메뉴 건너뛰기




Volumn 49, Issue 12, 2009, Pages 2774-2785

Docking of hydroxamic acids into HDAC1 and HDAC8: A rationalization of activity trends and selectivities

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL ENGINEERING; CHEMISTRY;

EID: 73349116582     PISSN: 15499596     EISSN: 1549960X     Source Type: Journal    
DOI: 10.1021/ci900288e     Document Type: Article
Times cited : (34)

References (60)
  • 2
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein, T.; Allis, C. D. Translating the histone code. Science 2001, 295, 1074-1080.
    • (2001) Science , vol.295 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 3
    • 6044256118 scopus 로고    scopus 로고
    • Histones and histone modifications
    • Peterson, C. L.; Laniel, M. A. Histones and histone modifications. Curr. Biol. 2004, 14, R546-551.
    • (2004) Curr. Biol. , vol.14
    • Peterson, C.L.1    Laniel, M.A.2
  • 4
    • 0032030770 scopus 로고    scopus 로고
    • Histone acetylation and transcriptional regulatory mechanisms
    • Strahl, K. Histone acetylation and transcriptional regulatory mechanism. Gene Dev. 1998, 12, 599-606. (Pubitemid 28134293)
    • (1998) Genes and Development , vol.12 , Issue.5 , pp. 599-606
    • Struhl, K.1
  • 5
    • 1942471702 scopus 로고    scopus 로고
    • Epigenetics and cancer: Implications for drag discovery and safety assessment
    • Moggs, J. G.; Goodman, J. I.; Trosko, J. E.; Roberts, R. A. Epigenetics and cancer: implications for drag discovery and safety assessment. Toxicol. APPl, Pharmacol. 2004, 196, 422-1130
    • (2004) Toxicol. APPl, Pharmacol. , vol.196 , pp. 422-1130
    • Moggs, J.G.1    Goodman, J.I.2    Trosko, J.E.3    Robert, R.A.4
  • 6
    • 67649986497 scopus 로고    scopus 로고
    • Inherent stereospecificity in the reaction of anatoxin B1. 8,9-epoxide with deoxyguanosine and efficiency of DNA catalysis
    • Brown, K. L.; Bren, U.; Stone, M. P.; Guengerich, F. P. Inherent stereospecificity in the reaction of anatoxin B1. 8,9-epoxide with deoxyguanosine and efficiency of DNA catalysis. Chem., Res. Toxicol. 2009, 22, 913-917.
    • (2009) Chem., Res. Toxicol. , vol.22 , pp. 913-917
    • Brown, K.L.1    Bren, U.2    Stone, M.P.3    Guengerich, F.P.4
  • 7
    • 68949221446 scopus 로고    scopus 로고
    • Steile and electrostatic effects at the C2 atom substituent influence replication and miscoding of the DNA deamination product deoxyxanthosine and analogs by DNA polymerases
    • Zhang, H.; Bren, U.; Kozekov, I. D.; Rizzo, C. J.; Stec, D. F.; Guengerich, F. P. Steile and electrostatic effects at the C2 atom substituent influence replication and miscoding of the DNA deamination product deoxyxanthosine and analogs by DNA polymerases. J. Mol. Biol. 2009, 392, 251-269.
    • (2009) J. Mol. Biol. , vol.392 , pp. 251-269
    • Zhang, H.1    Bren, U.2    Kozekov, I.D.3    Rizzo, C.J.4    Stec, D.F.5    Guengerich, F.P.6
  • 8
    • 0037291214 scopus 로고    scopus 로고
    • +-dependent tubulin deacetylase
    • DOI 10.1016/S1097-2765(03)00038-8
    • North, B. J.; Marshall, B. L.; Borra, M. T.; Denu, J. M.; Verdin, E. The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol. Cell 2003, 11, 437-444 (Pubitemid 36293837)
    • (2003) Molecular Cell , vol.11 , Issue.2 , pp. 437-444
    • North, B.J.1    Marshall, B.L.2    Borra, M.T.3    Denu, J.M.4    Verdin, E.5
  • 10
    • 27944433010 scopus 로고    scopus 로고
    • Structure and activity of enzymes that remove histone modifications
    • Holbert, M. A.; Marmorstein, R. Structure and activity of enzymes that remove histone modifications. Curr. Opin. Struct. Biol. 2005, 15, 673-680.
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 673-680
    • Holbert, M.A.1    Marmorstein, R.2
  • 12
    • 3242765335 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors - A new tool to treat cancer
    • DOI 10.1016/j.ctrv.2004.04.006, PII S0305737204000787
    • Somech, R.; Izraeli, S.; Amos, J. S. Histone deacetylase inhibitors-a new tool to treat cancer. Cancer Treat. Rev. 2004, 30, 461-472. (Pubitemid 38968126)
    • (2004) Cancer Treatment Reviews , vol.30 , Issue.5 , pp. 461-472
    • Somech, R.1    Izraeli, S.2    Simon, A.J.3
  • 15
    • 10844248177 scopus 로고    scopus 로고
    • Phase i study of oral CI-994 in combination with carboplatin and paclitaxel in the treatment of patients with advanced solid tumors
    • DOI 10.1081/CNV-200039852
    • Pauer, L. R.; Olivares, J.; Cunningham, C.; Williams, A.; Grove, W.; Kraker, A.; Olson, S.; Nemunaitis, J. Phase I study of oral CI-994 in combination with carboplatin and paclitaxel in the treatment of patients with, advanced solid tumors. Cancer Invest.- 2004, 22, 886-896. (Pubitemid 39665354)
    • (2004) Cancer Investigation , vol.22 , Issue.6 , pp. 886-896
    • Pauer, L.R.1    Olivares, J.2    Cunningham, C.3    Williams, A.4    Grove, W.5    Kraker, A.6    Olson, S.7    Nemunaitis, J.8
  • 16
    • 33745629366 scopus 로고    scopus 로고
    • Gemcitabine plus CI-994 offers no advantage over gemcitabine alone in the treatment of patients with advanced pancreatic cancer: Results of a phase II randomized, doubleblind, placebo-controlled, multicenter study
    • Richards, D. A.; Boehm, K. A.; Waterhouse, D. M.; Wagener, D. J.; Krishnamurthi, S. S.; Rosemurgy, A.; Grove, W.; Macdonald, K.; Gulyas, S.; Clark, M.; Dasse, K. D. Gemcitabine plus CI-994 offers no advantage over gemcitabine alone in the treatment of patients with advanced pancreatic cancer: results of a phase II randomized, doubleblind, placebo-controlled, multicenter study. Ann. Oncol. 2006, 17, 1096-1102.
    • (2006) Ann. Oncol. , vol.17 , pp. 1096-1102
    • Richards, D.A.1    Boehm, K.A.2    Waterhouse, D.M.3    Wagener, D.J.4    Krishnamurthi, S.S.5    Rosemurgy, A.6    Grove, W.7    Macdonald, K.8    Gulyas, S.9    Clark, M.10    Dasse, K.D.11
  • 18
  • 23
    • 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, D. F.; Helquist, P.; Wiech, N. L.; 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
  • 24
    • 0346099272 scopus 로고    scopus 로고
    • Design, synthesis, and activity of HDAC inhibitors with, a N-formyl hydroxylamine head group
    • Wu, T. Y. H.; Hassig, C.; Wu, Y.; Ding, S.; Schultz, P. G. Design, synthesis, and activity of HDAC inhibitors with, a N-formyl hydroxylamine head group. Bioorg. Med, Chem., Lett. 2004, 14, 449-453.
    • (2004) Bioorg. Med, Chem., Lett. , vol.14 , pp. 449-453
    • Wu, T.Y.H.1    Hassig, C.2    Wu, Y.3    Ding, S.4    Schultz, P.G.5
  • 25
    • 45749114198 scopus 로고    scopus 로고
    • Chemistry, biology, and QSAR studies of substituted biaryl hydroxamates and mercaptoacetamides as HDAC inhibitorsnanomolar-potency inhibitors of pancreatic cancer cell growth
    • Kozikowski, A. P.; Chen, Y.; Gaysin, A. M.; Savoy, D. N.; Billadeau, D. D.; Kim, K. H. Chemistry, biology, and QSAR studies of substituted biaryl hydroxamates and mercaptoacetamides as HDAC inhibitorsnanomolar-potency inhibitors of pancreatic cancer cell growth. ChemMedChem 2008, 3, 487-501.
    • (2008) ChemMedChem , vol.3 , pp. 487-501
    • Kozikowski, A.P.1    Chen, Y.2    Gaysin, A.M.3    Savoy, D.N.4    Billadeau, D.D.5    Kim, K.H.6
  • 30
    • 0035961036 scopus 로고    scopus 로고
    • Synthesis of 7200 small molecules based on a substructural analysis of the histone deacetylase inhibitors trichostatin and trapoxin
    • Sternson, S. M.; Wong, J. C.; Grozinger, C. M.; Schreiber, S. L. Synthesis of 7200 small molecules based on a substructural analysis of the histone deacetylase inhibitors trichostatin and trapoxin. Ore. Lett. 2001, 3, 4239-4242.
    • (2001) Ore. Lett. , vol.3 , pp. 4239-4242
    • Sternson, S.M.1    Wong, J.C.2    Grozinger, C.M.3    Schreiber, S.L.4
  • 31
    • 0344640906 scopus 로고    scopus 로고
    • Domain-selective small-molecule inhibitor of histone deactylase 6 (HDAC6)-mediated tubulin deacetylation
    • Haggarty, S. J.; Koeller, K. M.; Wong, J. C.; Grozinger, C. M. Schreiber, S. L. Domain-selective small-molecule inhibitor of histone deactylase 6 (HDAC6)-mediated tubulin deacetylation. Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 4389-4394.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , 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
  • 33
    • 3242793175 scopus 로고    scopus 로고
    • Expression of histone deacetylase 8, a class i histone deacetylase, is restricted to cells showing smooth muscle differentiation in normal human tissues
    • Waltregny, D.; De Leval, L.; Glenisson, W.; Ly Tran, S.; North, B. J.; Bellahcene, A.; Weidle, U.; Verdin, E.; Castronovo, V. Expression of Histone Deacetylase 8, a Class I Histone Deacetylase, Is Restricted to Cells Showing Smooth Muscle Differentiation in Normal Human Tissues. Am. J. Pathol- 2004, 165, 553-564. (Pubitemid 38971385)
    • (2004) American Journal of Pathology , vol.165 , Issue.2 , pp. 553-564
    • Waltregny, D.1    De Leval, L.2    Glenisson, W.3    Ly Tran, S.4    North, B.J.5    Bellahcene, A.6    Weidle, U.7    Verdin, E.8    Castronovo, V.9
  • 34
    • 20444487771 scopus 로고    scopus 로고
    • Histone deacetylase HDAC8 associates with smooth muscle α-actin and is essential for smooth muscle cell contractility
    • DOI 10.1096/fj.04-2303fje
    • Waltregny, D.; Glenisson, W.; Tran, S. L.; North, B. J.; Verdin, E.; Colige, A.; Castronovo, V. Histone deacetylase HDAC8 associates with smooth muscle-actin and is essential for smooth muscle cell contractility. FASEB J. 2005, 19, 966-968. (Pubitemid 40827719)
    • (2005) FASEB Journal , vol.19 , Issue.8 , pp. 966-968
    • Waltregny, D.1    Glenisson, W.2    Tran, S.L.3    North, B.J.4    Verdin, E.5    Colige, A.6    Castronovo, V.7
  • 35
    • 0037220731 scopus 로고    scopus 로고
    • The inv(16) fusion protein associates with corepressors via a smooth muscle myosin heavy-chain domain
    • Durst, K. L.; Lutterbach, B.; Kummalue, T.; Friedman, A. D.; Hiebert, S. W. The inv(16) Fusion Protein Associates with Corepressors via a Smooth Muscle Myosin Heavy-Chain Domain. Mol. Cell. Biol. 2003, 23, 607-619.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 607-619
    • Durst, K.L.1    Lutterbach, B.2    Kummalue, T.3    Friedman, A.D.4    Hiebert, S.W.5
  • 38
    • 2342603414 scopus 로고    scopus 로고
    • Induction of HDAC2 expression upon loss of APC in colorectal tumorigenesis
    • DOI 10.1016/S1535-6108(04)00114-X, PII S153561080400114X
    • Zhu, P.; Martin, E.; Mengwasser, J.; Schlag, P.; Janssen, K.-P.; Göttlicher, M. Induction of HDAC2 expression upon loss of APC in colorectal tumorigenesis. Cancer Cell 2004, 5, 455-463. (Pubitemid 38610247)
    • (2004) Cancer Cell , vol.5 , Issue.5 , pp. 455-463
    • Zhu, P.1    Martin, E.2    Mengwasser, J.3    Schlag, P.4    Janssen, K.-P.5    Gottlicher, M.6
  • 42
    • 35548947488 scopus 로고    scopus 로고
    • Substrate binding to histone deacetylases as shown by the crystal structure of the HDAC8-substrate complex
    • DOI 10.1038/sj.embor.7401047, PII 7401047
    • Vannini, A.; Volpari, C.; Gallinari, P.; Jones, P.; Mattu, M.; Carfi, A.; Defrancesco, R.; Steinkuhler, C.; Di Marco, S. Substrate binding to histone deacetylases as shown by the crystal structure of the HDAC8-substrate complex. EMBO Rep. 2007, 8, 879-884. (Pubitemid 350001433)
    • (2007) EMBO Reports , vol.8 , Issue.9 , pp. 879-884
    • Vannini, A.1    Volpari, C.2    Gallinari, P.3    Jones, P.4    Steinkuhler, C.5    Di Marco, S.6
  • 43
    • 58149144730 scopus 로고    scopus 로고
    • Structural studies of human histone deacetylase 8 and its sitespecific variants complexed with substrate and inhibitors
    • Dowling, D. P.; Gantt, S. L.; Gattis, S. G.; Fierke, C. A.; Christiansen, D. W. Structural studies of human histone deacetylase 8 and its sitespecific variants complexed with substrate and inhibitors. Biochemistry 2008, 47, 13554-13563.
    • (2008) Biochemistry , vol.47 , pp. 13554-13563
    • Dowling, D.P.1    Gantt, S.L.2    Gattis, S.G.3    Fierke, C.A.4    Christiansen, D.W.5
  • 45
    • 73349096238 scopus 로고    scopus 로고
    • ver. 7.5; Schrödinger Inc.: Portland, OR
    • Maestro, ver. 7.5; Schrödinger Inc.: Portland, OR, 1999.
    • (1999) Maestro
  • 46
    • 0012777850 scopus 로고    scopus 로고
    • ver. 8.5; Schrödinger Inc.: Portland, OR
    • Macromodel, ver. 8.5; Schrödinger Inc.: Portland, OR, 1999.
    • (1999) Macromodel
  • 47
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • Morris, G. M.; Goodsell, D. S.; Halliday, R. S.; Huey, R.; Hart, W. E.; Belew, R. K.; Olson, A. J. Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J. Comput Chem. 1998, 19, 1639-1662.
    • (1998) J. Comput Chem. , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 48
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • Jones, G.; Willett, P.; Glen, R. C.; Leach, A. R.; Taylor, R. J. Development and validation of a genetic algorithm for flexible docking. J. Mol. Biol. 1997, 267, 727-748.
    • (1997) J. Mol. Biol. , vol.267 , pp. 727-748
    • Jones, G.1    Willett, P.2    Glen, R.C.3    Leach, A.R.4    Taylor, R.J.5
  • 49
    • 0000577528 scopus 로고    scopus 로고
    • The object technology framework: An object-oriented, interface to molecular data and its application to collagen
    • Huang, C. C.; Couch, G. S.; Pettersen, E. F.; Ferrin, T. E. The object technology framework: an object-oriented, interface to molecular data and its application to collagen. Pac. Symp. Biocomput. 1996, 1, 724; http://www.cgl.ucsf.edu/chimera
    • (1996) Pac. Symp. Biocomput. , vol.1 , pp. 724
    • Huang, C.C.1    Couch, G.S.2    Pettersen, E.F.3    Ferrin, T.E.4
  • 50
    • 16344373015 scopus 로고    scopus 로고
    • Protein homology detection by HMM-HMM comparison
    • Soeding, J. Protein homology detection by HMM-HMM comparison. Bioinformatics 2005, 21, 951-960.
    • (2005) Bioinformatics , vol.21 , pp. 951-960
    • Soeding, J.1
  • 51
    • 0029887381 scopus 로고    scopus 로고
    • Hidden Markov models for sequence analysis: Extension and analysis of the basic method
    • Hughey, R.; Krogh, A. Hidden. Markov models for sequence analysis: Extension and analysis of the basic method. Computer Arml. Biosci. 1996, 12, 95-107. (Pubitemid 26166723)
    • (1996) Computer Applications in the Biosciences , vol.12 , Issue.2 , pp. 95-107
    • Hughey, R.1    Krogh, A.2
  • 52
  • 53
    • 0033810049 scopus 로고    scopus 로고
    • Modeling of loops in protein, structures
    • Fiser, A.; Do, R. K.; Sali, A. Modeling of loops in protein, structures. Protein Sci. 2000, 9, 1753.
    • (2000) Protein Sci. , vol.9 , pp. 1753
    • Fiser, A.1    Do, R.K.2    Sali, A.3
  • 54
    • 73349106778 scopus 로고    scopus 로고
    • Version 4.5; Multivariate Infometric Analysis Srl.: Perugia, Italy
    • GOLPE, Version 4.5; Multivariate Infometric Analysis Srl.: Perugia, Italy, 1999.
    • (1999) GOLPE
  • 55
    • 73349112828 scopus 로고    scopus 로고
    • Version. 22a; Molecular Discovery Ltd.: West Way House, Elms Parade, Oxford, U.K.
    • GRID, Version. 22a; Molecular Discovery Ltd.: West Way House, Elms Parade, Oxford, U.K., 2004.
    • (2004) GRID
  • 58
    • 12144291023 scopus 로고    scopus 로고
    • 3-(4-Aroyl-1-methyl-1H-pyrrol-2-yl)-N-hydroxy-2-propenamides as a New Class of Synthetic Histone Deacetylase Inhibitors. 3. Discovery of Novel Lead Compounds through Structure-Based Drug Design and Docking Studies
    • DOI 10.1021/jm031036f
    • Ragno, R.; Mai, A.; Massa, S.; Cerbara, I.; Valente, S.; Bottoni, P.; Scatena, R.; Jesacher, F.; Loidl, P.; Brosch, G. 3-(4-Aroyl-l-methyl1H-pyrrol-2- yl)-N-hydroxy-2-propenamides as a New Class of Synthetic Histone Deacetylase Inhibitors. 3. Discovery of Novel Lead Compounds through Structure-Based Drag Design and Docking Studies. J. Med. Chem 2004, 47, 1351-1359. (Pubitemid 38327463)
    • (2004) Journal of Medicinal Chemistry , vol.47 , Issue.6 , pp. 1351-1359
    • Ragno, R.1    Mai, A.2    Massa, S.3    Cerbara, I.4    Valente, S.5    Bottoni, P.6    Scatena, R.7    Jesacher, F.8    Loidl, P.9    Brosch, G.10
  • 60
    • 43049119236 scopus 로고    scopus 로고
    • The use of diversity profiling to characterize chemical modulators of the histone deacetylases
    • Blackwell, L.; Noms, J.; Suto, M. C.; Janzen, W. P. The use of diversity profiling to characterize chemical modulators of the histone deacetylases. Life Sci. 2008, 82, 1050-1058.
    • (2008) Life Sci. , vol.82 , pp. 1050-1058
    • Blackwell, L.1    Noms, J.2    Suto, M.C.3    Janzen, W.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.