The novel histone deacetylase inhibitor, LBH589, induces expression of DNA damage response genes and apoptosis in Ph− acute lymphoblastic leukemia cells

Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer

Minucci, S., & Pelicci, P. G. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1779 · Cited by 2,234

Acute Lymphoblastic Leukemia

Pui, C., & Evans, W. E. (1998) · New England Journal of Medicine · doi:10.1056/nejm199808273390907 · Cited by 841

Outcome of 609 adults after relapse of acute lymphoblastic leukemia (ALL); an MRC UKALL12/ECOG 2993 study

Fielding, A. K., Richards, S. M., Chopra, R., Lazarus, H. M., Litzow, M. R., Buck, G. A. N., Durrant, I. J., Luger, S. M., Marks, D. I., FRANKLIN, I. M., et al. (2006) · Blood · doi:10.1182/blood-2006-05-018192 · Cited by 841

Gene expression changes associated with progression and response in chronic myeloid leukemia

Radich, J. P., Dai, H., Mao, M., Oehler, V., Schelter, J., Druker, B., Sawyers, C., Shah, N., Stock, W., Willman, C. L., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510423103 · Cited by 583

Transcriptional signature of histone deacetylase inhibition in multiple myeloma: Biological and clinical implications

Mitsiades, C. S., Mitsiades, N., McMullan, C. J., Poulaki, V., Shringarpure, R., Hideshima, T., Akiyama, M., Chauhan, D., Munshi, N. C., Gu, X., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2536759100 · Cited by 537

CLINICAL DEVELOPMENT OF HISTONE DEACETYLASE INHIBITORS AS ANTICANCER AGENTS

Drummond, D. C., Noble, C. O., Kirpotin, D. B., Guo, Z., Scott, G. K., & Benz, C. C. (2005) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.45.120403.095825 · Cited by 494

Prospects: Histone deacetylase inhibitors

Dokmanovic, M., & Marks, P. A. (2005) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20532 · Cited by 487

Histone deacetylase inhibitors in cancer therapy

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Regulation of histone deacetylase activities

Sengupta, N., & Seto, E. (2004) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20179 · Cited by 357

GADD45b and GADD45g are cdc2/cyclinB1 kinase inhibitors with a role in S and G2/M cell cycle checkpoints induced by genotoxic stress

Vairapandi, M., Balliet, A. G., Hoffman‐Liebermann, B., & Liebermann, D. A. (2002) · Journal of Cellular Physiology · doi:10.1002/jcp.10140 · Cited by 343

Aberrant Epigenetic Landscape in Cancer: How Cellular Identity Goes Awry

Berdasco, M., & Esteller, M. (2010) · Developmental Cell · doi:10.1016/j.devcel.2010.10.005 · Cited by 651

Histone Deacetylase (HDAC) Inhibitor Kinetic Rate Constants Correlate with Cellular Histone Acetylation but Not Transcription and Cell Viability

Lauffer, B. E. L., Mintzer, R., Fong, R., Mukund, S., Tam, C., Zilberleyb, I., Flicke, B., Ritscher, A., Fedorowicz, G., Vallero, R., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.490706 · Cited by 429

Novel histone deacetylase inhibitors in clinical trials as anti-cancer agents

Tan, J., Cang, S., Ma, Y., Petrillo, R. L., & Liu, D. (2010) · Journal of Hematology & Oncology · doi:10.1186/1756-8722-3-5 · Cited by 425

Trials with ‘epigenetic’ drugs: An update

Nebbioso, A., Carafa, V., Benedetti, R., & Altucci, L. (2012) · Molecular Oncology · doi:10.1016/j.molonc.2012.09.004 · Cited by 242

Dietary phytochemicals, HDAC inhibition, and DNA damage/repair defects in cancer cells

Rajendran, P., Ho, E., Williams, D. E., & Dashwood, R. H. (2011) · Clinical Epigenetics · doi:10.1186/1868-7083-3-4 · Cited by 220

Phase II Study of Vorinostat for Treatment of Relapsed or Refractory Indolent Non-Hodgkin's Lymphoma and Mantle Cell Lymphoma

Kirschbaum, M. H., Frankel, P. H., Popplewell, L. L., Zain, J. M., Delioukina, M. L., Pullarkat, V. A., Matsuoka, D., Pulone, B., Rotter, A. J., Espinoza‐Delgado, I., et al. (2011) · Journal of Clinical Oncology · doi:10.1200/jco.2010.32.1398 · Cited by 217

γH2AX and its role in DNA double-strand break repairThis paper is one of a selection of papers published in this Special Issue, entitled 27th International West Coast Chromatin and Chromosome Conference, and has undergone the Journal's usual peer review process.

Fillingham, J., Keogh, M., & Krogan, N. J. (2006) · Biochemistry and Cell Biology · doi:10.1139/o06-072 · Cited by 199

Painful Pathways Induced by TLR Stimulation of Dorsal Root Ganglion Neurons

Jia, Q., Buzás, K., Fan, H., Cohen, J. I., Wang, K., Mont, E. K., Klinman, D. M., Oppenheim, J. J., & Howard, O. M. Z. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1001241 · Cited by 168

Genetic syndromes caused by mutations in epigenetic genes

Berdasco, M., & Esteller, M. (2013) · Human Genetics · doi:10.1007/s00439-013-1271-x · Cited by 176

Targeting Histone Deacetylases for Cancer Therapy: From Molecular Mechanisms to Clinical Implications

Li, Z., & Zhu, W. (2014) · International Journal of Biological Sciences · doi:10.7150/ijbs.9067 · Cited by 164

Oral tetrahydrouridine and decitabine for non-cytotoxic epigenetic gene regulation in sickle cell disease: A randomized phase 1 study

Molokie, R. E., Lavelle, D., Gowhari, M., Pacini, M., Krauz, L., Hassan, J., Ibañez, V., Ruiz, M. A., Ng, K. P., Woost, P. G., et al. (2017) · PLoS Medicine · doi:10.1371/journal.pmed.1002382 · Cited by 147

CS055 (Chidamide/HBI-8000), a novel histone deacetylase inhibitor, induces G1 arrest, ROS-dependent apoptosis and differentiation in human leukaemia cells

Gong, K., Xie, J., Yi, H., & Li, W. (2012) · Biochemical Journal · doi:10.1042/bj20111685 · Cited by 131

HDAC8 catalyzes the hydrolysis of long chain fatty acyl lysine

Aramsangtienchai, P., Spiegelman, N. A., He, B., Miller, S. P., Dai, L., Zhao, Y., & Lin, H. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00396 · Cited by 118

STAT3 Inhibition Is a Therapeutic Strategy for ABC-like Diffuse Large B-Cell Lymphoma

Scuto, A., Kujawski, M., Kowolik, C. M., Krymskaya, L., Wang, L., Weiss, L. M., DiGiusto, D. L., Yu, H., Forman, S. J., & Jove, R. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-2380 · Cited by 115

Targeting the acetylation signaling pathway in cancer therapy

Dang, F., & Wei, W. (2022) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2021.03.001 · Cited by 109

Advances in Chemical Priming to Enhance Abiotic Stress Tolerance in Plants

Sako, K., Nguyen, H. M., & Seki, M. (2020) · Plant and Cell Physiology · doi:10.1093/pcp/pcaa119 · Cited by 106

Combining Histone Deacetylase Inhibitor Vorinostat with Aurora Kinase Inhibitors Enhances Lymphoma Cell Killing with Repression of c-Myc, hTERT, and microRNA Levels

Kretzner, L., Scuto, A., Dino, P. M., Kowolik, C. M., Wu, J., Ventura, P. B., Jove, R., Forman, S. J., Yen, Y., & Kirschbaum, M. H. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-2259 · Cited by 103

HDAC inhibition by LBH589 affects the phenotype and function of human myeloid dendritic cells

Song, W., Tai, Y.-T., Tian, Z., Hideshima, T., Chauhan, D., Nanjappa, P., Exley, M. A., Anderson, K. C., & Munshi, N. C. (2010) · Leukemia · doi:10.1038/leu.2010.244 · Cited by 96

PI3K/mTOR Inhibition Markedly Potentiates HDAC Inhibitor Activity in NHL Cells through BIM- and MCL-1–Dependent Mechanisms In Vitro and In Vivo

Rahmani, M., Aust, M. M., Benson, E. C., Wallace, L. M., Friedberg, J. W., & Grant, S. (2014) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-0034 · Cited by 93

Stemness of B-cell Progenitors in Multiple Myeloma Bone Marrow

Boucher, K., Parquet, N., Widen, R. E., Shain, K. H., Baz, R., Alsina, M., Koomen, J. M., Anasetti, C., Dalton, W. S., & Perez, L. E. (2012) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-12-0531 · Cited by 87

Large-scale RNAi screening uncovers therapeutic targets in the parasite Schistosoma mansoni

Wang, J., Paz, C., Padalino, G., Coghlan, A., Lu, Z., Grădinaru, I., Collins, J. N. R., Berriman, M., Hoffmann, K. F., & Collins, J. J. (2020) · Science · doi:10.1126/science.abb7699 · Cited by 88

Selective Inhibition of HDAC1 and HDAC2 as a Potential Therapeutic Option for B-ALL

Stubbs, M. C., Kim, W.-I., Bariteau, M. A., Davis, T. N., Vempati, S., Minehart, J. C., Witkin, M. D., Qi, J., Krivtsov, A. V., Bradner, J. E., et al. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-1290 · Cited by 82

DAPK plays an important role in panobinostat-induced autophagy and commits cells to apoptosis under autophagy deficient conditions

Gandesiri, M., Chakilam, S., Ivanovska, J., Benderska, N., Ocker, M., Fazio, P. D., Feoktistova, M., Gali‐Muhtasib, H. U., Rave‐Fränk, M., Prante, O., et al. (2012) · APOPTOSIS · doi:10.1007/s10495-012-0757-7 · Cited by 80

A phase 2 study of vorinostat for treatment of relapsed or refractory Hodgkin lymphoma: Southwest Oncology Group Study S0517

Kirschbaum, M. H., Goldman, B. H., Zain, J. M., Cook, J. R., Rimsza, L. M., Forman, S. J., & Fisher, R. I. (2011) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.3109/10428194.2011.608448 · Cited by 73

Active DNA demethylation in post-mitotic neurons: A reason for optimism

Gavin, D. P., Chase, K. A., & Sharma, R. P. (2013) · Neuropharmacology · doi:10.1016/j.neuropharm.2013.07.036 · Cited by 72

Cell deaths: Involvement in the pathogenesis and intervention therapy of COVID-19

Li, X., Zhang, Z., Wang, Z., Gutiérrez-Castrellón, P., & Shi, H. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01043-6 · Cited by 67

Treatment of resistant metastatic melanoma using sequential epigenetic therapy (decitabine and panobinostat) combined with chemotherapy (temozolomide)

Xia, C., Leon-Ferre, R. A., Laux, D. E., Deutsch, J. M., Smith, B. J., Frees, M., & Milhem, M. M. (2014) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-014-2501-1 · Cited by 66

Design, synthesis and anticancer potential of NSC-319745 hydroxamic acid derivatives as DNMT and HDAC inhibitors

Yuan, Z., Sun, Q., Li, D., Miao, S., Chen, S., Song, L., Gao, C., Chen, Y., Tan, C., & Jiang, Y. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.04.017 · Cited by 62

SIRT1 activation enhances HDAC inhibition-mediated upregulation of GADD45G by repressing the binding of NF-κB/STAT3 complex to its promoter in malignant lymphoid cells

Scuto, A., Kirschbaum, M. H., Buettner, R., Kujawski, M., Cermak, J. M., Atadja, P. W., & Jove, R. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.159 · Cited by 62

Interconnecting molecular pathways in the pathogenesis and drug sensitivity of T-cell acute lymphoblastic leukemia

Sanda, T., Li, X., Gutiérrez, A., Ahn, Y., Neuberg, D. S., O’Neil, J., Strack, P. R., Winter, C. G., Winter, S. S., Larson, R. A., et al. (2009) · Blood · doi:10.1182/blood-2009-07-235143 · Cited by 60

Development of a versatile DNMT and HDAC inhibitor C02S modulating multiple cancer hallmarks for breast cancer therapy

Yuan, Z., Chen, S., Gao, C., Dai, Q., Zhang, C., Sun, Q., Lin, J., Guo, C., Chen, Y., & Jiang, Y. (2019) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2019.03.027 · Cited by 59

The HDAC inhibitor LBH589 (panobinostat) is an inhibitory modulator of aromatase gene expression

Chen, S., Ye, J., Kijima, I., & Evans, D. B. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1000917107 · Cited by 58

Inhibition of the proliferation of acquired aromatase inhibitor-resistant breast cancer cells by histone deacetylase inhibitor LBH589 (panobinostat)

Kubo, M., Kanaya, N., Petrossian, K., Ye, J., Warden, C., Liu, Z., Nishimura, R., Osako, T., Okido, M., Shimada, K., et al. (2012) · Breast Cancer Research and Treatment · doi:10.1007/s10549-012-2332-x · Cited by 58

Cytotoxic activity of the histone deacetylase inhibitor panobinostat (LBH589) in anaplastic thyroid cancer in vitro and in vivo

Catalano, M. G., Pugliese, M., Gargantini, E., Grange, C., Bussolati, B., Asioli, S., Bosco, O., Poli, R., Compagnone, A., Bandino, A., et al. (2011) · International Journal of Cancer · doi:10.1002/ijc.26057 · Cited by 56

CRISPR-based screens uncover determinants of immunotherapy response in multiple myeloma

Ramkumar, P., Abarientos, A., Tian, R., Seyler, M., Leong, J. T., Chen, M., Choudhry, P., Hechler, T., Shah, N. D., Wong, S. W. K., et al. (2020) · Blood Advances · doi:10.1182/bloodadvances.2019001346 · Cited by 55

The Role of HDACs in the Response of Cancer Cells to Cellular Stress and the Potential for Therapeutic Intervention

Alseksek, R. K., Ramadan, W. S. H., Saleh, E., & El‐Awady, R. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23158141 · Cited by 59

Targeting c-FLICE-like inhibitory protein (CFLAR) in cancer

Fulda, S. (2012) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2013.736499 · Cited by 56

SOX7 regulates MAPK/ERK-BIM mediated apoptosis in cancer cells

Sun, Q., Ding, L., Johnson, K. J., Zhou, S., Tyner, J. W., Yang, H. H., Doan, N., SAID, J. W., Xiao, J., Loh, X.-Y., et al. (2019) · Oncogene · doi:10.1038/s41388-019-0865-8 · Cited by 53

p53-Independent, Normal Stem Cell Sparing Epigenetic Differentiation Therapy for Myeloid and Other Malignancies

Saunthararajah, Y., Triozzi, P. L., Rini, B. I., Singh, A. D., Radivoyevitch, T., Sekeres, M. A., Advani, A. S., Tiu, R. V., Reu, F. J., Kalaycio, M. E., et al. (2012) · Seminars in Oncology · doi:10.1053/j.seminoncol.2011.11.011 · Cited by 54

HDAC inhibitor, scriptaid, induces glioma cell apoptosis through JNK activation and inhibits telomerase activity

Sharma, V., Koul, N., Joseph, C., Dixit, D., Ghosh, S., & Sen, E. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00844.x · Cited by 53

Fetal Hemoglobin Induction by Epigenetic Drugs

Lavelle, D., Engel, J. D., & Saunthararajah, Y. (2018) · Seminars in Hematology · doi:10.1053/j.seminhematol.2018.04.008 · Cited by 53

The role of death domain proteins in host response upon SARS-CoV-2 infection: modulation of programmed cell death and translational applications

Ivanisenko, N. V., Seyrek, K., Kolchanov, N. A., Иванисенко, В. А., & Lavrik, I. N. (2020) · Cell Death Discovery · doi:10.1038/s41420-020-00331-w · Cited by 51

Epigenetic Targets and their Inhibitors in Cancer Therapy

Zhao, L., Duan, Y., Lü, P., Zhang, Z., Zheng, X., Wang, J., & Feng, W. (2019) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026619666181224095449 · Cited by 52

Gene silencing of MIR22 in acute lymphoblastic leukaemia involves histone modifications independent of promoter DNA methylation

Li, X., Liu, J., Zhou, R., Huang, S., Huang, S., & Chen, X. (2009) · British Journal of Haematology · doi:10.1111/j.1365-2141.2009.07920.x · Cited by 46

Preclinical activity of LBH589 alone or in combination with chemotherapy in a xenogeneic mouse model of human acute lymphoblastic leukemia

Vilas‐Zornoza, A., Agirre, X., Abizanda, G., Moreno, C., Segura, V., Martino, A. D., José‐Eneriz, E. S., Miranda, E., Martín-Subero, J. I., Gárate, L., et al. (2012) · Leukemia · doi:10.1038/leu.2012.31 · Cited by 44

Epigenetics and Epi-miRNAs: Potential markers/therapeutics in leukemia

Memari, F., Joneidi, Z., Taheri, B., Aval, S. F., Roointan, A., & Zarghami, N. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.07.133 · Cited by 44

Histone acetylation: novel target for the treatment of acute lymphoblastic leukemia

Zhang, C., Zhong, J. F., Stucky, A., Chen, X., Press, M. F., & Zhang, X. (2015) · Clinical Epigenetics · doi:10.1186/s13148-015-0151-8 · Cited by 43

Clinical Trials Assessing Hypomethylating Agents Combined with Other Therapies: Causes for Failure and Potential Solutions

Zavras, P. D., Shastri, A., Goldfinger, M., Verma, A. K., & Saunthararajah, Y. (2021) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-21-2139 · Cited by 41

Dysregulation of Aromatase in Breast, Endometrial, and Ovarian Cancers

Manna, P. R., Molehin, D., & Ahmed, A. U. (2016) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2016.10.002 · Cited by 40

Histone deacetylase inhibitors in lymphoma

Copeland, A. R. M., Buglio, D., & Younes, A. (2010) · Current Opinion in Oncology · doi:10.1097/cco.0b013e32833d5954 · Cited by 39

Follicular lymphoma, a B cell malignancy addicted to epigenetic mutations

Korfi, K., Ali, S. E., Heward, J. A., & Fitzgibbon, J. (2017) · Epigenetics · doi:10.1080/15592294.2017.1282587 · Cited by 40

GADD45g acts as a novel tumor suppressor, and its activation suggests new combination regimens for the treatment of AML

Guo, D., Zhao, Y., Wang, N., You, N. Y., Zhu, W., Zhang, P., Ren, Q., Yin, J., Cheng, T., & Ma, X. (2021) · Blood · doi:10.1182/blood.2020008229 · Cited by 37

Targeting paediatric acute lymphoblastic leukaemia: novel therapies currently in development

Lee‐Sherick, A. B., Linger, R. M. A., Gore, L., Keating, A. K., & Graham, D. K. (2010) · British Journal of Haematology · doi:10.1111/j.1365-2141.2010.08282.x · Cited by 38

Panobinostat induces apoptosis via production of reactive oxygen species and synergizes with topoisomerase inhibitors in cervical cancer cells

Wasim, L., & Chopra, M. (2016) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2016.10.057 · Cited by 40

Panobinostat for the treatment of multiple myeloma

Neri, P. E., Bahlis, N. J., & Lonial, S. (2012) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2012.668883 · Cited by 38

Synergistic anti-leukemic interactions between panobinostat and MK-1775 in acute myeloid leukemia ex vivo

Qi, W., Zhang, W., Edwards, H. J., Chu, R. L., Madlambayan, G. J., Taub, J. W., Wang, Z., Wang, Y., Li, C., Lin, H., et al. (2015) · Cancer Biology & Therapy · doi:10.1080/15384047.2015.1095406 · Cited by 36

Co-exposure to polycyclic aromatic hydrocarbons and metals, four common polymorphisms in microRNA genes, and their gene-environment interactions: Influences on oxidative damage levels in Chinese coke oven workers

Xie, Y., Lin, T., Yang, M., Zhang, Z., Deng, N., Tang, M., Xiao, Y., Guo, H., & Deng, Q. (2019) · Environment International · doi:10.1016/j.envint.2019.105055 · Cited by 37

Synergistic antitumor interactions between MK-1775 and panobinostat in preclinical models of pancreatic cancer

Wang, G., Niu, X., Zhang, W., Caldwell, J. T., Edwards, H. J., Chen, W., Taub, J. W., Zhao, L., & Ge, Y. (2014) · Cancer Letters · doi:10.1016/j.canlet.2014.10.015 · Cited by 35

Design and Synthesis of Simplified Largazole Analogues as Isoform-Selective Human Lysine Deacetylase Inhibitors

Reddy, D. N., Ballante, F., Chuang, T., Pirolli, A., Marrocco, B., & Marshall, G. R. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01632 · Cited by 32

Linking epithelial-to-mesenchymal-transition and epigenetic modifications

Stadler, S. C., & Allis, C. D. (2012) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2012.06.007 · Cited by 33

Panobinostat penetrates the blood–brain barrier and achieves effective brain concentrations in a murine model

Homan, M. J., Franson, A. T., Ravi, K., Roberts, H. J., Pai, M. P., Liu, C., He, M., Matvekas, A., Koschmann, C. J., & Marini, B. L. (2021) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-021-04313-2 · Cited by 30

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

Novel Histone Deacetylase Inhibitors and HIV-1 Latency-Reversing Agents Identified by Large-Scale Virtual Screening

Divsalar, D. N., Simoben, C. V., Schonhofer, C., Richard, K., Sippl, W., Ntie‐Kang, F., & Tietjen, I. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00905 · Cited by 29

The Role of HDACs Inhibitors in Childhood and Adolescence AcuteLeukemias

Masetti, R., Serravalle, S., Biagi, C., & Pession, A. (2011) · BioMed Research International · doi:10.1155/2011/148046 · Cited by 29

Cytomegalovirus induces apoptosis in acute leukemia cells as a virus-versus-leukemia function

Koldehoff, M., Lindemann, M., Opalka, B., Bauer, S., Ross, R. S., & Elmaagacli, A. H. (2015) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.3109/10428194.2015.1032968 · Cited by 29

Anti-leukemic effects of histone deacetylase (HDAC) inhibition in acute lymphoblastic leukemia (ALL) cells: Shedding light on mitigating effects of NF-κB and autophagy on panobinostat cytotoxicity

Mehrpouri, M., Safaroghli‐Azar, A., Pourbagheri‐Sigaroodi, A., Momeny, M., & Bashash, D. (2020) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2020.173050 · Cited by 29

Targeting sickle cell disease root-cause pathophysiology with small molecules

Saunthararajah, Y. (2019) · Haematologica · doi:10.3324/haematol.2018.207530 · Cited by 30

Emerging Promise Of Epigenetics And Dna Methylation For The Diagnosis And Management Of Women‘S Cancers

Jones, A., Lechner, M., Fourkala, E.-O., Kristeleit, R. S., & Widschwendter, M. (2010) · Epigenomics · doi:10.2217/epi.09.47 · Cited by 27

Epimutational profile of hematologic malignancies as attractive target for new epigenetic therapies

Fratta, E., Montico, B., Rizzo, A., Colizzi, F., Sigalotti, L., & Dolcetti, R. (2016) · Oncotarget · doi:10.18632/oncotarget.10033 · Cited by 26

Histone deacetylase inhibitors: A new perspective for the treatment of leukemia

Abujamra, A. L., dos Santos, M. P., Roesler, R., Schwartsmann, G., & Brunetto, A. L. (2009) · Leukemia Research · doi:10.1016/j.leukres.2009.08.021 · Cited by 26

Dual inhibition of PI3K signaling and histone deacetylation halts proliferation and induces lethality in mantle cell lymphoma

Guo, H., Zeng, D., Zhang, H., Bell, T., Yao, J., Liu, Y., Huang, S., Li, C. J., Lorence, E., Zhou, S., et al. (2018) · Oncogene · doi:10.1038/s41388-018-0550-3 · Cited by 26

A phase I study of panobinostat in children with relapsed and refractory hematologic malignancies

Goldberg, J., Sulis, M. L., Bender, J. G., Jeha, S., Gardner, R. A., Pollard, J. A., Aquino, V., Laetsch, T. W., Winick, N. J., Fu, C., et al. (2020) · Pediatric Hematology and Oncology · doi:10.1080/08880018.2020.1752869 · Cited by 26

Discovery of indole-piperazine derivatives as selective histone deacetylase 6 inhibitors with neurite outgrowth-promoting activities and neuroprotective activities

Liang, T., Xie, Z., Dang, B., Wang, J., Zhang, T., Luan, X., Lu, T., Cao, C., & Chen, X. (2023) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2023.129148 · Cited by 26

HDAC inhibitors: Promising agents for leukemia treatment

Deng, Y., Qian, C., & He, J. (2023) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2023.09.023 · Cited by 25

Molecular Mechanism of the Cell Death Induced by the Histone Deacetylase Pan Inhibitor LBH589 (Panobinostat) in Wilms Tumor Cells

Yan-Fang, T., Li, Z., Li-Xiao, X., Fang, F., Lu, J., Li, G., Lan, C., Wang, N., Du, X., Sun, L., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0126566 · Cited by 25

Chemical application improves stress resilience in plants

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Chemotherapy with hybrid liposomes for acute lymphatic leukemia leading to apoptosis in vivo

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