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Volumn 10, Issue 6, 2018, Pages

Targeting histone deacetylases with natural and synthetic agents: An emerging anticancer strategy

Author keywords

Apoptosis; Cancer; Histone deacetylase inhibitors; Histone deacetylases; Natural HDACi; Vorinostat

Indexed keywords

ANTIINFECTIVE AGENT; BELINOSTAT; BUTEIN; CALMODULIN; DIALLYL DISULFIDE; HEAT SHOCK PROTEIN; HISTONE ACETYLTRANSFERASE; HISTONE DEACETYLASE; HISTONE DEACETYLASE INHIBITOR; HYPOXIA INDUCIBLE FACTOR; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; KAEMPFEROL; NATURAL PRODUCT; NONHISTONE PROTEIN; PANOBINOSTAT; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR; POLYKETIDE; PROTOCATECHUALDEHYDE; REACTIVE OXYGEN METABOLITE; RESVERATROL; ROMIDEPSIN; SINAPIC ACID; SIRTUIN; TEMOZOLOMIDE; TRANSCRIPTION FACTOR GATA 1; UNINDEXED DRUG; VINEGAR; VORINOSTAT; ZERUMBONE; ANTINEOPLASTIC AGENT; HISTONE;

EID: 85048316253     PISSN: None     EISSN: 20726643     Source Type: Journal    
DOI: 10.3390/nu10060731     Document Type: Review
Times cited : (176)

References (160)
  • 2
    • 84971492883 scopus 로고    scopus 로고
    • Drug Targets for Cancer Treatment: An Overview
    • Kumar, S.; Ahmad, M.K.; Waseem, M.; Pandey, A.K. Drug Targets for Cancer Treatment: An Overview. Med. Chem. 2015, 5, 115–123. [CrossRef]
    • (2015) Med. Chem , vol.5 , pp. 115-123
    • Kumar, S.1    Ahmad, M.K.2    Waseem, M.3    Pandey, A.K.4
  • 3
    • 84971455256 scopus 로고    scopus 로고
    • Medicinal attributes of major phenylpropanoids present in cinnamon
    • Sharma, U.K.; Sharma, A.K.; Pandey, A.K. Medicinal attributes of major phenylpropanoids present in cinnamon. BMC Complement. Altern. Med. 2016, 16, 156. [CrossRef] [PubMed]
    • (2016) BMC Complement. Altern. Med , vol.16
    • Sharma, U.K.1    Sharma, A.K.2    Pandey, A.K.3
  • 4
    • 85042606839 scopus 로고    scopus 로고
    • Oxidative stress-related microRNAs as diagnostic markers: A newer Insight in diagnostics
    • Maurya, P., Chandra, P., Eds.; Springer: Singapore
    • Kumar, S.; Pandey, A.K. Oxidative stress-related microRNAs as diagnostic markers: A newer Insight in diagnostics. In Oxidative Stress: Diagnostic Methods and Applications in Medical Science; Maurya, P., Chandra, P., Eds.; Springer: Singapore, 2017; pp. 113–125.
    • (2017) Oxidative Stress: Diagnostic Methods and Applications in Medical Science , pp. 113-125
    • Kumar, S.1    Pandey, A.K.2
  • 5
    • 84869880178 scopus 로고    scopus 로고
    • Histone deacetylases and cancer
    • Zahonero, B.B.; Parra, M. Histone deacetylases and cancer. Mol. Oncol. 2012, 6, 579–589. [CrossRef] [PubMed]
    • (2012) Mol. Oncol , vol.6 , pp. 579-589
    • Zahonero, B.B.1    Parra, M.2
  • 6
    • 84929598341 scopus 로고    scopus 로고
    • Histone Deacetylase Inhibitors in Clinical Studies as Templates for New Anticancer Agents
    • Mottamal, M.; Zheng, S.; Huang, T.L.; Wang, G. Histone Deacetylase Inhibitors in Clinical Studies as Templates for New Anticancer Agents. Molecules 2016, 20, 3898–3941. [CrossRef] [PubMed]
    • (2016) Molecules , vol.20 , pp. 3898-3941
    • Mottamal, M.1    Zheng, S.2    Huang, T.L.3    Wang, G.4
  • 7
    • 78651162036 scopus 로고
    • Acetylation and methylation of histones and their possible role in the regulation of Rna synthesis
    • Allfrey, V.G.; Faulkner, R.; Mirsky, A.E. Acetylation and methylation of histones and their possible role in the regulation of Rna synthesis. Proc. Natl. Acad. Sci. USA 1964, 51, 786–794. [CrossRef] [PubMed]
    • (1964) Proc. Natl. Acad. Sci. USA , vol.51 , pp. 786-794
    • Allfrey, V.G.1    Faulkner, R.2    Mirsky, A.E.3
  • 8
    • 0014409959 scopus 로고
    • Chemical studies of histone acetylation. The occurrence of epsilon-N-acetyllysine in the f2a1 histone
    • Gershey, E.L.; Vidali, G.; Allfrey, V.G. Chemical studies of histone acetylation. The occurrence of epsilon-N-acetyllysine in the f2a1 histone. J. Biol. Chem. 1968, 243, 5018–5022. [PubMed]
    • (1968) J. Biol. Chem , vol.243 , pp. 5018-5022
    • Gershey, E.L.1    Vidali, G.2    Allfrey, V.G.3
  • 9
    • 57749170458 scopus 로고    scopus 로고
    • The many roles of histone deacetylases in development and physiology: Implications for disease and therapy
    • Haberland, M.; Montgomery, R.L.; Olson, E.N. The many roles of histone deacetylases in development and physiology: implications for disease and therapy. Nat. Rev. Genet. 2009, 10, 32–42. [CrossRef] [PubMed]
    • (2009) Nat. Rev. Genet , vol.10 , pp. 32-42
    • Haberland, M.1    Montgomery, R.L.2    Olson, E.N.3
  • 10
    • 80054755362 scopus 로고    scopus 로고
    • Deacetylation of Nonhistone Proteins by HDACs and the Implications in Cancer
    • Yao, T.P., Seto, E., Handbook of Experimental Pharmacology; Springer: Berlin/Heidelberg, Germany
    • Peng, L.; Seto, E. Deacetylation of Nonhistone Proteins by HDACs and the Implications in Cancer. In Histone Deacetylases: The Biology and Clinical Implication; Yao, T.P., Seto, E., Eds.; Handbook of Experimental Pharmacology; Springer: Berlin/Heidelberg, Germany, 2011; Volume 206, pp. 39–56. ISBN 978-3-642-21631-2.
    • (2011) Histone Deacetylases: The Biology and Clinical Implication , vol.206 , pp. 39-56
    • Peng, L.1    Seto, E.2
  • 11
    • 84908217408 scopus 로고    scopus 로고
    • The Role of Dietary Histone Deacetylases (HDACs) Inhibitors in Health and Disease
    • Basset, S.A.; Barnett, M.P. The Role of Dietary Histone Deacetylases (HDACs) Inhibitors in Health and Disease. Nutrients 2014, 6, 4273–4301. [CrossRef] [PubMed]
    • (2014) Nutrients , vol.6 , pp. 4273-4301
    • Basset, S.A.1    Barnett, M.P.2
  • 12
    • 84872682242 scopus 로고    scopus 로고
    • Phytochemicals and cancer risk: A review of the epidemiological evidence
    • Miller, P.E.; Snyder, D.C. Phytochemicals and cancer risk: A review of the epidemiological evidence. Nutr. Clin. Pract. 2012, 27, 599–612. [CrossRef] [PubMed]
    • (2012) Nutr. Clin. Pract , vol.27 , pp. 599-612
    • Miller, P.E.1    Snyder, D.C.2
  • 13
    • 84879574291 scopus 로고    scopus 로고
    • Green tea and the risk of genetic cancer: Epidemiological evidence
    • Hou, I.C.; Amarnani, S.; Chong, M.T.; Bishayee, A. Green tea and the risk of genetic cancer: Epidemiological evidence. World J. Gastroenterol. 2013, 19, 3713–3722. [CrossRef] [PubMed]
    • (2013) World J. Gastroenterol , vol.19 , pp. 3713-3722
    • Hou, I.C.1    Amarnani, S.2    Chong, M.T.3    Bishayee, A.4
  • 14
    • 85020746241 scopus 로고    scopus 로고
    • Association of flavonoid-rich foods and flavonoids with risk of all-cause mortality
    • Ivey, K.L.; Jensen, M.K.; Hodgson, J.M.; Eliassen, A.H.; Cassidy, A.; Rimm, E.B. Association of flavonoid-rich foods and flavonoids with risk of all-cause mortality. Br. J. Nutr. 2017, 117, 1470–1477. [CrossRef] [PubMed]
    • (2017) Br. J. Nutr , vol.117 , pp. 1470-1477
    • Ivey, K.L.1    Jensen, M.K.2    Hodgson, J.M.3    Eliassen, A.H.4    Cassidy, A.5    Rimm, E.B.6
  • 15
    • 84896281851 scopus 로고    scopus 로고
    • Chemistry and biological activities of flavonoids: An overview
    • Kumar, S.; Pandey, A.K. Chemistry and biological activities of flavonoids: an overview. Sci. World J. 2013, 2013, 162750. [CrossRef] [PubMed]
    • Sci. World J , vol.2013 , pp. 2013
    • Kumar, S.1    Pandey, A.K.2
  • 16
    • 79952932076 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Molecular mechanisms of action and clinical trials as anti-cancer drugs
    • Kim, H.J.; Bae, S.C. Histone deacetylase inhibitors: Molecular mechanisms of action and clinical trials as anti-cancer drugs. Am. J. Transl. Res. 2011, 3, 166–179. [PubMed]
    • (2011) Am. J. Transl. Res , vol.3 , pp. 166-179
    • Kim, H.J.1    Bae, S.C.2
  • 17
    • 78649861862 scopus 로고    scopus 로고
    • Inhibitors to understand molecular mechanisms of NAD+-dependent deacetylases (Sirtuins)
    • Lawson, M.; Uciechowska, U.; Schemies, J.; Rumpf, T.; Jung, M.; Sippl, W. Inhibitors to understand molecular mechanisms of NAD+-dependent deacetylases (sirtuins). Biochim. Biophys. Acta 2010, 1799, 726–739. [CrossRef] [PubMed]
    • (2010) Biochim. Biophys. Acta , vol.1799 , pp. 726-739
    • Lawson, M.1    Uciechowska, U.2    Schemies, J.3    Rumpf, T.4    Jung, M.5    Sippl, W.6
  • 18
    • 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 1996, 272, 408–411. [CrossRef] [PubMed]
    • (1996) Science , vol.272 , pp. 408-411
    • Taunton, J.1    Hassig, C.A.2    Schreiber, S.L.3
  • 19
    • 0029850458 scopus 로고    scopus 로고
    • Transcriptional repression by YY1 is mediated by interaction with a mammalian homolog of the yeast global regulator RPD3
    • Yang, W.M.; Inouye, C.; Zeng, Y.; Bearss, D.; Seto, E. Transcriptional repression by YY1 is mediated by interaction with a mammalian homolog of the yeast global regulator RPD3. Proc. Natl. Acad. Sci. USA 1996, 93, 12845–12850. [CrossRef] [PubMed]
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12845-12850
    • Yang, W.M.1    Inouye, C.2    Zeng, Y.3    Bearss, D.4    Seto, E.5
  • 20
    • 0030834976 scopus 로고    scopus 로고
    • Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family
    • Yang, W.M.; Yao, Y.L.; Sun, J.M.; Davie, J.R.; Seto, E. Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family. J. Biol. Chem. 1997, 272, 28001–28007. [CrossRef] [PubMed]
    • (1997) J. Biol. Chem , vol.272 , pp. 28001-28007
    • Yang, W.M.1    Yao, Y.L.2    Sun, J.M.3    Davie, J.R.4    Seto, E.5
  • 21
    • 0033609055 scopus 로고    scopus 로고
    • Three proteins define a class of human histone deacetylases related to yeast Hda1p
    • Grozinger, C.M.; Hassig, C.A.; Schreiber, S.L. Three proteins define a class of human histone deacetylases related to yeast Hda1p. Proc. Natl. Acad. Sci. USA 1999, 96, 4868–4873. [CrossRef] [PubMed]
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4868-4873
    • Grozinger, C.M.1    Hassig, C.A.2    Schreiber, S.L.3
  • 22
    • 0033964223 scopus 로고    scopus 로고
    • Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression
    • Kao, H.Y.; Downes, M.; Ordentlich, P.; Evans, R.M. Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression. Genes Dev. 2000, 14, 55–66. [PubMed]
    • (2000) Genes Dev , vol.14 , pp. 55-66
    • Kao, H.Y.1    Downes, M.2    Ordentlich, P.3    Evans, R.M.4
  • 23
    • 84997777002 scopus 로고    scopus 로고
    • Natural Compound Histone Deacetylase Inhibitors (HDACi): Synergy with Inflammatory Signalling Pathway Modulators and Clinical Applications in Cancer
    • Losson, H.; Schnekenburger, M.; Dicato, M.; Diederich, M. Natural Compound Histone Deacetylase Inhibitors (HDACi): Synergy with Inflammatory Signalling Pathway Modulators and Clinical Applications in Cancer. Molecules 2016, 21, 1608. [CrossRef] [PubMed]
    • (2016) Molecules , vol.21
    • Losson, H.1    Schnekenburger, M.2    Dicato, M.3    Diederich, M.4
  • 24
    • 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. [CrossRef] [PubMed]
    • (2009) J. Clin. Oncol , vol.27 , pp. 5459-5468
    • Lane, A.A.1    Chabner, B.A.2
  • 25
    • 30344477367 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and the promise of epigenetic (And more) treatments for cancer
    • Minucci, S.; Pelicci, P.G. Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer. Nat. Rev. Cancer 2006, 6, 38–51. [CrossRef] [PubMed]
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 38-51
    • Minucci, S.1    Pelicci, P.G.2
  • 27
    • 84866039617 scopus 로고    scopus 로고
    • Histone deacetylase modulators provided by Mother Nature
    • Seidel, C.; Schnekenburger, M.; Dicato, M.; Diederich, M. Histone deacetylase modulators provided by Mother Nature. Genes Nutr. 2012, 7, 357. [CrossRef] [PubMed]
    • (2012) Genes Nutr , vol.7
    • Seidel, C.1    Schnekenburger, M.2    Dicato, M.3    Diederich, M.4
  • 30
    • 16844362441 scopus 로고    scopus 로고
    • Histone deacetylation in epigenetics: An attractive target for anticancer therapy
    • Mai, A.; Massa, S.; Rotili, D.; Cerbara, I.; Valente, S.; Pezzi, R.; Simeoni, S.; Ragno, R. Histone deacetylation in epigenetics: An attractive target for anticancer therapy. Med. Res. Rev. 2005, 25, 261–309. [CrossRef] [PubMed]
    • (2005) Med. Res. Rev , vol.25 , pp. 261-309
    • Mai, A.1    Massa, S.2    Rotili, D.3    Cerbara, I.4    Valente, S.5    Pezzi, R.6    Simeoni, S.7    Ragno, R.8
  • 31
  • 32
    • 61849144810 scopus 로고    scopus 로고
    • HDAC family: What are the cancer relevant targets
    • Witt, O.; Deubzer, H.E.; Milde, T.; Oehme, I. HDAC family: What are the cancer relevant targets? Cancer Letters 2009, 277, 8–21. [CrossRef] [PubMed]
    • (2009) Cancer Letters , vol.277 , pp. 8-21
    • Witt, O.1    Deubzer, H.E.2    Milde, T.3    Oehme, I.4
  • 33
    • 38549157208 scopus 로고    scopus 로고
    • Association of patterns of class I histone deacetylase expression with patient prognosis in gastric cancer: A retrospective analysis
    • Weichert, W.; Roske, V.A.; Gekeler, T.; Beckers, M.P.; Ebert, M.; Pross, M.; Dietel, C.; Denkert, C.; Rocken, C. Association of patterns of class I histone deacetylase expression with patient prognosis in gastric cancer: A retrospective analysis. Lancet Oncol. 2008, 9, 139–148. [CrossRef]
    • (2008) Lancet Oncol , vol.9 , pp. 139-148
    • Weichert, W.1    Roske, V.A.2    Gekeler, T.3    Beckers, M.P.4    Ebert, M.5    Pross, M.6    Dietel, C.7    Denkert, C.8    Rocken, C.9
  • 34
    • 38949086502 scopus 로고    scopus 로고
    • Histone deacetylases 1, 2 and 3 are highly expressed in prostate cancer and HDAC2 expression is associated with shorter PSA relapse time after radical prostatectomy
    • Weichert, W.; Roske, A.; Gekeler, V.; Beckers, T.; Stephan, C.; Jung, K.; Fritzsche, F.R.; Niesporek, S.; Denkert, C.; Dietel, M.; Kristiansen, G. Histone deacetylases 1, 2 and 3 are highly expressed in prostate cancer and HDAC2 expression is associated with shorter PSA relapse time after radical prostatectomy. Br. J. Cancer 2008, 98, 604–610. [CrossRef] [PubMed]
    • (2008) Br. J. Cancer , vol.98 , pp. 604-610
    • Weichert, W.1    Roske, A.2    Gekeler, V.3    Beckers, T.4    Stephan, C.5    Jung, K.6    Fritzsche, F.R.7    Niesporek, S.8    Denkert, C.9    Dietel, M.10    Kristiansen, G.11
  • 35
    • 41549159879 scopus 로고    scopus 로고
    • Histone deacetylase expression has independent prognostic impact in human colorectal cancer: Specific role of class I histone deacetylases in vitro and in vivo
    • Weichert, W.; Roske, A.; Niesporek, S.; Noske, A.; Buckendahl, A.C.; Dietel, M.; Gekeler, V.; Boehm, M.; Beckers, T.; Denkert, C. Class I histone deacetylase expression has independent prognostic impact in human colorectal cancer: Specific role of class I histone deacetylases in vitro and in vivo. Clin. Cancer Res. 2008, 14, 1669–1677. [CrossRef] [PubMed]
    • (2008) Clin. Cancer Res , vol.14 , pp. 1669-1677
    • Weichert, W.1    Roske, A.2    Niesporek, S.3    Noske, A.4    Buckendahl, A.C.5    Dietel, M.6    Gekeler, V.7    Boehm, M.8    Beckers, T.9    Denkert, C.10    Class, I.11
  • 36
    • 37049001617 scopus 로고    scopus 로고
    • Clinical significance of histone deacetylase 1 expression in patients with hepatocellular carcinoma
    • Rikimaru, T.; Taketomi, A.; Yamashita, Y.; Shirabe, K.; Hamatsu, T.; Shimada, M.; Maehara, Y. Clinical significance of histone deacetylase 1 expression in patients with hepatocellular carcinoma. Oncology 2007, 72, 69–74. [CrossRef] [PubMed]
    • (2007) Oncology , vol.72 , pp. 69-74
    • Rikimaru, T.1    Taketomi, A.2    Yamashita, Y.3    Shirabe, K.4    Hamatsu, T.5    Shimada, M.6    Maehara, Y.7
  • 38
    • 84994225360 scopus 로고    scopus 로고
    • HDAC and HDAC Inhibitor: From Cancer to Cardiovascular Diseases
    • Yoon, S.; Eom, G.H. HDAC and HDAC Inhibitor: From Cancer to Cardiovascular Diseases. Chonnam Med. J. 2016, 52, 1–11. [CrossRef] [PubMed]
    • (2016) Chonnam Med. J , vol.52 , pp. 1-11
    • Yoon, S.1    Eom, G.H.2
  • 42
    • 34547753111 scopus 로고    scopus 로고
    • Histone deacetylase 1 gene expression and sensitization of multidrug-resistant neuroblastoma cell lines to cytotoxic agents by depsipeptide
    • Keshelava, N.; Davicioni, E.; Wan, Z.; Ji, L.; Sposto, R.; Triche, T.J.; Reynolds, C.P. Histone deacetylase 1 gene expression and sensitization of multidrug-resistant neuroblastoma cell lines to cytotoxic agents by depsipeptide. J. Natl. Cancer Inst. 2007, 99, 1107–1119. [CrossRef] [PubMed]
    • (2007) J. Natl. Cancer Inst , vol.99 , pp. 1107-1119
    • Keshelava, N.1    Davicioni, E.2    Wan, Z.3    Ji, L.4    Sposto, R.5    Triche, T.J.6    Reynolds, C.P.7
  • 43
    • 17144378591 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase 2 increases apoptosis and p21Cip1/WAF1 expression, independent of histone deacetylase
    • Huang, B.H.; Laban, M.; Leung, C.H.; Lee, L.; Lee, C.K.; Salto-Tellez, M.; Raju, G.C.; Hooi, S.C. Inhibition of histone deacetylase 2 increases apoptosis and p21Cip1/WAF1 expression, independent of histone deacetylase. Cell Death Differ. 2005, 12, 395–404. [CrossRef] [PubMed]
    • (2005) Cell Death Differ , vol.12 , pp. 395-404
    • Huang, B.H.1    Laban, M.2    Leung, C.H.3    Lee, L.4    Lee, C.K.5    Salto-Tellez, M.6    Raju, G.C.7    Hooi, S.C.8
  • 44
    • 34248208217 scopus 로고    scopus 로고
    • Histone deacetylase 2 modulates p53 transcriptional activities through regulation of p53-DNA binding activity
    • Harms, K.L.; Chen, X. Histone deacetylase 2 modulates p53 transcriptional activities through regulation of p53-DNA binding activity. Cancer Res. 2007, 67, 3145–3152. [CrossRef] [PubMed]
    • (2007) Cancer Res , vol.67 , pp. 3145-3152
    • Harms, K.L.1    Chen, X.2
  • 45
    • 84892942381 scopus 로고    scopus 로고
    • New and emerging HDAC inhibitors for cancer treatment
    • West, A.C.; Johnstone, R.W. New and emerging HDAC inhibitors for cancer treatment. J. Clin. Investig. 2014, 124, 30–39. [CrossRef] [PubMed]
    • (2014) J. Clin. Investig , vol.124 , pp. 30-39
    • West, A.C.1    Johnstone, R.W.2
  • 47
    • 33744522801 scopus 로고    scopus 로고
    • Histone deacetylase 3 (HDAC3) is recruited to target promoters by PML-RARa as a component of the N-CoR co-repressor complex to repress transcription in vivo
    • Atsumi, A.; Tomita, A.; Kiyoi, H.; Naoe, T. Histone deacetylase 3 (HDAC3) is recruited to target promoters by PML-RARa as a component of the N-CoR co-repressor complex to repress transcription in vivo. Biochem. Biophys. Res. Commun. 2006, 345, 1471–1480. [CrossRef] [PubMed]
    • (2006) Biochem. Biophys. Res. Commun , vol.345 , pp. 1471-1480
    • Atsumi, A.1    Tomita, A.2    Kiyoi, H.3    Naoe, T.4
  • 50
    • 33745822471 scopus 로고    scopus 로고
    • Histone deacetylase 8 safeguards the human ever-shorter telomeres 1B (HEST1B) protein from ubiquitin-mediated degradation
    • Lee, H.; Sengupta, N.; Villagra, A.; Rezai-Zadeh, N.; Seto, E. Histone deacetylase 8 safeguards the human ever-shorter telomeres 1B (hEST1B) protein from ubiquitin-mediated degradation. Mol. Cell. Biol. 2006, 26, 5259–5269. [CrossRef] [PubMed]
    • (2006) Mol. Cell. Biol , vol.26 , pp. 5259-5269
    • Lee, H.1    Sengupta, N.2    Villagra, A.3    Rezai-Zadeh, N.4    Seto, E.5
  • 53
    • 80055077899 scopus 로고    scopus 로고
    • HDAC4 protein regulates HIF1alpha protein lysine acetylation and cancer cell response to hypoxia
    • Geng, H.; Harvey, C.T.; Pittsenbarger, J.; Liu, Q.; Beer, T.M.; Xue, C.; Qian, D.Z. HDAC4 protein regulates HIF1alpha protein lysine acetylation and cancer cell response to hypoxia. J. Biol. Chem. 2011, 286, 38095–38102. [CrossRef] [PubMed]
    • (2011) J. Biol. Chem , vol.286 , pp. 38095-38102
    • Geng, H.1    Harvey, C.T.2    Pittsenbarger, J.3    Liu, Q.4    Beer, T.M.5    Xue, C.6    Qian, D.Z.7
  • 56
    • 0346688568 scopus 로고    scopus 로고
    • Altered interaction of HDAC5 with GATA-1 during MEL cell differentiation
    • Watamoto, K.; Towatari, M.; Ozawa, Y.; Miyata, Y.; Okamoto, M.; Abe, A.; Naoe, T.; Saito, H. Altered interaction of HDAC5 with GATA-1 during MEL cell differentiation. Oncogene 2003, 22, 9176–9184. [CrossRef] [PubMed]
    • (2003) Oncogene , vol.22 , pp. 9176-9184
    • Watamoto, K.1    Towatari, M.2    Ozawa, Y.3    Miyata, Y.4    Okamoto, M.5    Abe, A.6    Naoe, T.7    Saito, H.8
  • 57
    • 4544322261 scopus 로고    scopus 로고
    • Reduced expression of class II histone deacetylase genes is associated with poor prognosis in lung cancer patients
    • Osada, H.; Tatematsu, Y.; Saito, H.; Yatabe, Y.; Mitsudomi, T.; Takahashi, T. Reduced expression of class II histone deacetylase genes is associated with poor prognosis in lung cancer patients. Int. J. Cancer 2004, 112, 26–32. [CrossRef] [PubMed]
    • (2004) Int. J. Cancer , vol.112 , pp. 26-32
    • Osada, H.1    Tatematsu, Y.2    Saito, H.3    Yatabe, Y.4    Mitsudomi, T.5    Takahashi, T.6
  • 59
    • 79953157671 scopus 로고    scopus 로고
    • Histone deacetylases 9 and 10 are required for homologous recombination
    • Kotian, S.; Liyanarachchi, S.; Zelent, A.; Parvin, J.D. Histone deacetylases 9 and 10 are required for homologous recombination. J. Biol. Chem. 2011, 286, 7722–7726. [CrossRef] [PubMed]
    • (2011) J. Biol. Chem , vol.286 , pp. 7722-7726
    • Kotian, S.1    Liyanarachchi, S.2    Zelent, A.3    Parvin, J.D.4
  • 62
    • 34547882857 scopus 로고    scopus 로고
    • Aberrant expression of histone deacetylase 6 in oral squamous cell carcinoma
    • Sakuma, T.; Uzawa, K.; Onda, T.; Shiiba, M.; Yokoe, H.; Shibahara, T.; Tanzawa, H. Aberrant expression of histone deacetylase 6 in oral squamous cell carcinoma. Int. J. Oncol. 2006, 29, 117–124. [CrossRef] [PubMed]
    • (2006) Int. J. Oncol , vol.29 , pp. 117-124
    • Sakuma, T.1    Uzawa, K.2    Onda, T.3    Shiiba, M.4    Yokoe, H.5    Shibahara, T.6    Tanzawa, H.7
  • 63
    • 0344640906 scopus 로고    scopus 로고
    • Domain-selective small-molecule inhibitor of histone deacetylase 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 deacetylase 6 (HDAC6)-mediated tubulin deacetylation. Proc. Natl. Acad. Sci. USA 2003, 100, 4389–4394. [CrossRef] [PubMed]
    • (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
  • 64
    • 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
    • Bali, P.; Pranpat, M.; Bradner, J.; Balasis, M.; Fiskus, W.; Guo, F.; Rocha, K.; Kumaraswamy, S.; Boyapalle, S.; Atadja, P.; et al. 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. [CrossRef] [PubMed]
    • (2005) J. Biol. Chem , vol.280 , 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
  • 66
    • 78651502605 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase 10 induces thioredoxin-interacting protein and causes accumulation of reactive oxygen species in SNU-620 human gastric cancer cells
    • Lee, J.H.; Jeong, E.G.; Choi, M.C.; Kim, S.H.; Park, J.H.; Song, S.H.; Park, J.; Bang, Y.J.; Kim, T.Y. Inhibition of histone deacetylase 10 induces thioredoxin-interacting protein and causes accumulation of reactive oxygen species in SNU-620 human gastric cancer cells. Mol. Cell. 2010, 30, 107–112. [CrossRef] [PubMed]
    • (2010) Mol. Cell , vol.30 , pp. 107-112
    • Lee, J.H.1    Jeong, E.G.2    Choi, M.C.3    Kim, S.H.4    Park, J.H.5    Song, S.H.6    Park, J.7    Bang, Y.J.8    Kim, T.Y.9
  • 67
    • 84927132915 scopus 로고    scopus 로고
    • Vascular endothelial growth factor and angiogenesis in the regulation of cutaneous wound repair
    • Johnson, E.K.; Wilgus, A.T. Vascular endothelial growth factor and angiogenesis in the regulation of cutaneous wound repair. Adv. Wound Care (New Rochelle), 2014, 3, 647–661. [CrossRef] [PubMed]
    • (2014) Adv. Wound Care (New Rochelle) , vol.3 , pp. 647-661
    • Johnson, E.K.1    Wilgus, A.T.2
  • 68
    • 39549088498 scopus 로고    scopus 로고
    • Class II histone deacetylases play pivotal roles in heat shock protein 90-mediated proteasomal degradation of vascular endothelial growth factor receptors. Biochem. Biophys. Res
    • Park, J.H.; Kim, S.H.; Choi, M.C.; Lee, J.; Oh, D.Y.; Im, S.A.; Bang, Y.J.; Kim, T.Y. Class II histone deacetylases play pivotal roles in heat shock protein 90-mediated proteasomal degradation of vascular endothelial growth factor receptors. Biochem. Biophys. Res. Commun. 2008, 368, 318–322. [CrossRef] [PubMed]
    • (2008) Commun , vol.368 , pp. 318-322
    • Park, J.H.1    Kim, S.H.2    Choi, M.C.3    Lee, J.4    Oh, D.Y.5    Im, S.A.6    Bang, Y.J.7    Kim, T.Y.8
  • 69
    • 27144475816 scopus 로고    scopus 로고
    • Histone deacetylases in acute myeloid leukaemia show a distinctive pattern of expression that changes selectively in response to deacetylase inhibitors
    • Bradbury, C.A.; Khanim, F.L.; Hayden, R.; Bunce, C.M.; White, D.A.; Drayson, M.T.; Craddock, C.; Turner, B.M. Histone deacetylases in acute myeloid leukaemia show a distinctive pattern of expression that changes selectively in response to deacetylase inhibitors. Leukemia 2005, 19, 1751–1759. [CrossRef] [PubMed]
    • (2005) Leukemia , vol.19 , pp. 1751-1759
    • Bradbury, C.A.1    Khanim, F.L.2    Hayden, R.3    Bunce, C.M.4    White, D.A.5    Drayson, M.T.6    Craddock, C.7    Turner, B.M.8
  • 70
    • 34247570492 scopus 로고    scopus 로고
    • Strong expression of a longevity-related protein, SIRT1, in Bowen’s disease
    • Hida, Y.; Kubo, Y.; Murao, K.; Arase, S. Strong expression of a longevity-related protein, SIRT1, in Bowen’s disease. Arch. Dermatol. Res. 2007, 299, 103–106. [CrossRef] [PubMed]
    • (2007) Arch. Dermatol. Res , vol.299 , pp. 103-106
    • Hida, Y.1    Kubo, Y.2    Murao, K.3    Arase, S.4
  • 75
    • 85048322603 scopus 로고    scopus 로고
    • Role for human SIRT2 NAD-dependent class II histone deacetylases in a Sin3-independent repression pathway
    • Dryden, S.C.; Nahhas, F.A.; Nowak, J.E.; Goustin, A.S.; Tainsky, M.A. Role for human SIRT2 NAD-dependent class II histone deacetylases in a Sin3-independent repression pathway. Genes Dev. 2003, 14, 45–54.
    • (2003) Genes Dev , vol.14 , pp. 45-54
    • Dryden, S.C.1    Nahhas, F.A.2    Nowak, J.E.3    Goustin, A.S.4    Tainsky, M.A.5
  • 76
    • 28544451205 scopus 로고    scopus 로고
    • Control of multidrug resistance gene mdr1 and cancer resistance to chemotherapy by the longevity gene sirt1
    • Chu, F.; Chou, P.M.; Zheng, X.; Mirkin, B.L.; Rebbaa, A. Control of multidrug resistance gene mdr1 and cancer resistance to chemotherapy by the longevity gene sirt1. Cancer Res. 2005, 65, 10183–10187. [CrossRef] [PubMed]
    • (2005) Cancer Res , vol.65 , pp. 10183-10187
    • Chu, F.1    Chou, P.M.2    Zheng, X.3    Mirkin, B.L.4    Rebbaa, A.5
  • 78
    • 79959819034 scopus 로고    scopus 로고
    • SirT3 suppresses hypoxia inducible factor 1alpha and tumor growth by inhibiting mitochondrial ROS production
    • Bell, E.L.; Emerling, B.M.; Ricoult, S.J.; Guarente, L. SirT3 suppresses hypoxia inducible factor 1alpha and tumor growth by inhibiting mitochondrial ROS production. Oncogene 2011, 30, 2986–2996. [CrossRef] [PubMed]
    • (2011) Oncogene , vol.30 , pp. 2986-2996
    • Bell, E.L.1    Emerling, B.M.2    Ricoult, S.J.3    Guarente, L.4
  • 79
    • 84855464431 scopus 로고    scopus 로고
    • Increased gene expression of histone deacetylases in patients with Philadelphia-negative chronic myeloproliferative neoplasms
    • Skov, V.; Larsen, T.S.; Thomassen, M.; Riley, C.H.; Jensen, M.K.; Bjerrum, O.W.; Kruse, T.A.; Hasselbalch, H.C. Increased gene expression of histone deacetylases in patients with Philadelphia-negative chronic myeloproliferative neoplasms. Leuk. Lymphoma 2012, 53, 123–129. [CrossRef] [PubMed]
    • (2012) Leuk. Lymphoma , vol.53 , pp. 123-129
    • Skov, V.1    Larsen, T.S.2    Thomassen, M.3    Riley, C.H.4    Jensen, M.K.5    Bjerrum, O.W.6    Kruse, T.A.7    Hasselbalch, H.C.8
  • 80
    • 0037067696 scopus 로고    scopus 로고
    • Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family
    • Gao, L.; Cueto, M.A.; Asselbergs, F.; Atadja, P. Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family. J. Biol. Chem. 2002, 277, 25748–25755. [CrossRef] [PubMed]
    • (2002) J. Biol. Chem , vol.277 , pp. 25748-25755
    • Gao, L.1    Cueto, M.A.2    Asselbergs, F.3    Atadja, P.4
  • 81
    • 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 1977, 268, 462–464. [CrossRef] [PubMed]
    • (1977) Nature , vol.268 , pp. 462-464
    • Riggs, M.G.1    Whittaker, R.G.2    Neumann, J.R.3    Ingram, V.M.4
  • 82
    • 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 inhibitor of mammalian histone deacetylase. J. Biol. Chem. 1993, 268, 22429–22435. [PubMed]
    • (1993) J. Biol. Chem , vol.268 , pp. 22429-22435
    • Kijima, M.1    Yoshida, M.2    Sugita, K.3    Horinouchi, S.4    Beppu, T.5
  • 83
    • 84991325493 scopus 로고    scopus 로고
    • HDACs and HDAC Inhibitors in Cancer Development and Therapy
    • Li, Y.; Seto, E. HDACs and HDAC Inhibitors in Cancer Development and Therapy. Cold Spring Harb. Perspect. Med. 2016, 6, 10. [CrossRef] [PubMed]
    • (2016) Cold Spring Harb. Perspect. Med , vol.6 , pp. 10
    • Li, Y.1    Seto, E.2
  • 86
    • 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. [PubMed]
    • (1990) J. Biol. Chem , vol.265 , pp. 17174-17179
    • Yoshida, M.1    Kijima, M.2    Akita, M.3    Beppu, T.4
  • 87
    • 0019132555 scopus 로고
    • Butyrate and related inhibitors of histone deacetylation block the induction of egg white genes by steroid harmones
    • Mcknight, G.S.; Hanger, L.; Palmiter, R.D. Butyrate and related inhibitors of histone deacetylation block the induction of egg white genes by steroid harmones. Cell 1980, 22, 469–477. [CrossRef]
    • (1980) Cell , vol.22 , pp. 469-477
    • McKnight, G.S.1    Hanger, L.2    Palmiter, R.D.3
  • 90
    • 84884297896 scopus 로고    scopus 로고
    • Histone deacetylase (HDAC) inhibitory and antiproliferative activities of phenolic-rich extracts derived from the rhizome of Hydnophytum formicarum Jack.: Sinapinic acid acts as HDAC inhibitor
    • Senawong, T.; Misuna, S.; Khaopha, S.; Nuchadomrong, S.; Sawatsitang, P.; Phaosiri, C.; Surapaitoon, A.; Sripa, B. Histone deacetylase (HDAC) inhibitory and antiproliferative activities of phenolic-rich extracts derived from the rhizome of Hydnophytum formicarum Jack.: Sinapinic acid acts as HDAC inhibitor. BMC Complement. Altern. Med. 2013, 13, 232. [CrossRef] [PubMed]
    • (2013) BMC Complement. Altern. Med , vol.13 , pp. 232
    • Senawong, T.1    Misuna, S.2    Khaopha, S.3    Nuchadomrong, S.4    Sawatsitang, P.5    Phaosiri, C.6    Surapaitoon, A.7    Sripa, B.8
  • 91
    • 84883340186 scopus 로고    scopus 로고
    • Resveratrol as a pan-HDAC inhibitor alters the acetylation status of histone [corrected] proteins in human-derived hepatoblastoma cells
    • Venturelli, S.; Berger, A.; Bocker, A.; Busch, C.; Weiland, T.; Noor, S.; Leischner, C.; Schleicher, S.; Mayer, M.; Weiss, T.S.; et al. Resveratrol as a pan-HDAC inhibitor alters the acetylation status of histone [corrected] proteins in human-derived hepatoblastoma cells. PLoS ONE 2013, 8, 73097. [CrossRef]
    • (2013) Plos ONE , vol.8
    • Venturelli, S.1    Berger, A.2    Bocker, A.3    Busch, C.4    Weiland, T.5    Noor, S.6    Leischner, C.7    Schleicher, S.8    Mayer, M.9    Weiss, T.S.10
  • 92
    • 84923345812 scopus 로고    scopus 로고
    • Aeroside VIII is a natural selective HDAC6 inhibitor that synergistically enhances the anticancer activity of HDAC inhibitor in HT29 cells
    • Ryu, H.W.; Lee, D.H.; Shin, D.H.; Kim, S.H.; Kwon, S.H. Aeroside VIII is a natural selective HDAC6 inhibitor that synergistically enhances the anticancer activity of HDAC inhibitor in HT29 cells. Planta Med. 2015, 81, 222–227. [CrossRef] [PubMed]
    • (2015) Planta Med , vol.81 , pp. 222-227
    • Ryu, H.W.1    Lee, D.H.2    Shin, D.H.3    Kim, S.H.4    Kwon, S.H.5
  • 96
    • 0025673805 scopus 로고
    • Isolation and structural elucidation of new cyclotetrapeptides, trapoxins A and B, having detransformation activities as antitumor agents
    • Itazaki, H.; Nagashima, K.; Sugita, K.; Yoshida, H.; Kawamura, Y.; Yasuda, Y.; Matsumoto, K.; Ishii, K.; Uotani, N.; Nakai, H.; et al. Isolation and structural elucidation of new cyclotetrapeptides, trapoxins A and B, having detransformation activities as antitumor agents. J. Antibiot. 1990, 43, 1524–1532. [CrossRef] [PubMed]
    • (1990) J. Antibiot , vol.43 , pp. 1524-1532
    • Itazaki, H.1    Nagashima, K.2    Sugita, K.3    Yoshida, H.4    Kawamura, Y.5    Yasuda, Y.6    Matsumoto, K.7    Ishii, K.8    Uotani, N.9    Nakai, H.10
  • 99
    • 55949099039 scopus 로고    scopus 로고
    • Enantioselective total synthesis of (+)-largazole, a potent inhibitor of histone deacetylase
    • Ghosh, A.K.; Kulkarni, S. Enantioselective total synthesis of (+)-largazole, a potent inhibitor of histone deacetylase. Org. Lett. 2008, 10, 3907–3909. [CrossRef] [PubMed]
    • (2008) Org. Lett , vol.10 , pp. 3907-3909
    • Ghosh, A.K.1    Kulkarni, S.2
  • 100
    • 3242755145 scopus 로고    scopus 로고
    • Diallyl disulfide (DADS) increases histone acetylation and p21(waf1/cip1) expression in human colon tumor cell lines
    • Druesne, N.; Pagniez, A.; Mayeur, C.; Thomas, M.; Cherbuy, C.; Duee, P.H.; Martel, P.; Chaumontet, C. Diallyl disulfide (DADS) increases histone acetylation and p21(waf1/cip1) expression in human colon tumor cell lines. Carcinogenesis 2004, 25, 1227–1236. [CrossRef] [PubMed]
    • (2004) Carcinogenesis , vol.25 , pp. 1227-1236
    • Druesne, N.1    Pagniez, A.2    Mayeur, C.3    Thomas, M.4    Cherbuy, C.5    Duee, P.H.6    Martel, P.7    Chaumontet, C.8
  • 101
    • 0036437194 scopus 로고    scopus 로고
    • DesBordes, C. Induction of histone acetylation and inhibition of growth of mouse erythroleukemia cells by S-allylmercaptocysteine
    • Lea, M.A.; Rasheed, M.; Randolph, V.M.; Khan, F.; Shareef, A.; desBordes, C. Induction of histone acetylation and inhibition of growth of mouse erythroleukemia cells by S-allylmercaptocysteine. Nutr. Cancer 2002, 43, 90–102. [CrossRef] [PubMed]
    • (2002) Nutr. Cancer , vol.43 , pp. 90-102
    • Lea, M.A.1    Rasheed, M.2    Randolph, V.M.3    Khan, F.4    Shareef, A.5
  • 102
    • 84874410182 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors (HDACIs): Multitargeted anticancer agents
    • Ververis, K.; Hiong, A.; Karagiannis, T.C.; Licciardi, P.V. Histone deacetylase inhibitors (HDACIs): Multitargeted anticancer agents. Biologics 2013, 7, 47–60. [CrossRef] [PubMed]
    • (2013) Biologics , vol.7 , pp. 47-60
    • Ververis, K.1    Hiong, A.2    Karagiannis, T.C.3    Licciardi, P.V.4
  • 103
    • 84904857496 scopus 로고    scopus 로고
    • The class I HDAC inhibitor romidepsin targets inflammatory breast cancer tumor emboli and synergizes with paclitaxel to inhibit metastasis
    • Robertson, F.M.; Chu, K.; Boley, K.M.; Ye, Z.; Liu, H.; Wright, M.C.; Moraes, R.; Zhang, X.; Green, T.L.; Barsky, S.H.; et al. The class I HDAC inhibitor romidepsin targets inflammatory breast cancer tumor emboli and synergizes with paclitaxel to inhibit metastasis. J. Exp. Ther. Oncol. 2013, 10, 219–233. [PubMed]
    • (2013) J. Exp. Ther. Oncol , vol.10 , pp. 219-233
    • Robertson, F.M.1    Chu, K.2    Boley, K.M.3    Ye, Z.4    Liu, H.5    Wright, M.C.6    Moraes, R.7    Zhang, X.8    Green, T.L.9    Barsky, S.H.10
  • 104
    • 84991442304 scopus 로고    scopus 로고
    • Combining the pan-aurora kinase inhibitor AMG 900 with histone deacetylase inhibitors enhances antitumor activity in prostate cancer
    • Paller, C.J.; Wissing, M.D.; Mendonca, J.; Sharma, A.; Kim, E.; Kim, H.S.; Kortenhorst, M.S.Q.; Gerber, S.; Rosen, M.; Shaikh, F.; et al. Combining the pan-aurora kinase inhibitor AMG 900 with histone deacetylase inhibitors enhances antitumor activity in prostate cancer. Cancer Med. 2014, 3, 1322–1335. [CrossRef] [PubMed]
    • (2014) Cancer Med , vol.3 , pp. 1322-1335
    • Paller, C.J.1    Wissing, M.D.2    Mendonca, J.3    Sharma, A.4    Kim, E.5    Kim, H.S.6    Kortenhorst, M.S.Q.7    Gerber, S.8    Rosen, M.9    Shaikh, F.10
  • 105
    • 84988842020 scopus 로고    scopus 로고
    • HDAC inhibitors in solid tumors and blood cancers
    • Ferrarelli, L.K. HDAC inhibitors in solid tumors and blood cancers. Sci. Signal. 2016, 9, ec216. [CrossRef]
    • (2016) Sci. Signal , vol.9
    • Ferrarelli, L.K.1
  • 106
    • 85037662256 scopus 로고    scopus 로고
    • Combination Therapies Targeting HDAC and IKK in Solid Tumors
    • Vancurova, I.; Uddin, M.M.; Zou, Y.; Vancura, A. Combination Therapies Targeting HDAC and IKK in Solid Tumors. Trends Pharmacol. Sci. 2018, 39, 295–306. [CrossRef] [PubMed]
    • (2018) Trends Pharmacol. Sci , vol.39 , pp. 295-306
    • Vancurova, I.1    Uddin, M.M.2    Zou, Y.3    Vancura, A.4
  • 107
    • 33846122993 scopus 로고    scopus 로고
    • Dimethyl sulfoxide to vorinostat: Development of this histone deacetylase inhibitor as an anticancer drug
    • Marks, P.A.; Breslow, R. Dimethyl sulfoxide to vorinostat: Development of this histone deacetylase inhibitor as an anticancer drug. Nat. Biotechnol. 2007, 25, 84–90. [CrossRef] [PubMed]
    • (2007) Nat. Biotechnol , vol.25 , pp. 84-90
    • Marks, P.A.1    Breslow, R.2
  • 109
    • 84872107995 scopus 로고    scopus 로고
    • Panobinostat activity in both bexarotene- exposed and -naive patients with refractory cutaneous T-cell lymphoma: Results of a phase II trial
    • Duvic, M.; Dummer, R.; Becker, J.C.; Poulalhon, N.; Ortiz Romero, P.; Grazia Bernengo, M.; Lebbé, C.; Assaf, C.; Squier, M.; Williams, D.; et al. Panobinostat activity in both bexarotene- exposed and -naive patients with refractory cutaneous T-cell lymphoma: Results of a phase II trial. Eur. J. Cancer 2013, 49, 386–394. [CrossRef] [PubMed]
    • (2013) Eur. J. Cancer , vol.49 , pp. 386-394
    • Duvic, M.1    Dummer, R.2    Becker, J.C.3    Poulalhon, N.4    Ortiz Romero, P.5    Grazia Bernengo, M.6    Lebbé, C.7    Assaf, C.8    Squier, M.9    Williams, D.10
  • 110
    • 77955168425 scopus 로고    scopus 로고
    • A pilot study of the Histone-Deacetylase inhibitor Givinostat in patients with JAK2V617F positive chronic myeloproliferative neoplasms
    • Rambaldi, A.; Dummer, R.; Becker, J.C.; Poulalhon, N.; Ortiz, R.P.; Grazia, B.M.; Lebbe, C.; Assaf, C.; Squier, M.; Williams, D.; et al. A pilot study of the Histone-Deacetylase inhibitor Givinostat in patients with JAK2V617F positive chronic myeloproliferative neoplasms. Br. J. Haematol. 2010, 150, 446–455. [CrossRef] [PubMed]
    • (2010) Br. J. Haematol , vol.150 , pp. 446-455
    • Rambaldi, A.1    Dummer, R.2    Becker, J.C.3    Poulalhon, N.4    Ortiz, R.P.5    Grazia, B.M.6    Lebbe, C.7    Assaf, C.8    Squier, M.9    Williams, D.10
  • 111
    • 79952280909 scopus 로고    scopus 로고
    • Phase I clinical, pharmacokinetic and pharmacodynamic study of SB939, an oral histone deacetylase (HDAC) inhibitor, in patients with advanced solid tumours
    • Razak, A.R.; Hotte, S.J.; Siu, L.L.; Chen, E.X.; Hirte, H.W.; Powers, J.; Walsh, W.; Stayner, L.A.; Laughlin, A.; Novotny-Diermayr, V.; et al. Phase I clinical, pharmacokinetic and pharmacodynamic study of SB939, an oral histone deacetylase (HDAC) inhibitor, in patients with advanced solid tumours. Br. J. Cancer 2011, 104, 756–762. [CrossRef] [PubMed]
    • (2011) Br. J. Cancer , vol.104 , pp. 756-762
    • Razak, A.R.1    Hotte, S.J.2    Siu, L.L.3    Chen, E.X.4    Hirte, H.W.5    Powers, J.6    Walsh, W.7    Stayner, L.A.8    Laughlin, A.9    Novotny-Diermayr, V.10
  • 112
    • 84855340600 scopus 로고    scopus 로고
    • Study of the histone deacetylase inhibitor entinostat in combination with 13-cis retinoic acid in patients with solid tumours
    • Pili, R.; Salumbides, B.; Zhao, M.; Altiok, S.; Qian, D.; Zwiebel, J.; Carducci, M.A.; Rudek, M.A. Phase I study of the histone deacetylase inhibitor entinostat in combination with 13-cis retinoic acid in patients with solid tumours. Br. J. Cancer 2012, 106, 77–84. [CrossRef] [PubMed]
    • (2012) Br. J. Cancer , vol.106 , pp. 77-84
    • Pili, R.1    Salumbides, B.2    Zhao, M.3    Altiok, S.4    Qian, D.5    Zwiebel, J.6    Carducci, M.A.7    Rudek, M.A.8    Phase, I.9
  • 113
    • 84860524932 scopus 로고    scopus 로고
    • A phase I pharmacokinetic and pharmacodynamics study of CHR-3996, an oral class I selective histone deacetylase inhibitor in refractory solid tumors
    • Banerji, U.; van Doorn, L.; Papadatos-Pastos, D.; Kristeleit, R.; Debnam, P.; Tall, M.; Stewart, A.; Raynaud, F.; Garrett, M.D.; Toal, M.; et al. A phase I pharmacokinetic and pharmacodynamics study of CHR-3996, an oral class I selective histone deacetylase inhibitor in refractory solid tumors. Clin. Cancer Res. 2012, 18, 2687–2694. [CrossRef] [PubMed]
    • (2012) Clin. Cancer Res , vol.18 , pp. 2687-2694
    • Banerji, U.1    Van Doorn, L.2    Papadatos-Pastos, D.3    Kristeleit, R.4    Debnam, P.5    Tall, M.6    Stewart, A.7    Raynaud, F.8    Garrett, M.D.9    Toal, M.10
  • 114
    • 84863795223 scopus 로고    scopus 로고
    • Phase I study of chidamide (CS055/HBI-8000), a new histone deacetylase inhibitor, in patients with advanced solid tumors and lymphomas
    • Dong, M.; Ning, Z.Q.; Xing, P.Y.; Xu, J.L.; Cao, H.X.; Dou, G.F.; Meng, Z.Y.; Shi, Y.K.; Lu, X.P.; Feng, F.Y. Phase I study of chidamide (CS055/HBI-8000), a new histone deacetylase inhibitor, in patients with advanced solid tumors and lymphomas. Cancer Chemother. Pharmacol. 2012, 69, 1413–1422. [CrossRef] [PubMed]
    • (2012) Cancer Chemother. Pharmacol , vol.69 , pp. 1413-1422
    • Dong, M.1    Ning, Z.Q.2    Xing, P.Y.3    Xu, J.L.4    Cao, H.X.5    Dou, G.F.6    Meng, Z.Y.7    Shi, Y.K.8    Lu, X.P.9    Feng, F.Y.10
  • 117
    • 84857522968 scopus 로고    scopus 로고
    • Results from a pivotal, open-label, phase II study of romidepsin in relapsed or refractory peripheral T-cell lymphoma after prior systemic therapy
    • Coiffier, B.; Pro, B.; Prince, H.M.; Foss, F.; Sokol, L.; Greenwood, M.; Caballero, D.; Borchmann, P.; Morschhauser, F.; Wilhelm, M.; et al. Results from a pivotal, open-label, phase II study of romidepsin in relapsed or refractory peripheral T-cell lymphoma after prior systemic therapy. J. Clin. Oncol. 2012, 30, 631–636. [CrossRef] [PubMed]
    • (2012) J. Clin. Oncol , vol.30 , pp. 631-636
    • Coiffier, B.1    Pro, B.2    Prince, H.M.3    Foss, F.4    Sokol, L.5    Greenwood, M.6    Caballero, D.7    Borchmann, P.8    Morschhauser, F.9    Wilhelm, M.10
  • 118
    • 33748451151 scopus 로고    scopus 로고
    • Anticancer activities of histone deacetylase inhibitors
    • Bolden, J.E.; Peart, M.J.; Johnstone, R.W. Anticancer activities of histone deacetylase inhibitors. Nat. Rev. Drug Discov. 2006, 5, 769–784. [CrossRef] [PubMed]
    • (2006) Nat. Rev. Drug Discov , vol.5 , pp. 769-784
    • Bolden, J.E.1    Peart, M.J.2    Johnstone, R.W.3
  • 119
    • 84978793036 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor induces cell apoptosis and cycle arrest in lung cancer cell via mitochondrial injury and p53 up-acetylation
    • Bao, L.; Diao, H.; Dong, N.; Xu, S.; Wang, B.; Mo, Q.; Yu, H.; Wang, X.; Chen, C. Histone deacetylase inhibitor induces cell apoptosis and cycle arrest in lung cancer cell via mitochondrial injury and p53 up-acetylation. Cell Biol. Toxicol. 2016, 32, 469–482. [CrossRef] [PubMed]
    • (2016) Cell Biol. Toxicol , vol.32 , pp. 469-482
    • Bao, L.1    Diao, H.2    Dong, N.3    Xu, S.4    Wang, B.5    Mo, Q.6    Yu, H.7    Wang, X.8    Chen, C.9
  • 120
    • 84859744612 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in cell pluripotency, differentiation, and reprogramming
    • Kretsovali, A.; Hadjimichael, C.; Charmpilas, N. Histone deacetylase inhibitors in cell pluripotency, differentiation, and reprogramming. Stem Cells Int. 2012, 2012, 184154. [CrossRef] [PubMed]
    • (2012) Stem Cells Int , vol.2012
    • Kretsovali, A.1    Hadjimichael, C.2    Charmpilas, N.3
  • 121
    • 0033604457 scopus 로고    scopus 로고
    • Induction of apoptosis in U937 human leukemia cells by suberoylanilide hydroxamic acid (SAHA) proceeds through pathways that are regulated by Bcl-2/Bcl-XL, c-Jun, and p21CIP1, but independent of p53
    • Vrana, J.A.; Decker, R.H.; Johnson, C.R.; Wang, Z.; Jarvis, W.D.; Richon, V.M.; Ehinger, M.; Fisher, P.B.; Grant, S. Induction of apoptosis in U937 human leukemia cells by suberoylanilide hydroxamic acid (SAHA) proceeds through pathways that are regulated by Bcl-2/Bcl-XL, c-Jun, and p21CIP1, but independent of p53. Oncogene 1999, 18, 7016–7025. [CrossRef] [PubMed]
    • (1999) Oncogene , vol.18 , pp. 7016-7025
    • Vrana, J.A.1    Decker, R.H.2    Johnson, C.R.3    Wang, Z.4    Jarvis, W.D.5    Richon, V.M.6    Ehinger, M.7    Fisher, P.B.8    Grant, S.9
  • 122
    • 0034730127 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation
    • Richon, V.M.; Sandhoff, T.W.; Rifkind, R.A.; Marks, P.A. Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation. Proc. Natl. Acad. Sci. USA 2000, 97, 10014–10019. [CrossRef] [PubMed]
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10014-10019
    • Richon, V.M.1    Sandhoff, T.W.2    Rifkind, R.A.3    Marks, P.A.4
  • 123
    • 34547864236 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Molecular mechanisms of action
    • Xu, W.S.; Parmigiani, R.B.; Marks, P.A. Histone deacetylase inhibitors: molecular mechanisms of action. Oncogene 2007, 26, 5541–5552. [CrossRef] [PubMed]
    • (2007) Oncogene , vol.26 , pp. 5541-5552
    • Xu, W.S.1    Parmigiani, R.B.2    Marks, P.A.3
  • 124
    • 85048337505 scopus 로고    scopus 로고
    • Hepatocellular carcinoma: Causes, mechanism of progression and biomarkers
    • Singh, A.K.; Kumar, R.; Pandey, A.K. Hepatocellular carcinoma: Causes, mechanism of progression and biomarkers. Curr. Chem. Genom. Transl. Med. 2018, Accepted-in press.
    • (2018) Curr. Chem. Genom. Transl. Med
    • Singh, A.K.1    Kumar, R.2    Pandey, A.K.3
  • 125
    • 0242458252 scopus 로고    scopus 로고
    • P15 (INK4b) in HDAC inhibitor-induced growth arrest
    • Hitomi, T.; Matsuzaki, Y.; Yokota, T.; Takaoka, Y.; Sakai, T. p15 (INK4b) in HDAC inhibitor-induced growth arrest. FEBS Lett 2003, 554, 347–350. [CrossRef]
    • (2003) FEBS Lett , vol.554 , pp. 347-350
    • Hitomi, T.1    Matsuzaki, Y.2    Yokota, T.3    Takaoka, Y.4    Sakai, T.5
  • 126
    • 0034672294 scopus 로고    scopus 로고
    • Effect of trichostatin A on cell growth and expression of cell cycle- and apoptosis-related molecules in humangastric and oral carcinoma cell lines
    • Suzuki, T.; Yokozaki, H.; Kuniyasu, H.; Hayashi, K.; Naka, K.; Ono, S.; Ishikawa, T.; Tahara, E.; Yasui, W. Effect of trichostatin A on cell growth and expression of cell cycle- and apoptosis-related molecules in humangastric and oral carcinoma cell lines. Int. J. Cancer 2000, 88, 992–997. [CrossRef]
    • (2000) Int. J. Cancer , vol.88 , pp. 992-997
    • Suzuki, T.1    Yokozaki, H.2    Kuniyasu, H.3    Hayashi, K.4    Naka, K.5    Ono, S.6    Ishikawa, T.7    Tahara, E.8    Yasui, W.9
  • 127
    • 4344666663 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors upregulate death receptor 5/TRAIL-R2 and sensitize apoptosis induced by TRAIL/APO2-L in human malignant tumor cells
    • Nakata, S.; Yoshida, T.; Horinaka, M.; Shiraishi, T.; Wakada, M.; Sakai, T. Histone deacetylase inhibitors upregulate death receptor 5/TRAIL-R2 and sensitize apoptosis induced by TRAIL/APO2-L in human malignant tumor cells. Oncogene 2004, 23, 6261–6271. [CrossRef] [PubMed]
    • (2004) Oncogene , vol.23 , pp. 6261-6271
    • Nakata, S.1    Yoshida, T.2    Horinaka, M.3    Shiraishi, T.4    Wakada, M.5    Sakai, T.6
  • 128
    • 0033199896 scopus 로고    scopus 로고
    • Hybrid polar histone deacetylase inhibitor induces apoptosis and CD95/ CD95 ligand expression in human neuroblastoma
    • Glick, R.D.; Swendeman, S.L.; Coffey, D.C.; Rifkind, R.A.; Marks, P.A.; Richon, V.M.; Michael, P.; La-Quaglia, M.P. Hybrid polar histone deacetylase inhibitor induces apoptosis and CD95/ CD95 ligand expression in human neuroblastoma. Cancer Res. 1999, 59, 4392–4399. [PubMed]
    • (1999) Cancer Res , vol.59 , pp. 4392-4399
    • Glick, R.D.1    Swendeman, S.L.2    Coffey, D.C.3    Rifkind, R.A.4    Marks, P.A.5    Richon, V.M.6    Michael, P.7    La-Quaglia, M.P.8
  • 130
    • 27644556419 scopus 로고    scopus 로고
    • Inhibitors of histone deacetylases target the Rb-E2F1 pathway for apoptosis induction through activation of proapoptotic protein Bim
    • Zhao, Y.; Tan, J.; Zhuang, L.; Jiang, X.; Liu, E.T.; Yu, Q. Inhibitors of histone deacetylases target the Rb-E2F1 pathway for apoptosis induction through activation of proapoptotic protein Bim. Proc. Natl. Acad. Sci. USA 2005, 102, 16090–16095. [CrossRef] [PubMed]
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 16090-16095
    • Zhao, Y.1    Tan, J.2    Zhuang, L.3    Jiang, X.4    Liu, E.T.5    Yu, Q.6
  • 131
    • 0037052687 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid (SAHA) overcomes multidrug resistance and induces cell death in P-glycoprotein-expressing cells
    • Ruefli, A.A.; Bernhard, D.; Tainton, K.M.; Kofler, R.; Smyth, M.J.; Johnstone, R.W. Suberoylanilide hydroxamic acid (SAHA) overcomes multidrug resistance and induces cell death in P-glycoprotein-expressing cells. Int. J. Cancer 2002, 99, 292–298. [CrossRef] [PubMed]
    • (2002) Int. J. Cancer , vol.99 , pp. 292-298
    • Ruefli, A.A.1    Bernhard, D.2    Tainton, K.M.3    Kofler, R.4    Smyth, M.J.5    Johnstone, R.W.6
  • 132
    • 84909947601 scopus 로고    scopus 로고
    • Cell cycle inhibitory activity of Piper longum against A549 cell line and its protective effect against metal-induced toxicity in rats
    • Sharma, A.K.; Kumar, S.; Chashoo, G.; Saxena, A.K.; Pandey, A.K. Cell cycle inhibitory activity of Piper longum against A549 cell line and its protective effect against metal-induced toxicity in rats. Ind. J. Biochem. Biophys. 2014, 51, 358–364.
    • (2014) Ind. J. Biochem. Biophys , vol.51 , pp. 358-364
    • Sharma, A.K.1    Kumar, S.2    Chashoo, G.3    Saxena, A.K.4    Pandey, A.K.5
  • 133
    • 30044434594 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor LAQ824 induces human leukemia cell death through a process involving XIAP down-regulation, oxidative injury, and the acid sphingomyelinase-dependent generation of ceramide
    • Rosato, R.R.; Maggio, S.C.; Almenara, J.A.; Payne, S.G.; Atadja, P.; Spiegel, S.; Dent, P.; Grant, S. The histone deacetylase inhibitor LAQ824 induces human leukemia cell death through a process involving XIAP down-regulation, oxidative injury, and the acid sphingomyelinase-dependent generation of ceramide. Mol. Pharmacol. 2006, 69, 216–225. [CrossRef] [PubMed]
    • (2006) Mol. Pharmacol , vol.69 , pp. 216-225
    • Rosato, R.R.1    Maggio, S.C.2    Almenara, J.A.3    Payne, S.G.4    Atadja, P.5    Spiegel, S.6    Dent, P.7    Grant, S.8
  • 134
    • 11144221007 scopus 로고    scopus 로고
    • Apoptotic and autophagic cell death induced by histone deacetylase inhibitors
    • Shao, Y.; Gao, Z.; Marks, P.A.; Jiang, X. Apoptotic and autophagic cell death induced by histone deacetylase inhibitors. Proc. Natl. Acad. Sci. USA 2004, 101, 18030–18035. [CrossRef] [PubMed]
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 18030-18035
    • Shao, Y.1    Gao, Z.2    Marks, P.A.3    Jiang, X.4
  • 135
    • 84941218863 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors induce autophagy through FOXO1-dependent pathways
    • Zhang, J.; Ng, S.; Wang, J.; Zhou, J.; Tan, S.H.; Yang, N.; Lin, Q.; Xia, D.; Shen, H.M. Histone deacetylase inhibitors induce autophagy through FOXO1-dependent pathways. Autophagy 2015, 11, 629–642. [CrossRef] [PubMed]
    • (2015) Autophagy , vol.11 , pp. 629-642
    • Zhang, J.1    Ng, S.2    Wang, J.3    Zhou, J.4    Tan, S.H.5    Yang, N.6    Lin, Q.7    Xia, D.8    Shen, H.M.9
  • 136
    • 57149105528 scopus 로고    scopus 로고
    • SAHA induces caspase-independent, autophagic cell death of endometrial stromal sarcoma cells by influencing the mTOR pathway
    • Hrzenjak, A.; Kremser, M.L.; Strohmeier, B.; Moinfar, F.; Zatloukal, K.; Denk, H. SAHA induces caspase-independent, autophagic cell death of endometrial stromal sarcoma cells by influencing the mTOR pathway. J. Pathol. 2008, 216, 495–504. [CrossRef] [PubMed]
    • (2008) J. Pathol , vol.216 , pp. 495-504
    • Hrzenjak, A.1    Kremser, M.L.2    Strohmeier, B.3    Moinfar, F.4    Zatloukal, K.5    Denk, H.6
  • 137
    • 78649299438 scopus 로고    scopus 로고
    • Autophagy potentiates the anti-cancer effects of the histone deacetylase inhibitors in hepatocellular carcinoma
    • Liu, Y.L.; Yang, P.M.; Shun, C.T.; Wu, M.S.; Weng, J.R.; Chen, C.C. Autophagy potentiates the anti-cancer effects of the histone deacetylase inhibitors in hepatocellular carcinoma. Autophagy 2010, 6, 1057–1065. [CrossRef] [PubMed]
    • (2010) Autophagy , vol.6 , pp. 1057-1065
    • Liu, Y.L.1    Yang, P.M.2    Shun, C.T.3    Wu, M.S.4    Weng, J.R.5    Chen, C.C.6
  • 138
    • 84896727159 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors potentiate vesicular stomatitis virus oncolysis in prostate cancer cells by modulating NF-B-dependent autophagy
    • Shulak, L.; Beljanski, V.; Chiang, C.; Dutta, M.; Van Grevenynghe, J.; Belgnaoui, S.M.; Nguyen, L.; Di Lenardo, T.; Semmes, O.J.; Lin, R.; et al. Histone deacetylase inhibitors potentiate vesicular stomatitis virus oncolysis in prostate cancer cells by modulating NF-B-dependent autophagy. J. Virol. 2014, 88, 2927–2940. [CrossRef] [PubMed]
    • (2014) J. Virol , vol.88 , pp. 2927-2940
    • Shulak, L.1    Beljanski, V.2    Chiang, C.3    Dutta, M.4    Van Grevenynghe, J.5    Belgnaoui, S.M.6    Nguyen, L.7    Di Lenardo, T.8    Semmes, O.J.9    Lin, R.10
  • 139
    • 41249099242 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase1 induces autophagy
    • Oh, M.; Choi, I.K.; Kwon, H.J. Inhibition of histone deacetylase1 induces autophagy. Biochem. Biophys. Res. Commun. 2008, 369, 1179–1183. [CrossRef] [PubMed]
    • (2008) Biochem. Biophys. Res. Commun , vol.369 , pp. 1179-1183
    • Oh, M.1    Choi, I.K.2    Kwon, H.J.3
  • 140
    • 84885639981 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid (SAHA) causes tumor growth slowdown and triggers autophagy in glioblastoma stem cells
    • Chiao, M.T.; Cheng, W.Y.; Yang, Y.C.; Shen, C.C.; Ko, J.L. Suberoylanilide hydroxamic acid (SAHA) causes tumor growth slowdown and triggers autophagy in glioblastoma stem cells. Autophagy 2013, 9, 1509–1526. [CrossRef] [PubMed]
    • (2013) Autophagy , vol.9 , pp. 1509-1526
    • Chiao, M.T.1    Cheng, W.Y.2    Yang, Y.C.3    Shen, C.C.4    Ko, J.L.5
  • 142
    • 33751249589 scopus 로고    scopus 로고
    • Effects of histone deacetylase inhibitors on HIF-1
    • Liang, D.; Kong, X.; Sang, N. Effects of histone deacetylase inhibitors on HIF-1. Cell Cycle 2006, 5, 2430–2435. [CrossRef] [PubMed]
    • (2006) Cell Cycle , vol.5 , pp. 2430-2435
    • Liang, D.1    Kong, X.2    Sang, N.3
  • 144
    • 33749006252 scopus 로고    scopus 로고
    • Histone deacetylases arenassociated with VHL-independent regulation of hypoxiainducible factor 1alpha
    • Qian, D.Z.; Kachhap, S.K.; Collis, S.J.; Verheul, H.M.; Carducci, M.A.; Atadja, P.; Pili, R. Class II histone deacetylases arenassociated with VHL-independent regulation of hypoxiainducible factor 1alpha. Cancer Res. 2006, 66, 8814–8821. [CrossRef] [PubMed]
    • (2006) Cancer Res , vol.66 , pp. 8814-8821
    • Qian, D.Z.1    Kachhap, S.K.2    Collis, S.J.3    Verheul, H.M.4    Carducci, M.A.5    Atadja, P.6    Pili, R.7    Class, I.I.8
  • 145
    • 33744963443 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors repress the transactivation potential of hypoxia-inducible factors independently of direct acetylation of HIF-alpha
    • Fath, D.M.; Kong, X.; Liang, D.; Lin, Z.; Chou, A.; Jiang, Y.; Fang, J.; Caro, J.; Sang, N. Histone deacetylase inhibitors repress the transactivation potential of hypoxia-inducible factors independently of direct acetylation of HIF-alpha. J. Biol. Chem. 2006, 281, 13612–13619. [CrossRef] [PubMed]
    • (2006) J. Biol. Chem , vol.281 , pp. 13612-13619
    • Fath, D.M.1    Kong, X.2    Liang, D.3    Lin, Z.4    Chou, A.5    Jiang, Y.6    Fang, J.7    Caro, J.8    Sang, N.9
  • 147
    • 0036134288 scopus 로고    scopus 로고
    • Induction of differentiation and suppression of malignant phenotype of human neuroblastoma BE(2)-C cells by valproic acid: Enhancement by combination with interferon
    • Cinatl, J.; Kotchetkov, R.; Blaheta, R.; Driever, P.H.; Vogel, J.U.; Cinatl, J. Induction of differentiation and suppression of malignant phenotype of human neuroblastoma BE(2)-C cells by valproic acid: Enhancement by combination with interferon. Int. J. Oncol. 2002, 20, 97–106. [CrossRef] [PubMed]
    • (2002) Int. J. Oncol , vol.20 , pp. 97-106
    • Cinatl, J.1    Kotchetkov, R.2    Blaheta, R.3    Driever, P.H.4    Vogel, J.U.5    Cinatl, J.6
  • 148
    • 85045006823 scopus 로고    scopus 로고
    • Renoprotective effect of cinnamaldehyde in food color induced toxicity
    • Sharma, U.K.; Kumar, R.; Gupta, A.; Ganguly, R.; Pandey, A.K. Renoprotective effect of cinnamaldehyde in food color induced toxicity. 3 Biotech 2018, 8, 212. [CrossRef] [PubMed]
    • (2018) Biotech , vol.3 , Issue.8
    • Sharma, U.K.1    Kumar, R.2    Gupta, A.3    Ganguly, R.4    Pandey, A.K.5
  • 149
    • 85030632281 scopus 로고    scopus 로고
    • Pharmacological activities of cinnamaldehyde and eugenol: Antioxidant, cytotoxic and anti-leishmanial studies
    • Sharma, U.K.; Sharma, A.K.; Gupta, A.; Kumar, R.; Pandey, A.; Pandey, A.K. Pharmacological activities of cinnamaldehyde and eugenol: antioxidant, cytotoxic and anti-leishmanial studies. Cell. Mol. Biol. (Noisy-le-grand) 2017, 63, 73–78. [CrossRef] [PubMed]
    • (2017) Cell. Mol. Biol. (Noisy-Le-Grand) , vol.63 , pp. 73-78
    • Sharma, U.K.1    Sharma, A.K.2    Gupta, A.3    Kumar, R.4    Pandey, A.5    Pandey, A.K.6
  • 150
    • 84901807992 scopus 로고    scopus 로고
    • In vitro antibacterial, antioxidant, cytotoxic activities of Parthenium hysterophorus and characterization of extracts by LC MS analysis
    • Kumar, S.; Pandey, S.; Pandey, A.K. In vitro antibacterial, antioxidant, cytotoxic activities of Parthenium hysterophorus and characterization of extracts by LC MS analysis. BioMed Res. Int. 2014, 2014, 495154. [CrossRef] [PubMed]
    • (2014) Biomed Res. Int
    • Kumar, S.1    Pandey, S.2    Pandey, A.K.3
  • 151
    • 85014874612 scopus 로고    scopus 로고
    • Protective effect of Bauhinia variegata leaf extracts against oxidative damage, cell proliferation and bacterial growth
    • Sharma, A.K.; Sharma, U.K.; Pandey, A.K. Protective effect of Bauhinia variegata leaf extracts against oxidative damage, cell proliferation and bacterial growth. Proc. Natl. Acad. Sci. India, Sect. B Biol. Sci. 2017, 87, 47–51. [CrossRef]
    • (2017) Proc. Natl. Acad. Sci. India, Sect. B Biol. Sci , vol.87 , pp. 47-51
    • Sharma, A.K.1    Sharma, U.K.2    Pandey, A.K.3
  • 152
    • 0038079767 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor MS-275 promotes differentiation or apoptosis in human leukemia cells through a process regulated by generation of reactive oxygen species and induction of p21CIP1/WAF1 1
    • Rosato, R.R.; Almenara, J.A.; Grant, S. The histone deacetylase inhibitor MS-275 promotes differentiation or apoptosis in human leukemia cells through a process regulated by generation of reactive oxygen species and induction of p21CIP1/WAF1 1. Cancer Res. 2003, 63, 3637–3645. [PubMed]
    • (2003) Cancer Res , vol.63 , pp. 3637-3645
    • Rosato, R.R.1    Almenara, J.A.2    Grant, S.3
  • 153
    • 0035845541 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor and chemotherapeutic agent suberoylanilide hydroximic acid (SAHA) induces a cell-death pathway characterized by cleavage of Bid and production of reactive oxygen species
    • Ruefli, A.A.; Ausserlechner, M.J.; Bernhard, D.; Sutton, V.R.; Tainton, K.M.; Kofler, R.; Smyth, M.J.; Johnstone, R.W. The histone deacetylase inhibitor and chemotherapeutic agent suberoylanilide hydroximic acid (SAHA) induces a cell-death pathway characterized by cleavage of Bid and production of reactive oxygen species. Proc. Natl. Acad. Sci. USA 2001, 98, 10833–10838. [CrossRef] [PubMed]
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10833-10838
    • Ruefli, A.A.1    Ausserlechner, M.J.2    Bernhard, D.3    Sutton, V.R.4    Tainton, K.M.5    Kofler, R.6    Smyth, M.J.7    Johnstone, R.W.8
  • 154
    • 85012092113 scopus 로고    scopus 로고
    • Free radicals: Health implications and their mitigation by herbals
    • Kumar, S.; Pandey, A.K. Free radicals: Health implications and their mitigation by herbals. Br. J. Med. Med. Res. 2015, 7, 438–457. [CrossRef]
    • (2015) Br. J. Med. Med. Res , vol.7 , pp. 438-457
    • Kumar, S.1    Pandey, A.K.2
  • 155
    • 33750288048 scopus 로고    scopus 로고
    • Intrinsic apoptotic and thioredoxin pathways in human prostate cancer cell response to histone deacetylase inhibitor
    • Xu, W.; Ngo, L.; Perez, G.; Dokmanovic, M.; Marks, P.A. Intrinsic apoptotic and thioredoxin pathways in human prostate cancer cell response to histone deacetylase inhibitor. Proc. Natl. Acad. Sci. USA 2006, 103, 15540–15545. [CrossRef] [PubMed]
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 15540-15545
    • Xu, W.1    Ngo, L.2    Perez, G.3    Dokmanovic, M.4    Marks, P.A.5
  • 157
    • 0141744707 scopus 로고    scopus 로고
    • Histone hyperacetylation in mitosis prevents sister chromatid separation and produces chromosome segregation defects
    • Cimini, D.; Mattiuzzo, M.; Torosantucci, L.; Degrassi, F. Histone hyperacetylation in mitosis prevents sister chromatid separation and produces chromosome segregation defects. Mol. Biol. Cell 2003, 14, 3821–3833. [CrossRef] [PubMed]
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3821-3833
    • Cimini, D.1    Mattiuzzo, M.2    Torosantucci, L.3    Degrassi, F.4
  • 158
    • 84890081756 scopus 로고    scopus 로고
    • Parthenium hysterophorus: A Probable Source of Anticancer, Antioxidant and Anti-HIV Agents
    • Kumar, S.; Chashoo, G.; Saxena, A.K.; Pandey, A.K. Parthenium hysterophorus: A Probable Source of Anticancer, Antioxidant and Anti-HIV Agents. BioMed Res. Int. 2013, 2013, 810734. [CrossRef] [PubMed]
    • (2013) Biomed Res. Int
    • Kumar, S.1    Chashoo, G.2    Saxena, A.K.3    Pandey, A.K.4
  • 159
    • 84904636264 scopus 로고    scopus 로고
    • The Therapeutic Potential of Class I Selective Histone Deacetylase Inhibitors in Ovarian Cancer
    • Khabele, D. The Therapeutic Potential of Class I Selective Histone Deacetylase Inhibitors in Ovarian Cancer. Front. Oncol. 2014, 4, 111. [CrossRef] [PubMed]
    • (2014) Front. Oncol , vol.4
    • Khabele, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.