{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\n Histone deacetylase 3 (HDAC3) emerges as a versatile epigenomic modifier that exerts context‐dependent effects by engaging in distinct corepressor complexes to shape chromatin structure and transcriptional programs. In inflammatory macrophages, for example, ligand‐bound and SUMOylated nuclear receptors such as PPARγ recruit a nuclear receptor corepressor (NCoR)–HDAC3 complex to inflammatory gene promoters, thereby preventing the signal‐dependent clearance of corepressors and maintaining transcriptional repression."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": " In contrast, HDAC3 displacement is critical for gene activation in response to kinase signalling; one study showed that PKM2‐mediated histone H3 phosphorylation leads to HDAC3 dissociation from promoters of cell cycle regulators, facilitating transcription."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n HDAC3 recruitment also displays a pronounced circadian rhythm in the liver. Its association with the nuclear receptor Rev‐erbα directs periodic histone deacetylation at metabolic gene loci, which in turn governs lipid homeostasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "3", "end_ref": "6"}]}, {"type": "t", "text": " In parallel, HDAC3 is co‐opted into pathways that regulate antioxidant and anti‐tumor responses; for instance, NF‑κB p65 can recruit HDAC3 to antioxidant response element (ARE)–associated promoters, thereby repressing Nrf2‐mediated transcription of cytoprotective genes."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "7"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n In cancer biology, aberrant HDAC3 expression has been linked to cellular proliferation and differentiation outcomes. Human colon cancers show increased HDAC3 levels that correlate with reduced expression of differentiation markers such as p21, while HDAC3 silencing in these cells restores maturation and induces apoptosis."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "8"}]}, {"type": "t", "text": " Conversely, in immune cells, HDAC3 acts as a “brake” on alternative macrophage activation by deacetylating histones at IL‑4–responsive regulatory regions."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "9"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n Beyond its repressive activities, HDAC3 plays critical roles in maintaining genomic stability and coordinating metabolism across tissues. Conditional deletion studies in mouse embryonic fibroblasts reveal that loss of HDAC3 leads to cell cycle delays, DNA damage in proliferating cells, and defective double‐strand break repair."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "10"}]}, {"type": "t", "text": " In the heart, cardiac‐specific ablation of HDAC3 disrupts metabolic homeostasis and triggers hypertrophy through excessive PPARα activity"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "11"}]}, {"type": "t", "text": ", and in the liver, HDAC3 depletion reroutes metabolic precursors toward lipid storage while paradoxically improving insulin sensitivity."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "12"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n Mechanistically, HDAC3’s deacetylase activity is conferred by its stable association with the conserved deacetylase-activating domain (DAD) of corepressors such as NCoR and SMRT."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "13"}]}, {"type": "t", "text": " Its function is further refined by direct interactions with transcription factors. For instance, HDAC3 deacetylates MEF2D to repress myogenic gene expression"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "15"}]}, {"type": "t", "text": ", while in brown adipose tissue it acts as a coactivator of estrogen-related receptor α (ERRα) by deacetylating PGC-1α to prime thermogenic gene transcription."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "16"}]}, {"type": "t", "text": " In adipogenesis, recruitment of HDAC3 by KLF6 mediates repression of Dlk1, thereby promoting preadipocyte differentiation."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "17"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n Additional layers of regulation arise from its dynamic interactions with other factors. HDAC3’s association with c‑Jun is modulated by phosphorylation-dependent events that relieve inhibitory complexes to allow gene activation"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "18"}]}, {"type": "t", "text": ", and in aggressive B-cell malignancies, c‑Myc cooperates with HDAC3 to epigenetically repress microRNAs, thereby contributing to transformation."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "19"}]}, {"type": "t", "text": " Moreover, HDAC3 activity is subject to modulation by hypoxic cues that repress specific long noncoding RNAs"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "20"}]}, {"type": "t", "text": "and by cellular mechanical signals that affect its nucleocytoplasmic distribution and thereby alter local histone acetylation."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "21"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n Collectively, these diverse studies illustrate that HDAC3 functions as an integrative hub—its recruitment by nuclear receptors (e.g. Rev‑erbα, TR) and transcription factors enables it to coordinate circadian rhythms"}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "4", "end_ref": "6"}]}, {"type": "t", "text": ", control cell cycle and DNA repair"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "10"}]}, {"type": "t", "text": ", regulate differentiation processes such as myogenesis and adipogenesis"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "15"}, {"type": "fg_f", "ref": "17"}]}, {"type": "t", "text": ", and modulate metabolic homeostasis in cardiac, hepatic, and brown adipose tissues."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "11"}, {"type": "fg_f", "ref": "16"}]}, {"type": "t", "text": " Furthermore, HDAC3 is incorporated into oncogenic pathways—for instance, the MAGE-A2 protein recruits HDAC3 to attenuate p53-dependent transactivation"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "22"}]}, {"type": "t", "text": "and Runx2-mediated transcription in osteoblast differentiation is similarly repressed."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "23"}]}, {"type": "t", "text": " Its role in brown adipogenesis extends to partnering with transcriptional regulators and corepressors to fine-tune thermogenic gene programs"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "24"}]}, {"type": "t", "text": ", and epithelial integrity in the intestine is maintained by HDAC3, which integrates signals from commensal bacteria."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "25"}]}, {"type": "t", "text": " Finally, during epithelial-mesenchymal transition in cancer, nuclear PKM2 interacts with TGIF2 to recruit HDAC3 for local histone deacetylation and suppression of E-cadherin."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "26"}]}, {"type": "t", "text": "\n "}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n Overall, HDAC3 acts as a central node linking chromatin modification to diverse signaling pathways and transcriptional networks that govern inflammation, metabolism, cell cycle progression, differentiation, and circadian regulation.\n "}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Gabriel Pascual, Amy L Fong, Sumito Ogawa, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A SUMOylation-dependent pathway mediates transrepression of inflammatory response genes by PPAR-gamma."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nature (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/nature03988"}], "href": "https://doi.org/10.1038/nature03988"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16127449"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16127449"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Weiwei Yang, Yan Xia, David Hawke, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PKM2 phosphorylates histone H3 and promotes gene transcription and tumorigenesis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.cell.2012.07.018"}], "href": "https://doi.org/10.1016/j.cell.2012.07.018"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22901803"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22901803"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Dan Feng, Tao Liu, Zheng Sun, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A circadian rhythm orchestrated by histone deacetylase 3 controls hepatic lipid metabolism."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Science (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1126/science.1198125"}], "href": "https://doi.org/10.1126/science.1198125"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21393543"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21393543"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Lei Yin, Mitchell A Lazar "}, {"type": "b", "children": [{"type": "t", "text": "The orphan nuclear receptor Rev-erbalpha recruits the N-CoR/histone deacetylase 3 corepressor to regulate the circadian Bmal1 gene."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Endocrinol (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1210/me.2005-0057"}], "href": "https://doi.org/10.1210/me.2005-0057"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15761026"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15761026"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Theresa Alenghat, Katherine Meyers, Shannon E Mullican, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Nuclear receptor corepressor and histone deacetylase 3 govern circadian metabolic physiology."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nature (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/nature07541"}], "href": "https://doi.org/10.1038/nature07541"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19037247"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19037247"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Yong Hoon Kim, Sajid A Marhon, Yuxiang Zhang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Rev-erbα dynamically modulates chromatin looping to control circadian gene transcription."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Science (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1126/science.aao6891"}], "href": "https://doi.org/10.1126/science.aao6891"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29439026"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29439026"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Guang-Hui Liu, Jing Qu, Xun Shen "}, {"type": "b", "children": [{"type": "t", "text": "NF-kappaB/p65 antagonizes Nrf2-ARE pathway by depriving CBP from Nrf2 and facilitating recruitment of HDAC3 to MafK."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochim Biophys Acta (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbamcr.2008.01.002"}], "href": "https://doi.org/10.1016/j.bbamcr.2008.01.002"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18241676"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18241676"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Andrew J Wilson, Do-Sun Byun, Natalia Popova, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Histone deacetylase 3 (HDAC3) and other class I HDACs regulate colon cell maturation and p21 expression and are deregulated in human colon cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M510023200"}], "href": "https://doi.org/10.1074/jbc.M510023200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16533812"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16533812"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Shannon E Mullican, Christine A Gaddis, Theresa Alenghat, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Histone deacetylase 3 is an epigenomic brake in macrophage alternative activation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Genes Dev (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1101/gad.175950.111"}], "href": "https://doi.org/10.1101/gad.175950.111"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22156208"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22156208"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Srividya Bhaskara, Brenda J Chyla, Joseph M Amann, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Deletion of histone deacetylase 3 reveals critical roles in S phase progression and DNA damage control."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.molcel.2008.02.030"}], "href": "https://doi.org/10.1016/j.molcel.2008.02.030"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18406327"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18406327"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Rusty L Montgomery, Matthew J Potthoff, Michael Haberland, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Maintenance of cardiac energy metabolism by histone deacetylase 3 in mice."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Clin Invest (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1172/JCI35847"}], "href": "https://doi.org/10.1172/JCI35847"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18830415"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18830415"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Zheng Sun, Russell A Miller, Rajesh T Patel, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Hepatic Hdac3 promotes gluconeogenesis by repressing lipid synthesis and sequestration."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Med (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/nm.2744"}], "href": "https://doi.org/10.1038/nm.2744"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22561686"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22561686"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Takahiro Ishizuka, Mitchell A Lazar "}, {"type": "b", "children": [{"type": "t", "text": "The N-CoR/histone deacetylase 3 complex is required for repression by thyroid hormone receptor."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Biol (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/MCB.23.15.5122-5131.2003"}], "href": "https://doi.org/10.1128/MCB.23.15.5122-5131.2003"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12861000"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12861000"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Seo-Hee You, Hee-Woong Lim, Zheng Sun, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Nuclear receptor co-repressors are required for the histone-deacetylase activity of HDAC3 in vivo."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Struct Mol Biol (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/nsmb.2476"}], "href": "https://doi.org/10.1038/nsmb.2476"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23292142"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23292142"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Serge Grégoire, Lin Xiao, Jianyun Nie, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Histone deacetylase 3 interacts with and deacetylates myocyte enhancer factor 2."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Biol (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/MCB.00882-06"}], "href": "https://doi.org/10.1128/MCB.00882-06"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17158926"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17158926"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Matthew J Emmett, Hee-Woong Lim, Jennifer Jager, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Histone deacetylase 3 prepares brown adipose tissue for acute thermogenic challenge."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nature (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/nature22819"}], "href": "https://doi.org/10.1038/nature22819"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28614293"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28614293"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Dan Li, Steven Yea, Side Li, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Krüppel-like factor-6 promotes preadipocyte differentiation through histone deacetylase 3-dependent repression of DLK1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M500463200"}], "href": "https://doi.org/10.1074/jbc.M500463200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15917248"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15917248"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Carsten Weiss, Sandra Schneider, Erwin F Wagner, et al. "}, {"type": "b", "children": [{"type": "t", "text": "JNK phosphorylation relieves HDAC3-dependent suppression of the transcriptional activity of c-Jun."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "EMBO J (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/emboj/cdg364"}], "href": "https://doi.org/10.1093/emboj/cdg364"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12853483"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12853483"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "X Zhang, X Chen, J Lin, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Myc represses miR-15a/miR-16-1 expression through recruitment of HDAC3 in mantle cell and other non-Hodgkin B-cell lymphomas."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncogene (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/onc.2011.470"}], "href": "https://doi.org/10.1038/onc.2011.470"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22002311"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22002311"}]}, {"type": "r", "ref": 20, "children": [{"type": "t", "text": "Fu Yang, Xi-song Huo, Sheng-xian Yuan, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Repression of the long noncoding RNA-LET by histone deacetylase 3 contributes to hypoxia-mediated metastasis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.molcel.2013.01.010"}], "href": "https://doi.org/10.1016/j.molcel.2013.01.010"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23395002"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23395002"}]}, {"type": "r", "ref": 21, "children": [{"type": "t", "text": "Nikhil Jain, K Venkatesan Iyer, Abhishek Kumar, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Cell geometric constraints induce modular gene-expression patterns via redistribution of HDAC3 regulated by actomyosin contractility."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.1300801110"}], "href": "https://doi.org/10.1073/pnas.1300801110"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23798429"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23798429"}]}, {"type": "r", "ref": 22, "children": [{"type": "t", "text": "Martin Monte, Marta Simonatto, Leticia Y Peche, et al. "}, {"type": "b", "children": [{"type": "t", "text": "MAGE-A tumor antigens target p53 transactivation function through histone deacetylase recruitment and confer resistance to chemotherapeutic agents."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.0510834103"}], "href": "https://doi.org/10.1073/pnas.0510834103"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16847267"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16847267"}]}, {"type": "r", "ref": 23, "children": [{"type": "t", "text": "Tania M Schroeder, Rachel A Kahler, Xiaodong Li, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Histone deacetylase 3 interacts with runx2 to repress the osteocalcin promoter and regulate osteoblast differentiation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M403702200"}], "href": "https://doi.org/10.1074/jbc.M403702200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15292260"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15292260"}]}, {"type": "r", "ref": 24, "children": [{"type": "t", "text": "Masaki Mori, Hironori Nakagami, Gerardo Rodriguez-Araujo, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Essential role for miR-196a in brown adipogenesis of white fat progenitor cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "PLoS Biol (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1371/journal.pbio.1001314"}], "href": "https://doi.org/10.1371/journal.pbio.1001314"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22545021"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22545021"}]}, {"type": "r", "ref": 25, "children": [{"type": "t", "text": "Theresa Alenghat, Lisa C Osborne, Steven A Saenz, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Histone deacetylase 3 coordinates commensal-bacteria-dependent intestinal homeostasis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nature (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/nature12687"}], "href": "https://doi.org/10.1038/nature12687"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24185009"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24185009"}]}, {"type": "r", "ref": 26, "children": [{"type": "t", "text": "Atsushi Hamabe, Masamitsu Konno, Nobuhiro Tanuma, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Role of pyruvate kinase M2 in transcriptional regulation leading to epithelial-mesenchymal transition."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.1407717111"}], "href": "https://doi.org/10.1073/pnas.1407717111"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25313085"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25313085"}]}]}]}