Cassidy, S.B. & Driscoll, D.J. Prader–Willi syndrome. Eur. J. Hum. Genet. 17, 3–13 (2009).
Buiting, K. Prader-Willi syndrome and Angelman syndrome. Am. J. Med. Genet. C. Semin. Med. Genet. 154C, 365–376 (2010).
Sahoo, T. et al. Prader-Willi phenotype caused by paternal deficiency for the HBII-85 C/D box small nucleolar RNA cluster. Nat. Genet. 40, 719–721 (2008).
de Smith, A.J. et al. A deletion of the HBII-85 class of small nucleolar RNAs (snoRNAs) is associated with hyperphagia, obesity and hypogonadism. Hum. Mol. Genet. 18, 3257–3265 (2009).
Duker, A.L. et al. Paternally inherited microdeletion at 15q11.2 confirms a significant role for the SNORD116 C/D box snoRNA cluster in Prader-Willi syndrome. Eur. J. Hum. Genet. 18, 1196–1201 (2010).
Bieth, E. et al. Highly restricted deletion of the SNORD116 region is implicated in Prader-Willi Syndrome. Eur. J. Hum. Genet. 23, 252–255 (2015).
Buiting, K. et al. Clinical phenotypes of MAGEL2 mutations and deletions. Orphanet J. Rare Dis. 9, 40 (2014).
Schaaf, C.P. et al. Truncating mutations of MAGEL2 cause Prader-Willi phenotypes and autism. Nat. Genet. 45, 1405–1408 (2013).
Kanber, D. et al. A paternal deletion of MKRN3, MAGEL2 and NDN does not result in Prader-Willi syndrome. Eur. J. Hum. Genet. 17, 582–590 (2009).
Runte, M. et al. The IC-SNURF-SNRPN transcript serves as a host for multiple small nucleolar RNA species and as an antisense RNA for UBE3A. Hum. Mol. Genet. 10, 2687–2700 (2001).
de los Santos, T., Schweizer, J., Rees, C.A. & Francke, U. Small evolutionarily conserved RNA, resembling C/D box small nucleolar RNA, is transcribed from PWCR1, a novel imprinted gene in the Prader-Willi deletion region, which Is highly expressed in brain. Am. J. Hum. Genet. 67, 1067–1082 (2000).
Gallagher, R.C., Pils, B., Albalwi, M. & Francke, U. Evidence for the role of PWCR1/HBII-85 C/D box small nucleolar RNAs in Prader-Willi syndrome. Am. J. Hum. Genet. 71, 669–678 (2002).
Saitoh, S. et al. Minimal definition of the imprinting center and fixation of chromosome 15q11-q13 epigenotype by imprinting mutations. Proc. Natl. Acad. Sci. USA 93, 7811–7815 (1996).
Fulmer-Smentek, S.B. & Francke, U. Association of acetylated histones with paternally expressed genes in the Prader–Willi deletion region. Hum. Mol. Genet. 10, 645–652 (2001).
Xin, Z., Allis, C.D. & Wagstaff, J. Parent-specific complementary patterns of histone H3 lysine 9 and H3 lysine 4 methylation at the Prader-Willi syndrome imprinting center. Am. J. Hum. Genet. 69, 1389–1394 (2001).
Saitoh, S. & Wada, T. Parent-of-origin specific histone acetylation and reactivation of a key imprinted gene locus in Prader-Willi syndrome. Am. J. Hum. Genet. 66, 1958–1962 (2000).
Xin, Z. et al. Role of histone methyltransferase G9a in CpG methylation of the Prader-Willi syndrome imprinting center. J. Biol. Chem. 278, 14996–15000 (2003).
Auclair, G. et al. EHMT2 directs DNA methylation for efficient gene silencing in mouse embryos. Genome Res. 26, 192–202 (2016).
Sutcliffe, J.S. et al. Deletions of a differentially methylated CpG island at the SNRPN gene define a putative imprinting control region. Nat. Genet. 8, 52–58 (1994).
Le Meur, E. et al. Dynamic developmental regulation of the large non-coding RNA associated with the mouse 7C imprinted chromosomal region. Dev. Biol. 286, 587–600 (2005).
Wu, M.Y., Tsai, T.F. & Beaudet, A.L. Deficiency of Rbbp1/Arid4a and Rbbp1l1/Arid4b alters epigenetic modifications and suppresses an imprinting defect in the PWS/AS domain. Genes Dev. 20, 2859–2870 (2006).
Huang, H.S. et al. Topoisomerase inhibitors unsilence the dormant allele of Ube3a in neurons. Nature 481, 185–189 (2011).
Vedadi, M. et al. A chemical probe selectively inhibits G9a and GLP methyltransferase activity in cells. Nat. Chem. Biol. 7, 566–574 (2011).
Liu, F. et al. Discovery of an in vivo chemical probe of the lysine methyltransferases G9a and GLP. J. Med. Chem. 56, 8931–8942 (2013).
Liu, F. et al. Optimization of cellular activity of G9a inhibitors 7-aminoalkoxy-quinazolines. J. Med. Chem. 54, 6139–6150 (2011).
Kubicek, S. et al. Reversal of H3K9me2 by a small-molecule inhibitor for the G9a histone methyltransferase. Mol. Cell 25, 473–481 (2007).
Leung, D.C. et al. Lysine methyltransferase G9a is required for de novo DNA methylation and the establishment, but not the maintenance, of proviral silencing. Proc. Natl. Acad. Sci. USA 108, 5718–5723 (2011).
Martins-Taylor, K. et al. Imprinted expression of UBE3A in non-neuronal cells from a Prader-Willi syndrome patient with an atypical deletion. Hum. Mol. Genet. 23, 2364–2373 (2014).
Boccaccio, I. et al. The human MAGEL2 gene and its mouse homologue are paternally expressed and mapped to the Prader-Willi region. Hum. Mol. Genet. 8, 2497–2505 (1999).
Chamberlain, S.J. et al. Induced pluripotent stem cell models of the genomic imprinting disorders Angelman and Prader-Willi syndromes. Proc. Natl. Acad. Sci. USA 107, 17668–17673 (2010).
Tsai, T.F., Jiang, Y.H., Bressler, J., Armstrong, D. & Beaudet, A.L. Paternal deletion from Snrpn to Ube3a in the mouse causes hypotonia, growth retardation and partial lethality and provides evidence for a gene contributing to Prader-Willi syndrome. Hum. Mol. Genet. 8, 1357–1364 (1999).
Chamberlain, S.J. & Brannan, C.I. The Prader-Willi syndrome imprinting center activates the paternally expressed murine Ube3a antisense transcript but represses paternal Ube3a. Genomics 73, 316–322 (2001).
Meng, L., Person, R.E. & Beaudet, A.L. Ube3a-ATS is an atypical RNA polymerase II transcript that represses the paternal expression of Ube3a. Hum. Mol. Genet. 21, 3001–3012 (2012).
Jiang, Y.H. et al. Mutation of the Angelman ubiquitin ligase in mice causes increased cytoplasmic p53 and deficits of contextual learning and long-term potentiation. Neuron 21, 799–811 (1998).
Epsztejn-Litman, S. et al. De novo DNA methylation promoted by G9a prevents reprogramming of embryonically silenced genes. Nat. Struct. Mol. Biol. 15, 1176–1183 (2008).
Tachibana, M., Matsumura, Y., Fukuda, M., Kimura, H. & Shinkai, Y. G9a/GLP complexes independently mediate H3K9 and DNA methylation to silence transcription. EMBO J. 27, 2681–2690 (2008).
Cruvinel, E. et al. Reactivation of maternal SNORD116 cluster via SETDB1 knockdown in Prader-Willi syndrome iPSCs. Hum. Mol. Genet. 23, 4674–4685 (2014).
Tachibana, M. et al. G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis. Genes Dev. 16, 1779–1791 (2002).
Yokochi, T. et al. G9a selectively represses a class of late-replicating genes at the nuclear periphery. Proc. Natl. Acad. Sci. USA 106, 19363–19368 (2009).
Shinkai, Y. & Tachibana, M. H3K9 methyltransferase G9a and the related molecule GLP. Genes Dev. 25, 781–788 (2011).
Collins, R.E. et al. The ankyrin repeats of G9a and GLP histone methyltransferases are mono- and dimethyllysine binding modules. Nat. Struct. Mol. Biol. 15, 245–250 (2008).
Collins, R. & Cheng, X. A case study in cross-talk: the histone lysine methyltransferases G9a and GLP. Nucleic Acids Res. 38, 3503–3511 (2010).
Bittencourt, D., Lee, B.H., Gao, L., Gerke, D.S. & Stallcup, M.R. Role of distinct surfaces of the G9a ankyrin repeat domain in histone and DNA methylation during embryonic stem cell self-renewal and differentiation. Epigenetics Chromatin 7, 27 (2014).
Pai, C.C. et al. A histone H3K36 chromatin switch coordinates DNA double-strand break repair pathway choice. Nat. Commun. 5, 4091 (2014).
Yamasaki, K. et al. Neurons but not glial cells show reciprocal imprinting of sense and antisense transcripts of Ube3a. Hum. Mol. Genet. 12, 837–847 (2003).
Galiveti, C.R., Raabe, C.A., Konthur, Z. & Rozhdestvensky, T.S. Differential regulation of non-protein coding RNAs from Prader-Willi Syndrome locus. Sci. Rep. 4, 6445 (2014).
Wen, B., Wu, H., Shinkai, Y., Irizarry, R.A. & Feinberg, A.P. Large histone H3 lysine 9 dimethylated chromatin blocks distinguish differentiated from embryonic stem cells. Nat. Genet. 41, 246–250 (2009).
Lu, X. et al. Chemical modification-assisted bisulfite sequencing (CAB-Seq) for 5-carboxylcytosine detection in DNA. J. Am. Chem. Soc. 135, 9315–9317 (2013).
Booth, M.J. et al. Oxidative bisulfite sequencing of 5-methylcytosine and 5-hydroxymethylcytosine. Nat. Protoc. 8, 1841–1851 (2013).
Huang, Y. et al. The behaviour of 5-hydroxymethylcytosine in bisulfite sequencing. PLoS One 5, e8888 (2010).
Garcia-Manero, G. et al. Randomized open-label phase II study of decitabine in patients with low- or intermediate-risk myelodysplastic syndromes. J. Clin. Oncol. 31, 2548–2553 (2013).
Treppendahl, M.B., Kristensen, L.S. & Grønbæk, K. Predicting response to epigenetic therapy. J. Clin. Invest. 124, 47–55 (2014).
Mackay, D.J. et al. A maternal hypomethylation syndrome presenting as transient neonatal diabetes mellitus. Hum. Genet. 120, 262–269 (2006).
Mackay, D.J. et al. Hypomethylation of multiple imprinted loci in individuals with transient neonatal diabetes is associated with mutations in ZFP57. Nat. Genet. 40, 949–951 (2008).
Carpenter, A.E. et al. CellProfiler: image analysis software for identifying and quantifying cell phenotypes. Genome Biol. 7, R100 (2006).
Wang, X., Xu, Q., Bey, A.L., Lee, Y. & Jiang, Y.H. Transcriptional and functional complexity of Shank3 provides a molecular framework to understand the phenotypic heterogeneity of SHANK3 causing autism and Shank3 mutant mice. Mol. Autism 5, 30 (2014).
Hatcher, J.P. et al. Development of SHIRPA to characterise the phenotype of gene-targeted mice. Behav. Brain Res. 125, 43–47 (2001).