Cloning and Characterization of a Novel Human Class I Histone Deacetylase That Functions as a Transcription Repressor

Molecular Cloning: A Laboratory Manual

Sambrook, J., Fritsch, E., & Maniatis, T. (1989) · UCLA - Biblioteca de Ciencias de la Salud · Cited by 133,589

Molecular cloning: A laboratory manual

Deininger, P. L. (1990) · Analytical Biochemistry · doi:10.1016/0003-2697(90)90595-z · Cited by 84,684

Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei

Dignam, J. D., Lebovitz, R. M., & Roeder, R. G. (1983) · Nucleic Acids Research · doi:10.1093/nar/11.5.1475 · Cited by 11,262

[6] Use of T7 RNA polymerase to direct expression of cloned genes

Studier, F. W., Rosenberg, A. H., Dunn, J. J., & Dubendorff, J. W. (1990) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(90)85008-c · Cited by 6,562

The Transcriptional Coactivators p300 and CBP Are Histone Acetyltransferases

Ogryzko, V. V., Schiltz, R. L., Russanova, V., Howard, B. H., & Nakatani, Y. (1996) · Cell · doi:10.1016/s0092-8674(00)82001-2 · Cited by 2,952

Histone acetylation in chromatin structure and transcription

Grunstein, M. (1997) · Nature · doi:10.1038/38664 · Cited by 2,884

Sequence and Characterization of a Coactivator for the Steroid Hormone Receptor Superfamily

Oñate, S. A., Tsai, S. Y., Tsai, M., & O’Malley, B. W. (1995) · Science · doi:10.1126/science.270.5240.1354 · Cited by 2,398

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. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44885-x · Cited by 1,856

A Mammalian Histone Deacetylase Related to the Yeast Transcriptional Regulator Rpd3p

Taunton, J., Hassig, C. A., & Schreiber, S. L. (1996) · Science · doi:10.1126/science.272.5260.408 · Cited by 1,829

Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors

Finnin, M. S., Donigian, J. R., Cohen, A., Richon, V. M., Rifkind, R. A., Marks, P. A., Breslow, R., & Pavletich, N. P. (1999) · Nature · doi:10.1038/43710 · Cited by 1,714

The X chromosome’s influences on the human brain

Jiang, Z., Sullivan, P. F., Li, T., Zhao, B., Wang, X., Luo, T., Huang, S.-C., Guan, P. Y., Chen, J., Yang, Y., et al. (2025) · Science Advances · doi:10.1126/sciadv.adq5360 · Cited by 20

Assessment for the identification of better HDAC inhibitor class through binding energy calculations and descriptor analysis

Kalyaanamoorthy, S., & Kumar, G. R. (2008) · Bioinformation · doi:10.6026/97320630003218 · Cited by 14

HDAC8 As an Emerging Target in Drug Discovery With Special Emphasis on Medicinal Chemistry

Rajaraman, S., Balakrishnan, R., Deshmukh, D., Ganorkar, A., Biswas, S., Pulya, S., & Ghosh, B. (2023) · Future Medicinal Chemistry · doi:10.4155/fmc-2023-0054 · Cited by 13

5 Histone Deacetylase Inhibitors: A Novel Class of Anti-Cancer Agents on its Way to the Market

Körner, M., & Tibes, U. (2008) · Progress in medicinal chemistry · doi:10.1016/s0079-6468(07)00005-7 · Cited by 13

Exploring the Potential of Phytocompounds for Targeting Epigenetic Mechanisms in Rheumatoid Arthritis: An In Silico Study Using Similarity Indexing

Deshpande, S. H., Bagewadi, Z. K., Khan, T. M. Y., Mahnashi, M. H., Shaikh, I. A., Alshehery, S., Khan, A. A., Patil, V. S., & Roy, S. (2023) · Molecules · doi:10.3390/molecules28062430 · Cited by 12

A role for the histone deacetylase HDAC4 in the life-cycle of HIV-1-based vectors

Smith, J. A., Yeung, J., Kao, G. D., & Daniel, R. (2010) · Virology Journal · doi:10.1186/1743-422x-7-237 · Cited by 12

Chromosomal organization and localization of the human histone deacetylase 9 gene (HDAC9)

Mahlknecht, U., Schnittger, S., Will, J., Çiçek, N., & Hoelzer, D. F. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00193-6 · Cited by 12

Application of Ligand- and Structure-Based Prediction Models for the Design of Alkylhydrazide-Based HDAC3 Inhibitors as Novel Anti-Cancer Compounds

Bülbül, E. F., Robaa, D., Sun, P., Mahmoudi, F., Melesina, J., Zessin, M., Schutkowski, M., & Sippl, W. (2023) · Pharmaceuticals · doi:10.3390/ph16070968 · Cited by 11

Identification of new quinic acid derivatives as histone deacetylase inhibitors by fluorescence-based cellular assay

Son, D., Kim, C. S., Lee, K. R., & Park, H. (2016) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2016.03.010 · Cited by 11

Binding mechanism and distant regulation of histone deacetylase 8 by PCI-34051

Luo, Y., Yan, Z., Chu, X., Zhang, Y., Qiu, Y., & Li, H. (2025) · Communications Biology · doi:10.1038/s42003-025-07649-0 · Cited by 10

Fluorescent molecular probe-based activity and inhibition monitoring of histone deacetylases

Roopa, Priya, B., Bhalla, V., Kumar, M., & Kumar, N. (2021) · Chemical Communications · doi:10.1039/d1cc04034k · Cited by 9

Histone deacetylase inhibitory activity of hydroxycapsaicin, a synthetic derivative of capsaicin, and its cytotoxic effects against human colon cancer cell lines

Senawong, T., Wongphakham, P., SAIWICHAI, T., Phaosiri, C., & Kumboonma, P. (2015) · TURKISH JOURNAL OF BIOLOGY · doi:10.3906/biy-1409-60 · Cited by 10

Effect of sodium butyrate on HDAC8 mRNA expression in colorectal cancer cell lines and molecular docking study of LHX1 - sodium butyrate interaction

Forouzesh, F., Ghiaghi, M., & Rahimi, H. (2020) · EXCLI journal · doi:10.17179/excli2020-2010 · Cited by 9

A detail survey and analysis of selectivity criteria for indole-based histone deacetylase 8 (HDAC8) inhibitors

Moinul, M., Amin, S. A., Khatun, S., Das, S., Jha, T., & Gayen, S. (2022) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2022.133967 · Cited by 9

Drug Discovery and Target Identification against Schistosomiasis: A Reality Check on Progress and Future Prospects

Cheuka, P. M. (2021) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026621666210924101805 · Cited by 11

Hit Identification and Functional Validation of Novel Dual Inhibitors of HDAC8 and Tubulin Identified by Combining Docking and Molecular Dynamics Simulations

Curcio, A., Rocca, R., Chiera, F., Cantafio, M. E. G., Valentino, I., Ganino, L., Murfone, P., Simone, A. D., Napoli, G. D., Alcaro, S., et al. (2024) · Antioxidants · doi:10.3390/antiox13111427 · Cited by 8

Phenolic compounds as histone deacetylase inhibitors: binding propensity and interaction insights from molecular docking and dynamics simulations

Uba, A. İ., & Zengin, G. (2023) · Amino Acids · doi:10.1007/s00726-023-03249-6 · Cited by 8

A miniaturized readout strategy for endogenous histone deacetylase activity

Jost, J. O., Hanswillemenke, A., & Schwarzer, D. (2015) · Molecular BioSystems · doi:10.1039/c5mb00326a · Cited by 7

Mutation in histone deacetylase HDA-3 leads to shortened locomotor healthspan in Caenorhabditis elegans

Kawamura, K., & MARUYAMA, I. N. (2020) · Aging · doi:10.18632/aging.202296 · Cited by 7

Discovery of non-substrate, environmentally sensitive turn-on fluorescent probes for imaging HDAC8 in tumor cells and tissue slices

Huang, C., Shu, Y., Zhu, Y., Liu, H., Wang, X., Wen, H., Liu, J., & Li, W. (2022) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2022.116821 · Cited by 7

Effects of trichostatin A on HDAC8 expression, proliferation and cell cycle of Molt-4 cells

He, J., Liu, H., & Chen, Y. (2006) · Journal of Huazhong University of Science and Technology [Medical Sciences] · doi:10.1007/s11596-006-0511-x · Cited by 7

Design and in silico screening of aryl allyl mercaptan analogs as potential histone deacetylases (HDAC) inhibitors

Singhal, S., Pathak, M., Agrawala, P. K., & Ojha, H. (2020) · Heliyon · doi:10.1016/j.heliyon.2020.e03517 · Cited by 6

An in silico mechanistic insight into HDAC8 activation facilitates the discovery of new small-molecule activators

Du, J., Li, W., Liu, B., Zhang, Y., Yu, J., Hou, X., & Fang, H. (2020) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2020.115607 · Cited by 6

Pharmacoepigenetics of Histone Deacetylase Inhibitors in Cancer

Garmpis, N., Damaskos, C., Garmpi, A., Valsami, S. I., & Dimitroulis, D. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-813939-4.00013-9 · Cited by 5

Inhibition of HDAC8 Reduces the Proliferation of Adult Neural Stem Cells in the Subventricular Zone

Fukuda, M., Fujita, Y., Hino, Y., Nakao, M., Shirahige, K., & Yamashita, T. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25052540 · Cited by 5

Lysine deacetylase inhibitors have low selectivity in cells and exhibit predominantly off‐target effects

Bornes, K. E., Moody, M. A., Huckaba, T. M., Benz, M. C., McConnell, E. C., Foroozesh, M. K., Barnes, V., Collins‐Burow, B. M., Burow, M. E., Watt, T. J., et al. (2024) · FEBS Open Bio · doi:10.1002/2211-5463.13896 · Cited by 6

Oxidative Stress and Cardiac Muscle

Maejima, Y., Zablocki, D., & Sadoshima, J. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-381510-1.00023-5 · Cited by 5

Acetanilide and bromoacetyl-lysine derivatives as activators for human histone deacetylase 8

Mukhtar, Y. M., Huang, Y., Liu, J., Chen, D., & Zheng, W. (2017) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2017.04.037 · Cited by 5

Molecular Structure and Function of Zinc-Dependent Histone Deacetylases

Christianson, D. W. (2026) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-051424-053005 · Cited by 4

Purification of active recombinant human histone deacetylase 1 (HDAC1) overexpressed in Escherichia coli

Stefan, A., Calonghi, N., Schipani, F., Piaz, F. D., Sartor, G., & Hochkoeppler, A. (2018) · Biotechnology Letters · doi:10.1007/s10529-018-2585-5 · Cited by 4

Purification and enzymatic assay of class I histone deacetylase enzymes

Adams, M. K., Banks, C. A. S., Miah, S., Killer, M., & Washburn, M. P. (2019) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2019.07.014 · Cited by 4

The transcriptional repression activity of STAF65γ is facilitated by promoter tethering and nuclear import of class IIa histone deacetylases

Hsieh, F., Chen, N.-T., Yao, Y.-L., Wang, S., Chen, J. J. W., Lai, C., & Yang, W. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.05.007 · Cited by 4

Evaluating the Effect of HDAC8 Inhibition in Malignant Peripheral Nerve Sheath Tumors

Lopez, G., & Pollock, R. E. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6527-4_27 · Cited by 4

Targeting cancers and metabolic disorders: The prospects of combining HDAC8 inhibitor and activator

Yusif, M. M. (2022) · European Journal of Medicinal Chemistry Reports · doi:10.1016/j.ejmcr.2022.100097 · Cited by 4

Escaping the Cut by Restriction Enzymes Through Single-Strand Self-Annealing of Host-Edited 12-bp and Longer Synthetic Palindromes

Castro-Chávez, F. (2011) · DNA and Cell Biology · doi:10.1089/dna.2011.1339 · Cited by 4

The pivotal role of the X-chromosome in the genetic architecture of the human brainPreprint

Jiang, Z., Sullivan, P. F., Li, T., Zhao, B., Wang, X., Luo, T., Huang, S., Guan, P. Y., Chen, J., Yang, Y., et al. (2023) · medRxiv · doi:10.1101/2023.08.30.23294848 · Cited by 4

Discovery of Histone Deacetylase 8-Specific Proteolysis-Targeting Chimeras with Anticancer Activity against Hematological Malignancies

Zhai, S., Kemkes, M., Kponomaizoun, C.-E., Gerhartz, J., Feller, F., Tu, J., Pieńkowska, D. E., Schliehe‐Diecks, J., Dressel, I., Gütschow, M., et al. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c00939 · Cited by 3

Histone Deacetylases, the Erasers of the Code

Lamberti, M. J., Vera, R. E., Vittar, N. B. R., & Schneider, G. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802389-1.00009-5 · Cited by 3

Epigenetic Targets and Cancer Drug Discovery

Woster, P. M. (2010) · Annual reports in medicinal chemistry · doi:10.1016/s0065-7743(10)45015-0 · Cited by 3

DNA Methylation and Histone Deacetylation: Interplay and Combined Therapy in Cancer

Qiu, Y., Shabashvili, D., Li, X., Kumari, P., Chen, M., & Zajac‐Kaye, M. (2012) · InTech eBooks · doi:10.5772/35977 · Cited by 3

Trichostatin a regulates hGCN5 expression and cell cycle on Daudi cells in vitro

Liu, H., Chen, Y., Cui, G., Wu, G., Wang, T., & Hu, J. (2006) · Journal of Huazhong University of Science and Technology [Medical Sciences] · doi:10.1007/s11596-006-0512-9 · Cited by 3

Experimental and Theoretical Investigation of the Coordination of 8-Hydroxquinoline Inhibitors to Biomimetic Zinc Complexes and Histone Deacetylase 8 (HDAC8)

Baudino, A. M., Ciaccio, H. F., Turski, M. J., Akins, X. A., Cao, P. S., Morales, E., Sommer, R. D., Johnson, A. R., Wink, D. J., Grice, K. A., et al. (2024) · Foundations · doi:10.3390/foundations4030024 · Cited by 2

The impactful role of the HDACs in the regulation of gene expression and as targets for disease therapy

Bree, B. A. V., & Eichner, L. J. (2026) · Science Advances · doi:10.1126/sciadv.aee7295 · Cited by 2

In Silico Discovery of Class IIb HDAC Inhibitors: The State of Art

Khatun, S., Amin, S. A., Gayen, S., & Jha, T. (2023) · Challenges and advances in computational chemistry and physics · doi:10.1007/978-3-031-33871-7_2 · Cited by 2

Inhibition of HDAC8 mitigates AKI by reducing DNA damage and promoting homologous recombination repair

Wang, Y., Yu, C. Y., Yu, J., Shen, F., Du, X., Liu, N., & Zhuang, S. (2024) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.70114 · Cited by 2

Manipulating Engram Histone Acetylation Alters Memory Consolidation

Watt, L., Glauser, L., Coda, D. M., & Gräff, J. (2025) · Hippocampus · doi:10.1002/hipo.70041 · Cited by 2

A Role for Cytoskeletal Protein Acetylation in Modulating Myometrial Activity

Europe‐Finner, G. N., Taggart, M. J., & Karolczak‐Bayatti, M. (2012) · Reproductive Sciences · doi:10.1177/1933719111432876 · Cited by 2

Novel Small Molecules in the Treatment of Lymphomas

Gerecitano, J. F., & O’Connor, O. A. (2008) · Springer eBooks · doi:10.1007/978-0-387-29346-2_14 · Cited by 2

HDAC inhibitors: A novel approach to hyperglycaemia management and treatment

Suchitra, M., Kusuma, P. K., Katagi, M. S., Venkateswarlu, G., & Mahalakshmi, P. (2023) · Health Sciences Review · doi:10.1016/j.hsr.2023.100137 · Cited by 3

Determining HDAC8 Substrate Specificity.

Wolfson, N. A. (2014) · Deep Blue (University of Michigan) · Cited by 2

Exploring the functions of JAKMIP1 in neuronal IL-6/STAT3 signaling and its relevance to chromosome 15q-duplication syndromePreprint

Gandawijaya, J., Martin, E.-R., Takamura, N., Harlow, C. E., Bamford, R. A., Mia, Z., Smith, R. G., Morgan, N. G., Inaba‐Inoue, S., Mill, J. S., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.21.683757 · Cited by 2

Zinc cofactor in human histone deacetylase 8: Requirement for function and opportunity for drug discovery

Garcia-Franco, P. M., Falcó-Martí, F. J., Jeblaoui, H., del Rio, M. A., Ortega-Alarcón, D., Vega, S., Galano-Frutos, J. J., Abián, O., & Velázquez‐Campoy, A. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.149851 · Cited by 1

Targeted HDAC8 inhibition with non-hydroxamate [1,2,4]triazolo[4,3-a] quinoline compounds

Bandaru, N. V. M. R., Fathima, A., Sengar, S., Schweipert, M., Chaitanya, K. S., Mohammed, M.-U.-R., Gore, S. T., Trinath, J., Sharma, V., Abbineni, C., et al. (2026) · Scientific Reports · doi:10.1038/s41598-026-38490-y · Cited by 1

The histone deacetylase family in health and disease

Wen, R., Yang, Y., Zhang, T., Zhang, S.-Y., Yang, X.-R., Zhang, L.-Y., Hao, P.-H., Zheng, Y., Ni, Y., & Zhang, T. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-026-02764-8 · Cited by 1

Docking belinostat into HDAC 8 using autodock tool

Thao, H. N., De, T., Hue, B. T. B., Tuan, N. T., Bach, L. T., Quoc, N. C., Si, N. T., Toan, N. H., & Quy, H. T. K. (2020) · Can Tho University Journal of Science · doi:10.22144/ctu.jen.2020.009 · Cited by 1

Histone modifications

Morse, R. H. (2024) · Elsevier eBooks · doi:10.1016/b978-0-12-814809-9.00002-0 · Cited by 1

Histone Deacetylases

Zheng, S., Barczak, W., Liu, G., & Thangue, N. B. L. (2024) · Royal Society of Chemistry eBooks · doi:10.1039/9781837674916-00228 · Cited by 1

Oncolytic Viruses and Histone Deacetylase Inhibitors

Patil, V. M., & Gupta, S. P. (2014) · CRC Press eBooks · doi:10.1201/b16780-14 · Cited by 1

Increasing the Yield of Thy-1 EGFP Expression in Insect and Mammalian Cells

Kasprzak, A. J. (2005) · Cited by 1

Function of the CHD4/Mi-2ß chromatin remodelling ATPase during neural development of Xenopus laevis

Nieberler, M. (2012) · Electronic Theses of LMU Munich (Ludwig-Maximilians-Universität München) · doi:10.5282/edoc.13954 · Cited by 1

Towards the Development of Tropolone Natural Product Derivatives as Novel, Potent Anticancer Therapeutics that Selectively Target Histone Deacetylase (HDAC) Enzymes

Ononye, S. N. (2013) · OpenCommons at University of Connecticut (University of Connecticut) · Cited by 1

The Role of Histone Deacetylases in Cytokine Regulation in Human Gestational Tissues

Munro, S. K. (2013) · ResearchSpace (University of Auckland) · Cited by 1

The role of class I histone deacetylases in cardiac development of chicken embryos

Engelmaier, C. (2011) · University of Vienna · doi:10.25365/thesis.15429

Funktionelle Charakterisierung bakterieller Histondeacetylase-ähnlicher Amidohydrolasen (HDAH)

Hildmann, C. (2005) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-609

A Potential Tumor Suppressive Role of SIRT1 in Cancer

Kabra, N. (2010) · Digital Commons - University of South Florida (University of South Florida)

Entwicklung von Substraten und Inhibitoren pharmakologisch relevanter Proteintargets

Riester, D. (2005) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-1405

Human histone deacetylase 1: Mutagenesis and small molecule studies

Wambua, M. K. (2013)

Entwicklung eines HTS-geeigneten Enzymtests für Histondeacetylasen zur Entwicklung von HDAC-Inhibitoren

Wegener, D. (2004) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-545

Einfluss der Histon Deacetylase 6 auf den Glucocorticoid Rezeptor-vermittelten Glucosestoffwechsel

Winkler, R. (2012) · Universitätsbibliothek der FU Berlin Hochschulschriftenstelle u. Dokumentenserver · doi:10.17169/refubium-4337

in adult T-cell leukemia/lymphoma HDAC8 and induces expression of FRA-2 is a direct target gene of SOX4

Higuchi, T., Nakayama, T., Arao, T., Nishio, K., & Yoshie, O. (2013)

The Biology of HDAC8, a Unique Class I Histone Deacetylase

Waltregny, D., & Castronovo, V. (2006) · Humana Press eBooks · doi:10.1385/1-59745-024-3:87

Mammalian Mat1 subunit of Transcription Factor IIH in gene-specific and general transcription

Helenius, K. (2011) · Työväentutkimus Vuosikirja

Erasers of Histone Acetylation: The Histone Deacetylase EnzymesPreprint

Seto, E., & Yoshida, M. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a018713 · Cited by 2,105

Role of Histone Deacetylases in Transcriptional Control of the Hepatic Stellate Cell Phenotype

Rombouts, K., Niki, T., Yoshida, M., & Geerts, A. E. (2003) · Elsevier eBooks · doi:10.1016/b978-012525251-5/50012-9

Structural and functional investigation of cargo recognition by exportins

Aksu, M. (2016) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-5929

Elucidating the Role of HDAC8 in Anthrax Lethal Toxin-Induced Pyroptosis and Cytokine Gene Silencing in Macrophages

Reid, C. (2015) · Scholarship@Western (Western University)

Histone Deacetylase 3 Coordinates Heart Development Through Stage-Specific Roles in Cardiac Progenitor Cells

Lewandowski, S. L. (2016) · eScholarship@UMassChan · doi:10.13028/m26p4d

Characterization and expression of histone deacetylase 1 (athd1) in Arabidopsis thaliana

Fong, M. K. (2005) · OakTrust (Texas A&M University Libraries)

Analysis of the physiological role of histone deacetylase 3 (HDAC3) and its regulation by inositol phosphates

Wright, L. C. (2017) · Figshare

Nghiên cứu tương tác của vorinostat với enzyme HDAC8 (1T67) bằng Autodock

Quốc, N. C., Đệ, T. Q., Tuân, N. T., & Huê, B. T. B. (2020) · Can Tho University Journal of Science · doi:10.22144/ctu.jvn.2020.145

Identification of AtHD2C as a novel regulator of ABA signaling in Arabidopsis thaliana

Sridhar, S. (2005) · doi:10.33915/etd.4194

Targeting (de)acetylation: A Diversity of Mechanism and Disease

Quaas, C. E., & Long, D. T. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-820472-6.00076-1

Histone Deacetylase Inhibitors

Sefhore, O., & Ling, S. (2021) · Resistance to targeted anti-cancer therapeutics · doi:10.1007/978-3-030-73440-4_7

Targeting Histone deacetylases (HDAC) for the treatment of soft tissue sarcoma

Lopez, G. (2013) · Digital Commons-TMC (Texas Medical Center)

Oncolytic Viruses and Histone Deacetylase Inhibitors

Patil, V. M., & Gupta, S. (2014) · CRC Press eBooks · doi:10.1201/b16780-15

Retinoids

Leid, M. E. (2003) · Wiley eBooks · doi:10.1002/0471266949.bmc065

Epigenomic Imaging of Neuropsychiatric Diseases

Bahari‐Javan, S. (2013) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-4280

Assessment of Epigenetic profile in Alzheimer's disease

Agbemenyah, H. Y. (2012) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-3213

Supplementary Methods from Binding of the JmjC Demethylase JARID1B to LSD1/NuRD Suppresses Angiogenesis and Metastasis in Breast Cancer Cells by Repressing Chemokine CCL14

Li, Q., Shi, L., Gui, B., Yu, W., Wang, J., Zhang, D., Han, X., Yao, Z., & Shang, Y. (2023) · doi:10.1158/0008-5472.22388570

Data from MGCD0103, a novel isotype-selective histone deacetylase inhibitor, has broad spectrum antitumor activity in vitro and in vivo

Fournel, M., Bonfils, C., Yu, H., Yan, P. T., Trachy-Bourget, M.-C., Kalita, A., Liu, J., Lu, A., Zhou, N. Z., Robert, M., et al. (2023) · doi:10.1158/1535-7163.c.6531123

Data from MGCD0103, a novel isotype-selective histone deacetylase inhibitor, has broad spectrum antitumor activity in vitro and in vivo

Fournel, M., Bonfils, C., Yu, H., Yan, P. T., Trachy-Bourget, M.-C., Kalita, A., Liu, J., Lu, A., Zhou, N. Z., Robert, M., et al. (2023) · doi:10.1158/1535-7163.c.6531123.v1

Supplementary Methods from Binding of the JmjC Demethylase JARID1B to LSD1/NuRD Suppresses Angiogenesis and Metastasis in Breast Cancer Cells by Repressing Chemokine CCL14

Li, Q., Shi, L., Gui, B., Yu, W., Wang, J., Zhang, D., Han, X., Yao, Z., & Shang, Y. (2023) · doi:10.1158/0008-5472.22388570.v1

Data from Histone Deacetylase Cytoplasmic Trapping by a Novel Fluorescent HDAC Inhibitor

Kong, Y., Jung, M., Wang, K., Grindrod, S. C., Velena, A., Lee, S. A., Dakshanamurthy, S., Yang, Y., Miessau, M., Zheng, C., et al. (2023) · doi:10.1158/1535-7163.c.6535311

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