Chemoproteomics profiling of HDAC inhibitors reveals selective targeting of HDAC complexes

Chromatin modifications and their function

Kouzarides, T. (2007) · Cell · doi:10.1016/j.cell.2007.02.005 · Cited by 10,883

Lysine acetylation targets protein complexes and co-regulates major cellular functions

Choudhary, C., Kumar, C., Gnad, F., Nielsen, M. L., Rehman, M., Walther, T. C., Olsen, J. V., & Mann, M. (2009) · Science · doi:10.1126/science.1175371 · Cited by 4,040

Anticancer activities of histone deacetylase inhibitors

Bolden, J. E., Peart, M. J., & Johnstone, R. W. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd2133 · Cited by 2,919

Proteome survey reveals modularity of the yeast cell machinery

Gavin, A., Aloy, P., Grandi, P., Krause, R., Böesche, M., Marzioch, M., Rau, C., Jensen, L. J., Bastuck, S., Dümpelfeld, B., et al. (2006) · Nature · doi:10.1038/nature04532 · Cited by 2,570

Pvclust: an R package for assessing the uncertainty in hierarchical clustering

Suzuki, R., & Shimodaira, H. (2006) · Bioinformatics · doi:10.1093/bioinformatics/btl117 · Cited by 2,456

Regulation of cellular metabolism by protein lysine acetylation

Zhao, S., Xu, W., Jiang, W., Yu, W., Lin, Y., Zhang, T., Yao, J., Zhou, L., Zeng, Y., Li, H., et al. (2010) · Science · doi:10.1126/science.1179689 · Cited by 1,910

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

Parts per Million Mass Accuracy on an Orbitrap Mass Spectrometer via Lock Mass Injection into a C-trap

Olsen, J. V., de Godoy, L. M. F., Li, G., Maček, B., Mortensen, P., Pesch, R., Makarov, A., Lange, O., Horning, S. R., & Mann, M. (2005) · Molecular & Cellular Proteomics · doi:10.1074/mcp.t500030-mcp200 · Cited by 1,539

Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis

Gregoretti, I., Lee, Y.-M., & Goodson, H. V. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.02.006 · Cited by 1,456

The Cell as a Collection of Protein Machines: Preparing the Next Generation of Molecular Biologists

Alberts, B. (1998) · Cell · doi:10.1016/s0092-8674(00)80922-8 · Cited by 1,411

Probing Chromatin-modifying Enzymes with Chemical Tools

Fischle, W., & Schwarzer, D. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.5b01023 · Cited by 15

A novel approach to detect resistance mechanisms reveals FGR as a factor mediating HDAC inhibitor SAHA resistance in B‐cell lymphoma

Joosten, M., Ginzel, S., Blex, C., Schmidt, D., Gombert, M., Chen, C., Linka, R. M., Gräbner, O., Hain, A., Hirsch, B., et al. (2016) · Molecular Oncology · doi:10.1016/j.molonc.2016.06.001 · Cited by 15

PAQMAN: Protein-nucleic acid affinity quantification by MAss spectrometry in nuclear extracts

Gräwe, C., Makowski, M. M., & Vermeulen, M. (2019) · Methods · doi:10.1016/j.ymeth.2019.12.003 · Cited by 15

Can a Win–Win Situation of Economy and Environment Be Achieved in Cities by the Government’s Environmental Regulations?

Li, X., Cheng, B., Hong, Q., & Xu, C. C. (2021) · Sustainability · doi:10.3390/su13115829 · Cited by 15

EFMC: Trends in Medicinal Chemistry and Chemical Biology

Auberson, Y. P., Arimondo, P. B., Duca, M., Essig, S., Grether, U., Rufer, A. C., Sbardella, G., Schopfer, U., Torrens, A., van der Stelt, M., et al. (2023) · ChemBioChem · doi:10.1002/cbic.202200690 · Cited by 16

Chemical proteomics and its impact on the drug discovery process

Miao, Q., Zhang, C., & Kast, J. (2012) · Expert Review of Proteomics · doi:10.1586/epr.12.22 · Cited by 15

Transcriptional repression of ER through hMAPK dependent histone deacetylation by class I HDACs

Plotkin, A. J., Volmar, C., Wahlestedt, C., Ayad, N. G., & El‐Ashry, D. (2014) · Breast Cancer Research and Treatment · doi:10.1007/s10549-014-3093-5 · Cited by 15

Derepressing nuclear pyruvate dehydrogenase induces therapeutic cancer cell reprogramming

Zhao, T., He, L., Wong, L. P., Mei, S., Xia, J., Xu, Y., Vranken, J. G. V., Mazzola, M. C., Chen, L., Rhee, C., et al. (2025) · Cell Metabolism · doi:10.1016/j.cmet.2025.05.009 · Cited by 14

The Class IIA Histone Deacetylase (HDAC) Inhibitor TMP269 Downregulates Ribosomal Proteins and Has Anti-Proliferative and Pro-Apoptotic Effects on AML Cells

Urwanisch, L., Unger, M. S., Sieberer, H., Dang, H.-H., Neuper, T., Regl, C., Vetter, J., Schaller, S., Winkler, S., Kerschbamer, E., et al. (2023) · Cancers · doi:10.3390/cancers15041039 · Cited by 14

Single-cell EpiChem jointly measures drug–chromatin binding and multimodal epigenome

Dong, C. F., Meng, X., Zhang, T., Guo, Z., Liu, Y., Wu, P., Chen, S., Zhou, F., Ma, Y., Xiong, H., et al. (2024) · Nature Methods · doi:10.1038/s41592-024-02360-0 · Cited by 17

Targeting transcription factor corepressors in tumor cells

Vaiopoulos, G., Kostakis, I. D., Athanasoula, K. C., & Papavassiliou, A. G. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-0986-5 · Cited by 14

Chemical Biology Approaches Confirm MCT4 as the Therapeutic Target of a Cellular Optimized Hit

Kawatkar, A., Clark, R., Hopcroft, L., Roaquin, D. A., Tomlinson, R., Zuhl, A. M., Lamont, G. M., Kettle, J. G., Critchlow, S. E., Castaldi, M. P., et al. (2023) · ACS Chemical Biology · doi:10.1021/acschembio.2c00666 · Cited by 14

TdIF1: a putative oncogene in NSCLC tumor progression

Zhang, Y., Wang, Z., Huang, Y., Ying, M., Wang, Y., Xiong, J., Liu, Q., Cao, F., Joshi, R., Liu, Y., et al. (2018) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-018-0030-9 · Cited by 14

A Comparative Study of Target Engagement Assays for HDAC1 Inhibitor Profiling

Asawa, R. R., Zakharov, A. V., Niehoff, T., Ata, C., Jadhav, A., Henderson, M. J., Simeonov, A. M., & Martinez, N. J. (2019) · SLAS DISCOVERY · doi:10.1177/2472555219883625 · Cited by 14

A Quantitative Proteomic Analysis of In Vitro Assembled Chromatin

Völker-Albert, M. C., Pusch, M. C., Fedisch, A., Schilcher, P., Schmidt, A., & Imhof, A. (2016) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m115.053553 · Cited by 14

The critical role of mode of action studies in kinetoplastid drug discovery

Fairlamb, A. H., & Wyllie, S. (2023) · Frontiers in Drug Discovery · doi:10.3389/fddsv.2023.1185679 · Cited by 13

HDAC10 inhibition represses melanoma cell growth and BRAF inhibitor resistance via upregulating SPARC expression

Ling, H., Li, Y., Peng, C., Yang, S., & Seto, E. (2024) · NAR Cancer · doi:10.1093/narcan/zcae018 · Cited by 13

Standardized processing of MALDI imaging raw data for enhancement of weak analyte signals in mouse models of gastric cancer and Alzheimer’s disease

Schwartz, M., Meyer, B., Wirnitzer, B., & Hopf, C. (2014) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-014-8356-9 · Cited by 13

Screening Pools of Compounds against Multiple Endogenously Expressed Targets in a Chemoproteomics Binding Assay

Salzer, E., Nixon, E., Drewes, G., Reinhard, F. B. M., Bergamini, G., & Rau, C. (2015) · SLAS TECHNOLOGY · doi:10.1177/2211068215595355 · Cited by 13

Chemical Tools for Probing Histone Deacetylase (HDAC) Activity

Minoshima, M., & Kikuchi, K. (2015) · Analytical Sciences · doi:10.2116/analsci.31.287 · Cited by 12

Design and development of histone deacetylase (HDAC) chemical probes for cell-based profiling

Albrow, V. E., Grimley, R. L., Clulow, J. A., Rose, C. R., Sun, J., Warmus, J. S., Tate, E. W., Jones, L. H., & Storer, R. I. (2016) · Molecular BioSystems · doi:10.1039/c6mb00109b · Cited by 13

Modulation of Donor-Specific Antibody Production After Organ Transplantation by Valproic Acid

Ye, J., Li, J., Zhou, M., Xia, R., Liu, R., & Yu, L. (2016) · Transplantation · doi:10.1097/tp.0000000000001197 · Cited by 13

Epigenetic mechanisms in Alzheimer's disease

Balázs, R. (2014) · Degenerative Neurological and Neuromuscular Disease · doi:10.2147/dnnd.s37341 · Cited by 15

Histone Deacetylases in Neurodegenerative Diseases and Their Potential Role as Therapeutic Targets: Shedding Light on Astrocytes

Pinheiro, P. D. S. M., Diniz, L. P., Franco, L. S., Siqueira, M., & Gomes, F. C. A. (2025) · Pharmaceuticals · doi:10.3390/ph18101471 · Cited by 13

Future strategies in epigenetic drug discovery

Drewes, G. (2011) · Drug Discovery Today Therapeutic Strategies · doi:10.1016/j.ddstr.2011.12.001 · Cited by 12

Rescuing lung development through embryonic inhibition of histone acetylation

Stokes, G., Li, Z., Talaba, N., Genthe, W., Brix, M. B., Pham, B., Wienhold, M. D., Sandok, G., Hernan, R., Wynn, J., et al. (2024) · Science Translational Medicine · doi:10.1126/scitranslmed.adc8930 · Cited by 12

DNTTIP2 Expression is Associated with Macrophage Infiltration and Malignant Characteristics in Low-Grade Glioma

Liu, Y.-J., Zeng, S.-H., Qian, W.-H., Tao, M.-X., Zhu, Y.-Y., & Li, J.-P. (2022) · Pharmacogenomics and Personalized Medicine · doi:10.2147/pgpm.s356326 · Cited by 12

UBE2B promotes ovarian cancer growth via promoting RAD18 mediated ZMYM2 monoubiquitination and stabilization

Zeng, X. R., Zheng, W. L., Sheng, Y., & Ma, H. (2022) · Bioengineered · doi:10.1080/21655979.2022.2048991 · Cited by 12

Synthetic Chromatin Approaches To Probe the Writing and Erasing of Histone Modifications

Fierz, B. (2014) · ChemMedChem · doi:10.1002/cmdc.201300487 · Cited by 12

Profiling technologies for the identification and characterization of small-molecule histone deacetylase inhibitors

Liao, D. (2015) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2015.10.006 · Cited by 13

Therapeutic Approaches to Histone Reprogramming in Retinal Degeneration

Berner, A., & Kleinman, M. E. (2015) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-17121-0_6 · Cited by 12

Trichostatin A blocks aldosterone‐induced Na+ transport and control of serum‐ and glucocorticoid‐inducible kinase 1 in cortical collecting duct cells

Mansley, M. K., Roe, A. J., Francis, S. L., Gill, J. H., Bailey, M. A., & Wilson, S. M. (2019) · British Journal of Pharmacology · doi:10.1111/bph.14837 · Cited by 11

Soy‐Derived Phytochemical Genistein Modifies Chromatome Topology to Restrict Cancer Cell Proliferation

Dutta, B., Park, J. E., Qing, I. T. Y., Kon, O. L., & Sze, S. K. (2018) · PROTEOMICS · doi:10.1002/pmic.201700474 · Cited by 12

Targeting G Protein‐Coupled Receptors by Capture Compound Mass Spectrometry: A Case Study with Sertindole

Blex, C., Michaelis, S., Schrey, A. K., Furkert, J., Eichhorst, J., Bartho, K., Quast, F. G., Marais, A., Hakelberg, M., Gruber, U., et al. (2017) · ChemBioChem · doi:10.1002/cbic.201700152 · Cited by 11

Antiandrogen-Equipped Histone Deacetylase Inhibitors Selectively Inhibit Androgen Receptor (AR) and AR-Splice Variant (AR-SV) in Castration-Resistant Prostate Cancer (CRPC)

Chandrasekaran, B., Tapadar, S., Wu, B., Saran, U., Tyagi, A., Johnston, A., Gaul, D. A., Oyelere, A. K., & Damodaran, C. (2023) · Cancers · doi:10.3390/cancers15061769 · Cited by 11

De novo missense variants in HDAC3 leading to epigenetic machinery dysfunction are associated with a variable neurodevelopmental disorder

Yoon, J. G., Lim, S.-K., Seo, H., Lee, S., Cho, J., Kim, S. Y., Koh, H. Y., Poduri, A., Ramakumaran, V. S., Vasudevan, P. C., et al. (2024) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2024.06.015 · Cited by 11

HDAC-driven mechanisms in anticancer resistance: epigenetics and beyond

Minisini, M., Mascaro, M., & Brancolini, C. (2024) · Cancer Drug Resistance · doi:10.20517/cdr.2024.103 · Cited by 11

The Plasma Protein Binding Proteome of Ertapenem: A Novel Compound-Centric Proteomic Approach for Elucidating Drug–Plasma Protein Binding Interactions

Baker, M. A., Schneider‐Futschik, E. K., Huang, J. X., Cooper, M. A., Li, J., & Velkov, T. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00700 · Cited by 11

Romidepsin in the Treatment of T-Cell Lymphoma†

Yang, L. P. H. (2011) · BioDrugs · doi:10.2165/11207660-000000000-00000 · Cited by 11

Strong Correlation between the Expression Levels of HDAC4 and SIRT6 in Hematological Malignancies of the Adults

Gaál, Z., Oláh, É., Rejtő, L., Erdődi, F., & Csernoch, L. J. (2016) · Pathology & Oncology Research · doi:10.1007/s12253-016-0139-5 · Cited by 11

Histone Deacetylase 2 (HDAC2) Inhibitors Containing Boron

Kavianpour, P., Gemmell, M., Kahlert, J. U., & Rendina, L. M. (2020) · ChemBioChem · doi:10.1002/cbic.202000131 · Cited by 11

Histone Deacetylase (HDAC) Inhibitors in Recent Clinical Trials for Cancer Therapy

Keller, K., & Jung, M. (2013) · Springer eBooks · doi:10.1007/978-3-642-38404-2_10 · Cited by 11

Cell-based multi-substrate assay coupled to UHPLC-ESI-MS/MS for a quick identification of class-specific HDAC inhibitors

Zwick, V., Simões‐Pires, C. A., & Cuendet, M. (2016) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2016.1180595 · Cited by 11

Novel antimyeloma therapeutic option with inhibition of the HDAC1-IRF4 axis and PIM kinase

Harada, T., Ohguchi, H., Oda, A., Nakao, M., Teramachi, J., Hiasa, M., Sumitani, R., Oura, M., Sogabe, K., Maruhashi, T., et al. (2022) · Blood Advances · doi:10.1182/bloodadvances.2022007155 · Cited by 12

Histone deacetylase 1 plays a predominant pro-oncogenic role in Eμ-myc driven B cell lymphoma

Pillonel, V., Reichert, N., Cao, C., Heideman, M. R., Yamaguchi, T., Matthias, G., Tzankov, A., & Matthias, P. (2016) · Scientific Reports · doi:10.1038/srep37772 · Cited by 10

Emerging tools to investigate bromodomain functions

Tchara, P.-E. K., Filippakopoulos, P., & Lambert, J. (2019) · Methods · doi:10.1016/j.ymeth.2019.11.003 · Cited by 12

The MLL3/4 complexes and MiDAC co-regulate H4K20ac to control a specific gene expression program

Wang, X., Rosikiewicz, W., Sedkov, Y., Mondal, B., Martinez, T. C., Kallappagoudar, S., Tvardovskiy, A., Bajpai, R., Xu, B., Pruett‐Miller, S. M., et al. (2022) · Life Science Alliance · doi:10.26508/lsa.202201572 · Cited by 10

Deoxycytidine kinase (dCK) inhibition is synthetic lethal with BRCA2 deficiency

Guantay, L., Garro, C., Siri, S. O., Pansa, M. F., Ghidelli, S., Paviolo, N. S., Racca, A. C., Nicotra, V. E., Radu, C. G., Bocco, J. L., et al. (2023) · Drug Resistance Updates · doi:10.1016/j.drup.2023.100932 · Cited by 10

Protein target discovery of drug and its reactive intermediate metabolite by using proteomic strategy

Hu, L., Fawcett, J. P., & Gu, J. (2012) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2012.02.001 · Cited by 10

Exposing the Molecular Screening Method of Indonesian Natural Products Derivate as Drug Candidates for Cervical Cancer.

Tambunan, U. S. F., Parikesit, A. A., Nasution, M. A. F., Hapsari, A., & Kerami, D. (2017) · Europe PMC (PubMed Central) · Cited by 9

Gse1, a component of the CoREST complex, is required for placenta development in the mouse

Hiver, S., Shimizu‐Mizuno, N., Ikawa, Y., Kajikawa, E., Sai, X., Nishimura, H., Takaoka, K., Nishimura, O., Kuraku, S., Tanaka, S., et al. (2023) · Developmental Biology · doi:10.1016/j.ydbio.2023.03.009 · Cited by 9

Defining cellular responses to HDAC-selective inhibitors reveals that efficient targeting of HDAC3 is required to elicit cytotoxicity and overcome naïve resistance to pan-HDACi in diffuse large B cell lymphoma

Havas, A. P., Tula-Sanchez, A. A., Steenhoek, H. M., Bhakta, A., Wingfield, T., Huntley, M. J., Nofal, A. S., Ahmed, T., Jaime-Frias, R., & Smith, C. L. (2023) · Translational Oncology · doi:10.1016/j.tranon.2023.101779 · Cited by 9

Chemical Proteomics in Drug Discovery

Drewes, G. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-364-6_2 · Cited by 9

Lysines Acetylome and Methylome Profiling of H3 and H4 Histones in Trichostatin A—Treated Stem Cells

Cozzolino, F., Iacobucci, I., Monaco, V., Angrisano, T., & Monti, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22042063 · Cited by 9

Affinity Enrichment Chemoproteomics for Target Deconvolution and Selectivity Profiling

Werner, T., Steidel, M., Eberl, H. C., & Bantscheff, M. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1024-4_17 · Cited by 9

The multi-target aspect of an MmpL3 inhibitor: The BM212 series of compounds bind EthR2, a transcriptional regulator of ethionamide activation

Moorey, A. R., Cabanillas, A., Batt, S. M., Ghidelli, S., Urones, B., Sanz, O., Lelièvre, J., Bantscheff, M., Cox, L. R., & Besra, G. S. (2021) · The Cell Surface · doi:10.1016/j.tcsw.2021.100068 · Cited by 8

Inhibition of class I HDACs preserves hair follicle inductivity in postnatal dermal cells

Park, M., Jang, S., Chung, J. H., Kwon, O., & Jo, S. J. (2021) · Scientific Reports · doi:10.1038/s41598-021-03508-0 · Cited by 10

Small Molecule Arranged Thermal Proximity Coaggregation (smarTPCA)—A Novel Approach to Characterize Protein–Protein Interactions in Living Cells by Similar Isothermal Dose–Responses

Lenz, T., & Stühler, K. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23105605 · Cited by 9

Autophagy inhibitor sensitizes MCF-7 breast cancer cells to novel cyclic tetrapeptide CTS203-induced caspase-9-dependent apoptotic cell death

Wang, S., LI, X., WANG, Q., & Xiu, Z. (2015) · Neoplasma · doi:10.4149/neo_2015_027 · Cited by 9

Application of Computational Proteomics and Lipidomics in Drug Discovery

Mishra, N. K., & Shukla, M. (2016) · Journal of Theoretical and Computational Science · doi:10.4172/2376-130x.1000105 · Cited by 9

TRPV4-Mediated Anti-nociceptive Effect of Suberanilohydroxamic Acid on Mechanical Pain

Choi, G., Yang, T., Yoo, S., Choi, S.-I., Lim, J. Y., Cho, P. S., & Hwang, S. W. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1093-x · Cited by 9

CoREST in pieces: Dismantling the CoREST complex for cancer therapy and beyond

Ismail, H., Chagraoui, J., & Sauvageau, G. (2025) · Science Advances · doi:10.1126/sciadv.ads6556 · Cited by 9

The Allosteric Regulator Inositol Phosphate Dramatically Affects the Efficacy and Selectivity of Inhibitors for Different HDAC Complexes

Pytel, W. A., Patel, U., Smalley, J. P., Millard, C. J., Brown, E. A., Pavan, A. R., Wang, S., Kalin, J. H., dos Santos, J. L., Cole, P. A., et al. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c08929 · Cited by 10

Harnessing Ionic Selectivity in Acetyltransferase Chemoproteomic Probes

Jing, Y., Montaño, J. L., Levy, M. J., López, J. E., Kung, P., Richardson, P., Krajewski, K., Florens, L. A., Washburn, M. P., & Meier, J. L. (2020) · ACS Chemical Biology · doi:10.1021/acschembio.0c00766 · Cited by 8

Quantitative proteomics analysis in small cell carcinoma of cervix reveals novel therapeutic targets

Qiu, H., Su, N., Wang, J., Yan, S., & Li, J. (2023) · Clinical Proteomics · doi:10.1186/s12014-023-09408-x · Cited by 8

Histone Deacetylase Inhibitors in Medical Therapeutics

Chun, P. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-803239-8.00034-x · Cited by 8

Deciphering lymphoma pathogenesis via state-of-the-art mass spectrometry-based quantitative proteomics

Psatha, K., Kollipara, L., Voutyraki, C., Divanach, P., Sickmann, A., Rassidakis, G. Z., Drakos, E., & Aivaliotis, M. (2016) · Journal of Chromatography B · doi:10.1016/j.jchromb.2016.11.005 · Cited by 10

Structurally Diverse Histone Deacetylase Photoreactive Probes: Design, Synthesis, and Photolabeling Studies in Live Cells and Tissue

Aboukhatwa, S. M., Hanigan, T. W., Taha, T. Y., Jayaprakash, N., Ranjan, R., El-Bastawissy, E. A., Elkersh, M. A., El-Moselhy, T. F., Frasor, J. M., Mahmud, N., et al. (2019) · ChemMedChem · doi:10.1002/cmdc.201900114 · Cited by 8

Nuclear Coregulatory Complexes in Tregs as Targets to Promote Anticancer Immune Responses

Christensen, L. M., & Hancock, W. W. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.909816 · Cited by 11

Definition of the transcription factor Td IF 1 consensus‐binding sequence through genomewide mapping of its binding sites

Koiwai, K., Kubota, T., Watanabe, N., Hori, K., Koiwai, O., & Masai, H. (2015) · Genes to Cells · doi:10.1111/gtc.12216 · Cited by 8

Mass Spectrometry-Based Chemoproteomic Approaches

Bantscheff, M. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-364-6_1 · Cited by 8

TdIF1 Recognizes a Specific DNA Sequence through Its Helix-Turn-Helix and AT-Hook Motifs to Regulate Gene Transcription

Kubota, T., Koiwai, O., Hori, K., Watanabe, N., & Koiwai, K. (2013) · PLoS ONE · doi:10.1371/journal.pone.0066710 · Cited by 8

Mapping Lysine Acetyltransferase–Ligand Interactions by Activity-Based Capture

Montgomery, D. C., & Meier, J. L. (2016) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2016.01.006 · Cited by 9

Synthesis of an Uncharged Tetra-cyclopeptide Acting as a Transmembrane Carrier: Enhanced Cellular and Nuclear Uptake

Hilário, F. F., Traore, M. D. M., Zwick, V., Berry, L., Simões‐Pires, C. A., Cuendet, M., Fantozzi, N., de Freitas, R. P., Maynadier, M., Wein, S., et al. (2017) · Organic Letters · doi:10.1021/acs.orglett.6b03776 · Cited by 8

Proteomic tools to study drug function

Mulder, C., Leijten, N. M., & Lemeer, S. (2018) · Current Opinion in Systems Biology · doi:10.1016/j.coisb.2018.05.002 · Cited by 8

Expression of the Neural REST/NRSF–SIN3 Transcriptional Corepressor Complex as a Target for Small-Molecule Inhibitors

Jayaprakash, S., Le, L. T. M., Sander, B. O., & Golas, M. M. (2020) · Molecular Biotechnology · doi:10.1007/s12033-020-00283-7 · Cited by 8

Suppression of tumor metastasis by a RECK-activating small molecule

Yoshida, Y., Yuki, K., Dan, S., Yamazaki, K., & Noda, M. (2022) · Scientific Reports · doi:10.1038/s41598-022-06288-3 · Cited by 8

Screening of histone deacetylase 1 inhibitors in natural products by capillary electrophoresis

Zhang, Y., Li, F., & Kang, J. (2017) · Analytical Methods · doi:10.1039/c7ay01428g · Cited by 7

HDAC inhibitors modulate Hippo pathway signaling in hormone positive breast cancer

Lin, T.-I., Tseng, Y.-R., Dong, M.-J., Lin, C.-Y., Chung, W.-T., Liu, C., Tsai, Y., Huang, C.-C., Tseng, L., Chao, T., et al. (2025) · Clinical Epigenetics · doi:10.1186/s13148-025-01834-y · Cited by 7

Untersuchung der Substratselektivität und Zusammensetzung endogener Histondeacetylase‐Komplexe durch chemische Sonden

Dose, A., Sindlinger, J., Bierlmeier, J., Bakirbas, A., Schulze‐Osthoff, K., Einsele‐Scholz, S., Hartl, M., Eßmann, F., Finkemeier, I., & Schwarzer, D. (2015) · Angewandte Chemie · doi:10.1002/ange.201508174 · Cited by 7

Computational analysis for selectivity of histone deacetylase inhibitor by replica-exchange umbrella sampling molecular dynamics simulations

Tsukamoto, S., Sakae, Y., Itoh, Y., Suzuki, T., & Okamoto, Y. (2018) · The Journal of Chemical Physics · doi:10.1063/1.5019209 · Cited by 7

Profiling Drug‐Protein Interactions by Micro Column Affinity Purification Combined with Label Free Quantification Proteomics†

Li, G., Xu, Y., Liu, G., Zheng, M., Zhang, X., Hang, Y., & Kang, J. (2020) · Chinese Journal of Chemistry · doi:10.1002/cjoc.202000353 · Cited by 7

Structural mass spectrometry decodes domain interaction and dynamics of the full-length Human Histone Deacetylase 2

Soloviev, Z., Bullock, J. M. A., James, J., Sauerwein, A. C., Nettleship, J. E., Owens, R. J., Hansen, D. F., Topf, M., & Thalassinos, K. (2022) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2022.140759 · Cited by 7

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Marcum, R. D., Hsieh, J., Giljen, M., Justice, E., Daffern, N., Zhang, Y., & Radhakrishnan, I. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101558 · Cited by 7

HDAC Inhibitors as Novel Therapeutics in Aging and Alzheimer’s Disease

Nott, A., Fass, D. M., Haggarty, S. J., & Tsai, L. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-391494-1.00008-2 · Cited by 8

A Quantitative Proteomics-Based Competition Binding Assay to Characterize pITAM–Protein Interactions

Hu, L., Li, Y., Lipchik, A. M., Geahlen, R. L., Parker, L. L., & Tao, W. A. (2013) · Analytical Chemistry · doi:10.1021/ac400359t · Cited by 7

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Hájek, R., Siegel, D. S. D., Orlowski, R. Z., Ludwig, H., Palumbo, A. P., & Dimopoulos, M. A. (2013) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.3109/10428194.2013.797084 · Cited by 7

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Chen, D., Xu, M., Wu, B., & Chen, L. (2017) · Journal of Otology · doi:10.1016/j.joto.2017.04.002 · Cited by 7

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Simerský, R., Chamrád, I., Kania, J., Strnad, M., Šebela, M., & Lenobel, R. (2017) · Plant Cell Reports · doi:10.1007/s00299-017-2174-4 · Cited by 7

Streamlined Target Deconvolution Approach Utilizing a Single Photoreactive Chloroalkane Capture Tag

Ohana, R. F., Levin, S., Hurst, R., Rosenblatt, M. M., Zimmerman, K., Machleidt, T., Wood, K. V., & Kirkland, T. A. (2021) · ACS Chemical Biology · doi:10.1021/acschembio.0c00987 · Cited by 6

Amidation inhibitors 4-phenyl-3-butenoic acid and 5-(acetylamino)-4-oxo-6-phenyl-2-hexenoic acid methyl ester are novel HDAC inhibitors with anti-tumorigenic properties

Ali, A., Burns, T. J., Lucrezi, J. D., May, S. W., Green, G. R., & Matesic, D. F. (2015) · Investigational New Drugs · doi:10.1007/s10637-015-0254-2 · Cited by 7

Preparation and characterization of vorinostat-coated beads for profiling of novel target proteins

Lu, C., Zhang, K., Zhang, Y., Tan, M., Li, Y., He, X., & Zhang, Y. (2014) · Journal of Chromatography A · doi:10.1016/j.chroma.2014.10.098 · Cited by 7

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Li, Y., Zhou, W., Meng, X., Murray, S., Li, L., Fronk, A., Lazaro-Camp, V. J., Wen, K., Wu, M., Dupuy, A. J., et al. (2022) · Cancers · doi:10.3390/cancers14194883 · Cited by 6

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Kempf, C. G., Dayebgadoh, G., Liu, X., & Washburn, M. P. (2017) · Expert Review of Proteomics · doi:10.1080/14789450.2017.1374860 · Cited by 6

Chemical biology approaches to study histone interactors

Burton, A. J., Hamza, G. M., Zhang, A. X., & Muir, T. W. (2021) · Biochemical Society Transactions · doi:10.1042/bst20210772 · Cited by 6

Mitotic deacetylase complex (MiDAC) recognizes the HIV-1 core promoter to control activated viral gene expression

Wilhelm, E., Poirier, M., Rocha, M. D., Bédard, M., McDonald, P. P., Lavigne, P., Hunter, C. L., & Bell, B. (2024) · PLoS Pathogens · doi:10.1371/journal.ppat.1011821 · Cited by 6

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Xu, H., Roberts, L. R., Chou, S., Pierce, B. S., Narayanan, A., & Jones, L. H. (2017) · MedChemComm · doi:10.1039/c6md00633g · Cited by 6

Comparison of polyphenol-rich wine grape seed flour-regulated fecal and blood microRNAs in high-fat, high-fructose diet-induced obese mice

Seo, K., YOKOYAMA, W. H., & Kim, H. (2020) · Journal of Functional Foods · doi:10.1016/j.jff.2020.104147 · Cited by 6

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Sun, H., Yang, K., Zhang, X., Fu, Y., Yarbro, J. M., Wu, Z., Chen, P., Chen, T., & Peng, J. (2022) · Biochemistry · doi:10.1021/acs.biochem.2c00256 · Cited by 5

1,3-Diarylpyrazolyl-acylsulfonamides Target HadAB/BC Complex in Mycobacterium tuberculosis

Singh, V., Grzegorzewicz, A. E., Fienberg, S., Müller, R. W., Khonde, L. P., Sanz, O., Alfonso, S., Urones, B., Drewes, G., Bantscheff, M., et al. (2022) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.2c00392 · Cited by 6

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Becher, I., Dittmann, A., Savitski, M. M., Hopf, C., Drewes, G., & Bantscheff, M. (2014) · ACS Chemical Biology · doi:10.1021/cb500235n · Cited by 60

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Millard, C. J., Watson, P. J., Fairall, L., & Schwabe, J. W. R. (2017) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2016.12.006 · Cited by 180

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Lechner, S., Küster, B., & München, T. U. (2023)

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Payne, N. C., & Mazitschek, R. (2022) · Cell chemical biology · doi:10.1016/j.chembiol.2022.03.002 · Cited by 33

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Luo, Y., & Li, H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228828 · Cited by 62