{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T06:21:36Z","timestamp":1790749296327,"version":"4.1.0"},"reference-count":53,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2017,9,19]],"date-time":"2017-09-19T00:00:00Z","timestamp":1505779200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2017,9,19]],"date-time":"2017-09-19T00:00:00Z","timestamp":1505779200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Sci Rep"],"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    Histone Deacetylase 11 (HDAC11) is highly expressed in the central nervous system where it has been reported to have roles in neural differentiation. In contrast with previous studies showing nuclear and cytoplasmic localisation, we observed synaptic enrichment of HDAC11. Knockout mouse models for HDACs 1\u20139 have been important for guiding the development of isoform specific HDAC inhibitors as effective therapeutics. Given the close relationship between HDAC11 and neural cells\n                    <jats:italic>in vitro<\/jats:italic>\n                    , we examined neural tissue in a previously uncharacterised\n                    <jats:italic>Hdac11<\/jats:italic>\n                    knockout mouse (\n                    <jats:italic>Hdac11<\/jats:italic>\n                    <jats:sup>KO\/KO<\/jats:sup>\n                    ). Loss of HDAC11 had no obvious impact on brain morphology and neural stem\/precursor cells isolated from\n                    <jats:italic>Hdac11<\/jats:italic>\n                    <jats:sup>KO\/KO<\/jats:sup>\n                    mice had comparable proliferation and differentiation characteristics. However, in differentiating neural cells we observed decreased expression of schizophrenia-associated gene\n                    <jats:italic>Fez1<\/jats:italic>\n                    (fasciculation and elongation protein zeta 1), a gene previously reported to be regulated by HDAC11 activity. FEZ1 has been associated with the dendritic growth of neurons and risk of schizophrenia via its interaction with DISC1 (disrupted in schizophrenia 1). Examination of cortical, cerebellar and hippocampal tissue reveal decreased\n                    <jats:italic>Fez1<\/jats:italic>\n                    expression specifically in the hippocampus of adult mice. The results of this study demonstrate that loss of HDAC11 has age dependent and brain-region specific consequences.\n                  <\/jats:p>","DOI":"10.1038\/s41598-017-11630-1","type":"journal-article","created":{"date-parts":[[2017,9,13]],"date-time":"2017-09-13T09:39:38Z","timestamp":1505295578000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":28,"title":["Disruption to schizophrenia-associated gene Fez1 in the hippocampus of HDAC11 knockout mice"],"prefix":"10.1038","volume":"7","author":[{"given":"Dale T.","family":"Bryant","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christian","family":"Landles","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aikaterini S.","family":"Papadopoulou","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Agnesska C.","family":"Benjamin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joshua K.","family":"Duckworth","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas","family":"Rosahl","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Caroline L.","family":"Benn","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4041-6305","authenticated-orcid":false,"given":"Gillian P.","family":"Bates","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2017,9,19]]},"reference":[{"key":"11630_CR1","doi-asserted-by":"publisher","first-page":"25748","DOI":"10.1074\/jbc.M111871200","volume":"277","author":"L Gao","year":"2002","unstructured":"Gao, L., Cueto, M. A., Asselbergs, F. & Atadja, P. Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family. J Biol. Chem. \n                           277, 25748\u201325755, https:\/\/doi.org\/10.1074\/jbc.M111871200 (2002).","journal-title":"J Biol. Chem."},{"key":"11630_CR2","doi-asserted-by":"publisher","first-page":"5036","DOI":"10.1093\/nar\/gkf660","volume":"30","author":"R Pandey","year":"2002","unstructured":"Pandey, R. et al. Analysis of histone acetyltransferase and histone deacetylase families of Arabidopsis thaliana suggests functional diversification of chromatin modification among multicellular eukaryotes. Nucleic Acids Res. \n                           30, 5036\u20135055, https:\/\/doi.org\/10.1093\/nar\/gkf660 (2002).","journal-title":"Nucleic Acids Res."},{"key":"11630_CR3","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1016\/j.jmb.2004.02.006","volume":"338","author":"IV Gregoretti","year":"2004","unstructured":"Gregoretti, I. V., Lee, Y. M. & Goodson, H. V. Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis. J. Mol. Biol. \n                           338, 17\u201331, https:\/\/doi.org\/10.1016\/j.jmb.2004.02.006 (2004).","journal-title":"J. Mol. Biol."},{"key":"11630_CR4","doi-asserted-by":"publisher","first-page":"206","DOI":"10.1038\/nrm2346","volume":"9","author":"XJ Yang","year":"2008","unstructured":"Yang, X. J. & Seto, E. The Rpd3\/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men. Nat. Rev. Mol. Cell Biol. \n                           9, 206\u2013218, https:\/\/doi.org\/10.1038\/nrm2346 (2008).","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"11630_CR5","doi-asserted-by":"publisher","first-page":"759","DOI":"10.1158\/1535-7163.MCT-07-2026","volume":"7","author":"M Fournel","year":"2008","unstructured":"Fournel, M. et al. MGCD0103, a novel isotype-selective histone deacetylase inhibitor, has broad spectrum antitumor activity in vitro and in vivo. Mol. Cancer Ther. \n                           7, 759\u2013768, https:\/\/doi.org\/10.1158\/1535-7163.MCT-07-2026 (2008).","journal-title":"Mol. Cancer Ther."},{"key":"11630_CR6","doi-asserted-by":"publisher","first-page":"6841","DOI":"10.1158\/1078-0432.CCR-09-0547","volume":"15","author":"J Arts","year":"2009","unstructured":"Arts, J. et al. JNJ-26481585, a novel \u201csecond-generation\u201d oral histone deacetylase inhibitor, shows broad-spectrum preclinical antitumoral activity. Clin. Cancer Res. \n                           15, 6841\u20136851, https:\/\/doi.org\/10.1158\/1078-0432.CCR-09-0547 (2009).","journal-title":"Clin. Cancer Res."},{"key":"11630_CR7","doi-asserted-by":"publisher","unstructured":"Tian, Y. et al. A sub-milligram-synthesis protocol for in vitro screening of HDAC11 inhibitors. Bioorg. Med. Chem. Lett., https:\/\/doi.org\/10.1016\/j.bmcl.2016.03.116 (2016).","DOI":"10.1016\/j.bmcl.2016.03.116"},{"key":"11630_CR8","doi-asserted-by":"publisher","first-page":"47","DOI":"10.1007\/BF02686117","volume":"31","author":"RS Broide","year":"2007","unstructured":"Broide, R. S. et al. Distribution of histone deacetylases 1\u201311 in the rat brain. J. Mol. Neurosci. \n                           31, 47\u201358, https:\/\/doi.org\/10.1007\/BF02686117 (2007).","journal-title":"J. Mol. Neurosci."},{"key":"11630_CR9","doi-asserted-by":"publisher","unstructured":"Liu, H., Hu, Q., Kaufman, A., D\u2019Ercole, A. J. & Ye, P. Developmental expression of histone deacetylase 11 in the murine brain. J. Neurosci. Res. 86, 537\u2013543, https:\/\/doi.org\/10.1002\/jnr.21521 (2008).","DOI":"10.1002\/jnr.21521"},{"key":"11630_CR10","doi-asserted-by":"publisher","unstructured":"Liu, H., Hu, Q., D\u2019Ercole A. J. & Ye, P. Histone deacetylase 11 regulates oligodendrocyte-specific gene expression and cell development in OL-1 oligodendroglia cells. Glia \n                           57, 1\u201312, https:\/\/doi.org\/10.1002\/glia.20729 (2009).","DOI":"10.1002\/glia.20729"},{"key":"11630_CR11","doi-asserted-by":"publisher","first-page":"159","DOI":"10.1055\/s-0032-1321789","volume":"45","author":"A Androutsellis-Theotokis","year":"2013","unstructured":"Androutsellis-Theotokis, A., Chrousos, G. P., McKay, R. D., DeCherney, A. H. & Kino, T. Expression profiles of the nuclear receptors and their transcriptional coregulators during differentiation of neural stem cells. Horm. Metab. Res. \n                           45, 159\u2013168, https:\/\/doi.org\/10.1055\/s-0032-1321789 (2013).","journal-title":"Horm. Metab. Res."},{"key":"11630_CR12","doi-asserted-by":"publisher","first-page":"3433","DOI":"10.4161\/cc.26433","volume":"12","author":"TK Bagui","year":"2013","unstructured":"Bagui, T. K., Sharma, S. S., Ma, L. & Pledger, W. J. Proliferative status regulates HDAC11 mRNA abundance in nontransformed fibroblasts. Cell Cycle \n                           12, 3433\u20133441, https:\/\/doi.org\/10.4161\/cc.26433 (2013).","journal-title":"Cell Cycle"},{"key":"11630_CR13","doi-asserted-by":"publisher","first-page":"296","DOI":"10.1111\/j.1601-183X.2009.00473.x","volume":"8","author":"GD Rosen","year":"2009","unstructured":"Rosen, G. D. et al. Genetic modulation of striatal volume by loci on Chrs 6 and 17 in BXD recombinant inbred mice. Genes Brain Behav. \n                           8, 296\u2013308, https:\/\/doi.org\/10.1111\/j.1601-183X.2009.00473.x (2009).","journal-title":"Genes Brain Behav."},{"key":"11630_CR14","doi-asserted-by":"publisher","DOI":"10.1186\/1471-2202-10-44","volume":"10","author":"SM Gaglani","year":"2009","unstructured":"Gaglani, S. M., Lu, L., Williams, R. W. & Rosen, G. D. The genetic control of neocortex volume and covariation with neocortical gene expression in mice. BMC Neurosci. \n                           10, 44, https:\/\/doi.org\/10.1186\/1471-2202-10-44 (2009).","journal-title":"BMC Neurosci."},{"key":"11630_CR15","doi-asserted-by":"publisher","first-page":"238","DOI":"10.1016\/j.neurobiolaging.2012.07.007","volume":"34","author":"B Inkster","year":"2013","unstructured":"Inkster, B. et al. Histone deacetylase gene variants predict brain volume changes in multiple sclerosis. Neurobiol. Aging \n                           34, 238\u2013247, https:\/\/doi.org\/10.1016\/j.neurobiolaging.2012.07.007 (2013).","journal-title":"Neurobiol. Aging"},{"key":"11630_CR16","doi-asserted-by":"publisher","first-page":"589","DOI":"10.3892\/ijmm.16.4.589","volume":"16","author":"S Voelter-Mahlknecht","year":"2005","unstructured":"Voelter-Mahlknecht, S., Ho, A. D. & Mahlknecht, U. Chromosomal organization and localization of the novel class IV human histone deacetylase 11 gene. Int. J. Mol. Med. \n                           16, 589\u2013598, https:\/\/doi.org\/10.3892\/ijmm.16.4.589 (2005).","journal-title":"Int. J. Mol. Med."},{"key":"11630_CR17","doi-asserted-by":"publisher","first-page":"5788","DOI":"10.1158\/1078-0432.CCR-13-1217","volume":"19","author":"W Dai","year":"2013","unstructured":"Dai, W. et al. Promoter CpG island methylation of genes in key cancer pathways associates with clinical outcome in high-grade serous ovarian cancer. Clin. Cancer Res. \n                           19, 5788\u20135797, https:\/\/doi.org\/10.1158\/1078-0432.CCR-13-1217 (2013).","journal-title":"Clin. Cancer Res."},{"key":"11630_CR18","doi-asserted-by":"publisher","first-page":"1200","DOI":"10.1016\/j.leukres.2013.07.016","volume":"37","author":"B Gruhn","year":"2013","unstructured":"Gruhn, B. et al. The expression of histone deacetylase 4 is associated with prednisone poor-response in childhood acute lymphoblastic leukemia. Leuk. Res. \n                           37, 1200\u20131207, https:\/\/doi.org\/10.1016\/j.leukres.2013.07.016 (2013).","journal-title":"Leuk. Res."},{"key":"11630_CR19","doi-asserted-by":"publisher","first-page":"123","DOI":"10.3109\/10428194.2011.597905","volume":"53","author":"V Skov","year":"2012","unstructured":"Skov, V. et al. Increased gene expression of histone deacetylases in patients with Philadelphia-negative chronic myeloproliferative neoplasms. Leuk. Lymphoma \n                           53, 123\u2013129, https:\/\/doi.org\/10.3109\/10428194.2011.597905 (2012).","journal-title":"Leuk. Lymphoma"},{"key":"11630_CR20","doi-asserted-by":"publisher","first-page":"2200","DOI":"10.1002\/ijc.27876","volume":"132","author":"HE Deubzer","year":"2013","unstructured":"Deubzer, H. E. et al. HDAC11 is a novel drug target in carcinomas. Int. J. Cancer \n                           132, 2200\u20132208, https:\/\/doi.org\/10.1002\/ijc.27876 (2013).","journal-title":"Int. J. Cancer"},{"key":"11630_CR21","doi-asserted-by":"publisher","DOI":"10.1038\/cddis.2017.49","volume":"8","author":"TM Thole","year":"2017","unstructured":"Thole, T. M. et al. Neuroblastoma cells depend on HDAC11 for mitotic cell cycle progression and survival. Cell Death Dis. \n                           8, e2635, https:\/\/doi.org\/10.1038\/cddis.2017.49 (2017).","journal-title":"Cell Death Dis."},{"key":"11630_CR22","doi-asserted-by":"publisher","first-page":"4351","DOI":"10.4161\/cc.9.21.13596","volume":"9","author":"PG Wong","year":"2010","unstructured":"Wong, P. G. et al. Chromatin unfolding by Cdt1 regulates MCM loading via opposing functions of HBO1 and HDAC11-geminin. Cell Cycle \n                           9, 4351\u20134363, https:\/\/doi.org\/10.4161\/cc.9.21.13596 (2010).","journal-title":"Cell Cycle"},{"key":"11630_CR23","doi-asserted-by":"publisher","first-page":"11446","DOI":"10.1074\/jbc.M809394200","volume":"284","author":"MA Glozak","year":"2009","unstructured":"Glozak, M. A. & Seto, E. Acetylation\/deacetylation modulates the stability of DNA replication licensing factor Cdt1. J Biol. Chem. \n                           284, 11446\u201311453, https:\/\/doi.org\/10.1074\/jbc.M809394200 (2009).","journal-title":"J Biol. Chem."},{"key":"11630_CR24","doi-asserted-by":"publisher","first-page":"92","DOI":"10.1038\/ni.1673","volume":"10","author":"A Villagra","year":"2009","unstructured":"Villagra, A. et al. The histone deacetylase HDAC11 regulates the expression of interleukin 10 and immune tolerance. Nat. Immunol. \n                           10, 92\u2013100, https:\/\/doi.org\/10.1038\/ni.1673 (2009).","journal-title":"Nat. Immunol."},{"key":"11630_CR25","doi-asserted-by":"publisher","first-page":"44","DOI":"10.1016\/j.molimm.2014.02.019","volume":"60","author":"F Cheng","year":"2014","unstructured":"Cheng, F. et al. Divergent roles of histone deacetylase 6 (HDAC6) and histone deacetylase 11 (HDAC11) on the transcriptional regulation of IL10 in antigen presenting cells. Mol. Immunol. \n                           60, 44\u201353, https:\/\/doi.org\/10.1016\/j.molimm.2014.02.019 (2014).","journal-title":"Mol. Immunol."},{"key":"11630_CR26","doi-asserted-by":"publisher","first-page":"552","DOI":"10.1016\/j.celrep.2014.03.022","volume":"7","author":"Y Watanabe","year":"2014","unstructured":"Watanabe, Y., Khodosevich, K. & Monyer, H. Dendrite development regulated by the schizophrenia-associated gene FEZ1 involves the ubiquitin proteasome system. Cell Rep. \n                           7, 552\u2013564, https:\/\/doi.org\/10.1016\/j.celrep.2014.03.022 (2014).","journal-title":"Cell Rep."},{"key":"11630_CR27","doi-asserted-by":"publisher","first-page":"1625","DOI":"10.1101\/gad.1809209","volume":"23","author":"M Haberland","year":"2009","unstructured":"Haberland, M., Mokalled, M. H., Montgomery, R. L. & Olson, E. N. Epigenetic control of skull morphogenesis by histone deacetylase 8. Genes Dev. \n                           23, 1625\u20131630, https:\/\/doi.org\/10.1101\/gad.1809209 (2009).","journal-title":"Genes Dev."},{"key":"11630_CR28","doi-asserted-by":"publisher","first-page":"32","DOI":"10.1038\/nrg2485","volume":"10","author":"M Haberland","year":"2009","unstructured":"Haberland, M., Montgomery, R. L. & Olson, E. N. The many roles of histone deacetylases in development and physiology: implications for disease and therapy. Nat. Rev. Genet. \n                           10, 32\u201342, https:\/\/doi.org\/10.1038\/nrg2485 (2009).","journal-title":"Nat. Rev. Genet."},{"key":"11630_CR29","doi-asserted-by":"publisher","unstructured":"Takase, K., Oda, S., Kuroda, M. & Funato, H. Monoaminergic and Neuropeptidergic Neurons Have Distinct Expression Profiles of Histone Deacetylases. PLoS One \n                           8, https:\/\/doi.org\/10.1371\/journal.pone.0058473 (2013).","DOI":"10.1371\/journal.pone.0058473"},{"key":"11630_CR30","doi-asserted-by":"publisher","first-page":"555","DOI":"10.1016\/j.cell.2004.10.024","volume":"119","author":"RB Vega","year":"2004","unstructured":"Vega, R. B. et al. Histone deacetylase 4 controls chondrocyte hypertrophy during skeletogenesis. Cell \n                           119, 555\u2013566, https:\/\/doi.org\/10.1016\/j.cell.2004.10.024 (2004).","journal-title":"Cell"},{"key":"11630_CR31","doi-asserted-by":"publisher","first-page":"321","DOI":"10.1016\/j.cell.2006.05.040","volume":"126","author":"S Chang","year":"2006","unstructured":"Chang, S. et al. Histone deacetylase 7 maintains vascular integrity by repressing matrix metalloproteinase 10. Cell \n                           126, 321\u2013334, https:\/\/doi.org\/10.1016\/j.cell.2006.05.040 (2006).","journal-title":"Cell"},{"key":"11630_CR32","doi-asserted-by":"publisher","first-page":"8467","DOI":"10.1128\/MCB.24.19.8467-8476.2004","volume":"24","author":"S Chang","year":"2004","unstructured":"Chang, S. et al. Histone deacetylases 5 and 9 govern responsiveness of the heart to a subset of stress signals and play redundant roles in heart development. Mol. Cell Biol. \n                           24, 8467\u20138476, https:\/\/doi.org\/10.1128\/MCB.24.19.8467-8476.2004 (2004).","journal-title":"Mol. Cell Biol."},{"key":"11630_CR33","doi-asserted-by":"publisher","first-page":"1688","DOI":"10.1128\/MCB.01154-06","volume":"28","author":"Y Zhang","year":"2008","unstructured":"Zhang, Y. et al. Mice lacking histone deacetylase 6 have hyperacetylated tubulin but are viable and develop normally. Mol. Cell Biol. \n                           28, 1688\u20131701, https:\/\/doi.org\/10.1128\/MCB.01154-06 (2008).","journal-title":"Mol. Cell Biol."},{"key":"11630_CR34","doi-asserted-by":"publisher","first-page":"479","DOI":"10.1016\/S0092-8674(02)00861-9","volume":"110","author":"CL Zhang","year":"2002","unstructured":"Zhang, C. L. et al. Class II histone deacetylases act as signal-responsive repressors of cardiac hypertrophy. Cell \n                           110, 479\u2013488, https:\/\/doi.org\/10.1016\/S0092-8674(02)00861-9 (2002).","journal-title":"Cell"},{"key":"11630_CR35","doi-asserted-by":"publisher","first-page":"322","DOI":"10.1016\/j.cell.2008.11.050","volume":"136","author":"AH Kim","year":"2009","unstructured":"Kim, A. H. et al. A centrosomal Cdc20-APC pathway controls dendrite morphogenesis in postmitotic neurons. Cell \n                           136, 322\u2013336, https:\/\/doi.org\/10.1016\/j.cell.2008.11.050 (2009).","journal-title":"Cell"},{"key":"11630_CR36","doi-asserted-by":"publisher","first-page":"559","DOI":"10.1016\/j.neuron.2011.09.032","volume":"72","author":"E Kang","year":"2011","unstructured":"Kang, E. et al. Interaction between FEZ1 and DISC1 in regulation of neuronal development and risk for schizophrenia. Neuron \n                           72, 559\u2013571, https:\/\/doi.org\/10.1016\/j.neuron.2011.09.032 (2011).","journal-title":"Neuron"},{"key":"11630_CR37","doi-asserted-by":"publisher","first-page":"1245","DOI":"10.1093\/hmg\/ddl040","volume":"15","author":"BK Lipska","year":"2006","unstructured":"Lipska, B. K. et al. Expression of DISC1 binding partners is reduced in schizophrenia and associated with DISC1 SNPs. Hum. Mol. Genet. \n                           15, 1245\u20131258, https:\/\/doi.org\/10.1093\/hmg\/ddl040 (2006).","journal-title":"Hum. Mol. Genet."},{"key":"11630_CR38","doi-asserted-by":"publisher","first-page":"550","DOI":"10.1001\/archgenpsychiatry.2011.1882","volume":"69","author":"G Sheng","year":"2012","unstructured":"Sheng, G., Demers, M., Subburaju, S. & Benes, F. M. Differences in the circuitry-based association of copy numbers and gene expression between the hippocampi of patients with schizophrenia and the hippocampi of patients with bipolar disorder. Arch. Gen. Psychiatry \n                           69, 550\u2013561, https:\/\/doi.org\/10.1001\/archgenpsychiatry.2011.1882 (2012).","journal-title":"Arch. Gen. Psychiatry"},{"key":"11630_CR39","doi-asserted-by":"publisher","first-page":"97","DOI":"10.1016\/j.schres.2014.09.029","volume":"160","author":"O Kebir","year":"2014","unstructured":"Kebir, O. et al. Family-based association study of common variants, rare mutation study and epistatic interaction detection in HDAC genes in schizophrenia. Schizophr. Res. \n                           160, 97\u2013103, https:\/\/doi.org\/10.1016\/j.schres.2014.09.029 (2014).","journal-title":"Schizophr. Res."},{"key":"11630_CR40","doi-asserted-by":"publisher","first-page":"1491","DOI":"10.4155\/fmc.13.141","volume":"5","author":"M Weiwer","year":"2013","unstructured":"Weiwer, M., Lewis, M. C., Wagner, F. F. & Holson, E. B. Therapeutic potential of isoform selective HDAC inhibitors for the treatment of schizophrenia. Future Med. Chem. \n                           5, 1491\u20131508, https:\/\/doi.org\/10.4155\/fmc.13.141 (2013).","journal-title":"Future Med. Chem."},{"key":"11630_CR41","doi-asserted-by":"publisher","first-page":"1162","DOI":"10.1111\/j.1476-5381.2011.01386.x","volume":"164","author":"CA Jones","year":"2011","unstructured":"Jones, C. A., Watson, D. J. & Fone, K. C. Animal models of schizophrenia. Br. J. Pharmacol. \n                           164, 1162\u20131194, https:\/\/doi.org\/10.1111\/j.1476-5381.2011.01386.x (2011).","journal-title":"Br. J. Pharmacol."},{"key":"11630_CR42","doi-asserted-by":"publisher","first-page":"3191","DOI":"10.1093\/hmg\/ddn215","volume":"17","author":"N Sakae","year":"2008","unstructured":"Sakae, N. et al. Mice lacking the schizophrenia-associated protein FEZ1 manifest hyperactivity and enhanced responsiveness to psychostimulants. Hum. Mol. Genet. \n                           17, 3191\u20133203, https:\/\/doi.org\/10.1093\/hmg\/ddn215 (2008).","journal-title":"Hum. Mol. Genet."},{"key":"11630_CR43","doi-asserted-by":"publisher","first-page":"72","DOI":"10.1038\/mp.2014.148","volume":"20","author":"DH Kavanagh","year":"2015","unstructured":"Kavanagh, D. H., Tansey, K. E., O\u2019Donovan, M. C. & Owen, M. J. Schizophrenia genetics: emerging themes for a complex disorder. Mol. Psychiatry \n                           20, 72\u201376, https:\/\/doi.org\/10.1038\/mp.2014.148 (2015).","journal-title":"Mol. Psychiatry"},{"key":"11630_CR44","doi-asserted-by":"publisher","first-page":"222","DOI":"10.1177\/0269881109348173","volume":"25","author":"L Host","year":"2011","unstructured":"Host, L., Dietrich, J. B., Carouge, D., Aunis, D. & Zwiller, J. Cocaine self-administration alters the expression of chromatin-remodelling proteins; modulation by histone deacetylase inhibition. J. Psychopharmacol. \n                           25, 222\u2013229, https:\/\/doi.org\/10.1177\/0269881109348173 (2011).","journal-title":"J. Psychopharmacol."},{"key":"11630_CR45","doi-asserted-by":"publisher","first-page":"1865","DOI":"10.1111\/acer.12465","volume":"38","author":"A Finegersh","year":"2014","unstructured":"Finegersh, A. & Homanics, G. E. Acute ethanol alters multiple histone modifications at model gene promoters in the cerebral cortex. Alcohol Clin. Exp. Res. \n                           38, 1865\u20131873, https:\/\/doi.org\/10.1111\/acer.12465 (2014).","journal-title":"Alcohol Clin. Exp. Res."},{"key":"11630_CR46","doi-asserted-by":"publisher","first-page":"178","DOI":"10.1016\/j.neuro.2014.10.008","volume":"45","author":"O Omonijo","year":"2014","unstructured":"Omonijo, O. et al. Differential effects of binge methamphetamine injections on the mRNA expression of histone deacetylases (HDACs) in the rat striatum. Neurotoxicology \n                           45, 178\u2013184, https:\/\/doi.org\/10.1016\/j.neuro.2014.10.008 (2014).","journal-title":"Neurotoxicology"},{"key":"11630_CR47","doi-asserted-by":"publisher","unstructured":"Torres, O. V. et al. An Acute Methamphetamine Injection Downregulates the Expression of Several Histone Deacetylases (HDACs) in the Mouse Nucleus Accumbens: Potential Regulatory Role of HDAC2 Expression. Neurotox. Res., https:\/\/doi.org\/10.1007\/s12640-015-9591-3 (2015).","DOI":"10.1007\/s12640-015-9591-3"},{"key":"11630_CR48","doi-asserted-by":"publisher","unstructured":"Conti, L. et al. Niche-independent symmetrical self-renewal of a mammalian tissue stem cell. Plos Biol. 3, 1594\u20131606, https:\/\/doi.org\/10.1371\/journal.pbio.0030283 (2005).","DOI":"10.1371\/journal.pbio.0030283"},{"key":"11630_CR49","doi-asserted-by":"publisher","first-page":"935","DOI":"10.1038\/nprot.2008.55","volume":"3","author":"A Chojnacki","year":"2008","unstructured":"Chojnacki, A. & Weiss, S. Production of neurons, astrocytes and oligodendrocytes from mammalian CNS stem cells. Nat. Protoc. \n                           3, 935\u2013940, https:\/\/doi.org\/10.1038\/nprot.2008.55 (2008).","journal-title":"Nat. Protoc."},{"key":"11630_CR50","doi-asserted-by":"publisher","unstructured":"Benn, C. L., Fox, H. & Bates, G. P. Optimisation of region-specific reference gene selection and relative gene expression analysis methods for pre-clinical trials of Huntington\u2019s disease. Mol. Neurodegener. 3, https:\/\/doi.org\/10.1186\/1750-1326-3-17 (2008).","DOI":"10.1186\/1750-1326-3-17"},{"key":"11630_CR51","doi-asserted-by":"publisher","first-page":"687","DOI":"10.1016\/S0076-6879(99)09045-X","volume":"309","author":"SW Davies","year":"1999","unstructured":"Davies, S. W. et al. Detection of polyglutamine aggregation in mouse models. Methods Enzymol. \n                           309, 687\u2013701, https:\/\/doi.org\/10.1016\/S0076-6879(99)09045-X (1999).","journal-title":"Methods Enzymol."},{"key":"11630_CR52","doi-asserted-by":"publisher","first-page":"459","DOI":"10.3233\/JHD-130080","volume":"2","author":"A Valencia","year":"2013","unstructured":"Valencia, A. et al. Striatal synaptosomes from Hdh140Q\/140Q knock-in mice have altered protein levels, novel sites of methionine oxidation, and excess glutamate release after stimulation. J. Huntingtons Dis. \n                           2, 459\u2013475, https:\/\/doi.org\/10.3233\/JHD-130080 (2013).","journal-title":"J. Huntingtons Dis."},{"key":"11630_CR53","doi-asserted-by":"publisher","first-page":"8808","DOI":"10.1074\/jbc.M109.075028","volume":"285","author":"C Landles","year":"2010","unstructured":"Landles, C. et al. Proteolysis of Mutant Huntingtin Produces an Exon 1 Fragment That Accumulates as an Aggregated Protein in Neuronal Nuclei in Huntington Disease. J. Biol. Chem. \n                           285, 8808\u20138823, https:\/\/doi.org\/10.1074\/jbc.M109.075028 (2010).","journal-title":"J. Biol. Chem."}],"container-title":["Scientific Reports"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41598-017-11630-1.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41598-017-11630-1","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41598-017-11630-1.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,12,23]],"date-time":"2022-12-23T06:08:55Z","timestamp":1671775735000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41598-017-11630-1"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,9,19]]},"references-count":53,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2017,12]]}},"alternative-id":["11630"],"URL":"https:\/\/doi.org\/10.1038\/s41598-017-11630-1","relation":{},"ISSN":["2045-2322"],"issn-type":[{"value":"2045-2322","type":"electronic"}],"subject":[],"published":{"date-parts":[[2017,9,19]]},"assertion":[{"value":"17 February 2017","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"25 August 2017","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"19 September 2017","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"J.K.D. and C.L.B. were employees of Neusentis, Pfizer Ltd. and T.R. is an employee of Merck & Co. All other authors declare no competing financial interests.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing Interests"}}],"article-number":"11900"}}