References
1. Philipps DMP (1963) The presence of acetyl groups in histones. Biochem J 87:258–263
2. Allfrey VG, Faulkner R, Mirsky AE (1964) Acetylation and methylation of histones and their
possible role in the regulation of RNA synthesis. Proc Natl Acad Sci U S A 51:786–794
3. Gallwitz D, Sekeris CE (1969) The acetylation of histones of rat liver nuclei in vitro by acetylCoA. Z Physiol Chem 350:150–154
4. Inoue A, Fujimoto D (1969) Enzymatic deacetylation of histone. Biochem Biophys Res
Commun 36:146–150
5. He M, Han Z, Liu L et al (2018) Chemical biology approaches for investigating the functions
of lysine acetyltransferases. Angew Chem Int Ed 57:1162–1184
6. Harmel R, Fiedler D (2018) Features and regulation of non-enzymatic posttranslational
modifications. Nat Chem Biol 14:244–252
7. Pérez-Salvia M, Esteller M (2017) Bromodomain inhibitors and cancer therapy: from structures to applications. Epigenetics 12:323–339
8. Lyon K, Stasevich TJ (2017) Imaging translational and post-translational gene regulatory
dynamics in living cells with antibody-based probes. Trends Genet 33:322–335
9. Drazic A, Myklebust LM, Ree R et al (2016) The world of protein acetylation. Biochim
Biophys Acta 1864:1372–1401
10. Jiang H, Zhang X, Chen X et al (2018) Protein lipidation: occurrence, mechanisms, biological
functions, and enabling technologies. Chem Rev 118:919–988
11. Reid MA, Dai Z, Locasale JW (2017) The impact of cellular metabolism on chromatin
dynamics and epigenetics. Nat Cell Biol 19:1298–1306
12. Yoshida M, Kudo N, Kosono S et al (2017) Chemical and structural biology of protein lysine
deacetylases. Proc Jpn Acad Ser B 93:297–321
13. Seto E, Yoshida M (2014) Erasers of histone acetylation: the histone deacetylase enzymes.
Cold Spring Harb Perspect Biol 6:a018713
14. Bertrand P (2010) Inside HDAC with HDAC inhibitors. Eur J Med Chem 45:2095–2116
15. Micelli C, Rastelli G (2015) Histone deacetylases: structural determinants of inhibitor selectivity. Drug Discov Today 20:718–735
16. Roche J, Bertrand P (2016) Inside HDACs with more selective HDAC inhibitors. Eur J Med
Chem 121:451–483
17. Kutil Z, Novakova Z, Meleshin M et al (2018) Histone deacetylase 11 is a fatty-acid deacylase.
ACS Chem Biol 13:685–693
18. Di Giorgio E, Brancolini C (2016) Regulation of class IIa HDAC activities: it is not only
matter of subcellular localization. Epigenomics 8:251–269
19. Desravines DC, Serna Martin I, Schneider R et al (2017) Structural characterization of the
SMRT corepressor interacting with histone deacetylase. Sci Rep 7:3678
20. Hai Y, Christianson DW (2016) Histone deacetylase 6 structure and molecular basis of
catalysis and inhibition. Nat Chem Biol 12:741–747
21. Yanginlar C, Logie C (2018) HDAC11 is a regulator of diverse immune functions. Biochem
Biophys Acta 1861:54–59
22. Zwergel C, Stazi G, Valente S et al (2016) Histone deacetylase inhibitors: updated studies in
various epigenetic-related diseases. J Clin Epigenetics 2:1–7
23. Manal M, Chandrasekar MJN, Priya JG et al (2016) Inhibitors of histone deacetylase as
antitumor agents: a critical review. Bioorg Chem 67:18–42
24. Ganesan A (2018) Epigenetic drug discovery: a success story for cofactor interference. Philos
Trans R Soc B 373:20170069
25. Khan A, Singh P, Srivastava K (2018) Synthesis, nature and utility of universal iron chelator –
siderophore: a review. Microbiol Res 212:103–111
26. Codd R (2008) Traversing the coordination chemistry and chemical biology of hydroxamic
acids. Coord Chem Rev 252:1387–1408
22
A. Ganesan
1. Philipps DMP (1963) The presence of acetyl groups in histones. Biochem J 87:258–263
2. Allfrey VG, Faulkner R, Mirsky AE (1964) Acetylation and methylation of histones and their
possible role in the regulation of RNA synthesis. Proc Natl Acad Sci U S A 51:786–794
3. Gallwitz D, Sekeris CE (1969) The acetylation of histones of rat liver nuclei in vitro by acetylCoA. Z Physiol Chem 350:150–154
4. Inoue A, Fujimoto D (1969) Enzymatic deacetylation of histone. Biochem Biophys Res
Commun 36:146–150
5. He M, Han Z, Liu L et al (2018) Chemical biology approaches for investigating the functions
of lysine acetyltransferases. Angew Chem Int Ed 57:1162–1184
6. Harmel R, Fiedler D (2018) Features and regulation of non-enzymatic posttranslational
modifications. Nat Chem Biol 14:244–252
7. Pérez-Salvia M, Esteller M (2017) Bromodomain inhibitors and cancer therapy: from structures to applications. Epigenetics 12:323–339
8. Lyon K, Stasevich TJ (2017) Imaging translational and post-translational gene regulatory
dynamics in living cells with antibody-based probes. Trends Genet 33:322–335
9. Drazic A, Myklebust LM, Ree R et al (2016) The world of protein acetylation. Biochim
Biophys Acta 1864:1372–1401
10. Jiang H, Zhang X, Chen X et al (2018) Protein lipidation: occurrence, mechanisms, biological
functions, and enabling technologies. Chem Rev 118:919–988
11. Reid MA, Dai Z, Locasale JW (2017) The impact of cellular metabolism on chromatin
dynamics and epigenetics. Nat Cell Biol 19:1298–1306
12. Yoshida M, Kudo N, Kosono S et al (2017) Chemical and structural biology of protein lysine
deacetylases. Proc Jpn Acad Ser B 93:297–321
13. Seto E, Yoshida M (2014) Erasers of histone acetylation: the histone deacetylase enzymes.
Cold Spring Harb Perspect Biol 6:a018713
14. Bertrand P (2010) Inside HDAC with HDAC inhibitors. Eur J Med Chem 45:2095–2116
15. Micelli C, Rastelli G (2015) Histone deacetylases: structural determinants of inhibitor selectivity. Drug Discov Today 20:718–735
16. Roche J, Bertrand P (2016) Inside HDACs with more selective HDAC inhibitors. Eur J Med
Chem 121:451–483
17. Kutil Z, Novakova Z, Meleshin M et al (2018) Histone deacetylase 11 is a fatty-acid deacylase.
ACS Chem Biol 13:685–693
18. Di Giorgio E, Brancolini C (2016) Regulation of class IIa HDAC activities: it is not only
matter of subcellular localization. Epigenomics 8:251–269
19. Desravines DC, Serna Martin I, Schneider R et al (2017) Structural characterization of the
SMRT corepressor interacting with histone deacetylase. Sci Rep 7:3678
20. Hai Y, Christianson DW (2016) Histone deacetylase 6 structure and molecular basis of
catalysis and inhibition. Nat Chem Biol 12:741–747
21. Yanginlar C, Logie C (2018) HDAC11 is a regulator of diverse immune functions. Biochem
Biophys Acta 1861:54–59
22. Zwergel C, Stazi G, Valente S et al (2016) Histone deacetylase inhibitors: updated studies in
various epigenetic-related diseases. J Clin Epigenetics 2:1–7
23. Manal M, Chandrasekar MJN, Priya JG et al (2016) Inhibitors of histone deacetylase as
antitumor agents: a critical review. Bioorg Chem 67:18–42
24. Ganesan A (2018) Epigenetic drug discovery: a success story for cofactor interference. Philos
Trans R Soc B 373:20170069
25. Khan A, Singh P, Srivastava K (2018) Synthesis, nature and utility of universal iron chelator –
siderophore: a review. Microbiol Res 212:103–111
26. Codd R (2008) Traversing the coordination chemistry and chemical biology of hydroxamic
acids. Coord Chem Rev 252:1387–1408
22
A. Ganesan