Development of a histone deacetylase 6 inhibitor and its biological effects
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Significance: We discovered a hydroxamic acid-based small-molecule N -hydroxy-4-(2-[(2-hydroxyethyl)(phenyl)amino]-2-oxoethyl)benzamide selectively inhibits histone deacetylase 6 catalytic activity in vivo and in vitro.
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HPOB potency against HDAC6 is comparable to SAHA-like inhibitors, but its potency against other isozymes is significantly reduced.
“Accordingly, the potency of HPOB against HDAC6 is comparable to SAHA-like inhibitors, but HPOB potency against other isozymes is significantly reduced.43”
From Histone deacetylase 6 structure and molecular basis of catalysis and inhibition (2016) · cites this paper as [43]
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HDAC6 is a microtubule-associated deacetylase
Hubbert, C., Guardiola, A., Shao, R., Kawaguchi, Y., Ito, A., Nixon, A., Yoshida, M., Wang, X.-F., & Yao, T.-P. (2002) · Nature · doi:10.1038/417455a · Cited by 2,403 · see citing works
Kawaguchi, Y., Kovacs, J. J., McLaurin, A. C., Vance, J. M., Ito, A., & Yao, T. (2003) · Cell · doi:10.1016/s0092-8674(03)00939-5 · Cited by 1,529 · see citing works
Marks, P. A., & Breslow, R. (2007) · Nature Biotechnology · doi:10.1038/nbt1272 · Cited by 1,198 · see citing works
Self-citationHDAC6 Regulates Hsp90 Acetylation and Chaperone-Dependent Activation of Glucocorticoid Receptor
Kovacs, J. J., Murphy, P. J. M., Gaillard, S., Zhao, X., Wu, J.-T., Nicchitta, C. V., Yoshida, M., Toft, D. O., Pratt, W. B., & Yao, T.-P. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.04.021 · Cited by 1,153 · see citing works
Sarkar, S., Davies, J. E., Huang, Z., Tunnacliffe, A., & Rubinsztein, D. C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609532200 · Cited by 1,142 · see citing works
Haggarty, S. J., Koeller, K. M., Wong, J. C., Grozinger, C. M., & Schreiber, S. L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0430973100 · Cited by 1,066 · see citing works
Rational Design and Simple Chemistry Yield a Superior, Neuroprotective HDAC6 Inhibitor, Tubastatin A
Butler, K. V., Kalin, J., Brochier, C., Vistoli, G., Langley, B., & Kozikowski, A. P. (2010) · Journal of the American Chemical Society · doi:10.1021/ja102758v · Cited by 801 · see citing works
HDAC6 controls autophagosome maturation essential for ubiquitin‐selective quality‐control autophagy
Lee, J., Koga, H., Kawaguchi, Y., Tang, W., Wong, E., Gao, Y., Pandey, U. B., Kaushik, S., Tresse, E., Lu, J., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2009.405 · Cited by 756 · see citing works
Self-citationHDAC6 Modulates Cell Motility by Altering the Acetylation Level of Cortactin
Zhang, X. M., Yuan, Z., Zhang, Y., Yong, S., Salas-Burgos, A., Koomen, J. M., Olashaw, N., Parsons, J. T., Yang, X., Dent, S., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.05.033 · Cited by 731 · see citing works
Chemical phylogenetics of histone deacetylases
Bradner, J. E., West, N., Grachan, M. L., Greenberg, E. F., Haggarty, S. J., Warnow, T., & Mazitschek, R. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.313 · Cited by 720 · see citing works
Santo, L., Hideshima, T., Kung, A. L., Tseng, J.-C., Tamang, D., Yang, M., Jarpe, M., van Duzer, J. H., Mazitschek, R., Ogier, W. C., et al. (2012) · Blood · doi:10.1182/blood-2011-10-387365 · Cited by 616 · see citing works
Butler, L. M., Agus, D. B., Scher, H. I., Higgins, B., Rose, A., Cordon‐Cardo, C., Thaler, H. T., Rifkind, R. A., Marks, P. A., & Richon, V. M. (2000) · PubMed · Cited by 613 · see citing works
Self-citationHideshima, T., Bradner, J. E., Wong, J. Y. Y., Chauhan, D., Richardson, P. G. G., Schreiber, S. L., & Anderson, K. C. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503221102 · Cited by 598 · see citing works
HDAC6: a key regulator of cytoskeleton, cell migration and cell–cell interactions
Valenzuela-Fernández, A., Cabrero, J. R., Serrador, J. M., & Sánchez‐Madrid, F. (2008) · Trends in Cell Biology · doi:10.1016/j.tcb.2008.04.003 · Cited by 500 · see citing works
Kwon, S., Zhang, Y., & Matthias, P. (2007) · Genes & Development · doi:10.1101/gad.461107 · Cited by 402 · see citing works
HDAC6 controls major cell response pathways to cytotoxic accumulation of protein aggregatesPreprint
Boyault, C., Zhang, Y., Fritah, S., Caron, C., Gilquin, B., Kwon, S. H., Garrido, C., Yao, T., Vourc’h, C., Matthias, P., et al. (2007) · Genes & Development · doi:10.1101/gad.436407 · Cited by 370 · see citing works
Histone deacetylase inhibitor induces DNA damage, which normal but not transformed cells can repair
Lee, J.-H., Choy, M. L., Ngo, L., Foster, S. S., & Marks, P. A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1008522107 · Cited by 364 · see citing works
Self-citationHistone deacetylase 6 plays a role as a distinct regulator of diverse cellular processes
Li, Y., Shin, D., & Kwon, S. H. (2012) · FEBS Journal · doi:10.1111/febs.12079 · Cited by 346 · see citing works
HDAC6 is a specific deacetylase of peroxiredoxins and is involved in redox regulation
Parmigiani, R. B., Xu, W., Venta-Perez, G., Erdjument‐Bromage, H., Yaneva, M., Tempst, P., & Marks, P. A. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803749105 · Cited by 325 · see citing works
Self-citationSimbulan-Rosenthal, C. M., Rosenthal, D. S., Iyer, S., Boulares, A. H., & Smulson, M. E. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.22.13703 · Cited by 277 · see citing works
Namdar, M., Perez, G., Ngo, L., & Marks, P. A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1013754107 · Cited by 207 · see citing works
Self-citationBergman, J. A., Woan, K. V., Perez-Villarroel, P., Villagra, A., Sotomayor, E. M., & Kozikowski, A. P. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm301098e · Cited by 200 · see citing works
Histone deacetylase inhibitors: A chemical genetics approach to understanding cellular functions
Marks, P. A. (2010) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2010.05.008 · Cited by 189 · see citing works
Self-citationDevelopment and therapeutic impact of HDAC6-selective inhibitors
Dallavalle, S., Pisano, C., & Zunino, F. (2012) · Biochemical Pharmacology · doi:10.1016/j.bcp.2012.06.014 · Cited by 137 · see citing works
Structural Origin of Selectivity in Class II-Selective Histone Deacetylase Inhibitors
Estiu, G. L., Greenberg, E. F., Harrison, C. B., Kwiatkowski, N. P., Mazitschek, R., Bradner, J. E., & Wiest, O. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm7015254 · Cited by 110 · see citing works
A Novel Class of Small Molecule Inhibitors of HDAC6
Inks, E. S., Josey, B. J., Jesinkey, S. R., & Chou, C. J. (2011) · ACS Chemical Biology · doi:10.1021/cb200134p · Cited by 103 · see citing works
Wang, L., Xiang, S., Williams, K. A., Dong, H., Bai, W., Nicosia, S. V., Khochbin, S., Bepler, G., & Zhang, X. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0044265 · Cited by 85 · see citing works
Novel HDAC6 isoform selective chiral small molecule histone deacetylase inhibitors
Smil, D. V., Manku, S., Chantigny, Y., Leit, S. M., Wahhab, A., Yan, T. P., Fournel, M., Maroun, C. R., Li, Z., Lemieux, A., et al. (2008) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2008.12.045 · Cited by 83 · see citing works
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Histone deacetylases and their inhibitors in cancer, neurological diseases and immune disorders
Falkenberg, K. J., & Johnstone, R. W. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4360 · Cited by 1,564 · see citing works
HDACs and HDAC Inhibitors in Cancer Development and TherapyPreprint
Li, Y., & Seto, E. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026831 · Cited by 1,309 · see citing works
Off-target toxicity is a common mechanism of action of cancer drugs undergoing clinical trials
Lin, A., Giuliano, C. J., Palladino, A. C., John, K. M., Abramowicz, C., Yuan, M. L., Sausville, E. L., Lukow, D. A., Liu, L., Chait, A. R., et al. (2019) · Science Translational Medicine · doi:10.1126/scitranslmed.aaw8412 · Cited by 747 · see citing works
Histone deacetylase 6 structure and molecular basis of catalysis and inhibition
Hai, Y., & Christianson, D. W. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2134 · Cited by 521 · see citing works
“43”
Inside HDACs with more selective HDAC inhibitors
Roche, J., & Bertrand, P. (2016) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2016.05.047 · Cited by 323 · see citing works
Targeting Metalloenzymes for Therapeutic Intervention
Chen, A. Y., Adamek, R. N., Dick, B. L., Credille, C. V., Morrison, C. N., & Cohen, S. M. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00201 · Cited by 277 · see citing works
HDAC6 as privileged target in drug discovery: A perspective
Pulya, S., Amin, S. A., Adhikari, N., Biswas, S., Jha, T., & Ghosh, B. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.105274 · Cited by 265 · see citing works
Targeting histone deacetylases for cancer therapy: Trends and challenges
Liang, T., Wang, F., Elhassan, R. M., Cheng, Y., Tang, X., Chen, W., Fang, H., & Hou, X. (2023) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2023.02.007 · Cited by 222 · see citing works
Histone Deacetylase 6 in Health and Disease
Seidel, C., Schnekenburger, M., Dicato, M. A., & Diederich, M. F. (2015) · Epigenomics · doi:10.2217/epi.14.69 · Cited by 216 · see citing works
Unusual zinc-binding mode of HDAC6-selective hydroxamate inhibitors
Porter, N. J., Mahendran, A., Breslow, R., & Christianson, D. W. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1718823114 · Cited by 190 · see citing works
Self-citationZhang, X., Qin-Ma, Wu, H.-P., Khamis, M. Y., Li, Y., Ma, L., & Liu, H. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01782 · Cited by 160 · see citing works
Recent advances in the discovery of potent and selective HDAC6 inhibitors
Wang, X.-X., Wan, R.-Z., & Liu, Z.-P. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.10.040 · Cited by 152 · see citing works
Next-generation of selective histone deacetylase inhibitors
Yang, F., Zhao, N., Ge, D., & Chen, Y. (2019) · RSC Advances · doi:10.1039/c9ra02985k · Cited by 144 · see citing works
Drugging the HDAC6–HSP90 interplay in malignant cells
Krämer, O. H., Mahboobi, S., & Sellmer, A. (2014) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2014.08.001 · Cited by 133 · see citing works
Strategies To Design Selective Histone Deacetylase Inhibitors
Melesina, J., Simoben, C. V., Praetorius, L., Bülbül, E. F., Robaa, D., & Sippl, W. (2021) · ChemMedChem · doi:10.1002/cmdc.202000934 · Cited by 118 · see citing works
Porter, N. J., Osko, J. D., Diedrich, D., Kurz, T., Hooker, J. M., Hansen, F. K., & Christianson, D. W. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01013 · Cited by 111 · see citing works
Yang, Z., Wang, T., Wang, F., Niu, T., Liu, Z., Chen, X. L., Long, C., Tang, M., Cao, D., Wang, X., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01342 · Cited by 111 · see citing works
Vögerl, K., Ong, N., Senger, J., Herp, D., Schmidtkunz, K., Marek, M., Müller, M., Bartel, K., Shaik, T. B., Porter, N. J., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01090 · Cited by 104 · see citing works
A patent review of IDO1 inhibitors for cancer
Cheong, J. E., Ekkati, A. R., & Sun, L. (2018) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2018.1441290 · Cited by 104 · see citing works
Husain, M., & Cheung, C. (2014) · Journal of Virology · doi:10.1128/jvi.00727-14 · Cited by 100 · see citing works
HDAC as onco target: Reviewing the synthetic approaches with SAR study of their inhibitors
Sangwan, R., Rajan, R., & Mandal, P. K. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.08.073 · Cited by 97 · see citing works
Géraldy, M. N. E., Morgen, M., Sehr, P. A., Steimbach, R. R., Moi, D., Ridinger, J., Oehme, I., Witt, O., Malz, M., Nogueira, M. S., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01936 · Cited by 96 · see citing works
Dabravolski, S. A., Sukhorukov, V. N., Kalmykov, V. A., Grechko, A. V., Shakhpazyan, N. K., & Orekhov, A. N. (2022) · Biomedicines · doi:10.3390/biomedicines10020254 · Cited by 96 · see citing works
HDAC6: A unique HDAC family member as a cancer target
Kaur, S., Rajoria, P., & Chopra, M. (2022) · Cellular Oncology · doi:10.1007/s13402-022-00704-6 · Cited by 95 · see citing works
Zhang, Y., Ying, J. B., Hong, J. J., Li, F., Fu, T. T., Yang, F. Y., Zheng, G. X., Yao, X., Lou, Y., Qiu, Y., et al. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00729 · Cited by 94 · see citing works
Epigenetic modulators as therapeutic targets in prostate cancer
Graça, I. C. R., Pereira-Silva, E., Henrique, R., Packham, G., Crabb, S. J., & Jerónimo, C. (2016) · Clinical Epigenetics · doi:10.1186/s13148-016-0264-8 · Cited by 88 · see citing works
Squaramides as Bioisosteres in Contemporary Drug Design
Agnew‐Francis, K. A., & Williams, C. M. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.0c00416 · Cited by 86 · see citing works
Small Molecules Targeting HATs, HDACs, and BRDs in Cancer Therapy
Wu, D., Qiu, Y., Jiao, Y., Qiu, Z., & Liu, D. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.560487 · Cited by 81 · see citing works
Bandyopadhaya, A., Tsurumi, A., Maura, D., Jeffrey, K. L., & Rahme, L. G. (2016) · Nature Microbiology · doi:10.1038/nmicrobiol.2016.174 · Cited by 79 · see citing works
Photoorganocatalytic One‐Pot Synthesis of Hydroxamic Acids from Aldehydes
Papadopoulos, G. N., & Kokotos, C. G. (2016) · Chemistry - A European Journal · doi:10.1002/chem.201600333 · Cited by 78 · see citing works
Koeneke, E., Witt, O., & Oehme, I. (2015) · Cells · doi:10.3390/cells4020135 · Cited by 74 · see citing works
Oh, B. R., Suh, D., Bae, D., Ha, N., Choi, Y. I., Yoo, H. J., Park, J. K., Lee, E. Y., Lee, E. B., & Song, Y. W. (2017) · Arthritis Research & Therapy · doi:10.1186/s13075-017-1357-2 · Cited by 72 · see citing works
Rabal, O., Sánchez-Arias, J. A., Cuadrado‐Tejedor, M., de Miguel, I., Pérez-González, M., García, C., Ugarte, A., de Mendoza, A. E., Sáez, E., Espelosin, M., et al. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.03.005 · Cited by 71 · see citing works
Entropy as a Driver of Selectivity for Inhibitor Binding to Histone Deacetylase 6
Porter, N. J., Wagner, F. F., & Christianson, D. W. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00367 · Cited by 64 · see citing works
Lu, B., Qiu, R., Wei, J., Wang, L., Zhang, Q., Li, M., Zhan, X., Chen, J., Hsieh, I.-Y., Yang, C., et al. (2024) · Nature Cancer · doi:10.1038/s43018-024-00816-y · Cited by 62 · see citing works
Seidel, C., Schnekenburger, M., Mazumder, A., Teiten, M.-H., Kirsch, G., Dicato, M. A., & Diederich, M. F. (2015) · Biochemical Pharmacology · doi:10.1016/j.bcp.2015.11.005 · Cited by 62 · see citing works
Identification of a Novel Aminotetralin Class of HDAC6 and HDAC8 Selective Inhibitors
Tang, G., Wong, J. C., Zhang, W., Wang, Z., Zhang, N., Peng, Z., Zhang, Z., Rong, Y., Li, S., Zhang, M., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm5008962 · Cited by 62 · see citing works
Design, synthesis and evaluate of novel dual FGFR1 and HDAC inhibitors bearing an indazole scaffold
Liu, J., Qian, C., Zhu, Y., Cai, J., He, Y., Li, J., Wang, T., Zhu, H., Li, Z., Li, W., et al. (2017) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2017.12.041 · Cited by 61 · see citing works
Histone Deacetylases and Histone Deacetylase Inhibitors in Neuroblastoma
Phimmachanh, M., Han, J. Z. R., O’Donnell, Y. E. I., Latham, S. L., & Croucher, D. R. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.578770 · Cited by 61 · see citing works
Epigenetic modifications as regulatory elements of autophagy in cancer
Sui, X., Zhu, J., Zhou, J., Wang, X., Li, D., Han, W., Fang, Y., & Pan, H. (2015) · Cancer Letters · doi:10.1016/j.canlet.2015.02.009 · Cited by 57 · see citing works
Shi, X., Liu, Y., Zhang, D., & Xiao, D. (2019) · Life Sciences · doi:10.1016/j.lfs.2019.116613 · Cited by 57 · see citing works
Vergani, B., Sandrone, G., Marchini, M., Ripamonti, C., Cellupica, E., Galbiati, E., Caprini, G., Pavich, G., Porro, G., Rocchio, I., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01194 · Cited by 56 · see citing works
Synthesis and applications of benzohydroxamic acid-based histone deacetylase inhibitors
Vreese, R. D., & D’hooghe, M. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.04.013 · Cited by 55 · see citing works
HDAC6 regulates microtubule stability and clustering of AChRs at neuromuscular junctions
Osseni, A., Ravel‐Chapuis, A., Thomas, J.-L., Gache, V., Schaeffer, L., & Jasmin, B. J. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.201901099 · Cited by 55 · see citing works
Chen, X., Chen, X., Steimbach, R. R., Wu, T., Li, H., Dan, W., Shi, P., Cao, C., Li, D., Miller, A. K., et al. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.111950 · Cited by 53 · see citing works
Rational design and diversity-oriented synthesis of peptoid-based selective HDAC6 inhibitors
Diedrich, D., Hamacher, A., Gertzen, C. G. W., Avelar, L. A. A., Reiß, G. J., Kurz, T., Gohlke, H., Kassack, M. U., & Hansen, F. K. (2016) · Chemical Communications · doi:10.1039/c5cc10301k · Cited by 52 · see citing works
Stenzel, K., Hamacher, A., Hansen, F. K., Gertzen, C. G. W., Senger, J., Marquardt, V., Marek, L., Marek, M., Romier, C., Remke, M., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01538 · Cited by 51 · see citing works
Kaliszczak, M. A., van Hechanova, E., Li, Y., Al-Sadah, H. A., Parzych, K., Auner, H. W., & Aboagye, E. O. (2018) · British Journal of Cancer · doi:10.1038/s41416-018-0232-5 · Cited by 51 · see citing works
Junkins, R. D., McCormick, C., & Lin, T. (2014) · Autophagy · doi:10.4161/auto.27750 · Cited by 51 · see citing works
HDAC 1 and 6 modulate cell invasion and migration in clear cell renal cell carcinoma
Ramakrishnan, S., Ku, S., Ciamporcero, E. S., Miles, K. M., Attwood, K. M., Chintala, S., Shen, L., Ellis, L., Sotomayor, P. C., Swetzig, W. M., et al. (2016) · BMC Cancer · doi:10.1186/s12885-016-2604-7 · Cited by 50 · see citing works
Anti-cancer effects of naturally derived compounds targeting histone deacetylase 6-related pathways
Lernoux, M., Schnekenburger, M., Dicato, M. A., & Diederich, M. F. (2017) · Pharmacological Research · doi:10.1016/j.phrs.2017.11.004 · Cited by 49 · see citing works
Zhang, I., Beus, M., Stochaj, U., Le, P. U., Zorc, B., Rajić, Z., Petrecca, K., & Maysinger, D. (2018) · Cell Death Discovery · doi:10.1038/s41420-018-0103-0 · Cited by 47 · see citing works
Limited efficacy of specific HDAC6 inhibition in urothelial cancer cells
Rosik, L., Niegisch, G., Fischer, U., Jung, M., Schulz, W. A., & Hoffmann, M. J. (2014) · Cancer Biology & Therapy · doi:10.4161/cbt.28469 · Cited by 47 · see citing works
Dual inhibitors of HDAC and other epigenetic regulators: A novel strategy for cancer treatment
Shirbhate, E., Singh, V. P., Jahoriya, V., Mishra, A., Veerasamy, R., Tiwari, A. K., & Rajak, H. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115938 · Cited by 45 · see citing works
Small molecules targeting HDAC6 for cancer treatment: Current progress and novel strategies
Huang, Z., Li, L., Cheng, B., & Li, D. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.117218 · Cited by 45 · see citing works
Timperley, C. M., Forman, J. E., Abdollahi, M. R., Al-Amri, A. S., Baulig, A., Benachour, D., Borrett, V. T., Cariño, F. A., Geist, M., González, D., et al. (2019) · Toxicology · doi:10.1016/j.tox.2019.01.004 · Cited by 45 · see citing works
Design and Synthesis of Orally Bioavailable Aminopyrrolidinone Histone Deacetylase 6 Inhibitors
Lin, X., Chen, W.-M., Qiu, Z., Guo, L., Zhu, W., Li, W., Wang, Z., Zhang, W., Zhang, Z., Rong, Y., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/jm502011f · Cited by 44 · see citing works
Zhang, W., Zhang, H., Jiao, F., Wang, L.-W., Zhang, H., & Gong, Z. (2017) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2017.10.103 · Cited by 44 · see citing works
Differential molecular mechanistic behavior of HDACs in cancer progression
Singh, T., Kaur, P., Singh, P., Singh, S., & Munshi, A. (2022) · Medical Oncology · doi:10.1007/s12032-022-01770-4 · Cited by 41 · see citing works
Methods for Hydroxamic Acid Synthesis
Alam, M. A. (2019) · Current Organic Chemistry · doi:10.2174/1385272823666190424142821 · Cited by 41 · see citing works
Development and pre-clinical testing of a novel hypoxia-activated KDAC inhibitor
Skwarska, A., Calder, E. D. D., Sneddon, D., Bolland, H. R., Odyniec, M. L., Mistry, I. N., Martin, J., Folkes, L. K., Conway, S. J., & Hammond, E. M. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.04.004 · Cited by 38 · see citing works
Vreese, R. D., Galle, L. M., Depetter, Y., Franceus, J., Desmet, T., Hecke, K. V., Benoy, V., Bosch, L. V. D., & D’hooghe, M. (2016) · Chemistry - A European Journal · doi:10.1002/chem.201604167 · Cited by 38 · see citing works
Creation of a histone deacetylase 6 inhibitor and its biological effects
Lee, J., Yao, Y., Mahendran, A., Ngo, L., Venta-Perez, G., Choy, M. L., Breslow, R., & Marks, P. A. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1515882112 · Cited by 37 · see citing works
Self-citationPark, J. K., Shon, S. H., Yoo, H. J., Suh, D., Bae, D., Shin, J., Jun, J. H., Ha, N., Song, H., Choi, Y. I., et al. (2021) · Arthritis Research & Therapy · doi:10.1186/s13075-021-02561-4 · Cited by 35 · see citing works
Li, Z., Li, Q., Chen, L., Chen, B.-D., Zhang, C., Wang, X., & Li, W. (2016) · Neurochemistry International · doi:10.1016/j.neuint.2016.08.004 · Cited by 34 · see citing works
Recent advancement of HDAC inhibitors against breast cancer
Mehmood, S. A., Sahu, K. K., Sengupta, S., Partap, S., Karpoormath, R. V., Kumar, B., & Kumar, D. (2023) · Medical Oncology · doi:10.1007/s12032-023-02058-x · Cited by 33 · see citing works
Synthesis of benzothiophene-based hydroxamic acids as potent and selective HDAC6 inhibitors
Vreese, R. D., Steen, N. V., Verhaeghe, T., Desmet, T., Bougarne, N., Bosscher, K. D., Benoy, V., Haeck, W., Bosch, L. V. D., & D’hooghe, M. (2015) · Chemical Communications · doi:10.1039/c5cc03295d · Cited by 32 · see citing works
Developing selective histone deacetylases (HDACs) inhibitors through ebselen and analogs
Wang, Y., Wallach, J. V., Duane, S., Wang, Y., Wu, J., Wang, J., Adejare, A., & Ma, H. (2017) · Drug Design Development and Therapy · doi:10.2147/dddt.s124977 · Cited by 32 · see citing works
HDAC6—An Emerging Target Against Chronic Myeloid Leukemia?
Losson, H., Schnekenburger, M., Dicato, M. A., & Diederich, M. F. (2020) · Cancers · doi:10.3390/cancers12020318 · Cited by 32 · see citing works
Zhang, X., Kang, H., Tao, Y., Li, Y., Zhao, J., Ya-Gao, Ma, L., & Liu, H. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113392 · Cited by 31 · see citing works
Chu, H., He, Q., Wang, J., Hu, Y. Q., Wang, Y., & Lin, Z. (2020) · New Journal of Chemistry · doi:10.1039/d0nj04704j · Cited by 30 · see citing works
Dual LSD1 and HDAC6 Inhibition Induces Doxorubicin Sensitivity in Acute Myeloid Leukemia Cells
Bulut, İ., Lee, A. F., Cevatemre, B., Ružić, D., Belle, R., Kawamura, A., Gul, S., Nikolic, K. M., Ganesan, A., & Açılan, C. (2022) · Cancers · doi:10.3390/cancers14236014 · Cited by 29 · see citing works
An Overview of HDAC Inhibitors and their Synthetic Routes
Peng, X., Liao, G., Sun, P., Yu, Z., & Chen, J. (2019) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026619666190227221507 · Cited by 28 · see citing works
Chen, X., Wang, J., Zhao, P., Dang, B., Liang, T., Steimbach, R. R., Miller, A. K., Liu, J., Wang, X., Zhang, T., et al. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115776 · Cited by 26 · see citing works
Wang, F., Zheng, L., Yi, Y., Yang, Z., Qiu, Q., Wang, X., Yan, W., Bai, P., Yang, J., Li, D., et al. (2018) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-17-0332 · Cited by 26 · see citing works
Zhang, Q.-Q., Zhang, W.-J., & Chang, S. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1168848 · Cited by 24 · see citing works
Bae, D., Lee, J., Ha, N., Park, J., Baek, J., Suh, D., Lim, H. S., Ko, S. M., Kim, T., Jeong, D. S., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-93232-6 · Cited by 24 · see citing works
Self-citationHighly fluorescent and HDAC6 selective scriptaid analogues
Fleming, C. L., Natoli, A. L., Schreuders, J., Devlin, M. G., Yoganantharajah, P., Gibert, Y., Leslie, K. G., New, E. J., Ashton, T. D., & Pfeffer, F. M. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.11.020 · Cited by 24 · see citing works
Sixto‐López, Y., Bello, M., & Correa‐Basurto, J. (2018) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2018.1557560 · Cited by 23 · see citing works
Discovery of a potent histone deacetylase (HDAC) 3/6 selective dual inhibitor
Soumyanarayanan, U., Ramanujulu, P. M., Mustafa, N. B., Haider, S. M., Nee, A. H. F., Tong, J. X., Tan, K. S. W., Chng, W. J., & Dymock, B. W. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.111755 · Cited by 23 · see citing works
Demyanenko, S. V., Dzreyan, V., & Uzdensky, A. B. (2020) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2020.06.010 · Cited by 23 · see citing works
Kwak, T. W., Lee, H. L., Song, Y. H., Kim, C., Kim, J., Seo, S.-J., Jeong, Y., & Kang, D. H. (2017) · International Journal of Nanomedicine · doi:10.2147/ijn.s141920 · Cited by 23 · see citing works
Analysis of class I and II histone deacetylase gene expression in human leukemia
Yang, H., Maddipoti, S., Quesada, A. E., Bohannan, Z. S., Cabrero, M., Colla, S., Wei, Y., Estecio, M. R., Wierda, W. G., Bueso-Ramos, C., et al. (2015) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.3109/10428194.2015.1034705 · Cited by 22 · see citing works
Phenylpyrrole-Based Hdac Inhibitors: Synthesis, Molecular Modeling and Biological Studies
Brindisi, M., Cavella, C., Brogi, S., Nebbioso, A., Senger, J., Maramai, S., Ciotta, A., Iside, C., Butini, S., Lamponi, S., et al. (2016) · Future Medicinal Chemistry · doi:10.4155/fmc-2016-0068 · Cited by 22 · see citing works
Lee, J. H., Kim, H. S., Jang, S. W., & Lee, G. R. (2022) · Scientific Reports · doi:10.1038/s41598-022-27230-7 · Cited by 21 · see citing works
Self-citationCombined Ligand and Fragment‐based Drug Design of Selective Histone Deacetylase – 6 Inhibitors
Ružić, D., Petković, M., Agbaba, D. D., Ganesan, A., & Nikolic, K. M. (2019) · Molecular Informatics · doi:10.1002/minf.201800083 · Cited by 21 · see citing works
Recent Advances in Small Molecular Modulators Targeting Histone Deacetylase 6
Xiao, Y., & Zhang, X. (2020) · Future Drug Discovery · doi:10.4155/fdd-2020-0023 · Cited by 20 · see citing works
Timperley, C. M., Forman, J. E., Abdollahi, M. R., Al-Amri, A. S., Baulig, A., Benachour, D., Borrett, V. T., Cariño, F. A., Curty, C., Geist, M., et al. (2021) · Toxicology · doi:10.1016/j.tox.2021.152967 · Cited by 19 · see citing works
Gu, X. Q., Zhang, H., Jiao, M.-R., Han, B. R., Zhang, Z., Li, J., & Zhang, Q. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.114090 · Cited by 17 · see citing works
Ragot, A., Pietropaolo, S., Vincent, J. D., Delage, P., Zhang, H., Allinquant, B., Leinekugel, X., Fischer, A., & Cho, Y. H. (2015) · Brain and Behavior · doi:10.1002/brb3.361 · Cited by 17 · see citing works
Simoben, C. V., Ghazy, E., Zeyen, P., Darwish, S., Schmidt, M., Romier, C., Robaa, D., & Sippl, W. (2021) · Molecules · doi:10.3390/molecules26092584 · Cited by 17 · see citing works
Rescue of CFTR NBD2 mutants N1303K and S1235R is influenced by the functioning of the autophagosome
Liu, Q., Sabirzhanova, I. B., Yanda, M. K., Bergbower, E. A. S., Boinot, C., Guggino, W. B., & Cebotaru, L. (2018) · Journal of Cystic Fibrosis · doi:10.1016/j.jcf.2018.05.016 · Cited by 16 · see citing works
Shin, J.-W., Choi, H., Nam, K.-M., Lee, H.-S., Kim, S.-A., Joe, H.-J., Toyama, K., & Park, K. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18071360 · Cited by 13 · see citing works
Wang, C.-Y., Liou, J., Tsai, A.-C., Lai, M.-J., Liu, Y., Lee, H., Wang, J.-C., Pan, S., & Teng, C. (2014) · Oncotarget · doi:10.18632/oncotarget.2451 · Cited by 13 · see citing works
The Role of HDAC6 in Glioblastoma Multiforme: A New Avenue to Therapeutic Interventions?
Spallotta, F., & Illi, B. (2024) · Biomedicines · doi:10.3390/biomedicines12112631 · Cited by 12 · see citing works
Khamis, M. Y., Wu, H.-P., Ma, Q., Li, Y., Ma, L., Zhang, X., & Liu, H. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.104754 · Cited by 12 · see citing works
Bagnall, N. H., Hines, B. M., Lucke, A. J., Gupta, P. K., Reid, R. C., Fairlie, D. P., & Kotze, A. C. (2017) · International Journal for Parasitology Drugs and Drug Resistance · doi:10.1016/j.ijpddr.2017.01.001 · Cited by 12 · see citing works
Poonia, P., Sharma, M., Jha, P. K., & Chopra, M. (2022) · Molecular Diversity · doi:10.1007/s11030-022-10540-3 · Cited by 11 · see citing works
Yan, G., Li, D., Zhong, X.-X., Liu, G., Wang, X., Lu, Y., Qin, F., Guo, Y., Duan, S., & Li, D. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1743760 · Cited by 11 · see citing works
Song, H., Hwang, Y. J., Ha, J. W., & Boo, Y. C. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21134589 · Cited by 11 · see citing works
- Authors
- Lee, J.-H., Mahendran, A., Yao, Y., Ngo, L., Venta-Perez, G., Choy, M. L., Kim, N., Ham, W.-S., Breslow, R., & Marks, P. A.
- Affiliations
- Memorial Sloan Kettering Cancer Center (US)
- Columbia University (US)
- Corresponding author
- Marks, Paul A.
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2013-09-10
- Volume
- 110
- Issue
- 39
- Pages
- 15704-15709
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC3785767
- OpenAlex
- W2148383035
- Cited by
- 141
- References
- 28
- Citations by year
- 2026: 5 · 2025: 7 · 2024: 6 · 2023: 7 · 2022: 7 · 2021: 15 · 2020: 15 · 2019: 17 · 2018: 16 · 2017: 12 · 2016: 14 · 2015: 13 · 2014: 7
- FWCI
- 5.53
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Servier
- National Cancer Institute (P30CA08748-44, P30CA008748)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme function and inhibition
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Keywords
- HDAC6, HDAC6 inhibitors, isoform-selective inhibition, hydroxamic acids, DNA-damaging agents, growth inhibition, small molecule inhibitors
- MeSH terms
- Vorinostat, Acetylation, Animals, Antineoplastic Agents, Autophagy, Cell Line, Transformed, Cell Survival, Doxorubicin, Etoposide, Histone Deacetylases, Histones, Humans, Hydroxamic Acids, Trehalose, Tubulin, Apoptosis, Xenograft Model Antitumor Assays, Cell Line, Tumor, Mice, DNA Breaks, Double-Stranded, Histone Deacetylase Inhibitors
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