Protein acetylation and deacetylation: An important regulatory modification in gene transcription (Review)

Epithelial-Mesenchymal Transitions in Development and Disease

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

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Histone deacetylases (HDACs): characterization of the classical HDAC family

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

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

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A unique chromatin signature uncovers early developmental enhancers in humans

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Microglia in Alzheimer’s disease

Hansen, D. V., Hanson, J. E., & Sheng, M. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201709069 · Cited by 1,935

Acetylation of Histones and Transcription-Related Factors

Sterner, D. E., & Berger, S. L. (2000) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.64.2.435-459.2000 · Cited by 1,824

Acetylation and deacetylation of non-histone proteins

Glozak, M. A., Sengupta, N., Zhang, X., & Seto, E. (2005) · Gene · doi:10.1016/j.gene.2005.09.010 · Cited by 1,584

A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis

Ahn, B.-H., Kim, H.-S., Song, S., Lee, I. H., Liu, J., Vassilopoulos, A., Deng, C.-X., & Finkel, T. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803790105 · Cited by 1,291

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

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

HDAC6 Regulates Hsp90 Acetylation and Chaperone-Dependent Activation of Glucocorticoid Receptor

Kovacs, J. J., Murphy, P. J. M., Gaillard, S., Zhao, X., Wu, J.-T., Nicchitta, C. V., Yoshida, M., Toft, D. O., Pratt, W. B., & Yao, T.-P. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.04.021 · Cited by 1,153

SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin

Michishita, E., McCord, R. A., Berber, E., Kioi, M., Padilla-Nash, H., Damian, M., Cheung, P., Kusumoto, R., Kawahara, T. L. A., Barrett, J. C., et al. (2008) · Nature · doi:10.1038/nature06736 · Cited by 1,111

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

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 905

Histone Deacetylase Inhibitors in Cancer Therapy

Lane, A. A., & Chabner, B. A. (2009) · Journal of Clinical Oncology · doi:10.1200/jco.2009.22.1291 · Cited by 893

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 842

Urine Output Assessment as a Clinical Quality Measure

Macedo, E. (2015) · The Nephron journals/Nephron journals · doi:10.1159/000437312 · Cited by 803

Human chronic myeloid leukemia stem cells are insensitive to imatinib despite inhibition of BCR-ABL activity

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Mitochondrial STAT3 Supports Ras-Dependent Oncogenic Transformation

Gough, D. J., Corlett, A., Schlessinger, K., Wegrzyn, J., Larner, A. C., & Levy, D. E. (2009) · Science · doi:10.1126/science.1171721 · Cited by 716

SIRT5 Regulates the Mitochondrial Lysine Succinylome and Metabolic Networks

Rardin, M. J., He, W., Nishida, Y., Newman, J. C., Carrico, C., Danielson, S. R., Guo, A., Gut, P., Sahu, A. K., Li, B., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.11.013 · Cited by 711

HDACs, histone deacetylation and gene transcription: from molecular biology to cancer therapeutics

Gallinari, P., Marco, S. D., Jones, P., Pallaoro, M., & Steinkühler, C. (2007) · Cell Research · doi:10.1038/sj.cr.7310149 · Cited by 678 · cited 5×

Glycolysis-mediated changes in acetyl-CoA and histone acetylation control the early differentiation of embryonic stem cells

Moussaieff, A., Rouleau, M., Kitsberg, D., Cohen, M., Levy, G., Barasch, D., Nemirovski, A., Shen-Orr, S., Laevsky, I., Amit, M., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.02.002 · Cited by 666

N-Terminal Acetylation of Cellular Proteins Creates Specific Degradation Signals

Hwang, C.-S., Shemorry, A., & Varshavsky, A. (2010) · Science · doi:10.1126/science.1183147 · Cited by 650

SIRT7 links H3K18 deacetylation to maintenance of oncogenic transformation

Barber, M. F., Michishita-Kioi, E., Xi, Y., Tasselli, L., Kioi, M., Moqtaderi, Z., Tennen, R. I., Paredes, S., Young, N. L., Chen, K., et al. (2012) · Nature · doi:10.1038/nature11043 · Cited by 635

Structure and functions of the GNAT superfamily of acetyltransferases

Vetting, M. W., de Carvalho, L. P. S., Yu, M. C., Hegde, S. S., Magnet, S., Roderick, S. L., & Blanchard, J. S. (2004) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2004.09.003 · Cited by 631

Cytosolic FoxO1 is essential for the induction of autophagy and tumour suppressor activity

Zhao, Y., Yang, J. H., Liao, W., Liu, X., Zhang, H., Wang, S., Wang, D., Feng, J., Yu, L., & Zhu, W. (2010) · Nature Cell Biology · doi:10.1038/ncb2069 · Cited by 630

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

p300/CBP‐mediated p53 acetylation is commonly induced by p53‐activating agents and inhibited by MDM2

Ito, A., Lai, C.-H., Zhao, X., Saito, S., Hamilton, M. H., Appella, E., & Yao, T. (2001) · The EMBO Journal · doi:10.1093/emboj/20.6.1331 · Cited by 597

Modulation of Intrinsically Disordered Protein Function by Post-translational Modifications

Bah, A., & Forman-Kay, J. D. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.695056 · Cited by 557

SIRT3 Is a Stress-Responsive Deacetylase in Cardiomyocytes That Protects Cells from Stress-Mediated Cell Death by Deacetylation of Ku70

Sundaresan, N. R., Samant, S. A., Pillai, V. B., Rajamohan, S. B., & Gupta, M. P. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00426-08 · Cited by 542

The TAK1-NLK Mitogen-Activated Protein Kinase Cascade Functions in the Wnt-5a/Ca 2+ Pathway To Antagonize Wnt/β-Catenin Signaling

Ishitani, T., Kishida, S., Hyodo‐Miura, J., Ueno, N., Yasuda, J., Waterman, M. L., Shibuyà, H., Moon, R. T., Ninomiya‐Tsuji, J., & Matsumoto, K. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.23.1.131-139.2003 · Cited by 540

Classifying AKI by Urine Output versus Serum Creatinine Level

Kellum, J. A., Sileanu, F. E., Murugan, R., Lucko, N., Shaw, A., & Clermont, G. (2015) · Journal of the American Society of Nephrology · doi:10.1681/asn.2014070724 · Cited by 528

SIRT4 Has Tumor-Suppressive Activity and Regulates the Cellular Metabolic Response to DNA Damage by Inhibiting Mitochondrial Glutamine Metabolism

Jeong, S. M., Xiao, C., Finley, L. W. S., Lahusen, T., Souza, A. L., Pierce, K., Li, Y.-H., Wang, X., Laurent, G., German, N. J., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.02.024 · Cited by 445

Acetylation of Smc3 by Eco1 Is Required for S Phase Sister Chromatid Cohesion in Both Human and Yeast

Zhang, J., Shi, X., Li, Y., Kim, B.-J., Jia, J., Huang, Z., Yang, T., Fu, X., Jung, S. Y., Wang, Y., et al. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.06.006 · Cited by 421

Role of histone acetylation in the control of gene expression

Verdone, L., Caserta, M., & Mauro, E. D. (2005) · Biochemistry and Cell Biology · doi:10.1139/o05-041 · Cited by 416

Activation of p53 by SIRT1 Inhibition Enhances Elimination of CML Leukemia Stem Cells in Combination with Imatinib

Li, L., Wang, L., Li, L., Wang, Z., Ho, Y., McDonald, T., Holyoake, T. L., Chen, W., & Bhatia, R. (2012) · Cancer Cell · doi:10.1016/j.ccr.2011.12.020 · Cited by 414

An Acetylation Site in the Middle Domain of Hsp90 Regulates Chaperone Function

Scroggins, B. T., Robzyk, K., Wang, D., Marcu, M. G., Tsutsumi, S., Beebe, K., Cotter, R. J., Felts, S., Toft, D., Karnitz, L., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2006.12.008 · Cited by 413

Sirtuin 3–dependent mitochondrial dynamic improvements protect against acute kidney injury

Morigi, M., Perico, L., Rota, C., Longaretti, L., Conti, S., Rottoli, D., Novelli, R., Remuzzi, G., & Benigni, A. (2015) · Journal of Clinical Investigation · doi:10.1172/jci77632 · Cited by 407

Sequence Determinants of Compaction in Intrinsically Disordered Proteins

Marsh, J. A., & Forman-Kay, J. D. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.02.006 · Cited by 382

DNA damage responses and p53 in the aging process

Ou, H.-L., & Schumacher, B. (2018) · Blood · doi:10.1182/blood-2017-07-746396 · Cited by 377

Physical and Functional HAT/HDAC Interplay Regulates Protein Acetylation Balance

Peserico, A., & Simone, C. (2010) · BioMed Research International · doi:10.1155/2011/371832 · Cited by 376

Architectural and Functional Commonalities between Enhancers and Promoters

Kim, T.-K., & Shiekhattar, R. (2015) · Cell · doi:10.1016/j.cell.2015.08.008 · Cited by 355

p53 Acetylation: Regulation and Consequences

Reed, S. M., & Quelle, D. E. (2014) · Cancers · doi:10.3390/cancers7010030 · Cited by 344

H3K27 acetylation activated-long non-coding RNA CCAT1 affects cell proliferation and migration by regulating SPRY4 and HOXB13 expression in esophageal squamous cell carcinoma

Zhang, E., Han, L., Yin, D., He, X., Hong, L., Si, X., Qiu, M., Xu, T., De, W., Xu, L., et al. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw1247 · Cited by 340

Iron overloaded polarizes macrophage to proinflammation phenotype through ROS /acetyl‐p53 pathway

Zhou, Y., Que, K., Zhang, Z., Yi, Z. J., Zhao, P., You, Y., Gong, J., & Liu, Z. (2018) · Cancer Medicine · doi:10.1002/cam4.1670 · Cited by 337

SAHA shows preferential cytotoxicity in mutant p53 cancer cells by destabilizing mutant p53 through inhibition of the HDAC6-Hsp90 chaperone axis

Li, D., Marchenko, N. D., & Moll, U. M. (2011) · Cell Death & Differentiation · doi:10.1038/cdd.2011.71 · Cited by 336

Injury-Induced HDAC5 Nuclear Export Is Essential for Axon Regeneration

Cho, Y., Sloutsky, R., Naegle, K. M., & Cavalli, V. (2013) · Cell · doi:10.1016/j.cell.2013.10.004 · Cited by 327

Nonenzymatic Protein Acylation as a Carbon Stress Regulated by Sirtuin Deacylases

Wagner, G. R., & Hirschey, M. D. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.03.027 · Cited by 323

Transcriptional/epigenetic regulator CBP/p300 in tumorigenesis: structural and functional versatility in target recognition

Wang, F., Marshall, C. B., & Ikura, M. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1254-4 · Cited by 317

Mechanisms and Dynamics of Protein Acetylation in Mitochondria

Baeza, J., Smallegan, M. J., & Denu, J. M. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.12.006 · Cited by 312

Building Sister Chromatid Cohesion: Smc3 Acetylation Counteracts an Antiestablishment Activity

Rowland, B. D., Roig, M. B., Nishino, T., Kurze, A., Uluocak, P., Mishra, A., Beckouët, F., Underwood, P., Metson, J., Imre, R., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.02.028 · Cited by 308

TGF-β Regulates miR-206 and miR-29 to Control Myogenic Differentiation through Regulation of HDAC4

Winbanks, C. E., Wang, B., Beyer, C., Koh, P., White, L. J., Kantharidis, P., & Gregorevic, P. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.192625 · Cited by 275

Microglial activation correlates in vivo with both tau and amyloid in Alzheimer’s disease

Dani, M., Wood, M., Mizoguchi, R., Fan, Z., Walker, Z., Morgan, R., Hinz, R., Biju, M., Kuruvilla, T., Brooks, D. J., et al. (2018) · Brain · doi:10.1093/brain/awy188 · Cited by 270

Acetylation of PGK1 promotes liver cancer cell proliferation and tumorigenesis

Hu, H., Zhu, W., Qin, J., Chen, M., Gong, L., Li, L., Liu, X., Tao, Y., Yin, H., Zhou, H., et al. (2016) · Hepatology · doi:10.1002/hep.28887 · Cited by 269

Lysine acetyltransferases and lysine deacetylases as targets for cardiovascular disease

Li, P., Ge, J., & Li, H. (2020) · Nature Reviews Cardiology · doi:10.1038/s41569-019-0235-9 · Cited by 269

Structural basis for allosteric, substrate-dependent stimulation of SIRT1 activity by resveratrolPreprint

Cao, D., Wang, M., Qiu, X., Liu, D., Jiang, H., Yang, N., & Xu, R.-M. (2015) · Genes & Development · doi:10.1101/gad.265462.115 · Cited by 267

Differential expression of histone deacetylases HDAC1, 2 and 3 in human breast cancer - overexpression of HDAC2 and HDAC3 is associated with clinicopathological indicators of disease progression

Müller, B. M., Jana, L., Kasajima, A., Lehmann, A., Prinzler, J., Budczies, J., Winzer, K., Dietel, M., Weichert, W., & Denkert, C. (2013) · BMC Cancer · doi:10.1186/1471-2407-13-215 · Cited by 266

Implications of STAT3 and STAT5 signaling on gene regulation and chromatin remodeling in hematopoietic cancer

Wingelhofer, B., Neubauer, H. A., Valent, P., Han, X., Constantinescu, S. N., Gunning, P. T., Müller, M. M., & Moriggl, R. (2018) · Leukemia · doi:10.1038/s41375-018-0117-x · Cited by 253

Histone acetyltransferases: challenges in targeting bi-substrate enzymes

Wapenaar, H., & Dekker, F. J. (2016) · Clinical Epigenetics · doi:10.1186/s13148-016-0225-2 · Cited by 251

MYC and the Control of ApoptosisPreprint

McMahon, S. B. (2014) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a014407 · Cited by 240

Histone H3 globular domain acetylation identifies a new class of enhancers

Pradeepa, M. M., Grimes, G. R., Kumar, Y., Olley, G., Taylor, G. C. A., Schneider, R., & Bickmore, W. A. (2016) · Nature Genetics · doi:10.1038/ng.3550 · Cited by 240 · cited 1×

Protein Bioinformatics Databases and Resources

Chen, C., Huang, H., & Wu, C. H. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-6783-4_1 · Cited by 235

ARID1A-mutated ovarian cancers depend on HDAC6 activity

Bitler, B. G., Wu, S., Park, P. H., Hai, Y., Aird, K. M., Wang, Y., Zhai, Y., Kossenkov, A. V., Vara-Ailor, A., Rauscher, F. J., et al. (2017) · Nature Cell Biology · doi:10.1038/ncb3582 · Cited by 232

The Cardiac Transcription Network Modulated by Gata4, Mef2a, Nkx2.5, Srf, Histone Modifications, and MicroRNAs

Schlesinger, J., Schueler, M., Grunert, M., Fischer, J. J., Zhang, Q., Krueger, T., Lange, M., Tönjes, M., Dunkel, I., & Sperling, S. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1001313 · Cited by 224

BET and HDAC inhibitors induce similar genes and biological effects and synergize to kill in Myc-induced murine lymphoma

Bhadury, J., Nilsson, L. M., Muralidharan, S. V., Green, L. C., Li, Z., Gesner, E. M., Hansen, H. C., Keller, U. B., McLure, K. G., & Nilsson, J. A. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1406722111 · Cited by 221

The diversity of lysine-acetylated proteins in Escherichia coli.

Yu, B. J., Kim, J. A., Moon, J. H., Ryu, S. E., & Pan, J. (2008) · PubMed · Cited by 213

MYST-family histone acetyltransferases: beyond chromatin

Sapountzi, V., & Côté, J. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0599-9 · Cited by 211

High levels of β-catenin signaling reduce osteogenic differentiation of stem cells in inflammatory microenvironments through inhibition of the noncanonical Wnt pathway

Liu, N., Shi, S., Deng, M., Tang, L. V., Zhang, G., Liu, N., Ding, B., Liu, W., Liu, Y., Shi, H., et al. (2011) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.440 · Cited by 201

Class II a HDAC s – new insights into their functions in physiology and pathology

Parra, M. (2014) · FEBS Journal · doi:10.1111/febs.13061 · Cited by 194

Acetylation of Snail Modulates the Cytokinome of Cancer Cells to Enhance the Recruitment of Macrophages

Hsu, D. S., Wang, H.-J., Tai, S., Chou, C.-H., Hsieh, C.-H., Chiu, P.-H., Chen, N., & Yang, M. (2014) · Cancer Cell · doi:10.1016/j.ccell.2014.09.002 · Cited by 194

Cell Death in the Kidney

Priante, G., Gianesello, L., Ceol, M., Prete, D. D., & Anglani, F. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20143598 · Cited by 189

Histone Deacetylase Inhibitor Enhances Recovery after AKI

Cosentino, C. C., Skrypnyk, N. I., Brilli, L. L., Chiba, T., Novitskaya, T., Woods, C., West, J. D., Korotchenko, V. N., McDermott, L. A., Day, B. W., et al. (2013) · Journal of the American Society of Nephrology · doi:10.1681/asn.2012111055 · Cited by 183

Intrinsic apoptotic and thioredoxin pathways in human prostate cancer cell response to histone deacetylase inhibitor

Xu, W., Ngo, L., Perez, G., Dokmanovic, M., & Marks, P. A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607518103 · Cited by 179

HBO1 histone acetylase is a coactivator of the replication licensing factor Cdt1Preprint

Miotto, B., & Struhl, K. (2008) · Genes & Development · doi:10.1101/gad.1674108 · Cited by 175

Histone Deacetylase: A Potential Therapeutic Target for Fibrotic Disorders

Pang, M., & Zhuang, S. (2010) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.110.168385 · Cited by 173

MOZ and MORF histone acetyltransferases interact with the Runt-domain transcription factor Runx2

Pelletier, N., Champagne, N., Stifani, S., & Yang, X. (2002) · Oncogene · doi:10.1038/sj.onc.1205367 · Cited by 171

SIRT1/3 Activation by Resveratrol Attenuates Acute Kidney Injury in a Septic Rat Model

Xu, S., Gao, Y., Zhang, Q., Wei, S., Chen, Z., Dai, X., Zeng, Z., & Zhao, K. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/7296092 · Cited by 171

Neuroprotective Functions for the Histone Deacetylase SIRT6

Kaluski, S., Portillo, M., Besnard, A., Stein, D., Einav, M., Zhong, L., Ueberham, U., Arendt, T., Mostoslavsky, R., Sahay, A., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.03.008 · Cited by 167

MOZ increases p53 acetylation and premature senescence through its complex formation with PML

Rokudai, S., Laptenko, O., Arnal, S. M., Taya, Y., Kitabayashi, I., & Prives, C. L. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1300490110 · Cited by 165

Crystal Structure of Yeast Esa1 Suggests a Unified Mechanism for Catalysis and Substrate Binding by Histone Acetyltransferases

Yan, Y. C., Barlev, N. A., Haley, R., Berger, S. L., & Marmorstein, R. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00116-7 · Cited by 165

Mitochondrial SIRT3 and heart disease

Pillai, V. B., Sundaresan, N. R., Jeevanandam, V., & Gupta, M. P. (2010) · Cardiovascular Research · doi:10.1093/cvr/cvq250 · Cited by 163

Bacterial protein acetylation: the dawning of a new age

Hu, L. I., Lima, B. P., & Wolfe, A. J. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07204.x · Cited by 162

Deacetylation of TFEB promotes fibrillar Aβ degradation by upregulating lysosomal biogenesis in microglia

Bao, J., Zheng, L., Zhang, Q., Li, X., Zhang, X., Li, Z., Bai, X., Zhang, Z., Huo, W., Zhao, X., et al. (2016) · Protein & Cell · doi:10.1007/s13238-016-0269-2 · Cited by 159

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

Prevention of Kidney Injury Following Rhabdomyolysis: A Systematic Review

Scharman, E. J., & Troutman, W. G. (2013) · Annals of Pharmacotherapy · doi:10.1345/aph.1r215 · Cited by 151

Sirt1 regulates canonical TGF-β signalling to control fibroblast activation and tissue fibrosis

Zerr, P., Palumbo‐Zerr, K., Huang, J., Tomčík, M., Šumová, B., Distler, O., Schett, G. A., & Distler, J. H. W. (2014) · Annals of the Rheumatic Diseases · doi:10.1136/annrheumdis-2014-205740 · Cited by 151

Lysine Acetyltransferase GCN5 Potentiates the Growth of Non-small Cell Lung Cancer via Promotion of E2F1, Cyclin D1, and Cyclin E1 Expression

Chen, L., Wei, T., Si, X., Wang, Q., Li, Y., Leng, Y., Deng, A., Chen, J., Wang, G., Zhu, S., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.458737 · Cited by 150

Mechanisms, Detection, and Relevance of Protein Acetylation in Prokaryotes

Christensen, D. G., Baumgartner, J. T., Xie, X., Jew, K., Basisty, N., Schilling, B., Kuhn, M. L., & Wolfe, A. J. (2019) · mBio · doi:10.1128/mbio.02708-18 · Cited by 148

The histone deacetylase, SIRT1, contributes to the resistance of young mice to ischemia/reperfusion-induced acute kidney injury

Fan, H. X., Yang, H., Li, Y., Wang, Y., He, W., & Hao, C. (2013) · Kidney International · doi:10.1038/ki.2012.394 · Cited by 147

Acetyltransferase GCN5 regulates autophagy and lysosome biogenesis by targeting TFEB

Wang, Y., Huang, Y., Liu, J., Zhang, J., Xu, M., You, Z., Peng, C., Gong, Z., & Liu, W. (2019) · EMBO Reports · doi:10.15252/embr.201948335 · Cited by 147

Nε−Lysine Acetylation of a Bacterial Transcription Factor Inhibits Its DNA-Binding Activity

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