고
    • Synthesis of 7200 small molecules based on a substructural analysis of the histone deacetylase inhibitors trichostatin and trapoxin
    • Sternson SM, Wong JC, Grozinger CM, Schreiber SL. Synthesis of 7200 small molecules based on a substructural analysis of the histone deacetylase inhibitors trichostatin and trapoxin. Org Lett 2001;3:4239-4242.
    • (2001) Org Lett , vol.3 , pp. 4239-4242
    • Sternson, S.M.1    Wong, J.C.2    Grozinger, C.M.3    Schreiber, S.L.4
  • 42
    • 49449113465 scopus 로고    scopus 로고
    • Functional differences in epigenetic modulators - Superiority of mercaptoacetamide-based histone deacetylase inhibitors relative to hydroxamates in cortical neuron neuroprotection studies
    • Kozikowski AP, Tapadar S, Luchini DN, Kim KH, Billadeau DD. functional differences in epigenetic modulators - superiority of mercaptoacetamide-based histone deacetylase inhibitors relative to hydroxamates in cortical neuron neuroprotection studies. J Med Chem 2008;51: 4370-4373.
    • (2008) J Med Chem , vol.51 , pp. 4370-4373
    • Kozikowski, A.P.1    Tapadar, S.2    Luchini, D.N.3    Kim, K.H.4    Billadeau, D.D.5
  • 50
    • 0035914304 scopus 로고    scopus 로고
    • Identification of a Class of Small Molecule Inhibitors of the Sirtuin Family of NAD-dependent Deacetylases by Phenotypic Screening
    • DOI 10.1074/jbc.M106779200
    • Grozinger CM, Chao ED, Blackwell HE, Moazed D, Schreiber SL. Identification of a class of small molecule inhibitors of the sirtuin family of NAD-dependent deacetylases by phenotypic screening. J Biol Chem 2001;276:38837-38843. (Pubitemid 37371246)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.42 , pp. 38837-38843
    • Grozinger, C.M.1    Chao, E.D.2    Blackwell, H.E.3    Moazed, D.4    Schreiber, S.L.5
  • 52
    • 33845925314 scopus 로고    scopus 로고
    • Design, synthesis, potency, and cytoselectivity of anticancer agents derived by parallel synthesis from α-aminosuberic acid
    • Kahnberg P, Lucke AJ, Glenn MP, Boyle GM, Tyndall JD, Parsons PG, Fairlie DP. Design, synthesis, potency, and cytoselectivity of anticancer agents derived by parallel synthesis from α-aminosuberic acid. J Med Chem 2006;49:7611-7622.
    • (2006) J Med Chem , vol.49 , pp. 7611-7622
    • Kahnberg, P.1    Lucke, A.J.2    Glenn, M.P.3    Boyle, G.M.4    Tyndall, J.D.5    Parsons, P.G.6    Fairlie, D.P.7
  • 53
    • 6244283606 scopus 로고    scopus 로고
    • Critical evaluation of search algorithms for automated molecular docking and database screening
    • Ewing TJA, Kuntz ID. Critical evaluation of search algorithms for automated molecular docking and database screening. J Comput Chem 1997;18:1175-1189.
    • (1997) J Comput Chem , vol.18 , pp. 1175-1189
    • Ewing, T.J.A.1    Kuntz, I.D.2
  • 56
    • 0030599010 scopus 로고    scopus 로고
    • A fast flexible docking method using an incremental construction algorithm
    • DOI 10.1006/jmbi.1996.0477
    • Rarey M, Kramer B, Lengauer T, Klebe G. A fast flexible docking method using an incremental construction algorithm. J Mol Biol 1996;261:470-489. (Pubitemid 26335901)
    • (1996) Journal of Molecular Biology , vol.261 , Issue.3 , pp. 470-489
    • Rarey, M.1    Kramer, B.2    Lengauer, T.3    Klebe, G.4
  • 57
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • DOI 10.1006/jmbi.1996.0897
    • Jones G, Willett P, Glen RC, Leach AR, Taylor R. Development and validation of a genetic algorithm for flexible docking. J Mol Biol 1997;267:727-748. (Pubitemid 27170693)
    • (1997) Journal of Molecular Biology , vol.267 , Issue.3 , pp. 727-748
    • Jones, G.1    Willett, P.2    Glen, R.C.3    Leach, A.R.4    Taylor, R.5
  • 61
    • 0036725277 scopus 로고    scopus 로고
    • Molecular dynamics simulations of biomolecules
    • Karplus M, McCammon JA. Molecular dynamics simulations of biomolecules. Nat Struct Biol 2002;9:646-652.
    • (2002) Nat Struct Biol , vol.9 , pp. 646-652
    • Karplus, M.1    McCammon, J.A.2
  • 62
    • 1442328108 scopus 로고    scopus 로고
    • Advances in biomolecular simulations: Methodology and recent applications
    • DOI 10.1017/S0033583503003895
    • Norberg J, Nilsson L. Advances in biomolecular simulations: Methodology and recent applications. Q Rev Biophys 2003;36:257-306. (Pubitemid 38268659)
    • (2003) Quarterly Reviews of Biophysics , vol.36 , Issue.3 , pp. 257-306
    • Norberg, J.1    Nilsson, L.2
  • 67
    • 0037434511 scopus 로고    scopus 로고
    • 3-(4-Aroyl-1-methyl-1H-2-pyrrolyl)-N-hydroxy-2-alkylamides as a new class of synthetic histone deacetylase inhibitors. 1. Design, synthesis, biological evaluation, and binding mode studies performed through three different docking procedures
    • Mai A, Massa S, Ragno R, Cerbara I, Jesacher F, Loidl P, Brosch G. 3-(4-Aroyl-1-methyl-1H-2-pyrrolyl)-N-hydroxy-2-alkylamides as a new class of synthetic histone deacetylase inhibitors. 1. Design, synthesis, biological evaluation, and binding mode studies performed through three different docking procedures. J Med Chem 2003;46:512-524.
    • (2003) J Med Chem , vol.46 , pp. 512-524
    • Mai, A.1    Massa, S.2    Ragno, R.3    Cerbara, I.4    Jesacher, F.5    Loidl, P.6    Brosch, G.7
  • 68
    • 1242273835 scopus 로고    scopus 로고
    • 3-(4-Aroyl-1-methyl-1H-2-pyrrolyl)-N-hydroxy-2-propenamides as a new class of synthetic histone deacetylase inhibitors. 2. Effect of pyrrole-C2 and/or -C4 substitutions on biological activity
    • Mai A, Massa S, Cerbara I, Valente S, Ragno R, Bottoni P, Scatena R, Loidl P, Brosch G. 3-(4-Aroyl-1-methyl-1H-2-pyrrolyl)-N-hydroxy-2-propenamides as a new class of synthetic histone deacetylase inhibitors. 2. Effect of pyrrole-C2 and/or -C4 substitutions on biological activity. J Med Chem 2004;47:1098-1109.
    • (2004) J Med Chem , vol.47 , pp. 1098-1109
    • Mai, A.1    Massa, S.2    Cerbara, I.3    Valente, S.4    Ragno, R.5    Bottoni, P.6    Scatena, R.7    Loidl, P.8    Brosch, G.9
  • 69
    • 2942545807 scopus 로고    scopus 로고
    • On the function of the 14 Å long internal cavity of histone deacetylase-like protein: Implications for the design of histone deacetylase inhibitors
    • Wang DF, Wiest O, Helquist P, Lan-Hargest HY, Wiech NL. On the function of the 14 Å long internal cavity of histone deacetylase-like protein: Implications for the design of histone deacetylase inhibitors. J Med Chem 2004;47:3409-3417.
    • (2004) J Med Chem , vol.47 , pp. 3409-3417
    • Wang, D.F.1    Wiest, O.2    Helquist, P.3    Lan-Hargest, H.Y.4    Wiech, N.L.5
  • 70
    • 27444435580 scopus 로고    scopus 로고
    • Toward selective histone deacetylase inhibitor design: Homology modeling, docking studies, and molecular dynamics simulations of human class I histone deacetylases
    • DOI 10.1021/jm0505011
    • Wang DF, Helquist P, Wiech NL, Wiest O. Toward selective histone deacetylase inhibitor design: Homology modeling, docking studies, and molecular dynamics simulations of human class I histone deacetylases. J Med Chem 2005;48:6936-6947. (Pubitemid 41533115)
    • (2005) Journal of Medicinal Chemistry , vol.48 , Issue.22 , pp. 6936-6947
    • Wang, D.-F.1    Helquist, P.2    Wiech, N.L.3    Wiest, O.4
  • 71
    • 52449112167 scopus 로고    scopus 로고
    • Residues in the 11 Å channel of histone deacetylase 1 promote catalytic activity: Implications for designing isoform-selective histone deacetylase inhibitors
    • Weerasinghe SV, Estiu G, Wiest O, Pflum MK. Residues in the 11 Å channel of histone deacetylase 1 promote catalytic activity: Implications for designing isoform-selective histone deacetylase inhibitors. J Med Chem 2008;51:5542-5551.
    • (2008) J Med Chem , vol.51 , pp. 5542-5551
    • Weerasinghe, S.V.1    Estiu, G.2    Wiest, O.3    Pflum, M.K.4
  • 72
    • 50849136880 scopus 로고    scopus 로고
    • Comparative molecular dynamics simulations of histone deacetylase-like prote Binding modes and free energy analysis to hydroxamic acid inhibitors
    • Yan CL, Xiu ZL, Li XH, Li SM, Hao C, Teng H. Comparative molecular dynamics simulations of histone deacetylase-like protein: Binding modes and free energy analysis to hydroxamic acid inhibitors. Proteins 2008;73:134-149.
    • (2008) Proteins , vol.73 , pp. 134-149
    • Yan, C.L.1    Xiu, Z.L.2    Li, X.H.3    Li, S.M.4    Hao, C.5    Teng, H.6
  • 73
    • 0023751431 scopus 로고
    • Comparative molecular field analysis (CoMFA). 1. Effect of shape on binding of steroids to carrier proteins
    • Cramer RD, Patterson DE, Bunce JD. Comparative molecular field analysis (CoMFA). 1. Effect of shape on binding of steroids to carrier proteins. J Am Chem Soc 1988;110: 5959-5967.
    • (1988) J Am Chem Soc , vol.110 , pp. 5959-5967
    • Cramer, R.D.1    Patterson, D.E.2    Bunce, J.D.3
  • 74
    • 0027944195 scopus 로고
    • Molecular similarity indices in a comparative analysis (CoMSIA) of drug molecules to correlate and predict their biological activity
    • DOI 10.1021/jm00050a010
    • Klebe G, Abraham U, Mietzner T. Molecular similarity indices in a comparative analysis (CoMSIA) of drug molecules to correlate and predict their biological activity. J Med Chem 1994;37:4130-4146. (Pubitemid 24379702)
    • (1994) Journal of Medicinal Chemistry , vol.37 , Issue.24 , pp. 4130-4146
    • Klebe, G.1    Abraham, U.2    Mietzner, T.3
  • 75
    • 23644454402 scopus 로고    scopus 로고
    • Exploration of a binding mode of indole amide analogues as potent histone deacetylase inhibitors and 3D-QSAR analyses
    • DOI 10.1016/j.bmc.2005.05.016, PII S0968089605004256
    • Guo YS, Xiao JF, Guo ZR, Chu FM, Cheng YH, Wu S. Exploration of a binding mode of indole amide analogues as potent histone deacetylase inhibitors and 3D-QSAR analyses. Bioorg Med Chem 2005;13:5424-5434. (Pubitemid 41132620)
    • (2005) Bioorganic and Medicinal Chemistry , vol.13 , Issue.18 , pp. 5424-5434
    • Guo, Y.1    Xiao, J.2    Guo, Z.3    Chu, F.4    Cheng, Y.5    Wu, S.6
  • 76
    • 34250630576 scopus 로고    scopus 로고
    • Comparison between 2D and 3D-QSAR approaches to correlate inhibitor activity for a series of indole amide hydroxamic acids
    • DOI 10.1002/qsar.200630021
    • Katritzky AR, Slavov SH, Dobchev DA, Karelson M. Comparison Between 2D and 3D-QSAR Approaches to Correlate Inhibitor Activity for a Series of Indole Amide Hydroxamic Acids. QSAR Comb Sci 2007;26:333-345. (Pubitemid 46932860)
    • (2007) QSAR and Combinatorial Science , vol.26 , Issue.3 , pp. 333-345
    • Katritzky, A.R.1    Slavov, S.H.2    Dobchev, D.A.3    Karelson, M.4
  • 78
    • 40649097784 scopus 로고    scopus 로고
    • Identification of ligand features essential for HDACs inhibitors by pharmacophore modeling
    • Chen YD, Jiang YJ, Zhou JW, Yu QS, You QD. Identification of ligand features essential for HDACs inhibitors by pharmacophore modeling. J Mol Graph Model 2008;26:1160-1168.
    • (2008) J Mol Graph Model , vol.26 , pp. 1160-1168
    • Chen, Y.D.1    Jiang, Y.J.2    Zhou, J.W.3    Yu, Q.S.4    You, Q.D.5
  • 80
    • 65249163549 scopus 로고    scopus 로고
    • Novel Inhibitors of Human Histone Deacetylase (HDAC) Identified by QSAR Modeling of Known Inhibitors, Virtual Screening, and Experimental Validation
    • Tang H, Wang XS, Huang XP, Roth BL, Butler KV, Kozikowski AP, Jung M, Tropsha A. Novel Inhibitors of Human Histone Deacetylase (HDAC) Identified by QSAR Modeling of Known Inhibitors, Virtual Screening, and Experimental Validation. J Chem Inf Model 2009;49:461-476.
    • (2009) J Chem Inf Model , vol.49 , pp. 461-476
    • Tang, H.1    Wang, X.S.2    Huang, X.P.3    Roth, B.L.4    Butler, K.V.5    Kozikowski, A.P.6    Jung, M.7    Tropsha, A.8
  • 81
    • 37449006536 scopus 로고    scopus 로고
    • Pharmacophore modeling and virtual screening studies to design some potential histone deacetylase inhibitors as new leads
    • Vadivelan S, Sinha BN, Rambabu G, Boppana K, Jagarlapudi SA. Pharmacophore modeling and virtual screening studies to design some potential histone deacetylase inhibitors as new leads. J Mol Graph Model 2008;26:935-946.
    • (2008) J Mol Graph Model , vol.26 , pp. 935-946
    • Vadivelan, S.1    Sinha, B.N.2    Rambabu, G.3    Boppana, K.4    Jagarlapudi, S.A.5
  • 83
    • 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 1990;265:17174-17179. (Pubitemid 20334262)
    • (1990) Journal of Biological Chemistry , vol.265 , Issue.28 , pp. 17174-17179
    • Yoshida, M.1    Kijima, M.2    Akita, M.3    Beppu, T.4
  • 84
    • 0027378351 scopus 로고
    • Trapoxin, an antitumor cyclic tetrapeptide, is an irreversible inhibitor of mammalian histone deacetylase
    • Kijima M, Yoshida M, Sugita K, Horinouchi S, Beppu T. Trapoxin, an antitumor cyclic tetrapeptide, is an irreversible inhibitior of mammalian histone deacetylase. J Biol Chem 1993;268:22429-22435. (Pubitemid 23318291)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.30 , pp. 22429-22435
    • Kijima, M.1    Yoshida, M.2    Sugita, K.3    Horinouchi, S.4    Beppu, T.5
  • 85
    • 0023065338 scopus 로고
    • Analogues of the cytostatic and antimitogenic agents chlamydocin and HC-toxin: Synthesis and biological activity of chloromethyl ketone and diazomethyl ketone functionalized cyclic tetrapeptides
    • Shute RE, Dunlap B, Rich DH. Analogues of the cytostatic and antimitogenic agents chlamydocin and HC-toxin synthesis and biological activity of chloromethyl ketone and diazomethyl ketone functionalized cyclic tetrapeptidest. J Med Chem 1987;30:71-78. (Pubitemid 17221619)
    • (1987) Journal of Medicinal Chemistry , vol.30 , Issue.1 , pp. 71-78
    • Shute, R.E.1    Dunlap, B.2    Rich, D.H.3
  • 87
    • 0028258610 scopus 로고
    • FR901228, a novel antitumor bicyclic depsipeptide produced by chromobacterium violaceum No. 968 1. Taxonomy, fermentation, isolation, physico-chemical and biological properties, and antitumor activity
    • Ueda H, Nakajima H, Hori Y, Fujita T, Nishimura M, Goto T, Okuhara M. FR901228, a novel antitumor bicyclic depsipeptide produced by chromobacterium violaceum No. 968 1. Taxonomy, fermentation, isolation, physico-chemical and biological properties, and antitumor activity. J Antibiotics 1994;47:301-310.
    • (1994) J Antibiotics , vol.47 , pp. 301-310
    • Ueda, H.1    Nakajima, H.2    Hori, Y.3    Fujita, T.4    Nishimura, M.5    Goto, T.6    Okuhara, M.7
  • 88
    • 0029603564 scopus 로고
    • Cytotoxic compounds from a two-sponge association
    • Jung JH, Sim CJ, Lee CO. Cytotoxic compounds from a two-sponge association. J Nat Prod 1995;58:1722-1726.
    • (1995) J Nat Prod , vol.58 , pp. 1722-1726
    • Jung, J.H.1    Sim, C.J.2    Lee, C.O.3
  • 89
    • 0031947168 scopus 로고    scopus 로고
    • A new lysine derivative and new 3-bromopyrrole carboxylic acid derivative from two marine sponges
    • DOI 10.1021/np970479h
    • Li CJ, Schmitz FJ, Kelly-Borges M. A new lysine derivative and new 3-bromopyrrole carboxylic acid derivative from two marine sponges. J Nat Prod 1998;61:387-389. (Pubitemid 28160733)
    • (1998) Journal of Natural Products , vol.61 , Issue.3 , pp. 387-389
    • Li, C.-J.1    Schmitz, F.J.2    Kelly-Borges, M.3
  • 91
    • 37349061341 scopus 로고    scopus 로고
    • A natural histone deacetylase inhibitor, Psammaplin A, induces cell cycle arrest and apoptosis in human endometrial cancer cells
    • DOI 10.1016/j.ygyno.2007.08.098, PII S0090825807007135
    • Ahn MY, Jung JH, Na YJ, Kim HS. A natural histone deacetylase inhibitor, Psammaplin A, induces cell cycle arrest and apoptosis in human endometrial cancer cells. Gynecol Oncol 2008;108:27-33. (Pubitemid 350299431)
    • (2008) Gynecologic Oncology , vol.108 , Issue.1 , pp. 27-33
    • Ahn, M.Y.1    Jung, J.H.2    Na, Y.J.3    Kim, H.S.4
  • 92
    • 39049135494 scopus 로고    scopus 로고
    • Structure and activity of largazole, a potent antiproliferative agent from the Floridian marine cyanobacterium Symploca sp
    • DOI 10.1021/ja7110064
    • Taori K, Paul VJ, Luesch H. Structure and activity of largazole, a potent antiproliferative agent from the floridian marine Cyanobacterium Symploca sp. J Am Chem Soc 2008;130:1806-1807. (Pubitemid 351238618)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.6 , pp. 1806-1807
    • Taori, K.1    Paul, V.J.2    Luesch, H.3
  • 93
    • 46049100010 scopus 로고    scopus 로고
    • Total synthesis and molecular target of largazole, a histone deacetylase inhibitor
    • DOI 10.1021/ja8013727
    • Ying Y, Taori K, Kim H, Hong J, Luesch H. Total synthesis and molecular target of largazole, a histone deacetylase inhibitor. J Am Chem Soc 2008;130:8455-8459. (Pubitemid 351898566)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.26 , pp. 8455-8459
    • Ying, Y.1    Taori, K.2    Kim, H.3    Hong, J.4    Luesch, H.5
  • 94
    • 50249144006 scopus 로고    scopus 로고
    • Total synthesis and biological mode of action of largazole: A potent class I histone deacetylase inhibitor
    • Bowers A, West N, Taunton J, Schreiber SL, Bradner JE, Williams RM. Total synthesis and biological mode of action of largazole: A potent class I histone deacetylase inhibitor. J Am Chem Soc 2008;130:11219-11222.
    • (2008) J Am Chem Soc , vol.130 , pp. 11219-11222
    • Bowers, A.1    West, N.2    Taunton, J.3    Schreiber, S.L.4    Bradner, J.E.5    Williams, R.M.6
  • 96
    • 0346025398 scopus 로고    scopus 로고
    • Cyclic Tetrapeptides Bearing a Sulfhydryl Group Potently Inhibit Histone Deacetylases
    • DOI 10.1021/ol036098e
    • Nishino N, Jose B, Okamura S, Ebisusaki S, Kato T, Sumida Y, Yoshida M. Cyclic tetrapeptides bearing a sulfhydryl group potently inhibit histone deacetylases. Org Lett 2003;5:5079-5082. (Pubitemid 38073003)
    • (2003) Organic Letters , vol.5 , Issue.26 , pp. 5079-5082
    • Nishino, N.1    Jose, B.2    Okamura, S.3    Ebisusaki, S.4    Kato, T.5    Sumida, Y.6    Yoshida, M.7
  • 99
    • 0030068129 scopus 로고    scopus 로고
    • Cell cycle regulatory proteins are targets for induced differentiation of transformed cells: Molecular and clinical studies employing hybrid polar compounds
    • Marks PA, Richon VM, Rifkind RA. Cell cycle regulatory proteins are targets for induced differentiation of transformed cells: Molecular and clinical studies employing hybrid polar compounds. Int J Hematol 1996;63:1-17.
    • (1996) Int J Hematol , vol.63 , pp. 1-17
    • Marks, P.A.1    Richon, V.M.2    Rifkind, R.A.3
  • 101
    • 33846649707 scopus 로고    scopus 로고
    • Activity-based probes for proteomic profiling of histone deacetylase complexes
    • Salisbury CM, Cravatt BF. Activity-based probes for proteomic profiling of histone deacetylase complexes. Proc Natl Acad Sci USA 2007;104:1171-1176.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 1171-1176
    • Salisbury, C.M.1    Cravatt, B.F.2
  • 102
    • 39549102872 scopus 로고    scopus 로고
    • Optimization of activity-based probes for proteomic profiling of histone deacetylase complexes
    • Salisbury CM, Cravatt BF. Optimization of activity-based probes for proteomic profiling of histone deacetylase complexes. J Am Chem Soc 2008;130:2184-2194.
    • (2008) J Am Chem Soc , vol.130 , pp. 2184-2194
    • Salisbury, C.M.1    Cravatt, B.F.2
  • 104
    • 37349017604 scopus 로고    scopus 로고
    • Dual inhibitors of inosine monophosphate dehydrogenase and histone deacetylases for cancer treatment
    • DOI 10.1021/jm070864w
    • Chen L, Wilson D, Jayaram HN, Pankiewicz KW. Dual inhibitors of inosine monophosphate dehydrogenase and histone deacetylases for cancer treatment. J Med Chem 2007;50:6685-6691. (Pubitemid 350309105)
    • (2007) Journal of Medicinal Chemistry , vol.50 , Issue.26 , pp. 6685-6691
    • Chen, L.1    Wilson, D.2    Jayaram, H.N.3    Pankiewicz, K.W.4
  • 105
    • 0031863587 scopus 로고    scopus 로고
    • Differentiation and reduction of intracellular GTP levels in HL-60 and U937 cells upon treatment with IMP dehydrogenase inhibitors
    • Inai K, Tsutani H, Yamauchi T, Nakamura T, Ueda T. Differentiation and reduction of intracellular GTP levels in HL-60 and U937 cells upon treatment with IMP dehydrogenase inhibitors. Adv Exp Med Biol 1998;431:549-553. (Pubitemid 28236834)
    • (1998) Advances in Experimental Medicine and Biology , vol.431 , pp. 549-553
    • Inai, K.1    Tsutani, H.2    Yamauchi, T.3    Nakamura, T.4    Ueda, T.5
  • 106
    • 17044386266 scopus 로고    scopus 로고
    • Synergy between imatinib and mycophenolic acid in inducing apoptosis in cell lines expressing Bcr-Abl
    • DOI 10.1182/blood-2004-10-3864
    • Gu JJ, Santiago L, Mitchell BS. Synergy between imatinib and mycophenolic acid in inducing apoptosis in cell lines expressing Bcr-Abl. Blood 2005;105:3270-3277. (Pubitemid 40504349)
    • (2005) Blood , vol.105 , Issue.8 , pp. 3270-3277
    • Gu, J.J.1    Santiago, L.2    Mitchell, B.S.3
  • 107


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.