[1] Esclatine A, Chaumorcel M, Codogno P. Macroautophagy signaling and regulation. Curr Top Microbiol Immunol, 2009, 335: 33–70. <\p>
[2] Klionsky DJ. The molecular machinery of autophagy: un-answered questions. J Cell Sci, 2005, 118(Pt 1): 7–18. <\p>
[3] Walsh CM, Edinger AL. The complex interplay between autophagy, apoptosis, and necrotic signals promotes T-cell homeostasis. Immunol Rev, 2010, 236(1): 95–109. <\p>
[4] Tschan MP, Simon HU. The role of autophagy in antican-cer therapy: promises and uncertainties. J Intern Med, 2010, 268(5): 410–418. <\p>
[5] Zhuang W, Qin Z, Liang Z. The role of autophagy in sen-sitizing malignant glioma cells to radiation therapy. Acta Biochim Biophys Sin (Shanghai), 2009, 41(5): 341–351. <\p>
[6] Levine B, Yuan J. Autophagy in cell death: an innocent convict? J Clin Invest, 2005, 115(10): 2679–2688. <\p>
[7] Chen Y, Klionsky DJ. The regulation of autophagy-unanswered questions. J Cell Sci, 2011, 124(Pt 2): 161–170. <\p>
[8] Torres-Padilla ME, Parfitt DE, Kouzarides T, Zernicka- Goetz M. Histone arginine methylation regulates pluripotency in the early mouse embryo. Nature, 2007, 445(7124): 214– 218. <\p>
[9] Fraga MF, Ballestar E, Villar-Garea A, Boix-Chornet M, Espada J, Schotta G, Bonaldi T, Haydon C, Ropero S, Petrie K, Iyer NG, Pérez-Rosado A, Calvo E, Lopez JA, Cano A, Calasanz MJ, Colomer D, Piris MA, Ahn N, Im-hof A, Caldas C, Jenuwein T, Esteller M. Loss of acetyla-tion at Lys16 and trimethylation at Lys20 of histone H4 is a common hallmark of human cancer. Nat Genet, 2005, 37(4): 391–400. <\p>
[10] Füllgrabe J, Lynch-Day MA, Heldring N, Li WB, Struijk RB, Ma Q, Hermanson O, Rosenfeld MG, Klionsky DJ, Joseph B. The histone H4 lysine 16 acetyltransferase hMOF regulates the outcome of autophagy. Nature, 2013, 500(7463): 468–471. <\p>
[11] Carrozza MJ, Utley RT, Workman JL, Côté J. The diverse functions of histone acetyltransferase complexes. Trends Genet, 2003, 19(6): 321–329. <\p>
[12] Yan Y, Barlev NA, Haley RH, Berger SL, Marmorstein R. Crystal structure of yeast Esa1 suggests a unified mecha-nism for catalysis and substrate binding by histone acetyltransferases. Mol Cell, 2000, 6(5): 1195–1205. <\p>
[13] Yan Y, Harper S, Speicher DW, Marmorstein R. The cata-lytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediate. Nat Struct Biol, 2002, 9(11): 862–869. <\p>
[14] Roth SY, Denu JM, Allis CD. Histone acetyltransferases. Annu Rev Biochem, 2001, 70: 81–120. <\p>
[15] Utley RT, Côté J. The MYST family of histone acetyltransferases. Curr Top Microbiol Immunol, 2003, 274: 203–236. <\p>
[16] Akhtar A, Becker PB. The histone H4 acetyltransferase MOF uses a C2HC zinc finger for substrate recognition. EMBO Rep, 2001, 2(2): 113–118. <\p>
[17] Bone JR, Lavender J, Richman R, Palmer MJ, Turner BM, Kuroda MI. Acetylated histone H4 on the male X chromo-some is associated with dosage compensation in Droso-phila. Genes Dev, 1994, 8(1): 96–104. <\p>
[18] Smith ER, Pannuti A, Gu WG, Steurnagel A, Cook RG, Allis CD, Lucchesi JC. The drosophila MSL complex ac-etylates histone H4 at lysine 16, a chromatin modification linked to dosage compensation. Mol Cell Biol, 2000, 20(1): 312–318. <\p>
[19] Akhtar A, Zink D, Becker PB. Chromodomains are pro-tein-RNA interaction modules. Nature, 2000, 407(6802): 405–409. <\p>
[20] Buscaino A, Köcher T, Kind JH, Holz H, Taipale M, Wagner K, Wilm M, Akhtar A. MOF-regulated acetylation of MSL-3 in the Drosophila dosage compensation com-plex. Mol Cell, 2003, 11(5): 1265–1277. <\p>
[21] Morales V, Str |