Chemical editing of macrocyclic natural products and kinetic profiling reveal slow, tight-binding histone deacetylase inhibitors with picomolar affinities

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 · see citing works

The many roles of histone deacetylases in development and physiology: implications for disease and therapy

Haberland, M., Montgomery, R. L., & Olson, E. N. (2008) · Nature Reviews Genetics · doi:10.1038/nrg2485 · Cited by 2,541 · see citing works

Sirtuins as regulators of metabolism and healthspan

Houtkooper, R. H., Pirinen, E., & Auwerx, J. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3293 · Cited by 2,008 · see citing works

HDAC2 negatively regulates memory formation and synaptic plasticity

Guan, J.-S., Haggarty, S. J., Giacometti, E., Dannenberg, J.-H., Joseph, N., Gao, J., Nieland, T. J. F., Zhou, Y., Wang, X., Mazitschek, R., et al. (2009) · Nature · doi:10.1038/nature07925 · Cited by 1,644 · see citing works

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

Drug-target residence time and its implications for lead optimization

Copeland, R. A., Pompliano, D. L., & Meek, T. D. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd2082 · Cited by 1,464 · see citing works

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 · see citing works

Sirt5 Is a NAD-Dependent Protein Lysine Demalonylase and Desuccinylase

Du, J., Zhou, Y., Su, X., Yu, J. J., Khan, S., Jiang, H., Kim, J., Woo, J., Kim, J. H., Choi, B. H., et al. (2011) · Science · doi:10.1126/science.1207861 · Cited by 1,429 · see citing works

Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins

Frye, R. A. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3000 · Cited by 1,409 · see citing works

New and emerging HDAC inhibitors for cancer treatment

West, A. C., & Johnstone, R. W. (2014) · Journal of Clinical Investigation · doi:10.1172/jci69738 · Cited by 1,404 · see citing works

Dimethyl sulfoxide to vorinostat: development of this histone deacetylase inhibitor as an anticancer drug

Marks, P. A., & Breslow, R. (2007) · Nature Biotechnology · doi:10.1038/nbt1272 · Cited by 1,198 · see citing works

Administration of vorinostat disrupts HIV-1 latency in patients on antiretroviral therapy

Archin, N. M., Liberty, A. L., Kashuba, A. D. M., Choudhary, S. K., Kuruc, J. D., Crooks, A. M., Parker, D., Anderson, E. M., Kearney, M. F., Strain, M. C., et al. (2012) · Nature · doi:10.1038/nature11286 · Cited by 1,149 · see citing works

Metabolic regulation of gene expression through histone acylations

Sabari, B. R., Zhang, D., Allis, C. D., & Zhao, Y. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.140 · Cited by 1,134 · see citing works

An epigenetic blockade of cognitive functions in the neurodegenerating brain

Gräff, J., Rei, D., Guan, J.-S., Wang, W.-Y., Seo, J., Hennig, K. M., Nieland, T. J. F., Fass, D. M., Kao, P. F., Kahn, M., et al. (2012) · Nature · doi:10.1038/nature10849 · Cited by 853 · see citing works

Lysine glutarylation is a protein posttranslational modification regulated by SIRT5

Tan, M., Peng, C., Anderson, K. A., Chhoy, P., Xie, Z., Dai, L., Park, J., Chen, Y., Huang, H., Zhang, Y., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.03.014 · Cited by 844 · see citing works

The drug–target residence time model: a 10-year retrospective

Copeland, R. A. (2015) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2015.18 · Cited by 726 · 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

Therapeutic application of histone deacetylase inhibitors for central nervous system disorders

Kazantsev, A. G., & Thompson, L. M. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2681 · Cited by 715 · see citing works

SIRT6 regulates TNF-α secretion through hydrolysis of long-chain fatty acyl lysine

Jiang, H., Khan, S., Wang, Y., Charron, G., He, B., Sebastian, C., Du, J., Kim, R., Ge, E., Mostoslavsky, R., et al. (2013) · Nature · doi:10.1038/nature12038 · Cited by 697 · 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

Structure of Hdac3 Bound to Co-Repressor and Inositol Tetraphosphate

Watson, P. J., Fairall, L., Santos, G. M., & Schwabe, J. W. R. (2012) · Nature · doi:10.1038/nature10728 · Cited by 505 · see citing works

The n →π* Interaction

Newberry, R. W., & Raines, R. T. (2017) · Accounts of Chemical Research · doi:10.1021/acs.accounts.7b00121 · Cited by 495 · see citing works

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 · see citing works

Potent histone deacetylase inhibitors built from trichostatin A and cyclic tetrapeptide antibiotics including trapoxin

Furumai, R., Komatsu, Y., Nishino, N., Khochbin, S., Yoshida, M., & Horinouchi, S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.1.87 · Cited by 412 · see citing works

SIRT4 is a lysine deacylase that controls leucine metabolism and insulin secretion

Anderson, K. A., Huynh, F. K., Fisher-Wellman, K., Stuart, J. D., Peterson, B. S., Douros, J. D., Wagner, G. R., Thompson, J. W., Madsen, A. S., Green, M. F., et al. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.03.003 · Cited by 326 · see citing works

Nature of Amide Carbonyl−Carbonyl Interactions in Proteins

Choudhary, A., Gandla, D., Krow, G. R., et al. (2009) · Journal of the American Chemical Society · doi:10.1021/ja901188y · Cited by 287 · see citing works

Studies on liver alcohol dehydrogenase complexes

Yonetani, T., & Theorell, H. (1964) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(64)90184-5 · Cited by 282 · see citing works

Acetylation site specificities of lysine deacetylase inhibitors in human cells

Schölz, C., Weinert, B. T., Wagner, S., Beli, P., Miyake, Y., Qi, J., Jensen, L. J., Streicher, W. W., McCarthy, A. R., Westwood, N. J., et al. (2015) · Nature Biotechnology · doi:10.1038/nbt.3130 · Cited by 271 · see citing works

Total Synthesis and Molecular Target of Largazole, a Histone Deacetylase Inhibitor

Ying, Y., Taori, K., Kim, H., Hong, J., & Luesch, H. (2008) · Journal of the American Chemical Society · doi:10.1021/ja8013727 · Cited by 222 · see citing works

HDAC4 Regulates Neuronal Survival in Normal and Diseased Retinas

Chen, B., & Cepko, C. L. (2009) · Science · doi:10.1126/science.1166226 · Cited by 192 · see citing works

Total Synthesis and Biological Mode of Action of Largazole: A Potent Class I Histone Deacetylase Inhibitor

Bowers, A., West, N., Taunton, J., Schreiber, S. L., Bradner, J. E., & Williams, R. M. (2008) · Journal of the American Chemical Society · doi:10.1021/ja8033763 · Cited by 165 · see citing works

Apicidins: Novel cyclic tetrapeptides as coccidiostats and antimalarial agents from Fusarium pallidoroseum

Singh, S. B., Zink, D. L., Polishook, J. D., Dombrowski, A. W., Darkin‐Rattray, S. J., Schmatz, D. M., & GOETZ, M. A. (1996) · Tetrahedron Letters · doi:10.1016/0040-4039(96)01844-8 · Cited by 133 · see citing works

HDAC inhibitors in HIV

Wightman, F., Ellenberg, P. C., Churchill, M. J., & Lewin, S. R. (2011) · Immunology and Cell Biology · doi:10.1038/icb.2011.95 · Cited by 123 · see citing works

Profiling of Substrates for Zinc‐dependent Lysine Deacylase Enzymes: HDAC3 Exhibits Decrotonylase Activity In Vitro

Madsen, A. S., & Olsen, C. A. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201203754 · Cited by 122 · see citing works

Design, Synthesis, Biological Evaluation, and Structural Characterization of Potent Histone Deacetylase Inhibitors Based on Cyclic α/β-Tetrapeptide Architectures

Montero, A., Beierle, J. M., Olsen, C. A., & Ghadiri, M. R. (2009) · Journal of the American Chemical Society · doi:10.1021/ja809508f · Cited by 83 · see citing works

The Effect of Various Zinc Binding Groups on Inhibition of Histone Deacetylases 1–11

Madsen, A. S., Kristensen, H. M. E., Lanz, G., & Olsen, C. A. (2013) · ChemMedChem · doi:10.1002/cmdc.201300433 · Cited by 67 · see citing works

Macrolactamization versus Macrolactonization: Total Synthesis of FK228, the Depsipeptide Histone Deacetylase Inhibitor

Wen, S., Packham, G., & Ganesan, A. (2008) · The Journal of Organic Chemistry · doi:10.1021/jo801866z · Cited by 64 · see citing works

Total synthesis of largazole and analogues: HDAC inhibition, antiproliferative activity and metabolic stability

Benelkebir, H., Marie, S., Hayden, A. L., Lyle, J., Loadman, P. M., Crabb, S. J., Packham, G., & Ganesan, A. (2011) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2011.02.024 · Cited by 58 · see citing works

Discovery of HDAC Inhibitors That Lack an Active Site Zn2+-Binding Functional Group

Vickers, C. J., Olsen, C. A., Leman, L. J., & Ghadiri, M. R. (2012) · ACS Medicinal Chemistry Letters · doi:10.1021/ml300081u · Cited by 57 · see citing works

Total Synthesis of Azumamide A and Azumamide E, Evaluation as Histone Deacetylase Inhibitors, and Design of a More Potent Analogue

Wen, S., Carey, K. L., Nakao, Y., et al. (2007) · Organic Letters · doi:10.1021/ol070046y · Cited by 55 · see citing works

Selectivity and Kinetic Requirements of HDAC Inhibitors as Progranulin Enhancers for Treating Frontotemporal Dementia

She, A., Kurtser, I., Reis, S. A., Hennig, K. M., Lai, J. F., Lang, A., Zhao, W.-N., Mazitschek, R., Dickerson, B. C., Herz, J., et al. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2017.06.010 · Cited by 50 · see citing works

Natural and Synthetic Macrocyclic Inhibitors of the Histone Deacetylase Enzymes

Maolanon, A. R., Kristensen, H. M. E., Leman, L. J., Ghadiri, M. R., & Olsen, C. A. (2016) · ChemBioChem · doi:10.1002/cbic.201600519 · Cited by 49 · see citing works

Analysis of the combined effect of two linear inhibitors on a single enzyme

Martínez-Irujo, J. J., Villahermosa, M. L., Mercapide, J., Cabodevilla, J. F., & Santiago, E. (1998) · Biochemical Journal · doi:10.1042/bj3290689 · Cited by 44 · see citing works

Total Synthesis and Full Histone Deacetylase Inhibitory Profiling of Azumamides A–E as Well as β2- epi-Azumamide E and β3-epi-Azumamide E

Villadsen, J. S., Stephansen, H. M., Maolanon, A. R., Harris, P., & Olsen, C. A. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm4008449 · Cited by 40 · see citing works

Structure and solution conformation of the cytostatic cyclic tetrapeptide WF-3161, cyclo[L-leucyl-L-pipecolyl-L-(2-amino-8-oxo-9,10-epoxydecanoyl)-D-phenylalanyl]

Kawai, M., Pottorf, R. S., & Rich, D. H. (1986) · Journal of Medicinal Chemistry · doi:10.1021/jm00161a046 · Cited by 39 · see citing works

Effects of Thionation and Fluorination on Cis–Trans Isomerization in Tertiary Amides: An Investigation of N-Alkylglycine (Peptoid) Rotamers

Engel‐Andreasen, J., Wich, K., Laursen, J. S., Harris, P., & Olsen, C. A. (2015) · The Journal of Organic Chemistry · doi:10.1021/acs.joc.5b00048 · Cited by 26 · see citing works

Inhibition of Maize Histone Deacetylases by HC Toxin, the Host-Selective Toxin of Cochliobolus carbonum

Brosch, G., Ransom, R., Lechner, T., et al. (1995) · The Plant Cell · doi:10.2307/3870201 · Cited by 24 · see citing works

Synthesis of the Thiazole–Thiazoline Fragment of Largazole Analogues

Diness, F., Nielsen, D. S., & Fairlie, D. P. (2011) · The Journal of Organic Chemistry · doi:10.1021/jo201675r · Cited by 21 · see citing works

Solution, solid phase and computational structures of apicidin and its backbone‐reduced analogs

Kranz, M., Murray, P. J., Taylor, S., et al. (2005) · Journal of Peptide Science · doi:10.1002/psc.738 · Cited by 20 · see citing works

Methyl Effect in Azumamides Provides Insight Into Histone Deacetylase Inhibition by Macrocycles

Maolanon, A. R., Villadsen, J. S., Christensen, N. J., Hoeck, C. R., Friis, T., Harris, P., Gotfredsen, C. H., Fristrup, P., & Olsen, C. A. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm501399d · Cited by 20 · see citing works

An azumamide C analogue without the zinc-binding functionality

Villadsen, J. S., Kitir, B., Wich, K., Friis, T., Madsen, A. S., & Olsen, C. A. (2014) · MedChemComm · doi:10.1039/c4md00252k · Cited by 19 · see citing works

Histone deacetylase 11 is an ε-N-Myristoyllysine hydrolase

Moreno-Yruela, C., Galleano, I., Madsen, A. S., & Olsen, C. A. (2018) · Cell Chemical Biology · doi:10.1016/j.chembiol.2018.04.007 · Cited by 149 · see citing works

The Zinc-Binding Group Effect: Lessons from Non-Hydroxamic Acid Vorinostat Analogs

Geurs, S., Clarisse, D., De Bosscher, K., & D’hooghe, M. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00226 · Cited by 58 · see citing works

Histone Deacetylase Inhibitors: A Review on Class-I Specific Inhibition

Behera, J., Jayaprakash, V., & Sinha, B. N. (2015) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/1389557515666150521162237 · Cited by 28 · see citing works

Potential non-oncological applications of histone deacetylase inhibitors.

Ververis, K., & Karagiannis, T. C. (2011) · Europe PMC (PubMed Central) · Cited by 29 · see citing works

Overview of the Classical Histone Deacetylase Enzymes and Histone Deacetylase Inhibitors

Ververis, K., & Karagiannis, T. C. (2012) · ISRN Cell Biology · doi:10.5402/2012/130360 · Cited by 18 · see citing works

Review for "A straightforward method for measuring binding affinities of ligands to proteins of unknown concentration in biological tissues"

(2025) · doi:10.1039/d5sc02460a/v2/review3

The shielding effect of metal complexes on the binding affinities of ligands to metalloproteins

Chen, D., Li, Y., Guo, W. F., Li, Y., Savidge, T., Li, X., & Fan, X. (2018) · Physical Chemistry Chemical Physics · doi:10.1039/c8cp06555a · Cited by 6 · see citing works