Targeting the acetylation signaling pathway in cancer therapy

Hallmarks of Cancer: The Next Generation

Hanahan, D., & Weinberg, R. A. (2011) · Cell · doi:10.1016/j.cell.2011.02.013 · Cited by 66,590 · see citing works

Nutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1

Rodgers, J. T., Lerin, C., Haas, W., Gygi, S. P., Spiegelman, B. M., & Puigserver, P. (2005) · Nature · doi:10.1038/nature03354 · Cited by 3,160 · see citing works

hSIR2SIRT1 Functions as an NAD-Dependent p53 Deacetylase

Vaziri, H., Dessain, S. K., Eaton, E. N., Imai, S., Frye, R. A., Pandita, T. K., Guarente, L., & Weinberg, R. A. (2001) · Cell · doi:10.1016/s0092-8674(01)00527-x · Cited by 2,653 · see citing works

ACETYLATION AND METHYLATION OF HISTONES AND THEIR POSSIBLE ROLE IN THE REGULATION OF RNA SYNTHESIS

Allfrey, V. G., Faulkner, R. D., & Mirsky, A. E. (1964) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.51.5.786 · Cited by 2,649 · see citing works

Activation of p53 Sequence-Specific DNA Binding by Acetylation of the p53 C-Terminal Domain

Gu, W., & Roeder, R. G. (1997) · Cell · doi:10.1016/s0092-8674(00)80521-8 · Cited by 2,559 · 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

The two NF-κB activation pathways and their role in innate and adaptive immunity

Bonizzi, G., & Karin, M. (2004) · Trends in Immunology · doi:10.1016/j.it.2004.03.008 · Cited by 2,535 · see citing works

Genomic instability — an evolving hallmark of cancer

Negrini, S., Gorgoulis, V. G., & Halazonetis, T. D. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2858 · Cited by 2,397 · see citing works

Negative Control of p53 by Sir2α Promotes Cell Survival under Stress

Luo, J., Nikolaev, A. Y., Imai, S.-I., Chen, D., Su, F., Shiloh, A., Guarente, L., & Gu, W. (2001) · Cell · doi:10.1016/s0092-8674(01)00524-4 · Cited by 2,081 · see citing works

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 2,019 · see citing works

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 · see citing works

Vascular Endothelial Growth Factor (VEGF) and Its Receptor (VEGFR) Signaling in Angiogenesis: A Crucial Target for Anti- and Pro-Angiogenic Therapies

Shibuya, M. (2011) · Genes & Cancer · doi:10.1177/1947601911423031 · Cited by 1,778 · see citing works

Immune evasion in cancer: mechanistic basis and therapeutic strategies

Vinay, D. S., Ryan, E. P., Pawelec, G., Talib, W. H., Stagg, J., Elkord, E., Lichtor, T., Decker, W. K., Whelan, R. L., Kumara, H. M. C. S., et al. (2015) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2015.03.004 · Cited by 1,625 · see citing works

Substrate and Functional Diversity of Lysine Acetylation Revealed by a Proteomics Survey

Kim, S. C., Sprung, R., Chen, Y., Xu, Y., Ball, H., Pei, J., Cheng, T., Kho, Y., Xiao, H., Xiao, L., et al. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.06.026 · Cited by 1,487 · see citing works

Angiogenesis in cancer

Nishida, N., Yano, H., Nishida, T., Kamura, T., & Kojiro, M. (2006) · Vascular Health and Risk Management · doi:10.2147/vhrm.2006.2.3.213 · Cited by 1,467 · 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

Acetyl Coenzyme A: A Central Metabolite and Second Messenger

Pietrocola, F., Galluzzi, L., Pedro, J. M. B., Madeo, F., & Kroemer, G. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.014 · Cited by 1,349 · see citing works

The growing landscape of lysine acetylation links metabolism and cell signalling

Choudhary, C., Weinert, B. T., Nishida, Y., Verdin, E., & Mann, M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3841 · Cited by 1,324 · see citing works

Regulation of pgc-1α, a nodal regulator of mitochondrial biogenesis

Fernandez-Marcos, P. J., & Auwerx, J. (2011) · The American Journal of Clinical Nutrition · doi:10.3945/ajcn.110.001917 · Cited by 1,237 · see citing works

Functions and mechanisms of non-histone protein acetylation

Narita, T., Weinert, B. T., & Choudhary, C. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0081-3 · Cited by 1,232 · see citing works

Duration of Nuclear NF-κB Action Regulated by Reversible Acetylation

Chen, L., Fischle, W., Verdin, E. M., & Greene, W. C. (2001) · Science · doi:10.1126/science.1062374 · Cited by 1,231 · see citing works

Histone Deacetylase Inhibitors as Anticancer Drugs

Eckschlager, T., Plch, J., Stiborova, M., & Hrabeta, J. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18071414 · Cited by 1,206 · see citing works

DNA damage activates p53 through a phosphorylation–acetylation cascade

Sakaguchi, K., Herrera, J. E., Saito, S., Miki, T., Bustin, M., Vassilev, A., Anderson, C. W., & Appella, E. (1998) · Genes & Development · doi:10.1101/gad.12.18.2831 · Cited by 1,204 · see citing works

NF-κB and the immune response

Hayden, M. S., West, A. P., & Ghosh, S. (2006) · Oncogene · doi:10.1038/sj.onc.1209943 · Cited by 1,178 · see citing works

Alcohol Metabolism

Cederbaum, A. I. (2012) · Clinics in Liver Disease · doi:10.1016/j.cld.2012.08.002 · Cited by 1,145 · see citing works

Reprogramming glucose metabolism in cancer: can it be exploited for cancer therapy?

Hay, N. (2016) · Nature reviews. Cancer · doi:10.1038/nrc.2016.77 · Cited by 1,124 · see citing works

Acetylation of Metabolic Enzymes Coordinates Carbon Source Utilization and Metabolic Flux

Wang, Q., Zhang, Y., Yang, C., Xiong, H., Lin, Y., Yao, J., Li, H., Xie, L., Zhao, W., Yao, Y., et al. (2010) · Science · doi:10.1126/science.1179687 · Cited by 1,008 · see citing works

The role of histone deacetylases (HDACs) in human cancer

Ropero, S., & Esteller, M. (2007) · Molecular Oncology · doi:10.1016/j.molonc.2007.01.001 · Cited by 1,007 · see citing works

New nomenclature for chromatin-modifying enzymes

Allis, C. D., Berger, S. L., Cote, J., Dent, S., Jenuwien, T., Kouzarides, T., Pillus, L., Reinberg, D., Shi, Y., Shiekhattar, R., et al. (2007) · Cell · doi:10.1016/j.cell.2007.10.039 · Cited by 957 · see citing works

Rb Interacts with Histone Deacetylase to Repress Transcription

Luo, R. X., Postigo, A. A., & Dean, D. C. (1998) · Cell · doi:10.1016/s0092-8674(00)80940-x · Cited by 957 · see citing works

A class of hybrid polar inducers of transformed cell differentiation inhibits histone deacetylases

Richon, V. M., Emiliani, S., Verdin, E., Webb, Y., Breslow, R., Rifkind, R. A., & Marks, P. A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.6.3003 · Cited by 914 · see citing works

Acetyl-CoA and the regulation of metabolism: mechanisms and consequences

Shi, L., & Tu, B. P. (2015) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2015.02.003 · Cited by 903 · see citing works

50 years of protein acetylation: from gene regulation to epigenetics, metabolism and beyond

Verdin, E. M., & Ott, M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3931 · Cited by 876 · see citing works

Discovery of a selective catalytic p300/CBP inhibitor that targets lineage-specific tumours

Lasko, L. M., Jakob, C. G., Edalji, R. P., Qiu, W., Montgomery, D., Digiammarino, E. L., Hansen, T. M., Risi, R. M., Frey, R., Manaves, V., et al. (2017) · Nature · doi:10.1038/nature24028 · Cited by 858 · see citing works

Acetylation Is Indispensable for p53 Activation

Tang, Y., Zhao, W., Chen, Y., Zhao, Y., & Gu, W. (2008) · Cell · doi:10.1016/j.cell.2008.03.025 · Cited by 838 · see citing works

The world of protein acetylation

Drazic, A., Myklebust, L. M., Ree, R., & Arnesen, T. (2016) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2016.06.007 · Cited by 799 · see citing works

Acetylation of the p53 DNA-binding domain regulates apoptosis induction.

Sykes, S. M., Mellert, H. S., Holbert, M. A., Li, K., Marmorstein, R., Lane, W. S., & McMahon, S. B. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.11.026 · Cited by 752 · see citing works

A role for the Tip60 histone acetyltransferase in the acetylation and activation of ATM

Sun, Y., Jiang, X., Chen, S., Fernandes, N., & Price, B. D. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504211102 · Cited by 738 · see citing works

Untitled work

(2002) · PubMed · Cited by 732 · see citing works

Tip60-Dependent Acetylation of p53 Modulates the Decision between Cell-Cycle Arrest and Apoptosis

Tang, Y., Luo, J., Zhang, W., & Gu, W. J. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.11.021 · Cited by 724 · see citing works

Acetylation of p53 Activates Transcription through Recruitment of Coactivators/Histone Acetyltransferases

Barlev, N. A., Liu, L., Chehab, N. H., Mansfield, K., Harris, K. G., Halazonetis, T. D., & Berger, S. L. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00414-2 · Cited by 710 · see citing works

A synthetic inhibitor of histone deacetylase, MS-27-275, with marked in vivo antitumor activity against human tumors

Saito, A., Yamashita, T., Mariko, Y., Nosaka, Y., Tsuchiya, K., Ando, T., Suzuki, T., Tsuruo, T., & Nakanishi, O. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.8.4592 · Cited by 696 · see citing works

Post-translational modifications regulating the activity and function of the nuclear factor kappa B pathway

Perkins, N. D. (2006) · Oncogene · doi:10.1038/sj.onc.1209937 · Cited by 674 · see citing works

Combination Therapy With Histone Deacetylase Inhibitors (HDACi) for the Treatment of Cancer: Achieving the Full Therapeutic Potential of HDACi

Suraweera, A., O'Byrne, K. J., & Richard, D. J. (2018) · Frontiers in Oncology · doi:10.3389/fonc.2018.00092 · Cited by 671 · see citing works

Virtual ligand screening of the p300/CBP histone acetyltransferase: identification of a selective small molecule inhibitor

Bowers, E. M., Yan, G., Mukherjee, C., Orry, A., Wang, L., Holbert, M. A., Crump, N. T., Hazzalin, C. A., Liszczak, G., Yuan, H., et al. (2010) · Chemistry & Biology · doi:10.1016/j.chembiol.2010.03.006 · Cited by 666 · see citing works

Human HDAC1 and HDAC2 function in the DNA-damage response to promote DNA nonhomologous end-joining

Miller, K. M., Tjeertes, J. V., Coates, J., Legube, G., Polo, S. E., Britton, S., & Jackson, S. P. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1899 · Cited by 629 · see citing works

Preclinical activity, pharmacodynamic, and pharmacokinetic properties of a selective HDAC6 inhibitor, ACY-1215, in combination with bortezomib in multiple myeloma

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

SIRT1 Controls Endothelial Angiogenic Functions During Vascular Growth

Potente, M., Ghaeni, L., Baldessari, D., Mostoslavsky, R., Rossig, L., Dequiedt, F., Haendeler, J., Mione, M., Dejana, E., Alt, F. W., et al. (2007) · Genes & Development · doi:10.1101/gad.435107 · Cited by 608 · see citing works

Acetylation Targets the M2 Isoform of Pyruvate Kinase for Degradation through Chaperone-Mediated Autophagy and Promotes Tumor Growth

Lv, L., Dong, L., Zhao, D., Lin, R., Chu, Y., Zhang, H., Zha, Z., Liu, Y., Li, Z., Xu, Y., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.04.025 · Cited by 605 · see citing works

Class IIa Histone Deacetylases Are Hormone-Activated Regulators of FOXO and Mammalian Glucose Homeostasis

Mihaylova, M. M., Vasquez, D. S., Ravnskjær, K., Denechaud, P., Yu, R. T., Alvarez, J. G. A., Downes, M., Evans, R. M., Montminy, M., & Shaw, R. J. (2011) · Cell · doi:10.1016/j.cell.2011.03.043 · Cited by 554 · see citing works

Involvement of Foxo transcription factors in angiogenesis and postnatal neovascularization

Potente, M., Urbich, C., Sasaki, K., Hofmann, W. K., Heeschen, C., Aicher, A., Kollipara, R., DePinho, R. A., Zeiher, A. M., & Dimmeler, S. (2005) · Journal of Clinical Investigation · doi:10.1172/jci23126 · Cited by 527 · see citing works

Acetylation of Foxo1 alters its DNA-binding ability and sensitivity to phosphorylation

Matsuzaki, H., Daitoku, H., Hatta, M., Aoyama, H., Yoshimochi, K., & Fukamizu, A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502738102 · Cited by 479 · see citing works

Acetylation Is Crucial for p53-Mediated Ferroptosis and Tumor Suppression

Wang, S.-J., Li, D., Ou, Y., Jiang, L., Chen, Y., Zhao, Y., & Gu, W. J. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.09.022 · Cited by 463 · see citing works

A novel histone deacetylase 8 (HDAC8)-specific inhibitor PCI-34051 induces apoptosis in T-cell lymphomas

Balasubramanian, S., Ramos, J., Luo, W., Sirisawad, M., Verner, E., & Buggy, J. J. (2008) · Leukemia · doi:10.1038/leu.2008.9 · Cited by 458 · see citing works

GCN5 acetyltransferase complex controls glucose metabolism through transcriptional repression of PGC-1α

Lerin, C., Rodgers, J. T., Kalume, D. E., Kim, S.-H., Pandey, A., & Puigserver, P. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.04.013 · Cited by 443 · see citing works

Trichostatin A is a histone deacetylase inhibitor with potent antitumor activity against breast cancer in vivo.

Vigushin, D. M., Ali, S., Pace, P., Mirsaidi, N., Ito, K., Adcock, I. M., & Coombes, R. C. (2001) · PubMed · Cited by 439 · see citing works

Defective DNA single-strand break repair in spinocerebellar ataxia with axonal neuropathy-1

El‐Khamisy, S. F., Saifi, G. M., Weinfeld, M., Johansson, F., Helleday, T., Lupski, J. R., & Caldecott, K. W. (2005) · Nature · doi:10.1038/nature03314 · Cited by 426 · see citing works

Acetylation Regulates Gluconeogenesis by Promoting PEPCK1 Degradation via Recruiting the UBR5 Ubiquitin Ligase

Jiang, W., Wang, S., Xiao, M., Lin, Y., Zhou, L., Lei, Q., Xiong, Y., Guan, K., & Zhao, S. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.04.028 · Cited by 415 · see citing works

Protein post-translational modifications and regulation of pluripotency in human stem cells

Wang, Y.-C., Peterson, S. E., & Loring, J. F. (2013) · Cell Research · doi:10.1038/cr.2013.151 · Cited by 390 · see citing works

Acetylation-dependent regulation of PD-L1 nuclear translocation dictates the efficacy of anti-PD-1 immunotherapy

Gao, Y., Nihira, N. T., Bu, X., Chu, C., Zhang, J., Kołodziejczyk, A., Fan, Y., Chan, N. T., Ma, L., Liu, J., et al. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-0562-4 · Cited by 390 · see citing works

SIRT2 regulates NF-κB-dependent gene expression through deacetylation of p65 Lys310

Rothgiesser, K., Erener, S., Waibel, S., Lüscher, B., & Hottiger, M. O. (2010) · Journal of Cell Science · doi:10.1242/jcs.073783 · Cited by 376 · see citing works

Lysine Acetylation Goes Global: From Epigenetics to Metabolism and Therapeutics

Ali, I., Conrad, R. J., Verdin, E. M., & Ott, M. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00181 · Cited by 366 · see citing works

Small Changes Huge Impact: The Role of Protein Posttranslational Modifications in Cellular Homeostasis and Disease

Karve, T. M., & Cheema, A. K. (2011) · Journal of Amino Acids · doi:10.4061/2011/207691 · Cited by 364 · see citing works

The c-MYC Oncoprotein Is a Substrate of the Acetyltransferases hGCN5/PCAF and TIP60

Patel, J. H., Du, Y., Ard, P. G., Phillips, C., Carella, B. A., Chen, C., Rakowski, C., Chatterjee, C., Lieberman, P. M., Lane, W. S., et al. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.24.10826-10834.2004 · Cited by 354 · see citing works

Regulation of intermediary metabolism by protein acetylation

Guan, K., & Xiong, Y. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.09.003 · Cited by 353 · see citing works

The Deacetylase SIRT1 Promotes Membrane Localization and Activation of Akt and PDK1 During Tumorigenesis and Cardiac Hypertrophy

Sundaresan, N. R., Pillai, V. B., Wolfgeher, D., Samant, S. A., Vasudevan, P., Parekh, V., Raghuraman, H., Cunningham, J. M., Gupta, M., & Gupta, M. P. (2011) · Science Signaling · doi:10.1126/scisignal.2001465 · Cited by 345 · see citing works

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

Fournel, M., Bonfils, C., Hou, Y., Yan, P. T., Trachy-Bourget, M.-C., Kalita, A., Liu, J., Lu, A., Zhou, N. Z., Robert, M., et al. (2008) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-07-2026 · Cited by 338 · see citing works

Mitogenic and Oncogenic Stimulation of K433 Acetylation Promotes PKM2 Protein Kinase Activity and Nuclear Localization

Lv, L., Xu, Y.-P., Zhao, D., Li, F.-L., Wang, W., Sasaki, N., Jiang, Y., Zhou, X., Li, T.-T., Guan, K., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.09.004 · Cited by 335 · see citing works

Protein acetylation in metabolism – metabolites and cofactors

Menzies, K. J., Zhang, H., Katsyuba, E., & Auwerx, J. (2016) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2015.181 · Cited by 331 · see citing works

p53 Acetylation: Regulation and Consequences

Reed, S. M., & Quelle, D. E. (2014) · Cancers · doi:10.3390/cancers7010030 · Cited by 330 · see citing works

Inhibitors of histone acetyltransferases KAT6A/B induce senescence and arrest tumour growth

Baell, J. B., Leaver, D. J., Hermans, S. J., Kelly, G. L., Brennan, M. S., Downer, N. L., Nguyen, N. H., Wichmann, J., McRae, H. M., Yang, Y., et al. (2018) · Nature · doi:10.1038/s41586-018-0387-5 · Cited by 321 · see citing works

DNA Damage-Induced Acetylation of Lysine 3016 of ATM Activates ATM Kinase Activity

Sun, Y., Xu, Y., Roy, K., & Price, B. D. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01382-07 · Cited by 319 · see citing works

HDAC Inhibitors as Epigenetic Regulators of the Immune System: Impacts on Cancer Therapy and Inflammatory Diseases

Hull, E. E., Montgomery, M. R., & Leyva, K. J. (2016) · BioMed Research International · doi:10.1155/2016/8797206 · Cited by 316 · see citing works

Pharmacodynamic response and inhibition of growth of human tumor xenografts by the novel histone deacetylase inhibitor PXD101.

Plumb, J. A., Finn, P. W., Williams, R. J., Bandara, M. J., Romero, M., Watkins, C. J., Thangue, N. B. L., & Brown, R. E. (2003) · PubMed · Cited by 312 · see citing works

Nonhistone protein acetylation as cancer therapy targets

Singh, B. N., Zhang, G., Hwa, Y. L., Li, J., Dowdy, S. C., & Jiang, S. (2010) · Expert Review of Anticancer Therapy · doi:10.1586/era.10.62 · Cited by 302 · see citing works

Histone deacetylase inhibitors in cancer treatment

Vigushin, D. M., & Coombes, R. C. (2002) · Anti-Cancer Drugs · doi:10.1097/00001813-200201000-00001 · Cited by 301 · see citing works

Acetylation control of the retinoblastoma tumour-suppressor protein

Chan, H. M., Krstic–Demonacos, M., Smith, L. M., Demonacos, C., & Thangue, N. B. L. (2001) · Nature Cell Biology · doi:10.1038/35083062 · Cited by 282 · see citing works

Targeting Tumor Angiogenesis with Histone Deacetylase Inhibitors: the Hydroxamic Acid Derivative LBH589

Qian, D. Z., Kato, Y., Shabbeer, S., Wei, Y., Verheul, H. M. W., Salumbides, B. C., Sanni, T. B., Atadja, P. W., & Пили, Р. (2006) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-05-1132 · Cited by 267 · see citing works

Chlamydomonas alpha-tubulin is posttranslationally modified in the flagella during flagellar assembly.

L’Hernault, S. W., & Rosenbaum, J. L. (1983) · The Journal of Cell Biology · doi:10.1083/jcb.97.1.258 · Cited by 255 · see citing works

Angiogenesis inhibitors in cancer therapy: mechanistic perspective on classification and treatment rationales

El-Kenawi, A., & El‐Remessy, A. B. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12344 · Cited by 252 · see citing works

Histone H3-K56 acetylation is important for genomic stability in mammals

Yuan, J., Pu, M., Zhang, Z., & Lou, Z. (2009) · Cell Cycle · doi:10.4161/cc.8.11.8620 · Cited by 247 · see citing works

A Hormone-Dependent Module Regulating Energy Balance

Wang, B., Moya, N., Niessen, S., Hoover, H. S., Mihaylova, M. M., Shaw, R. J., Yates, J. R., Fischer, W. H., Thomas, J. B., & Montminy, M. (2011) · Cell · doi:10.1016/j.cell.2011.04.013 · Cited by 242 · see citing works

FoxO1, the transcriptional chief of staff of energy metabolism

Kousteni, S. (2011) · Bone · doi:10.1016/j.bone.2011.06.034 · Cited by 240 · see citing works

CBP30, a selective CBP/p300 bromodomain inhibitor, suppresses human Th17 responses

Hammitzsch, A., Tallant, C., Fedorov, O., O'Mahony, A., Brennan, P., Hay, D., Martínez, F., Al-Mossawi, M. H., Dewit, J., Vecellio, M., et al. (2015) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1501956112 · Cited by 239 · see citing works

Mechanistic insights into the regulation of metabolic enzymes by acetylation

Xiong, Y., & Guan, K. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201202056 · Cited by 238 · see citing works

Generation of a Selective Small Molecule Inhibitor of the CBP/p300 Bromodomain for Leukemia Therapy

Picaud, S., Fedorov, O., Thanasopoulou, A., Leonards, K., Jones, K. L., Meier, J. C., Olzscha, H., Monteiro, O., Martin, S., Philpott, M., et al. (2015) · Cancer Research · doi:10.1158/0008-5472.can-15-0236 · Cited by 230 · see citing works

PCAF Modulates PTEN Activity

Okumura, K., Mendoza, M. C., Bachoo, R. M., DePinho, R. A., Cavenee, W. K., & Furnari, F. B. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605391200 · Cited by 222 · see citing works

Acetylation-Dependent Regulation of Skp2 Function

Inuzuka, H., Gao, D., Finley, L. W. S., Yang, W., Wan, L., Fukushima, H., Chin, Y. R., Zhai, B., Shaik, S., Lau, A. W., et al. (2012) · Cell · doi:10.1016/j.cell.2012.05.038 · Cited by 218 · see citing works

Dual Regulation of c-Myc by p300 via Acetylation-Dependent Control of Myc Protein Turnover and Coactivation of Myc-Induced Transcription

Faiola, F., Liu, X., Lo, S.-Y., Pan, S., Zhang, K., Lymar, E. S., Farina, A. N., & Martinez, E. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.23.10220-10234.2005 · Cited by 218 · see citing works

Sirtuins in glucose and lipid metabolism

Ye, X., Li, M., Hou, T., Gao, T., Zhu, W., & Yang, Y. (2016) · Oncotarget · doi:10.18632/oncotarget.12157 · Cited by 215 · see citing works

Acetylation-Dependent Signal Transduction for Type I Interferon Receptor

Tang, X., Gao, J., Guan, Y. A., McLane, K. E., Yuan, Z., Ramratnam, B., & Chin, Y. E. (2007) · Cell · doi:10.1016/j.cell.2007.07.034 · Cited by 211 · see citing works

Class I Histone Deacetylase Inhibitor Entinostat Suppresses Regulatory T Cells and Enhances Immunotherapies in Renal and Prostate Cancer Models

Shen, L., Ciesielski, M. J., Ramakrishnan, S., Miles, K. M., Ellis, L., Sotomayor, P. C., Shrikant, P. A., Fenstermaker, R. A., & Пили, Р. (2012) · PLoS ONE · doi:10.1371/journal.pone.0030815 · Cited by 205 · see citing works

Regulation of STAT signaling by acetylation

Zhuang, S. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2013.05.007 · Cited by 199 · see citing works

Class IIb HDAC6 regulates endothelial cell migration and angiogenesis by deacetylation of cortactin

Kaluza, D., Krøll, J., Gesierich, S., Yao, T., Boon, R. A., Hergenreider, E., Tjwa, M., Rössig, L., Seto, E., Augustin, H. G., et al. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.298 · Cited by 196 · see citing works

Histone Deacetylase 7 Silencing Alters Endothelial Cell Migration, a Key Step in Angiogenesis

Mottet, D., Bellahcène, A., Pirotte, S., Waltregny, D., Deroanne, C., Lamour, V., Lidereau, R., & Castronovo, V. (2007) · Circulation Research · doi:10.1161/circresaha.107.149377 · Cited by 192 · see citing works

Mammalian Sirtuins and Energy Metabolism

Li, X., & Kazgan, N. (2011) · International Journal of Biological Sciences · doi:10.7150/ijbs.7.575 · Cited by 192 · see citing works

Histone Deacetylase (HDAC) Inhibitors with a Novel Connecting Unit Linker Region Reveal a Selectivity Profile for HDAC4 and HDAC5 with Improved Activity against Chemoresistant Cancer Cells

Marek, L., Hamacher, A., Hansen, F. K., Kuna, K., Gohlke, H., Kassack, M. U., & Kurz, T. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm301254q · Cited by 185 · see citing works

Glucose Metabolism on Tumor Plasticity, Diagnosis, and Treatment

Lin, X., Xiao, Z., Chen, T., Liang, S. H., & Guo, H. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.00317 · Cited by 176 · see citing works

Selective HDAC6 inhibitors improve anti-PD-1 immune checkpoint blockade therapy by decreasing the anti-inflammatory phenotype of macrophages and down-regulation of immunosuppressive proteins in tumor cells

Knox, T., Sahakian, E., Banik, D., Hadley, M., Palmer, E., Noonepalle, S., Kim, J., Powers, J., Gracia-Hernandez, M., Oliveira, V., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-42237-3 · Cited by 170 · see citing works

PTEN Acetylation Modulates Its Interaction with PDZ Domain

Ikenoue, T., Inoki, K., Zhao, B., & Guan, K. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-1107 · Cited by 168 · see citing works

Glucose Metabolism Drives Histone Acetylation Landscape Transitions that Dictate Muscle Stem Cell Function

Yucel, N., Wang, Y. X., Mai, T., Porpiglia, E., Lund, P. J., Markov, G., Garcia, B. A., Bendall, S. C., Angelo, M., & Blau, H. M. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.05.092 · Cited by 159 · see citing works

Studies of acetylation and deacetylation in high mobility group proteins. Identification of the sites of acetylation in HMG-1.

Sterner, R., Vidali, G., & Allfrey, V. G. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86524-9 · Cited by 156 · see citing works

c-Myc Modulation and Acetylation Is a Key HDAC Inhibitor Target in Cancer

Nebbioso, A., Carafa, V., Conte, M., Tambaro, F. P., Abbondanza, C., Martens, J. H. A., Nees, M., Benedetti, R., Pallavicini, I., Minucci, S., et al. (2016) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-15-2388 · Cited by 156 · see citing works

SIRT6 deacetylates PKM2 to suppress its nuclear localization and oncogenic functions

Bhardwaj, A., & Das, S. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1520045113 · Cited by 154 · see citing works

Hdac7 promotes lung tumorigenesis by inhibiting Stat3 activation

Lei, Y., Liu, L., Zhang, S., Guo, S., Li, X., Wang, J., Su, B., Fang, Y., Chen, X., Ke, H., et al. (2017) · Molecular Cancer · doi:10.1186/s12943-017-0736-2 · Cited by 152 · see citing works

Deacetylation of the retinoblastoma tumour suppressor protein by SIRT1

Wong, S., & Weber, J. D. (2007) · Biochemical Journal · doi:10.1042/bj20070151 · Cited by 145 · see citing works

Small-Molecule Inhibitors of Histone Acetyltransferase Activity: Identification and Biological Properties

Mai, A., Rotili, D., Tarantino, D., Ornaghi, P., Tosi, F., Vicidomini, C., Sbardella, G., Nebbioso, A., Miceli, M., Altucci, L., et al. (2006) · Journal of Medicinal Chemistry · doi:10.1021/jm060601m · Cited by 145 · see citing works

SIRT7-mediated ATM deacetylation is essential for its deactivation and DNA damage repair

Tang, M., Li, Z., Zhang, C., Lu, X., Tu, B., Cao, Z., Li, Y., Chen, Y., Jiang, L., Wang, H., et al. (2019) · Science Advances · doi:10.1126/sciadv.aav1118 · Cited by 142 · see citing works

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

Scuto, A., Kirschbaum, M., Kowolik, C., Kretzner, L., Juhasz, A., Atadja, P., Pullarkat, V., Bhatia, R., Forman, S., Yen, Y., et al. (2008) · Blood · doi:10.1182/blood-2007-10-117762 · Cited by 141 · see citing works

VEGF amplifies transcription through ETS1 acetylation to enable angiogenesis

Chen, J., Fu, Y., Day, D. S., Sun, Y., Wang, S., Liang, X., Gu, F., Zhang, F., Stevens, S. M., Zhou, P., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00405-x · Cited by 126 · see citing works

Glucose-dependent acetylation of Rictor promotes targeted cancer therapy resistance

Masui, K., Tanaka, K., Ikegami, S., Villa, G. R., Yang, H., Yong, W. H., Cloughesy, T. F., Yamagata, K., Arai, N., Cavenee, W. K., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1511759112 · Cited by 123 · see citing works

Regulation of RAS oncogenicity by acetylation

Yang, M. H., Nickerson, S., Kim, E. T., Liot, C., Laurent, G., Spang, R., Philips, M. R., Shan, Y., Shaw, D. E., Bar‐Sagi, D., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1201487109 · Cited by 119 · see citing works

Author Correction: Selective HDAC6 inhibitors improve anti-PD-1 immune checkpoint blockade therapy by decreasing the anti-inflammatory phenotype of macrophages and down-regulation of immunosuppressive proteins in tumor cells

Knox, T. J., Sahakian, E., Banik, D., Hadley, M. M., Palmer, E., Noonepalle, S. K. R., Kim, J. S., Powers, J. J., Gracia-Hernandez, M., Oliveira, V. A., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-51403-6 · Cited by 118 · see citing works

HDAC3 inhibition upregulates PD-L1 expression in B-cell lymphomas and augments the efficacy of anti-PD-L1 therapy

Deng, S., Hu, Q., Zhang, H., Yang, F., Peng, C., & Huang, C. (2019) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-18-1068 · Cited by 116 · see citing works

KAT2A/KAT2B-targeted acetylome reveals a role for PLK4 acetylation in preventing centrosome amplification

Fournier, M. L., Orpinell, M., Grauffel, C., Scheer, E., Garnier, J., Ye, T., Chavant, V., Joint, M., Esashi, F., Dejaegere, A. P., et al. (2016) · Nature Communications · doi:10.1038/ncomms13227 · Cited by 114 · see citing works

HDAC Inhibition Suppresses Primary Immune Responses, Enhances Secondary Immune Responses, and Abrogates Autoimmunity During Tumor Immunotherapy

Bridle, B. W., Chen, L., Lemay, C. G., Diallo, J., Pol, J. G., Nguyen, A., Capretta, A. A., He, R., Bramson, J. L., Bell, J. C., et al. (2013) · Molecular Therapy · doi:10.1038/mt.2012.265 · Cited by 109 · see citing works

Inhibiting histone deacetylases suppresses glucose metabolism and hepatocellular carcinoma growth by restoring FBP1 expression

Yang, H. J., Jin, X., Yan, Y., Shao, Y., Pan, Y., Roberts, L. R., Zhang, J., Huang, H., & Jiang, J. (2017) · Scientific Reports · doi:10.1038/srep43864 · Cited by 100 · see citing works

HDAC inhibitors overcome immunotherapy resistance in B-cell lymphoma

Wang, X., Waschke, B. C., Woolaver, R. A., Chen, S. M. Y., Chen, Z., & Wang, J. H. (2020) · Protein & Cell · doi:10.1007/s13238-020-00694-x · Cited by 98 · see citing works

The acetylation of RelA in Lys310 dictates the NF-κB-dependent response in post-ischemic injury

Lanzillotta, A., Sarnico, I., Ingrassia, R., Boroni, F., Branca, C., Benarese, M., Faraco, G., Blasi, F., Chiarugi, A., Spano, P., et al. (2010) · Cell Death and Disease · doi:10.1038/cddis.2010.76 · Cited by 97 · see citing works

VEGF Stimulates HDAC7 Phosphorylation and Cytoplasmic Accumulation Modulating Matrix Metalloproteinase Expression and Angiogenesis

Ha, C. H., Jhun, B. S., Kao, H., & Jin, Z. (2008) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.108.172528 · Cited by 97 · see citing works

Identification and Characterization of a Novel p300-mediated p53 Acetylation Site, Lysine 305

Wang, Y.-H., Tsay, Y.-G., Tan, B. C.-M., Lo, W.-Y., & Lee, S.-C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212574200 · Cited by 92 · see citing works

Histone Deacetylase 6 (HDAC6) Is an Essential Modifier of Glucocorticoid-Induced Hepatic Gluconeogenesis

Winkler, R., Benz, V., Clemenz, M., Bloch, M., Foryst‐Ludwig, A., Wardat, S., Witte, N., Trappiel, M., Namsolleck, P., Mai, K., et al. (2011) · Diabetes · doi:10.2337/db11-0313 · Cited by 92 · see citing works

Multiple Site Acetylation of Rictor Stimulates Mammalian Target of Rapamycin Complex 2 (mTORC2)-dependent Phosphorylation of Akt Protein

Glidden, E. J., Gray, L. G., Vemuru, S., Li, D., Harris, T. E., & Mayo, M. W. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.304337 · Cited by 88 · see citing works

Glucose Metabolism as a Target of Histone Deacetylase Inhibitors

Wardell, S. E., Ilkayeva, O., Wieman, H. L., Frigo, D. E., Rathmell, J. C., Newgard, C. B., & McDonnell, D. P. (2008) · Molecular Endocrinology · doi:10.1210/me.2008-0179 · Cited by 79 · see citing works

KATching-Up on Small Molecule Modulators of Lysine Acetyltransferases

Simon, R. P., Robaa, D., Alhalabi, Z., Sippl, W., & Jung, M. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01502 · Cited by 77 · see citing works

Pharmacological Sirt6 inhibition improves glucose tolerance in a type 2 diabetes mouse model

Sociali, G., Magnone, M., Ravera, S., Damonte, P., Vigliarolo, T., von Holtey, M., Vellone, V. G., Millo, E., Caffa, I., Cea, M., et al. (2017) · The FASEB Journal · doi:10.1096/fj.201601294r · Cited by 76 · see citing works

Regulation of Immune Responses by Histone Deacetylase Inhibitors

Licciardi, P. V., & Karagiannis, T. C. (2012) · ISRN Hematology · doi:10.5402/2012/690901 · Cited by 75 · see citing works

Sirtuin 6 regulates glucose-stimulated insulin secretion in mouse pancreatic beta cells

Xiong, X., Wang, G., Tao, R., Wu, P., Kono, T., Li, K., Ding, W., Tong, X., Tersey, S. A., Harris, R. A., et al. (2015) · Diabetologia · doi:10.1007/s00125-015-3778-2 · Cited by 72 · see citing works

Posttranslational Modifications of the Retinoblastoma Tumor Suppressor Protein as Determinants of Function

MacDonald, J. I., & Dick, F. A. (2012) · Genes & Cancer · doi:10.1177/1947601912473305 · Cited by 69 · see citing works

PTEN activation through K163 acetylation by inhibiting HDAC6 contributes to tumour inhibition

Meng, Z., Jia, L.-F., & Gan, Y. (2015) · Oncogene · doi:10.1038/onc.2015.293 · Cited by 68 · see citing works

Dynamic Acetylation of Phosphoenolpyruvate Carboxykinase Toggles Enzyme Activity between Gluconeogenic and Anaplerotic Reactions

Latorre‐Muro, P., Baeza, J., Armstrong, E. A., Hurtado‐Guerrero, R., Corzana, F., Wu, L. E., Sinclair, D. A., López‐Buesa, P., Carrodeguas, J. A., & Denu, J. M. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.07.031 · Cited by 68 · see citing works

HDAC10 promotes lung cancer proliferation via AKT phosphorylation

Yang, Y., Huang, Y., Wang, Z., Wang, H.-T., Duan, B., Ye, D., Wang, C., Jing, R., Leng, Y., Xi, J., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.10673 · Cited by 67 · see citing works

Histone H1 acetylation at lysine 85 regulates chromatin condensation and genome stability upon DNA damage

Li, Y., Li, Z., Dong, L., Tang, M., Zhang, P., Zhang, C., Cao, Z., Zhu, Q., Chen, Y., Wang, H., et al. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky568 · Cited by 67 · see citing works

HDAC8 promotes the dissemination of breast cancer cells via AKT/GSK-3β/Snail signals

An, P., Chen, F., Li, Z., Ling, Y., Peng, Y., Zhang, H., Li, J., Chen, Z., & Wang, H. (2020) · Oncogene · doi:10.1038/s41388-020-1337-x · Cited by 67 · see citing works

Acetylation of Rb by PCAF is required for nuclear localization and keratinocyte differentiation

Pickard, A., Wong, P., & McCance, D. J. (2010) · Journal of Cell Science · doi:10.1242/jcs.068924 · Cited by 66 · see citing works

Acetylation of AGO2 promotes cancer progression by increasing oncogenic miR-19b biogenesis

Zhang, H., Wang, Y., Dou, J., et al. (2018) · Oncogene · doi:10.1038/s41388-018-0530-7 · Cited by 66 · see citing works

The role of histone deacetylase 7 (HDAC7) in cancer cell proliferation: regulation on c-Myc

Zhu, C.-H., Chen, Q., Xie, Z., Ai, J., Tong, L., Ding, J., & Geng, M. (2010) · Journal of Molecular Medicine · doi:10.1007/s00109-010-0701-7 · Cited by 65 · see citing works

HDAC8-dependent deacetylation of PKM2 directs nuclear localization and glycolysis to promote proliferation in hepatocellular carcinoma

Zhang, R., Shen, M., Wu, C., Chen, Y., Lu, J., Li, J., Zhao, L., Meng, H., Zhou, X., Huang, G., et al. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-03212-3 · Cited by 64 · see citing works

A Novel Cell-Permeable, Selective, and Noncompetitive Inhibitor of KAT3 Histone Acetyltransferases from a Combined Molecular Pruning/Classical Isosterism Approach

Milite, C., Feoli, A., Sasaki, K., Pietra, V. L., Balzano, A. L., Marinelli, L., Mai, A., Novellino, E., Castellano, S., Tosco, A., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/jm5019687 · Cited by 54 · see citing works

Lysine Deacetylation by HDAC6 Regulates the Kinase Activity of AKT in Human Neural Progenitor Cells

Iaconelli, J., Lalonde, J., Watmuff, B., Liu, B., Mazitschek, R., Haggarty, S. J., & Karmacharya, R. (2017) · ACS Chemical Biology · doi:10.1021/acschembio.6b01014 · Cited by 51 · see citing works

Histone deacetylase 5 regulates glucose uptake and insulin action in muscle cells

Raichur, S., Teh, S. H., Ohwaki, K., Gaur, V., Long, Y. C., Hargreaves, M., McGee, S. L., & Kusunoki, J. (2012) · Journal of Molecular Endocrinology · doi:10.1530/jme-12-0095 · Cited by 50 · see citing works

HDAC5, a Key Component in Temporal Regulation of p53-Mediated Transactivation in Response to Genotoxic Stress

Sen, N., Kumari, R., Singh, M. I., & Das, S. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.09.003 · Cited by 49 · see citing works

Y08197 is a novel and selective CBP/EP300 bromodomain inhibitor for the treatment of prostate cancer

Zou, L., Xiang, Q., Xue, X., Zhang, C., Li, C., Wang, C., Li, Q., Wang, R., Wu, S., Zhou, Y., et al. (2019) · Acta Pharmacologica Sinica · doi:10.1038/s41401-019-0237-5 · Cited by 48 · see citing works

Role of Sirtuins in Tumor Angiogenesis

Edatt, L., Poyyakkara, A., Raji, G. R., Ramachandran, V., Shankar, S. S., & Kumar, V. B. S. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2019.01516 · Cited by 43 · see citing works

Discovery of Benzoylsulfonohydrazides as Potent Inhibitors of the Histone Acetyltransferase KAT6A

Leaver, D. J., Cleary, B., Nguyen, N. H., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b00665 · Cited by 42 · see citing works

Reversible acetylation regulates vascular endothelial growth factor receptor-2 activity

Zecchin, A., Pattarini, L., Gutiérrez, M. I., et al. (2014) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mju010 · Cited by 37 · see citing works

Acetylation and Deacetylation of DNA Repair Proteins in Cancers

Li, S., Shi, B., Liu, X., & An, H. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.573502 · Cited by 37 · see citing works

Histone deacetylase inhibitors interfere with angiogenesis by decreasing endothelial VEGFR ‐2 protein half‐life in part via a VE ‐cadherin‐dependent mechanism

Hrgović, I., Doll, M., Pinter, A., et al. (2016) · Experimental Dermatology · doi:10.1111/exd.13159 · Cited by 36 · see citing works

HDAC10 promotes angiogenesis in endothelial cells through the PTPN22/ERK axis

Duan, B., Ye, D., Zhu, S., Jia, W., Lu, C., Wang, G., Guo, X., Yu, Y., Wu, C., & Kang, J. (2017) · Oncotarget · doi:10.18632/oncotarget.18130 · Cited by 31 · see citing works

Lysines 3241 and 3260 of DNA-PKcs are important for genomic stability and radioresistance

Mori, E., Davis, A. J., Hasegawa, M., & Chen, D. J. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.06.048 · Cited by 14 · see citing works

Self-acetylation at the active site of phosphoenolpyruvate carboxykinase (PCK1) controls enzyme activity

Latorre‐Muro, P., Baeza, J., Hurtado‐Guerrero, R., Hicks, T., Delso, I., Hernández-Ruiz, C., Velázquez‐Campoy, A., Lawton, A. J., Angulo, J., Denu, J. M., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.015103 · Cited by 12 · see citing works

Inhibition of lysine acetyltransferases impairs tumor angiogenesis acting on both endothelial and tumor cells

Martile, M. D., Gabellini, C., Desideri, M., Matraxia, M., Farini, V., Valentini, E., Carradori, S., Ercolani, C., Buglioni, S., Secci, D., et al. (2020) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-020-01604-z · Cited by 8 · see citing works

KAT2-mediated acetylation switches the mode of PALB2 chromatin association to safeguard genome integrity

Fournier, M. L., Rodrigue, A., Milano, L., Bleuyard, J., Couturier, A. M., Wall, J., Ellins, J., Hester, S., Smerdon, S. J., Tora, L., et al. (2022) · eLife · doi:10.7554/elife.57736 · Cited by 8 · see citing works

KAT2-mediated acetylation switches the mode of PALB2 chromatin association to safeguard genome integrityPreprint

Fournier, M. L., Bleuyard, J., Couturier, A. M., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/735811 · Cited by 1 · see citing works

Gut microbiota-derived short-chain fatty acids regulate gastrointestinal tumor immunity: a novel therapeutic strategy?

Dong, Y., Zhang, K., Wei, J., Ding, Y., Wang, X., Hou, H., Wu, J., Liu, T., Wang, B., & Cao, H. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1158200 · Cited by 107 · see citing works

Acetyl-CoA metabolism as a therapeutic target for cancer

Chen, G., Bao, B., Cheng, Y., Tian, M., Song, J., Zheng, L., & Tong, Q. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115741 · Cited by 54 · see citing works

Inhibition of acetylation, is it enough to fight cancer?

López-Bañuelos, L., & Vega, L. (2022) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2022.103752 · Cited by 32 · see citing works

HDAC4 mediated LHPP deacetylation enhances its destabilization and promotes the proliferation and metastasis of nasopharyngeal carcinoma

Sun, X., Zhang, K., Peng, X., Zhou, P., Qu, C., Yang, L., & Shen, L. (2023) · Cancer Letters · doi:10.1016/j.canlet.2023.216158 · Cited by 21 · see citing works

Acetylation: a new target for protein degradation in cancer

Crawford, C. E. W., & Burslem, G. M. (2025) · Trends in Cancer · doi:10.1016/j.trecan.2025.01.013 · Cited by 20 · see citing works

Histone acetyltransferases are crucial regulators in NF-κB mediated inflammation

Ghizzoni, M., Haisma, H. J., Maarsingh, H., & Dekker, F. J. (2011) · Drug Discovery Today · doi:10.1016/j.drudis.2011.03.009 · Cited by 136 · see citing works

Acetylation of histone deacetylase 6 by p300 attenuates its deacetylase activity

Han, Y., Jeong, H. M., Jin, Y.-H., Kim, Y.-J., Jeong, H. G., Yeo, C., & Lee, K.-Y. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.03.147 · Cited by 58 · see citing works

Modulation of cellular processes by histone and non-histone protein acetylation

Shvedunova, M., & Akhtar, A. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00441-y · Cited by 975 · see citing works

Acetylation of Sirt2 by p300 attenuates its deacetylase activity

Han, Y., Jin, Y.-H., Kim, Y.-J., Kang, B. Y., Choi, H.-J., Kim, D., Yeo, C., & Lee, K.-Y. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.08.042 · Cited by 101 · see citing works

Modulation of Histone Deacetylase 6 (HDAC6) Nuclear Import and Tubulin Deacetylase Activity through Acetylation

Liu, Y., Peng, L., Seto, E., Huang, S., & Qiu, Y. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.371120 · Cited by 144 · see citing works