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Volumn 58, Issue 8, 2015, Pages 3512-3521

Discovery of orally available runt-related transcription factor 3 (RUNX3) modulators for anticancer chemotherapy by epigenetic activation and protein stabilization

Author keywords

[No Author keywords available]

Indexed keywords

3 [1 [3 (2 ETHOXYPHENYL)PROPYL] 2 OXO 1,2 DIHYDROPYRIDIN 3 YL] N HYDROXYACRYLAMIDE; AGENTS AFFECTING PROTEIN METABOLISM; ANTINEOPLASTIC AGENT; BUSPIRONE; EPIGENETIC READER DOMAIN INHIBITOR; HISTONE DEACETYLASE INHIBITOR; N HYDROXY 3 [1 [3 (3 METHOXYPHENYL)PROPYL] 2 OXO 1,2 DIHYDROPYRIDIN 3 YL]ACRYLAMIDE; N HYDROXY 3 [2 OXO 1 (QUINOLIN 2 YLMETHYL) 1,2 DIHYDROPYRIDIN 3 YL]ACRYLAMIDE; PYRIDONE DERIVATIVE; RUNT RELATED TRANSCRIPTION FACTOR 3 MODULATOR; SMALL MOLECULE TRANSPORT AGENT; TRANSCRIPTION FACTOR RUNX3; UNCLASSIFIED DRUG; VORINOSTAT;

EID: 84928494317     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/acs.jmedchem.5b00062     Document Type: Article
Times cited : (5)

References (36)
  • 2
    • 84894034702 scopus 로고    scopus 로고
    • Improved synthesis and structural reassignment of MC1568: a class IIa selective HDAC inhibitor
    • Fleming, C. L.; Ashton, T. D.; Gaur, V.; McGee, S. L.; Pfeffer, F. M. Improved synthesis and structural reassignment of MC1568: a class IIa selective HDAC inhibitor J. Med. Chem. 2014, 57, 1132-1135
    • (2014) J. Med. Chem. , vol.57 , pp. 1132-1135
    • Fleming, C.L.1    Ashton, T.D.2    Gaur, V.3    McGee, S.L.4    Pfeffer, F.M.5
  • 3
    • 80052814243 scopus 로고    scopus 로고
    • Isoform-selective HDAC inhibitors: closing in on translational medicine for the heart
    • McKinsey, T. A. Isoform-selective HDAC inhibitors: closing in on translational medicine for the heart J. Mol. Cell. Cardiol. 2011, 51, 491-496
    • (2011) J. Mol. Cell. Cardiol. , vol.51 , pp. 491-496
    • McKinsey, T.A.1
  • 5
    • 41149089267 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: from bench to clinic
    • Paris, M.; Porcelloni, M.; Binaschi, M.; Fattori, D. Histone deacetylase inhibitors: from bench to clinic J. Med. Chem. 2008, 51, 1505-1529
    • (2008) J. Med. Chem. , vol.51 , pp. 1505-1529
    • Paris, M.1    Porcelloni, M.2    Binaschi, M.3    Fattori, D.4
  • 6
    • 73949128107 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in cancer therapy
    • Lane, A. A.; Chabner, B. A. Histone deacetylase inhibitors in cancer therapy J. Clin. Oncol. 2009, 27, 5459-5468
    • (2009) J. Clin. Oncol. , vol.27 , pp. 5459-5468
    • Lane, A.A.1    Chabner, B.A.2
  • 8
    • 33644856123 scopus 로고    scopus 로고
    • Epigenetic therapy of cancer: past, present and future
    • Yoo, C. B.; Jones, P. A. Epigenetic therapy of cancer: past, present and future Nat. Rev. Drug Discovery 2006, 5, 37-50
    • (2006) Nat. Rev. Drug Discovery , vol.5 , pp. 37-50
    • Yoo, C.B.1    Jones, P.A.2
  • 9
    • 1542514783 scopus 로고    scopus 로고
    • Targeted histone deacetylase inhibition for cancer therapy
    • Vigushin, D. M.; Coombes, R. C. Targeted histone deacetylase inhibition for cancer therapy Curr. Cancer Drug Targets 2004, 4, 205-218
    • (2004) Curr. Cancer Drug Targets , vol.4 , pp. 205-218
    • Vigushin, D.M.1    Coombes, R.C.2
  • 10
    • 84864434739 scopus 로고    scopus 로고
    • Emerging epigenetic targets and therapies in cancer medicine
    • Popovic, R.; Licht, J. D. Emerging epigenetic targets and therapies in cancer medicine Cancer Discovery 2012, 2, 405-413
    • (2012) Cancer Discovery , vol.2 , pp. 405-413
    • Popovic, R.1    Licht, J.D.2
  • 11
    • 84860652628 scopus 로고    scopus 로고
    • Epigenetic mechanisms in tumorigenesis, tumor cell heterogeneity and drug resistance
    • Wilting, R. H.; Dannenberg, J. H. Epigenetic mechanisms in tumorigenesis, tumor cell heterogeneity and drug resistance Drug Resist. Updates 2012, 15, 21-38
    • (2012) Drug Resist. Updates , vol.15 , pp. 21-38
    • Wilting, R.H.1    Dannenberg, J.H.2
  • 13
    • 84869869682 scopus 로고    scopus 로고
    • HDAC inhibitor-based therapies: Can we interpret the code?
    • New, M.; Olzscha, H.; La Thangue, N. B. HDAC inhibitor-based therapies: Can we interpret the code? Mol. Oncol. 2012, 6, 637-656
    • (2012) Mol. Oncol. , vol.6 , pp. 637-656
    • New, M.1    Olzscha, H.2    La Thangue, N.B.3
  • 14
    • 84867082035 scopus 로고    scopus 로고
    • Epigenetic cancer therapy: rationales, targets and drugs
    • Rius, M.; Lyko, F. Epigenetic cancer therapy: rationales, targets and drugs Oncogene 2012, 31, 4257-4265
    • (2012) Oncogene , vol.31 , pp. 4257-4265
    • Rius, M.1    Lyko, F.2
  • 16
    • 84874688338 scopus 로고    scopus 로고
    • Histone deacetylases as targets for treatment of multiple diseases
    • Tang, J.; Yan, H.; Zhuang, S. Histone deacetylases as targets for treatment of multiple diseases Clin. Sci. 2013, 124, 651-662
    • (2013) Clin. Sci. , vol.124 , pp. 651-662
    • Tang, J.1    Yan, H.2    Zhuang, S.3
  • 17
    • 77952237515 scopus 로고    scopus 로고
    • RUNX3 is multifunctional in carcinogenesis of multiple solid tumors
    • Chuang, L. S.; Ito, Y. RUNX3 is multifunctional in carcinogenesis of multiple solid tumors Oncogene 2010, 29, 2605-2615
    • (2010) Oncogene , vol.29 , pp. 2605-2615
    • Chuang, L.S.1    Ito, Y.2
  • 19
    • 79251644456 scopus 로고    scopus 로고
    • New insights into the inactivation of gastric tumor suppressor RUNX3: the role of H. pylori infection
    • Tsang, Y. H.; Lamb, A.; Chen, L. F. New insights into the inactivation of gastric tumor suppressor RUNX3: the role of H. pylori infection J. Cell. Biochem. 2011, 112, 381-386
    • (2011) J. Cell. Biochem. , vol.112 , pp. 381-386
    • Tsang, Y.H.1    Lamb, A.2    Chen, L.F.3
  • 20
    • 32044468546 scopus 로고    scopus 로고
    • Phosphorylation, acetylation and ubiquitination: the molecular basis of RUNX regulation
    • Bae, S. C.; Lee, Y. H. Phosphorylation, acetylation and ubiquitination: the molecular basis of RUNX regulation Gene 2006, 366, 58-66
    • (2006) Gene , vol.366 , pp. 58-66
    • Bae, S.C.1    Lee, Y.H.2
  • 22
    • 3142720638 scopus 로고    scopus 로고
    • Transforming growth factor-beta stimulates p300-dependent RUNX3 acetylation, which inhibits ubiquitination-mediated degradation
    • Jin, Y. H.; Jeon, E. J.; Li, Q. L.; Lee, Y. H.; Choi, J. K.; Kim, W. J.; Lee, K. Y.; Bae, S. C. Transforming growth factor-beta stimulates p300-dependent RUNX3 acetylation, which inhibits ubiquitination-mediated degradation J. Biol. Chem. 2004, 279, 29409-29417
    • (2004) J. Biol. Chem. , vol.279 , pp. 29409-29417
    • Jin, Y.H.1    Jeon, E.J.2    Li, Q.L.3    Lee, Y.H.4    Choi, J.K.5    Kim, W.J.6    Lee, K.Y.7    Bae, S.C.8
  • 23
    • 58249123443 scopus 로고    scopus 로고
    • Hypoxic silencing of tumor suppressor RUNX3 by histone modification in gastric cancer cells
    • Lee, S. H.; Kim, J.; Kim, W. H.; Lee, Y. M. Hypoxic silencing of tumor suppressor RUNX3 by histone modification in gastric cancer cells Oncogene 2009, 28, 184-194
    • (2009) Oncogene , vol.28 , pp. 184-194
    • Lee, S.H.1    Kim, J.2    Kim, W.H.3    Lee, Y.M.4
  • 25
    • 84896719529 scopus 로고    scopus 로고
    • Lactam-based HDAC inhibitors for anticancer chemotherapy: restoration of RUNX3 by posttranslational modification and epigenetic control
    • Cho, M.; Choi, E.; Kim, J. H.; Kim, H.; Kim, H. M.; Lee, J. I.; Hwang, K. C.; Kim, H. J.; Han, G. Lactam-based HDAC inhibitors for anticancer chemotherapy: restoration of RUNX3 by posttranslational modification and epigenetic control ChemMedChem 2014, 9, 649-656
    • (2014) ChemMedChem , vol.9 , pp. 649-656
    • Cho, M.1    Choi, E.2    Kim, J.H.3    Kim, H.4    Kim, H.M.5    Lee, J.I.6    Hwang, K.C.7    Kim, H.J.8    Han, G.9
  • 27
    • 84870986026 scopus 로고    scopus 로고
    • Property-based optimization of hydroxamate-based gamma-lactam HDAC inhibitors to improve their metabolic stability and pharmacokinetic profiles
    • Choi, E.; Lee, C.; Cho, M.; Seo, J. J.; Yang, J. S.; Oh, S. J.; Lee, K.; Park, S. K.; Kim, H. M.; Kwon, H. J.; Han, G. Property-based optimization of hydroxamate-based gamma-lactam HDAC inhibitors to improve their metabolic stability and pharmacokinetic profiles J. Med. Chem. 2012, 55, 10766-10770
    • (2012) J. Med. Chem. , vol.55 , pp. 10766-10770
    • Choi, E.1    Lee, C.2    Cho, M.3    Seo, J.J.4    Yang, J.S.5    Oh, S.J.6    Lee, K.7    Park, S.K.8    Kim, H.M.9    Kwon, H.J.10    Han, G.11
  • 31
    • 39349093681 scopus 로고    scopus 로고
    • In vitro metabolism of KBH-A40, a novel delta-lactam-based histone deacetylase (HDAC) inhibitor, in human liver microsomes and serum
    • Kim, H. M.; Oh, S. J.; Park, S. K.; Han, G.; Kim, K.; Lee, K. S.; Kang, J. S.; Nam, M.; Lee, K. In vitro metabolism of KBH-A40, a novel delta-lactam-based histone deacetylase (HDAC) inhibitor, in human liver microsomes and serum Xenobiotica 2008, 38, 281-293
    • (2008) Xenobiotica , vol.38 , pp. 281-293
    • Kim, H.M.1    Oh, S.J.2    Park, S.K.3    Han, G.4    Kim, K.5    Lee, K.S.6    Kang, J.S.7    Nam, M.8    Lee, K.9
  • 32
    • 78651366134 scopus 로고    scopus 로고
    • Evaluation of the pharmacokinetics and metabolism of a novel histone deacetylase inhibitor, KBH-A40, in rats
    • Oh, S. J.; Lee, K.; Ryu, J.; Yu, H. E.; Han, G.; Park, S. K.; Kang, J. S.; Kim, H. M.; Kim, Y. C. Evaluation of the pharmacokinetics and metabolism of a novel histone deacetylase inhibitor, KBH-A40, in rats Xenobiotica 2011, 41, 155-163
    • (2011) Xenobiotica , vol.41 , pp. 155-163
    • Oh, S.J.1    Lee, K.2    Ryu, J.3    Yu, H.E.4    Han, G.5    Park, S.K.6    Kang, J.S.7    Kim, H.M.8    Kim, Y.C.9
  • 33
    • 34248220985 scopus 로고    scopus 로고
    • In vitro phase I cytochrome P450 metabolism, permeability and pharmacokinetics of SB639, a novel histone deacetylase inhibitor in preclinical species
    • Venkatesh, P. R.; Goh, E.; Zeng, P.; New, L. S.; Xin, L.; Pasha, M. K.; Sangthongpitag, K.; Yeo, P.; Kantharaj, E. In vitro phase I cytochrome P450 metabolism, permeability and pharmacokinetics of SB639, a novel histone deacetylase inhibitor in preclinical species Biol. Pharm. Bull. 2007, 30, 1021-1024
    • (2007) Biol. Pharm. Bull. , vol.30 , pp. 1021-1024
    • Venkatesh, P.R.1    Goh, E.2    Zeng, P.3    New, L.S.4    Xin, L.5    Pasha, M.K.6    Sangthongpitag, K.7    Yeo, P.8    Kantharaj, E.9
  • 34
    • 0021100690 scopus 로고
    • Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
    • Dignam, J. D.; Lebovitz, R. M.; Roeder, R. G. Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei Nucleic Acids Res. 1983, 11, 1475-1489
    • (1983) Nucleic Acids Res. , vol.11 , pp. 1475-1489
    • Dignam, J.D.1    Lebovitz, R.M.2    Roeder, R.G.3


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