Histone Deacetylase 3 Interacts with and Deacetylates Myocyte Enhancer Factor 2
Open accessAbstract
The myocyte enhancer factor 2 (MEF2) family of transcription factors is not only important for controlling gene expression in normal cellular programs, like muscle differentiation, T-cell apoptosis, neuronal survival, and synaptic differentiation, but has also been linked to cardiac hypertrophy and other pathological conditions. Lysine acetylation has been shown to modulate MEF2 function, but it is not so clear which deacetylase(s) is involved. We report here that treatment of HEK293 cells with trichostatin A or nicotinamide upregulated MEF2D acetylation, suggesting that different deacetylases catalyze the deacetylation. Related to the trichostatin A sensitivity, histone deacetylase 4 (HDAC4) and HDAC5, two known partners of MEF2, exhibited little deacetylase activity towards MEF2D. In contrast, HDAC3 efficiently deacetylated MEF2D in vitro and in vivo. This was specific, since HDAC1, HDAC2, and HDAC8 failed to do so. While HDAC4, HDAC5, HDAC7, and HDAC9 are known to recognize primarily the MEF2-specific domain, we found that HDAC3 interacts directly with the MADS box. In addition, HDAC3 associated with the acetyltransferases p300 and p300/CBP-associated factor (PCAF) to reverse autoacetylation. Furthermore, the nuclear receptor corepressor SMRT (silencing mediator of retinoid acid and thyroid hormone receptor) stimulated the deacetylase activity of HDAC3 towards MEF2 and PCAF. Supporting the physical interaction and deacetylase activity, HDAC3 repressed MEF2-dependent transcription and inhibited myogenesis. These results reveal an unexpected role for HDAC3 and suggest a novel pathway through which MEF2 activity is controlled in vivo.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Sirt1 and HDAC3, but not HDAC4 or -5, efficiently deacetylate MEF2D, contributing to MEF2D-dependent transcriptional repression.
“More recently, it has been shown that both Sirt1 (28) and HDAC3 (29), and not HDAC4 or -5, efficiently deacetylate MEF2D, thus contributing to MEF2Ddependent transcriptional repression.”
From Unraveling the hidden catalytic activity of vertebrate class IIa histone deacetylases (2007) · cites this paper as [29]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
The Transcriptional Coactivators p300 and CBP Are Histone Acetyltransferases
Ogryzko, V. V., Schiltz, R. L., Russanova, V., Howard, B. H., & Nakatani, Y. (1996) · Cell · doi:10.1016/s0092-8674(00)82001-2 · Cited by 2,952 · 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
HDAC6 is a microtubule-associated deacetylase
Hubbert, C., Guardiola, A., Shao, R., Kawaguchi, Y., Ito, A., Nixon, A., Yoshida, M., Wang, X.-F., & Yao, T.-P. (2002) · Nature · doi:10.1038/417455a · Cited by 2,403 · 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
A transcriptional co-repressor that interacts with nuclear hormone receptors
Chen, J. D., & Evans, R. M. (1995) · Nature · doi:10.1038/377454a0 · Cited by 1,794 · see citing works
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 1,766 · see citing works
The Human Sir2 Ortholog, SIRT2, Is an NAD+-Dependent Tubulin Deacetylase
North, B. J., Marshall, B. L., Borra, M. T., Denu, J. M., & Verdin, E. M. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00038-8 · Cited by 1,542 · see citing works
The Sir2 Family of Protein Deacetylases
Blander, G., & Guarente, L. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073651 · Cited by 1,496 · 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
Self-citationA p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A
Yang, X., Ogryzko, V. V., Nishikawa, J., Howard, B. H., & Nakatani, Y. (1996) · Nature · doi:10.1038/382319a0 · Cited by 1,473 · see citing works
Self-citationGregoretti, 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
Acetylation: a regulatory modification to rival phosphorylation?
Kouzarides, T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.6.1176 · Cited by 1,155 · see citing works
Deacetylation of p53 modulates its effect on cell growth and apoptosis
Luo, J., Su, F., Chen, D., Shiloh, A., & Gu, W. J. (2000) · Nature · doi:10.1038/35042612 · Cited by 818 · see citing works
Histone Deacetylase 4 Controls Chondrocyte Hypertrophy during Skeletogenesis
Vega, R. B., Matsuda, K., Oh, J., Barbosa, A. C. C., Yang, X., Meadows, E., McAnally, J., Pomajzl, C., Shelton, J. M., Richardson, J. A., et al. (2004) · Cell · doi:10.1016/j.cell.2004.10.024 · Cited by 805 · see citing works
Self-citationStat3 Dimerization Regulated by Reversible Acetylation of a Single Lysine Residue
Yuan, Z.-L., Guan, Y.-J., Chatterjee, D., & Chin, Y. E. (2005) · Science · doi:10.1126/science.1105166 · Cited by 790 · see citing works
Activation of the transcription factor MEF2C by the MAP kinase p38 in inflammation
Han, J., Jiang, Y., Li, Z., Kravchenko, V. V., & Ulevitch, R. J. (1997) · Nature · doi:10.1038/386296a0 · Cited by 766 · see citing works
MEF2: a calcium-dependent regulator of cell division, differentiation and death
McKinsey, T. A., Zhang, C. L., & Olson, E. N. (2002) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)02031-x · Cited by 691 · see citing works
Class II histone deacetylases: versatile regulators
Verdin, E., Dequiedt, F., & Kasler, H. G. (2003) · Trends in Genetics · doi:10.1016/s0168-9525(03)00073-8 · Cited by 664 · see citing works
Both corepressor proteins SMRT and N‐CoR exist in large protein complexes containing HDAC3
Li, J., Wang, J., Wang, J., Nawaz, Z., Liu, J. M., Qin, J., & Wong, J. (2000) · The EMBO Journal · doi:10.1093/emboj/19.16.4342 · Cited by 629 · see citing works
Self-citationThe SMRT and N-CoR Corepressors Are Activating Cofactors for Histone Deacetylase 3
Guenther, M. G., Barak, O., & Lazar, M. A. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.18.6091-6101.2001 · Cited by 611 · see citing works
Baek, S. H., Ohgi, K., Rose, D., Koo, E., Glass, C., & Rosenfeld, M. (2002) · Cell · doi:10.1016/s0092-8674(02)00809-7 · Cited by 591 · see citing works
Sir2 Regulates Skeletal Muscle Differentiation as a Potential Sensor of the Redox State
Fulco, M., Schiltz, R. L., Iezzi, S., King, M. T., Zhao, P., Kashiwaya, Y., Hoffman, E. P., Veech, R. L., & Sartorelli, V. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00226-0 · Cited by 590 · see citing works
Activity-Dependent Regulation of MEF2 Transcription Factors Suppresses Excitatory Synapse Number
Flavell, S. W., Cowan, C. W., Kim, T.-K., Greer, P. L., Lin, Y., Paradis, S., Griffith, E. C., Hu, L. S., Chen, C., & Greenberg, M. E. (2006) · Science · doi:10.1126/science.1122511 · Cited by 573 · see citing works
Grozinger, C. M., & Schreiber, S. L. (2002) · Chemistry & Biology · doi:10.1016/s1074-5521(02)00092-3 · Cited by 537 · see citing works
Vega, R. B., Harrison, B. C., Meadows, E., Roberts, C. R., Papst, P. J., Olson, E. N., & McKinsey, T. A. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.19.8374-8385.2004 · Cited by 512 · see citing works
PDSM, a motif for phosphorylation-dependent SUMO modification
Hietakangas, V., Anckar, J., Blomster, H. A., Fujimoto, M., Palvimo, J. J., Nakai, A., & Sistonen, L. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503698102 · Cited by 501 · see citing works
A core SMRT corepressor complex containing HDAC3 and TBL1, a WD40-repeat protein linked to deafness
Guenther, M. G., Lane, W. S., Fischle, W., Verdin, E., Lazar, M. A., & Shiekhattar, R. (2000) · Genes & Development · doi:10.1101/gad.14.9.1048 · Cited by 489 · see citing works
Microarray Deacetylation Maps Determine Genome-Wide Functions for Yeast Histone Deacetylases
Robyr, D., Suka, Y., Xénarios, I., Kurdistani, S. K., Wang, A., Suka, N., & Grunstein, M. R. (2002) · Cell · doi:10.1016/s0092-8674(02)00746-8 · Cited by 468 · see citing works
A Calcium-Regulated MEF2 Sumoylation Switch Controls Postsynaptic Differentiation
Shalizi, A., Gaudilliere, B. L., Yuan, Z., Stegmüller, J., Shirogane, T., Ge, Q., Tan, Y. L., Schulman, B. A., Harper, J. W., & Bonni, A. (2006) · Science · doi:10.1126/science.1122513 · Cited by 456 · see citing works
p300 Transcriptional Repression Is Mediated by SUMO Modification
Girdwood, D., Bumpass, D. C., Vaughan, O. A., Thain, A., Anderson, L. A., Snowden, A. W., Garcia-Wilson, E., Perkins, N. D., & Hay, R. T. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00141-2 · Cited by 448 · see citing works
Regulation of the MEF2 Family of Transcription Factors by p38
Zhao, M. F., New, L., Kravchenko, V. V., Kato, Y., Gram, H., Padova, F. D., Olson, E. N., Ulevitch, R. J., & Han, J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.1.21 · Cited by 438 · see citing works
Yang, W., Yao, Y., Sun, J.-M., Davie, J., & Seto, E. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.44.28001 · Cited by 433 · see citing works
Self-citationKao, H., Downes, M., Ordentlich, P., & Evans, R. M. (2000) · Genes & Development · doi:10.1101/gad.14.1.55 · Cited by 424 · see citing works
Regulation of the p300 HAT domain via a novel activation loop
Thompson, P. R., Wang, D., Wang, L., Fulco, M., Pediconi, N., Zhang, D., An, W., Ge, Q., Roeder, R. G., Wong, J., et al. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb740 · Cited by 423 · see citing works
Self-citationDifferential Roles of p300 and PCAF Acetyltransferases in Muscle Differentiation
Puri, P., Sartorelli, V., Yang, X., Hamamori, Y., Ogryzko, V. V., Howard, B. H., Kedes, L., Wang, J. Y. J., Graessmann, A., Nakatani, Y., et al. (1997) · Molecular Cell · doi:10.1016/s1097-2765(00)80005-2 · Cited by 419 · see citing works
Self-citationClass II Histone Deacetylases: from Sequence to Function, Regulation, and Clinical Implication
Yang, X., & Grégoire, S. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.8.2873-2884.2005 · Cited by 419 · see citing works
Self-citationAcetylation inactivates the transcriptional repressor BCL6
Bereshchenko, O., Gu, W. J., & Dalla‐Favera, R. (2002) · Nature Genetics · doi:10.1038/ng1018 · Cited by 394 · see citing works
The histone deacetylase-3 complex contains nuclear receptor corepressors
Wen, Y.-D., Perissi, V., Staszewski, L. M., Yang, W.-M., Krones, A., Glass, C. K., Rosenfeld, M. G., & Seto, E. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.13.7202 · Cited by 378 · see citing works
Self-citationLaganière, J., Deblois, G., Lefèbvre, C., Bataille, A. R., Robert, F., & Giguère, V. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505575102 · Cited by 367 · see citing works
Sartorelli, V., Huang, J., Hamamori, Y., & Kedes, L. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.2.1010 · Cited by 367 · see citing works
Functional significance of histone deacetylase diversity
Khochbin, S., Verdel, A., Lemercier, C., & Seigneurin-Berny, D. (2001) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(00)00174-x · Cited by 366 · see citing works
Lysine acetylation and the bromodomain: a new partnership for signaling
Yang, X. (2004) · BioEssays · doi:10.1002/bies.20104 · Cited by 359 · see citing works
Self-citationBouras, T., Fu, M., Sauve, A. A., Wang, F., Quong, A. A., Perkins, N. D., Hay, R. T., Gu, W. J., & Pestell, R. G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m408748200 · Cited by 354 · see citing works
Huang, E. Y., Zhang, J., Miska, E. A., Guenther, M. G., Kouzarides, T., & Lazar, M. A. (2000) · Genes & Development · doi:10.1101/gad.14.1.45 · Cited by 325 · see citing works
Runx2 (Cbfa1, AML-3) Interacts with Histone Deacetylase 6 and Represses the p21 CIP1/WAF1 Promoter
Westendorf, J. J., Zaidi, S. K., Cascino, J. E., Kahler, R. A., van Wijnen, A. J., Lian, J. B., Yoshida, M., Stein, G. S., & Li, X. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.22.7982-7992.2002 · Cited by 319 · see citing works
HDAC4, a Human Histone Deacetylase Related to Yeast HDA1, Is a Transcriptional Corepressor
Wang, A. H., Bertos, N. R., Vezmar, M., Pelletier, N., Crosato, M., Heng, H. H., Th’ng, J., Han, J., & Yang, X.-J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.11.7816 · Cited by 294 · see citing works
Self-citationCharacterization of a human RPD3 ortholog, HDAC3
Emiliani, S., Fischle, W., Lint, C. M. V., Al-Abed, Y., & Verdin, E. M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.6.2795 · Cited by 292 · see citing works
Kasler, H. G., Victoria, J. G., Duramad, O., & Winoto, A. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.22.8382-8389.2000 · Cited by 267 · see citing works
Regulation of MEF2 by Histone Deacetylase 4- and SIRT1 Deacetylase-Mediated Lysine Modifications
Zhao, X., Sternsdorf, T., Bolger, T. A., Evans, R. M., & Yao, T.-P. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.19.8456-8464.2005 · Cited by 264 · see citing works
Gong, X., Tang, X., Wiedmann, M. W., Xuemin, W., Peng, J., Zheng, D., Blair, L. A. C., Marshall, J. J., & Mao, Z. (2003) · Neuron · doi:10.1016/s0896-6273(03)00191-0 · Cited by 260 · see citing works
Functional Domains of Histone Deacetylase-3
Yang, W., Tsai, S., Wen, Y., Fejér, G., & Seto, E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m105993200 · Cited by 247 · see citing works
Self-citationSchroeder, T. M., Kahler, R. A., Li, X., & Westendorf, J. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403702200 · Cited by 244 · see citing works
Zhang, X. M., Ozawa, Y., Lee, H., Wen, Y., Tan, T., Wadzinski, B. E., & Seto, E. (2005) · Genes & Development · doi:10.1101/gad.1286005 · Cited by 222 · see citing works
Self-citationSMRT Derepression by the IκB Kinase α
Hoberg, J. E., Yeung, F., & Mayo, M. W. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.10.010 · Cited by 220 · see citing works
Jin, Y.-H., Jeon, E.-J., Li, Q.-L., Lee, Y. H., Choi, J.-K., Kim, W.-J., Lee, K.-Y., & Bae, S.-C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313120200 · Cited by 211 · see citing works
Grégoire, S., & Yang, X. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.6.2273-2287.2005 · Cited by 207 · see citing works
Self-citationRegulatory Role of MEF2D in Serum Induction of the c- jun Promoter
Han, T.-H., & Prywes, R. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.6.2907 · Cited by 174 · see citing works
Control of MEF2 Transcriptional Activity by Coordinated Phosphorylation and Sumoylation
Grégoire, S., Tremblay, A., Xiao, L., Yang, Q., Ma, K., Nie, J., Mao, Z., Wu, Z., Giguère, V., & Yang, X. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509471200 · Cited by 171 · see citing works
Self-citationDequiedt, F., Lint, J. V., Lecomte, E., Duppen, V. V., Seufferlein, T. T. W., Vandenheede, J. R., Wattiez, R., & Kettmann, R. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20042034 · Cited by 171 · see citing works
A Mechanism for Coordinating Chromatin Modification and Preinitiation Complex Assembly
Black, J. C., Choi, J. E., Lombardo, S. R., & Carey, M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.07.018 · Cited by 168 · see citing works
Ma, K., Chan, J. K. L., Zhu, G., & Wu, Z. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.9.3575-3582.2005 · Cited by 165 · see citing works
Interaction of myocyte enhancer factor 2 (MEF2) with a mitogen-activated protein kinase, ERK5/BMK1
Yang, C.-H., Ornatsky, O., McDermott, J. C., Cruz, T. F., & Prody, C. A. (1998) · Nucleic Acids Research · doi:10.1093/nar/26.20.4771 · Cited by 161 · see citing works
Genome wide analysis of nucleosome density histone acetylation and HDAC function in fission yeast
Wirén, M., Silverstein, R. A., Sinha, I., Walfridsson, J., Lee, H.-M., Laurenson, P., Pillus, L., Robyr, D., Grunstein, M. R., & Ekwall, K. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600758 · Cited by 155 · see citing works
Big Mitogen-activated Kinase Regulates Multiple Members of the MEF2 Protein Family
Kato, Y., Zhao, M. F., Morikawa, A., Sugiyama, T., Chakravortty, D., Koide, N., Yoshida, T., Tapping, R. I., Yang, Y. C., Yokochi, T., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001573200 · Cited by 154 · see citing works
Negative regulation of histone deacetylase 8 activity by cyclic AMP-dependent protein kinase A
Lee, H., Rezai-Zadeh, N., & Seto, E. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.2.765-773.2004 · Cited by 153 · see citing works
Self-citationLiu, S., Liu, P., Borras, A. M., Chatila, T. A., & Speck, S. H. (1997) · The EMBO Journal · doi:10.1093/emboj/16.1.143 · Cited by 140 · see citing works
Parra, M., Kasler, H. G., McKinsey, T. A., Olson, E. N., & Verdin, E. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m413396200 · Cited by 138 · see citing works
A Recurrent Phospho-Sumoyl Switch in Transcriptional Repression and Beyond
Yang, X., & Grégoire, S. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.08.009 · Cited by 117 · see citing works
Self-citationRegulation of MEF2 by p38 MAPK and Its Implication in Cardiomyocyte Biology
Han, J. (2000) · Trends in Cardiovascular Medicine · doi:10.1016/s1050-1738(00)00039-6 · Cited by 115 · see citing works
Mechanism of Recruitment of Class II Histone Deacetylases by Myocyte Enhancer Factor-2
Han, A., He, J., Wu, Y., Liu, J. O., & Chen, L. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.10.033 · Cited by 107 · see citing works
Mechanisms of P/CAF auto-acetylation
Santos-Rosa, H. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg655 · Cited by 105 · see citing works
SMRT and N-CoR Corepressors Are Regulated by Distinct Kinase Signaling Pathways*
Jonas, B., & Privalsky, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410128200 · Cited by 101 · see citing works
Codina, A., Love, J. D., Li, Y., Lazar, M. A., Neuhaus, D., & Schwabe, J. W. R. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500299102 · Cited by 95 · see citing works
Foglietti, C., Filocamo, G., Cundari, E., de Rinaldis, E., Lahm, A., Cortese, R., & Steinkühler, C. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511945200 · Cited by 90 · see citing works
Interaction of Histone Acetylases and Deacetylases In Vivo
Yamagoe, S., Kanno, T., Kanno, Y., Sasaki, S., Siegel, R. M., Lenardo, M. J., Humphrey, G. W., Wang, Y., Nakatani, Y., Howard, B. H., et al. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.3.1025-1033.2003 · Cited by 86 · see citing works
Zhu, B., & Gulick, T. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.18.8264-8275.2004 · Cited by 84 · see citing works
Histone deacetylase 3 binds to and regulates the GCMa transcription factor
Chuang, H. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl048 · Cited by 83 · see citing works
Phosphorylation-facilitated sumoylation of MEF2C negatively regulates its transcriptional activity
Kang, J., Gocke, C. B., & Yu, H. (2006) · BMC Biochemistry · doi:10.1186/1471-2091-7-5 · Cited by 82 · see citing works
Xu, Q., Yu, L., Liu, L., Cheung, C. F., Li, X., Yee, S., Yang, X., & Wu, Z. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.02-02-0016 · Cited by 77 · see citing works
Self-citationIndividual histone deacetylases in Drosophila modulate transcription of distinct genes
Cho, Y., Griswold, A., Campbell, C., & Min, K.-T. (2005) · Genomics · doi:10.1016/j.ygeno.2005.07.007 · Cited by 71 · see citing works
The Pro279Leu variant in the transcription factor MEF2A is associated with myocardial infarction
González, P., García-Castro, M., Reguero, J. R., Batalla, A., Ordóñez, A. G., Palop, R. L., Lozano, I., Montes, M., Álvarez, V., & Coto, E. (2005) · Journal of Medical Genetics · doi:10.1136/jmg.2005.035071 · Cited by 61 · see citing works
SMRTe Inhibits MEF2C Transcriptional Activation by Targeting HDAC4 and 5 to Nuclear Domains
Wu, X., Li, H., Park, E.-J., & Chen, J. D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100412200 · Cited by 59 · see citing works
Identification of a novel fusion gene in a pre‐B acute lymphoblastic leukemia with t(1;19)(q23;p13)
Yuki, Y., Imoto, I., Imaizumi, M., Hibi, S., Kaneko, Y., Amagasa, T., & Inazawa, J. (2004) · Cancer Science · doi:10.1111/j.1349-7006.2004.tb03240.x · Cited by 52 · see citing works
AcK-knowledge Reversible Acetylation
Cohen, T., & Yao, T. (2004) · Science s STKE · doi:10.1126/stke.2452004pe42 · Cited by 51 · see citing works
Calmodulin‐dependent protein kinase IV regulates nuclear export of Cabin1 during T‐cell activation
Pan, F., Means, A. R., & Liu, J. O. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600685 · Cited by 40 · see citing works
Expression, purification, and analysis of MOZ and MORF histone acetyltransferases
Pelletier, N. (2003) · Methods · doi:10.1016/s1046-2023(03)00084-7 · Cited by 20 · see citing works
Flagged first, then by citations
1 of the 87 references couldn’t be matched to a known paper.
Research works printed but not linked: 1
- [72]Xu, Q., L. Yu, L. Liu, C. F. Cheung, X. Li, S. K. Yee, X.-J. Yang, and Z. Wu. 2002. The p38 MAPK, CaMK and calcineurin-mediated signaling pathways transcriptionally regulate myogenin expression. Mol. Biol. Cell 13:1940-1952. [DOI] [PMC free article] [PubMed] [Google Scholar]
Cited by
Sorted by citations
Histone Deacetylase Inhibitors: Overview and Perspectives
Dokmanovic, M., Clarke, C., & Marks, P. A. (2007) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-07-0324 · Cited by 1,173 · see citing works
Yang, X.-J., & Seto, E. (2007) · Oncogene · doi:10.1038/sj.onc.1210599 · Cited by 1,040 · see citing works
Self-citationTherapeutic 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
Unraveling the hidden catalytic activity of vertebrate class IIa histone deacetylases
Lahm, A., Paolini, C., Pallaoro, M., Nardi, M. C., Jones, P., Neddermann, P., Sambucini, S., Bottomley, M. J., Lo Surdo, P., Carfı́, A., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0706487104 · Cited by 566 · see citing works
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
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
Bhaskara, S., Chyla, B., Amann, J. M., Knutson, S. K., Cortez, D., Sun, Z., & Hiebert, S. W. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.02.030 · Cited by 369 · see citing works
Maintenance of cardiac energy metabolism by histone deacetylase 3 in mice
Montgomery, R. L., Potthoff, M. J., Haberland, M., Qi, X., Matsuzaki, S., Humphries, K. M., Richardson, J. A., Bassel‐Duby, R., & Olson, E. N. (2008) · Journal of Clinical Investigation · doi:10.1172/jci35847 · Cited by 363 · 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
Regulation of fetal gene expression in heart failure
Dirkx, E., Martins, P. A. D. C., & Windt, L. J. D. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.07.023 · Cited by 282 · see citing works
Liver-specific deletion of histone deacetylase 3 disrupts metabolic transcriptional networks
Knutson, S. K., Chyla, B. J., Amann, J. M., Bhaskara, S., Huppert, S. S., & Hiebert, S. W. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.51 · Cited by 271 · see citing works
NCoR1 Is a Conserved Physiological Modulator of Muscle Mass and Oxidative Function
Yamamoto, H., Williams, E. G., Mouchiroud, L., Cantó, C., Fan, W., Downes, M., Héligon, C., Barish, G. D., Desvergne, B., Evans, R. M., et al. (2011) · Cell · doi:10.1016/j.cell.2011.10.017 · Cited by 261 · see citing works
Schuetz, A., Min, J., Allali‐Hassani, A., Schapira, M., Shuen, M., Loppnau, P., Mazitschek, R., Kwiatkowski, N. P., Lewis, T. A., Maglathin, R. L., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m707362200 · Cited by 261 · see citing works
Galmozzi, A., Mitro, N., Ferrari, A., Gers, E., Gilardi, F., Godio, C., Cermenati, G., Gualerzi, A., Donetti, E., Rotili, D., et al. (2012) · Diabetes · doi:10.2337/db12-0548 · Cited by 236 · see citing works
HDACs and HDAC inhibitors in colon cancer
Mariadason, J. M. (2008) · Epigenetics · doi:10.4161/epi.3.1.5736 · Cited by 226 · see citing works
HDAC3: taking the SMRT-N-CoRrect road to repression
Karagianni, P., & Wong, J. (2007) · Oncogene · doi:10.1038/sj.onc.1210612 · Cited by 221 · see citing works
Self-citationNuclear receptor co-repressors are required for the histone-deacetylase activity of HDAC3 in vivo
You, S.-H., Lim, H., Sun, Z., Broache, M., Won, K., & Lazar, M. A. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2476 · Cited by 200 · see citing works
The role of histone deacetylases in prostate cancer
Abbas, A., & Gupta, S. (2008) · Epigenetics · doi:10.4161/epi.3.6.7273 · Cited by 156 · see citing works
Quantitative Control of Adaptive Cardiac Hypertrophy by Acetyltransferase p300
Wei, J. Q., Shehadeh, L. A., Mitrani, J. M., Pessanha, M. G., Slepak, T. I., Webster, K. A., & Bishopric, N. H. (2008) · Circulation · doi:10.1161/circulationaha.107.760488 · Cited by 140 · see citing works
Histone Deacetylase-1 (HDAC1) Is a Molecular Switch between Neuronal Survival and Death
Bardai, F. H., Price, V. J., Zaayman, M., Wang, L., & D’Mello, S. R. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.394544 · Cited by 134 · see citing works
Song, C., Kanthasamy, A. G., Jin, H., Anantharam, V., & Kanthasamy, A. G. (2011) · NeuroToxicology · doi:10.1016/j.neuro.2011.05.018 · Cited by 131 · see citing works
HDAC3 and the molecular brake pad hypothesis
McQuown, S. C., & Wood, M. A. (2011) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2011.04.005 · Cited by 122 · see citing works
The promise and perils of HDAC inhibitors in neurodegeneration
Didonna, A., & Opal, P. (2014) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.147 · Cited by 120 · see citing works
Concise Review: Epigenetic Regulation of Myogenesis in Health and Disease
Sincennes, M., Brun, C. E., & Rudnicki, M. A. (2016) · Stem Cells Translational Medicine · doi:10.5966/sctm.2015-0266 · Cited by 114 · see citing works
Tuning acetylation levels with HAT activators: Therapeutic strategy in neurodegenerative diseases
Selvi, B. R., Cassel, J., Kundu, T. K., & Boutillier, A. (2010) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2010.08.012 · Cited by 117 · see citing works
Xiang, J., Zhang, N., Sun, H., Su, L., Zhang, C., Xu, H., Feng, J., Wang, M., Chen, J., Liu, L., et al. (2019) · Gastroenterology · doi:10.1053/j.gastro.2019.10.025 · Cited by 113 · see citing works
Nuclear receptor coactivators: structural and functional biochemistry
Bulynko, Y. A., & O’Malley, B. W. (2011) · Biochemistry · doi:10.1021/bi101762x · Cited by 113 · see citing works
Yao, Y.-L., & Yang, W.-M. (2010) · Journal of Biomedicine and Biotechnology · doi:10.1155/2011/146493 · Cited by 120 · see citing works
Transcriptional Coregulators: Fine-Tuning Metabolism
Mouchiroud, L., Eichner, L. J., Shaw, R. J., & Auwerx, J. H. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.03.027 · Cited by 111 · see citing works
Roles and Targets of Class I and IIa Histone Deacetylases in Cardiac Hypertrophy
Kee, H. J., & Kook, H. (2010) · BioMed Research International · doi:10.1155/2011/928326 · Cited by 110 · see citing works
Insulin and mTOR Pathway Regulate HDAC3-Mediated Deacetylation and Activation of PGK1
Wang, S., Jiang, B., Zhang, T., Liu, L., Wang, Y., Wang, Y., Chen, X., Lin, H., Zhou, L., Xia, Y., et al. (2015) · PLoS Biology · doi:10.1371/journal.pbio.1002243 · Cited by 109 · see citing works
Acetyltransferases (HATs) as Targets for Neurological Therapeutics
Schneider‐Anthony, A., Chatterjee, S., Bousiges, O., Selvi, B. R., Swaminathan, A., Cassel, R., Blanc, F., Kundu, T. K., & Boutillier, A. (2013) · Neurotherapeutics · doi:10.1007/s13311-013-0204-7 · Cited by 108 · see citing works
Histone deacetylases in cardiovascular and metabolic diseases
Bagchi, R. A., & Weeks, K. L. (2019) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2019.04.003 · Cited by 108 · see citing works
Jung, S.-B., Kim, C., Naqvi, A., Yamamori, T., Mattagajasingh, I., Hoffman, T. A., Cole, M. P., Kumar, A., DeRicco, J. S., Jeon, B. H., et al. (2010) · Circulation Research · doi:10.1161/circresaha.110.222968 · Cited by 106 · see citing works
Deacetylation of Nonhistone Proteins by HDACs and the Implications in Cancer
Peng, L., & Seto, E. (2011) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-21631-2_3 · Cited by 105 · see citing works
Self-citationSuzuki, T., Kasuya, Y., Itoh, Y., Ota, Y., Zhan, P., Asamitsu, K., Nakagawa, H., Okamoto, T., & Miyata, N. (2013) · PLoS ONE · doi:10.1371/journal.pone.0068669 · Cited by 104 · see citing works
FOXP3+ regulatory T cell development and function require histone/protein deacetylase 3
Wang, L., Liu, Y., Han, R., Beier, U. H., Bhatti, T. R., Akimova, T., Greene, M. I., Hiebert, S. W., & Hancock, W. W. (2015) · Journal of Clinical Investigation · doi:10.1172/jci77088 · Cited by 103 · see citing works
Inhibition of HDAC3 promotes ligand-independent PPARγ activation by protein acetylation
Jiang, X., Ye, X., Guo, W., Lu, H., & Gao, Z. (2014) · Journal of Molecular Endocrinology · doi:10.1530/jme-14-0066 · Cited by 102 · see citing works
Transcription and beyond: the role of mammalian class I lysine deacetylases
Moser, M. A., Hagelkrüys, A., & Seiser, C. (2013) · Chromosoma · doi:10.1007/s00412-013-0441-x · Cited by 96 · see citing works
Walkinshaw, D. R., Weist, R., Kim, G.-W., You, L., Xiao, L., Nie, J., Li, C. S., Zhao, S., Xu, M., & Yang, X. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.456996 · Cited by 98 · see citing works
Self-citationHa, 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
Jia, H., Wang, Y., Morris, C. D., Jacques, V., Gottesfeld, J. M., Rusche, J. R., & Thomas, E. A. (2016) · PLoS ONE · doi:10.1371/journal.pone.0152498 · Cited by 95 · see citing works
Metabolic reprogramming by class I and II histone deacetylases
Mihaylova, M. M., & Shaw, R. J. (2012) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2012.09.003 · Cited by 95 · see citing works
Mitochondrial alteration in type 2 diabetes and obesity: An epigenetic link
Cheng, Z., & Almeida, F. A. (2014) · Cell Cycle · doi:10.4161/cc.28189 · Cited by 94 · see citing works
Myocyte enhancer factor 2C in hematopoiesis and leukemia
Canté-Barrett, K., Pieters, R., & Meijerink, J. (2014) · Oncogene · doi:10.1038/onc.2013.56 · Cited by 91 · see citing works
HDAC3 Is Negatively Regulated by the Nuclear Protein DBC1
Chini, C. C. S., Escande, C., Nin, V., & Chini, E. N. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.153270 · Cited by 88 · see citing works
Suelves, N., Kirkham-McCarthy, L., Lahue, R. S., & Ginés, S. (2017) · Scientific Reports · doi:10.1038/s41598-017-05125-2 · Cited by 83 · see citing works
Zha, L., Li, F., Wu, R., Artinian, L. R., Rehder, V., Yu, L., Liang, H., Xue, B., & Shi, H. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.662650 · Cited by 81 · see citing works
What Causes a Broken Heart—Molecular Insights into Heart Failure
Barry, S. P., & Townsend, P. A. (2010) · International review of cytology · doi:10.1016/s1937-6448(10)84003-1 · Cited by 78 · see citing works
Histone Deacetylase 7 and FoxA1 in Estrogen-Mediated Repression of RPRM
Malik, S., Jiang, S., Garee, J. P., Verdin, E. M., Lee, A. V., O’Malley, B. W., Zhang, M., Belaguli, N. S., & Oesterreich, S. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00907-09 · Cited by 79 · see citing works
Autoacetylation Regulates P/CAF Nuclear Localization
Blanco-García, N., Asensio-Juan, E., de la Cruz, X., & Martínez‐Balbás, M. A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806075200 · Cited by 73 · see citing works
Histone deacetylases in viral infections
Herbein, G., & Wendling, D. (2010) · Clinical Epigenetics · doi:10.1007/s13148-010-0003-5 · Cited by 72 · see citing works
Histone Deacetylase 9 (HDAC9) Regulates the Functions of the ATDC (TRIM29) Protein
Yuan, Z., Peng, L., Radhakrishnan, R., & Seto, E. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.179333 · Cited by 71 · see citing works
Self-citationEpigenetics of Autism Spectrum Disorder: Histone Deacetylases
Tseng, C.-E. J., McDougle, C. J., Hooker, J. M., & Zürcher, N. R. (2021) · Biological Psychiatry · doi:10.1016/j.biopsych.2021.11.021 · Cited by 71 · see citing works
Choi, J., Jang, H., Kim, H., Lee, J., Kim, S., Cho, E., & Youn, H. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt873 · Cited by 69 · see citing works
MEF2C is activated by multiple mechanisms in a subset of T-acute lymphoblastic leukemia cell lines
Nagel, S., Meyer, C., Quentmeier, H., Kaufmann, M., Drexler, H., & MacLeod, R. (2008) · Leukemia · doi:10.1038/sj.leu.2405067 · Cited by 65 · see citing works
Moores, R., Brilha, S., Schutgens, F., Elkington, P. T., & Friedland, J. S. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00602 · Cited by 61 · see citing works
Ganai, S. A., Banday, S., Farooq, Z., & Altaf, M. (2016) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2016.07.001 · Cited by 60 · see citing works
Huynh, N. C., Everts, V. E., Pavasant, P., & Ampornaramveth, R. S. (2015) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25429 · Cited by 59 · see citing works
Aude-Garcia, C., Collin-Faure, V., Bausinger, H., Hanau, D., Rabilloud, T., & Lemercier, C. (2010) · Biochemical Journal · doi:10.1042/bj20100131 · Cited by 49 · see citing works
Selective class IIa HDAC inhibitors: myth or reality
Giorgio, E. D., Gagliostro, E., & Brancolini, C. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1727-8 · Cited by 57 · see citing works
Essential and Unexpected Role of Yin Yang 1 to Promote Mesodermal Cardiac Differentiation
Grégoire, S., Karra, R., Passer, D., Deutsch, M.-A., Krane, M., Feistritzer, R., Sturzu, A. C., Domian, I. J., Saga, Y., & Wu, S. M. (2013) · Circulation Research · doi:10.1161/circresaha.113.259259 · Cited by 58 · see citing works
Self-citationMozzetta, C., Sartorelli, V., & Puri, P. (2024) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2024.01.007 · Cited by 57 · see citing works
Mechanism of histone deacetylases in cardiac hypertrophy and its therapeutic inhibitors
Han, Y., Nie, J., Wang, D. W., & Li, N. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.931475 · Cited by 56 · see citing works
Self-citationTrichostatin A prevents neointimal hyperplasia via activation of Krüppel like factor 4
Kee, H. J., Kwon, J., Shin, S., Ahn, Y., Jeong, M. H., & Kook, H. (2011) · Vascular Pharmacology · doi:10.1016/j.vph.2011.07.001 · Cited by 55 · see citing works
Thomas, E. A. (2014) · Pharmaceuticals · doi:10.3390/ph7060634 · Cited by 51 · see citing works
Histone acetylation in neuronal (dys)function
Bonnaud, E. M., Suberbielle, E., & Malnou, C. E. (2016) · BioMolecular Concepts · doi:10.1515/bmc-2016-0002 · Cited by 54 · see citing works
Liu, G., Gramling, S. J. B., Munoz, D., Cheng, D., Azad, A. K., Mirshams, M., Chen, Z., Xu, W., Roberts, H. N., Shepherd, F. A., et al. (2011) · Oncogene · doi:10.1038/onc.2011.81 · Cited by 54 · see citing works
Minamiya, Y., Ono, T., Saito, H., Takahashi, N., Ito, M., Motoyama, S., & Ogawa, J. (2010) · Tumor Biology · doi:10.1007/s13277-010-0066-0 · Cited by 53 · see citing works
Lkhagva, B., Kao, Y., Lee, T.-I., Lee, T., Cheng, W., & Chen, Y. (2018) · Epigenetics · doi:10.1080/15592294.2018.1460032 · Cited by 53 · see citing works
Therapeutic potential of selective histone deacetylase 3 inhibition
Zhang, L., Chen, Y., Jiang, Q., Song, W., & Zhang, L. J. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.10.072 · Cited by 51 · see citing works
Epigenetics and autosomal dominant polycystic kidney disease
Li, X. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2010.10.008 · Cited by 52 · see citing works
Function of the Active Site Lysine Autoacetylation in Tip60 Catalysis
Yang, C., Wu, J., & Zheng, Y. G. (2012) · PLoS ONE · doi:10.1371/journal.pone.0032886 · Cited by 51 · see citing works
Identifying targets for the restoration and reactivation of BRM
Kahali, B., Gramling, S. J. B., Marquez, S. B., Thompson, K., Lu, L., & Reisman, D. (2013) · Oncogene · doi:10.1038/onc.2012.613 · Cited by 51 · see citing works
The role and molecular mechanism of epigenetics in cardiac hypertrophy
Lei, H. C., Hu, J., Sun, K., & Xu, D. (2020) · Heart Failure Reviews · doi:10.1007/s10741-020-09959-3 · Cited by 51 · see citing works
Wu, Y., Dey, R., Han, A., Jayathilaka, N., Philips, M. A., Ye, J., & Chen, L. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.01.067 · Cited by 47 · see citing works
Beyond Mutations: Additional Mechanisms and Implications of SWI/SNF Complex Inactivation
Marquez, S. B., Thompson, K. W., Lu, L., & Reisman, D. (2015) · Frontiers in Oncology · doi:10.3389/fonc.2014.00372 · Cited by 49 · see citing works
Histone deacetylase 3 regulates microglial function through histone deacetylation
Meleady, L., Towriss, M., Kim, J. S., Bacarac, V., Dang, V., Rowland, M. E., & Ciernia, A. V. (2023) · Epigenetics · doi:10.1080/15592294.2023.2241008 · Cited by 47 · see citing works
Metabolism, cytoskeleton and cellular signalling in the grip of protein Nϵ ‐ and O‐acetylation
Yang, X., & Grégoire, S. (2007) · EMBO Reports · doi:10.1038/sj.embor.7400977 · Cited by 48 · see citing works
Self-citationMyoD Acetylation Influences Temporal Patterns of Skeletal Muscle Gene Expression
Padova, M. D., Caretti, G., Zhao, P., Hoffman, E. P., & Sartorelli, V. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m707309200 · Cited by 47 · see citing works
Class I and IIa Histone Deacetylases Have Opposite Effects on Sclerostin Gene Regulation
Baertschi, S., Baur, N., Lueders-Lefevre, V., Voshol, J., & Keller, H. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.564997 · Cited by 46 · see citing works
The silencing of the SWI/SNF subunit and anticancer gene BRM in Rhabdoid tumors
Kahali, B., Yu, J., Marquez, S. B., Thompson, K. W., Liang, S. Y., Lü, L., & Reisman, D. (2014) · Oncotarget · doi:10.18632/oncotarget.1945 · Cited by 46 · see citing works
Sodium Butyrate-Modulated Mitochondrial Function in High-Insulin Induced HepG2 Cell Dysfunction
Zhao, T., Gu, J., Zhang, H., Wang, Z., Zhang, W., Zhao, Y., Zheng, Y., Zhang, W., Zhou, H., Zhang, G., et al. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/1904609 · Cited by 46 · see citing works
Galectin-9 Protein Expression in Endothelial Cells Is Positively Regulated by Histone Deacetylase 3
Alam, S., Li, H., Margariti, A., Martin, D., Zampetaki, A., Habi, O., COCKERILL, G. W., Hu, Y., Xu, Q., & Zeng, L. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.242289 · Cited by 45 · see citing works
Epigenetic Mechanisms of Gene Regulation in Amyotrophic Lateral Sclerosis
Jimenez‐Pacheco, A., Franco, J. M., Lopez, S., Gómez‐Zumaquero, J. M., Leal‐Lasarte, M., Caballero-Hernández, D. E., Cejudo‐Guillén, M., & Pozo, D. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-53889-1_14 · Cited by 45 · see citing works
Epigenetic Regulation of HIV-1 Transcription
Tripathy, M. K., Abbas, W., & Herbein, G. (2011) · Epigenomics · doi:10.2217/epi.11.61 · Cited by 43 · see citing works
Reversal of pathological cardiac hypertrophy via the MEF2-coregulator interface
Wei, J., Joshi, S., Speransky, S. R., Crowley, C., Jayathilaka, N., Lei, X., Wu, Y., Gai, D., Jain, S. K., Hoosien, M., et al. (2017) · JCI Insight · doi:10.1172/jci.insight.91068 · Cited by 43 · see citing works
Liu, S., Fang, X., Wen, X., Liu, J.-S., Alip, M., Sun, T., Wang, Y. Y., & Chen, H. (2024) · World Journal of Stem Cells · doi:10.4252/wjsc.v16.i3.245 · Cited by 41 · see citing works
Perry, R. L. S., Yang, C.-C., Soora, N., Salma, J., Marback, M., Naghibi, L., Ilyas, H., Chan, J., Gordon, J. W., & McDermott, J. C. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00227-08 · Cited by 41 · see citing works
SIRT7 activates p53 by enhancing PCAF-mediated MDM2 degradation to arrest the cell cycle
Lu, Y.-F., Xu, X.-P., Lu, X.-P., Zhu, Q., Liu, G., Bao, Y.-T., Wen, H., Li, Y.-L., Gu, W., & Zhu, W.-G. (2020) · Oncogene · doi:10.1038/s41388-020-1305-5 · Cited by 40 · see citing works
Literature-based priors for gene regulatory networks
Steele, E., Tucker, A., Hoen, P. A. C. ’., & Schuemie, M. J. (2009) · Bioinformatics · doi:10.1093/bioinformatics/btp277 · Cited by 39 · see citing works
Lee, H., Song, M., Seok, Y. M., Kang, S., Kim, S., & Kim, I. (2015) · PLoS ONE · doi:10.1371/journal.pone.0136801 · Cited by 39 · see citing works
Myocyte Enhancer Factor 2 Transcription Factors in Heart Development and Disease
Black, B. L., & Cripps, R. M. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-381332-9.00030-x · Cited by 37 · see citing works
Han, K. A., Shin, W. H., Jung, S., Seol, W., Seo, H., Ko, C. J., & Chung, K. C. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw363 · Cited by 36 · see citing works
Daems, C., Di‐Luoffo, M., Paradis, E., & Tremblay, J. (2015) · Endocrinology · doi:10.1210/en.2014-1964 · Cited by 36 · see citing works
Rajan, A., Shi, H., & Xue, B. (2018) · Scientific Reports · doi:10.1038/s41598-018-31560-w · Cited by 35 · see citing works
Hess, L., Moos, V., Lauber, A. A., Reiter, W., Schuster, M. K., Hartl, N., Lackner, D. H., Boenke, T., Koren, A., Guzzardo, P. M., et al. (2022) · PLoS Genetics · doi:10.1371/journal.pgen.1010376 · Cited by 36 · see citing works
Angelelli, C., Magli, A., Ferrari, D., Ganassi, M., Matafora, V., Parise, F., Razzini, G., Bachi, A., Ferrari, S. M., & Molinari, S. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm1114 · Cited by 34 · see citing works
Dionyssiou, M. G., Nowacki, N., Hashemi, S., Zhao, J., Kerr, A., Tsushima, R. G., & McDermott, J. C. (2012) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2012.10.013 · Cited by 33 · see citing works
Taylor, J. M., Ghorbel, S., & Nicot, C. (2009) · BMC Genomics · doi:10.1186/1471-2164-10-311 · Cited by 32 · see citing works
- Authors
- Grégoire, S., Xiao, L., Nie, J., Zhang, X., Xu, M., Li, J., Wong, J., Seto, E., & Yang, X.-J.
- Affiliations
- McGill University Health Centre (CA)
- Moffitt Cancer Center (US)
- Baylor College of Medicine (US)
- Corresponding author
- Yang, Xiang-Jiao
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2007-02-01
- Volume
- 27
- Issue
- 4
- Pages
- 1280-1295
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC1800729
- OpenAlex
- W2170524079
- Cited by
- 203
- References
- 87
- Citations by year
- 2026: 3 · 2025: 8 · 2024: 7 · 2023: 4 · 2022: 9 · 2021: 4 · 2020: 12 · 2019: 6 · 2018: 7 · 2017: 10 · 2016: 9 · 2015: 12 · 2014: 12 · 2013: 15 · 2012: 12
- FWCI
- 5.04
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular and Cellular Biology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Cancer Institute
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Keywords
- HDAC3, MEF2, MEF2D, lysine acetylation, protein deacetylation, MADS-box, P300, PCAF, SMRT, transcriptional repression, myogenesis, trichostatin A, nicotinamide, HDAC4, HDAC5
- MeSH terms
- Histone Deacetylase 3, p300-CBP-Associated Factor, Acetylation, Animals, Binding Sites, Histone Deacetylases, Humans, Models, Genetic, Nuclear Proteins, Protein Binding, Repressor Proteins, Transcription Factors, Transcription, Genetic, Protein Structure, Tertiary, Myogenic Regulatory Factors, Cell Cycle Proteins, Protein Transport, Muscle Development, Protein Interaction Mapping, Myoblasts, p300-CBP Transcription Factors, Mice, Histone Acetyltransferases, Nuclear Receptor Co-Repressor 1, MEF2 Transcription Factors
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
