Abstract
Histone posttranslational modifications or PTMs are epigenetic marks. They have essential functions in multiple cellular systems, including transcription, DNA repair, and chromatin dynamics. Histone modifications regulate chromatin remodeling, thereby controlling gene expression or gene silencing. Alterations in histone modifications or PTMS due to histone modifiers, which are different classes of histone acetylase and histone deacetylases enzymes, develop cancer and other metabolic diseases. This chapter has given importance on methylation, acetylation, and ubiquitylation of histones. We have shown how these small molecules change the function of histones in develo** cancer. We have also discussed various histone modifiers and their role in manipulating histone marks that increase or decrease the aggressiveness of cancer. This chapter has checked the importance of H3K4Me2/Me3, H3K27Me3, H4K12Ac, H4K16Ac, H4K27Ac, and H3K18Ac as a biomarker in different cancers, including glioma, hepatocellular carcinoma, gastric cancer, colorectal cancer, breast cancer, pancreatic cancer, and nonsmall cell lung cancer.
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References
An S, Camarillo JM, Huang TYT, Li D, Morris JA, Zoltek MA, Qi J, Behbahani M, Kambhampati M, Kelleher NL, Nazarian J, Thomas PM, Saratsis AM (2020) Histone tail analysis reveals H3K36me2 and H4K16ac as epigenetic signatures of diffuse intrinsic pontine glioma. J Exp Clin Cancer Res 39(1):1–16. https://doi.org/10.1186/s13046-020-01773-x
Atanassov BS, Mohan RD, Lan X, Kuang X, Lu Y, Lin K, McIvor E, Li W, Zhang Y, Florens L, Byrum SD, Mackintosh SG, Calhoun-Davis T, Koutelou E, Wang L, Tang DG, Tackett AJ, Washburn MP, Workman JL, Dent SYR (2016) ATXN7L3 and ENY2 coordinate activity of multiple H2B deubiquitinases important for cellular proliferation and tumor growth. Mol Cell 62(4):558–571. https://doi.org/10.1016/j.molcel.2016.03.030
Audia JE, Campbell RM (2016) Histone modifications and cancer. Cold Spring Harb Perspect Biol 8(4). https://doi.org/10.1101/cshperspect.a019521
Bannister AJ, Kouzarides T (2011) Regulation of chromatin by histone modifications. Cell Res 21(3):381–395. https://doi.org/10.1038/cr.2011.22
Barber MF, Michishita-Kioi E, ** Y, Tasselli L, Kioi M, Moqtaderi Z, Tennen RI, Paredes S, Young NL, Chen K, Struhl K, Garcia BA, Gozanil O, Li W, Chua KF (2012) SIRT7 links H3K18 deacetylation to maintenance of oncogenic transformation. Nature 487(7405):114–118. https://doi.org/10.1038/nature11043
Barlési F, Giaccone G, Gallegos-Ruiz MI, Loundou A, Span SW, Lefesvre P, Kruyt FAE, Rodriguez JA (2007) Global histone modifications predict prognosis of resected non-small-cell lung cancer. J Clin Oncol 25(28):4358–4364. https://doi.org/10.1200/JCO.2007.11.2599
Bhatnagar S, Gazin C, Chamberlain L, Ou J, Zhu X, Tushir JS, Virbasius CM, Lin L, Zhu LJ, Wajapeyee N, Green MR (2014) TRIM37 is a new histone H2A ubiquitin ligase and breast cancer oncoprotein. Nature 516(729):116–120. https://doi.org/10.1038/nature13955
Bhattacharya S, Reddy D, Ingle A, Khade B, Gupta S (2016) Brief communication: featured article: histone H2A mono-ubiquitination and cellular transformation are inversely related in N-nitrosodiethylamine-induced hepatocellular carcinoma. Exp Biol Med 241(16):1739–1744. https://doi.org/10.1177/1535370216649262
Cai MY, Tong ZT, Zhu W, Wen ZZ, Rao HL, Kong LL, Guan XY, Kung HF, Zeng YX, **e D (2011) H3K27me3 protein is a promising predictive biomarker of patients’ survival and chemoradioresistance in human nasopharyngeal carcinoma. Mol Med 17(11):1137–1145. https://doi.org/10.2119/molmed.2011.00054
Cai LY, Chen SJ, **ao SH, Sun QJ, Ding CH, Zheng BN, Zhu XY, Liu SQ, Yang F, Yang YX, Zhou B, Luo C, Zhang X, **e WF (2021) Targeting p300/CBP attenuates hepatocellular carcinoma progression through epigenetic regulation of metabolism. Cancer Res 81(4):860–872. https://doi.org/10.1158/0008-5472.CAN-20-1323
Cao J, Yan Q (2012) Histone ubiquitination and deubiquitination in transcription, DNA damage response, and cancer. Front Oncol 2(MAR):1–9. https://doi.org/10.3389/fonc.2012.00026
Chen A, Kleiman FE, Manley JL, Ouchi T (2002) Autoubiquitination of the BRCA1·BARD1 RING ubiquitin ligase. J Biol Chem 277(24):22085–22092. https://doi.org/10.1074/jbc.M201252200
Chen X, Song N, Matsumoto K, Nanashima A, Nagayasu T, Hayashi T, Ying M, Endo D, Wu Z, Koji T (2013) High expression of trimethylated histone H3 at lysine 27 predicts better prognosis in non-small cell lung cancer. Int J Oncol 43(5):1467–1480. https://doi.org/10.3892/ijo.2013.2062
Chen F, Qi S, Zhang X, Wu J, Yang X, Wang R (2019) LncRNA PLAC2 activated by H3K27 acetylationpromotes cell proliferation and invasion via the activation ofWnt/β-catenin pathway in oral squamous cell carcinoma. Int J Oncol 54(4):1183–1194. https://doi.org/10.3892/ijo.2019.4707
Cloos PAC, Christensen J, Agger K, Helin K (2008) Erasing the methyl mark: Histone demethylases at the center of cellular differentiation and disease. Genes Dev 22(9):1115–1140. https://doi.org/10.1101/gad.1652908
Cohen-Carmon D, Meshorer E (2012) Polyglutamine (polyQ) disorders. Nucleus 3(5):433–441. https://doi.org/10.4161/nucl.21481
Cole AJ, Clifton-Bligh R, Marsh DJ (2015) Histone H2B monoubiquitination: roles to play in human malignancy. Endocr Relat Cancer 22(1):T19–T33. https://doi.org/10.1530/ERC-14-0185
Damodaran S, Damaschke N, Gawdzik J, Yang B, Shi C, Allen GO, Huang W, Denu J, Jarrard D (2017) Dysregulation of Sirtuin 2 (SIRT2) and histone H3K18 acetylation pathways associates with adverse prostate cancer outcomes. BMC Cancer 17(1):1–8. https://doi.org/10.1186/s12885-017-3853-9
Dawson MA, Kouzarides T (2012) Cancer epigenetics: from mechanism to therapy. Cell 150(1):12–27. https://doi.org/10.1016/j.cell.2012.06.013
Deng L, Meng T, Chen L, Wei W, Wang P (2020) The role of ubiquitination in tumorigenesis and targeted drug discovery. Signal Trans Target Therapy 5(1). https://doi.org/10.1038/s41392-020-0107-0
Dong H, Hu J, Zou K, Ye M, Chen Y, Wu C, Chen X, Han M (2021) Correction to: Activation of LncRNA TINCR by H3K27 acetylation promotes Trastuzumab resistance and epithelial-mesenchymal transition by targeting MicroRNA-125b in breast cancer (Mol Cancer (2019) 18(1):3. 10.1186/s12943-018-0931-9). Mol Cancer 20(1):1–18. https://doi.org/10.1186/s12943-021-01385-9
Eissenberg JC, Shilatifard A (2010) Histone H3 lysine 4 (H3K4) methylation in development and differentiation. Dev Biol 339(2):240–249. https://doi.org/10.1016/j.ydbio.2009.08.017
Elsheikh SE, Green AR, Rakha EA, Powe DG, Ahmed RA, Collins HM, Soria D, Garibaldi JM, Paish CE, Ammar AA, Grainge MJ, Ball GR, Abdelghany MK, Martinez-Pomares L, Heery DM, Ellis IO (2009) Global histone modifications in breast cancer correlate with tumor phenotypes, prognostic factors, and patient outcome. Cancer Res 69(9):3802–3809. https://doi.org/10.1158/0008-5472.CAN-08-3907
Füllgrabe J, Kavanagh E, Joseph B (2011) Histone onco-modifications. Oncogene 30(31):3391–3403. https://doi.org/10.1038/onc.2011.121
Fyodorov DV, Zhou BR, Skoultchi AI, Bai Y (2018) Emerging roles of linker histones in regulating chromatin structure and function. Nat Rev Mol Cell Biol 19(3):192–206. https://doi.org/10.1038/nrm.2017.94
Haider R, Massa F, Kaminski L, Clavel S, Djabari Z, Robert G, Laurent K, Michiels JF, Durand M, Ricci JE, Tanti JF, Bost F, Ambrosetti D (2017) Sirtuin 7: a new marker of aggressiveness in prostate cancer. Oncotarget 8(44):77309–77316. https://doi.org/10.18632/oncotarget.20468
Hałasa M, Wawruszak A, Przybyszewska A, Jaruga A, Guz M, Kałafut J, Stepulak A, Cybulski M (2019) H3K18Ac as a marker of cancer progression and potential target of anti-cancer therapy. Cells 8(5):485. https://doi.org/10.3390/cells8050485
Hamamoto R, Silva FP, Tsuge M, Nishidate T, Katagiri T, Nakamura Y, Furukawa Y (2006) Enhanced SMYD3 expression is essential for the growth of breast cancer cells. Cancer Sci 97(2):113–118. https://doi.org/10.1111/j.1349-7006.2006.00146.x
Hayami S, Kelly JD, Cho HS, Yoshimatsu M, Unoki M, Tsunoda T, Field HI, Neal DE, Yamaue H, Ponder BAJ, Nakamura Y, Hamamoto R (2011) Overexpression of LSD1 contributes to human carcinogenesis through chromatin regulation in various cancers. Int J Cancer 128(3):574–586. https://doi.org/10.1002/ijc.25349
He C, Xu J, Zhang J, **e D, Ye H, **ao Z, Cai M, Xu K, Zeng Y, Li H, Wang J (2012) High expression of trimethylated histone H3 lysine 4 is associated with poor prognosis in hepatocellular carcinoma. Hum Pathol 43(9):1425–1435. https://doi.org/10.1016/j.humpath.2011.11.003
Huang T, Garcia R, Qi J, Lulla R, Horbinski C, Behdad A, Wadhwani N, Shilatifard A, James C, Saratsis A (2018) Detection of histone H3 K27M mutation and post-translational modifications in pediatric diffuse midline glioma via tissue immunohistochemistry informs diagnosis and clinical outcomes. Oncotarget 9(98):37112–37124. https://doi.org/10.18632/oncotarget.26430
Huo Q, Li Z, Cheng L, Yang F, **e N (2020) SIRT7 is a prognostic biomarker associated with immune infiltration in luminal breast cancer. Front Oncol 10(May). https://doi.org/10.3389/fonc.2020.00621
Jha S, Rajagopalan D, Hora S, Jadhav SP (2017) Breast cancer: from transcriptional control to clinical outcome. Breast Cancer Biol Med. https://doi.org/10.5772/66888
Juliano CN, Izetti P, Pereira MP, Dos Santos AP, Bravosi CP, Abujamra AL, Prolla PA, Osvaldt AB, Edelweiss MIA (2016) H4K12 and H3K18 acetylation associates with poor prognosis in pancreatic cancer. Appl Immunohistochem Mol Morphol 24(5):337–344. https://doi.org/10.1097/PAI.0000000000000194
Karczmarski J, Rubel T, Paziewska A, Mikula M, Bujko M, Kober P, Dadlez M, Ostrowski J (2014) Histone H3 lysine 27 acetylation is altered in colon cancer. Clin Proteomics 11(1):1–10. https://doi.org/10.1186/1559-0275-11-24
Karim MF, Yoshizawa T, Sato Y, Sawa T, Tomizawa K, Akaike T, Yamagata K (2013) Inhibition of H3K18 deacetylation of Sirt7 by Myb-binding protein 1a (Mybbp1a). Biochem Biophys Res Commun 441(1):157–163. https://doi.org/10.1016/j.bbrc.2013.10.020
Keating ST, El-Osta A (2012) Chromatin modifications associated with diabetes. J Cardiovasc Transl Res 5(4):399–412. https://doi.org/10.1007/s12265-012-9380-9
Khan SA (2015) Global histone post-translational modifications and cancer: biomarkers for diagnosis, prognosis and treatment? World J Biol Chem 6(4):333. https://doi.org/10.4331/wjbc.v6.i4.333
Kim KH, Roberts CWM (2016) Targeting EZH2 in cancer. Nat Med 22(2):128–134. https://doi.org/10.1038/nm.4036
Klose RJ, Zhang Y (2007) Regulation of histone methylation by demethylimination and demethylation. Nat Rev Mol Cell Biol 8(4):307–318. https://doi.org/10.1038/nrm2143
Kouzarides T (2007) Chromatin modifications and their function. Cell 128(4):693–705. https://doi.org/10.1016/j.cell.2007.02.005
Krivtsov AV, Armstrong SA (2007) MLL translocations, histone modifications and leukaemia stem-cell development. Nat Rev Cancer 7(11):823–833. https://doi.org/10.1038/nrc2253
Lan X, Atanassov BS, Li W, Zhang Y, Florens L, Mohan RD, Galardy PJ, Washburn MP, Workman JL, Dent SYR (2016) USP44 is an integral component of N-CoR that contributes to gene repression by deubiquitinating histone H2B. Cell Rep 17(9):2382–2393. https://doi.org/10.1016/j.celrep.2016.10.076
Lee HS, Jung W, Lee E, Chang H, Choi JH, Kim HG, Kim A, Kim BH (2016) SIRT7, H3K18ac, and ELK4 immunohistochemical expression in hepatocellular carcinoma. J Pathol Transl Med 50(5):337–344. https://doi.org/10.4132/jptm.2016.05.20
Li Y, Seto E (2016) HDACs and HDAC inhibitors in cancer development and therapy. Cold Spring Harbor Perspect Med 6(10). https://doi.org/10.1101/cshperspect.a026831
Liu Q, Wang MW (2016) Histone lysine methyltransferases as anti-cancer targets for drug discovery. Acta Pharmacol Sin 37(10):1273–1280. https://doi.org/10.1038/aps.2016.64
Liu BL, Cheng JX, Zhang X, Wang R, Zhang W, Lin H, **ao X, Cai S, Chen XY, Cheng H (2010) Global histone modification patterns as prognostic markers to classify glioma patients. Cancer Epidemiol Biomark Prev 19(11):2888–2896. https://doi.org/10.1158/1055-9965.EPI-10-0454
Lutz L, Fitzner IC, Ahrens T, Geibler AL, Makowiec F, Hopt UT, Bogatyreva L, Hauschke D, Werner M, Lassmann S (2016) Histone modifiers and marks define heterogeneous groups of colorectal carcinomas and affect responses to HDAC inhibitors in vitro. Am J Cancer Res 6(3):664–676
Malik S, Villanova L, Tanaka S, Aonuma M, Roy N, Berber E, Pollack JR, Michishita-Kioi E, Chua KF (2015) SIRT7 inactivation reverses metastatic phenotypes in epithelial and mesenchymal tumors. Sci Rep 5:1–9. https://doi.org/10.1038/srep09841
Mancuso M, Matassa DS, Conte M, Colella G, Rana G, Fucci L, Piscopo M (2009) H3K4 histone methylation in oral squamous cell carcinoma. Acta Biochim Pol 56(3):405–410. https://doi.org/10.18388/abp.2009_2473
Manuyakorn A, Paulus R, Farrell J, Dawson NA, Tze S, Cheung-Lau G, Hines OJ, Reber H, Seligson DB, Horvath S, Kurdistani SK, Guha C, Dawson DW (2010) Cellular histone modification patterns predict prognosis and treatment response in resectable pancreatic adenocarcinoma: results from RTOG 9704. J Clin Oncol 28(8):1358–1365. https://doi.org/10.1200/JCO.2009.24.5639
Marmorstein R, Zhou MM (2014) Writers and readers of histone acetylation: Structure, mechanism, and inhibition. Cold Spring Harb Perspect Biol 6(7). https://doi.org/10.1101/cshperspect.a018762
Nakazawa T, Kondo T, Ma D, Niu D, Mochizuki K, Kawasaki T, Yamane T, Iino H, Fujii H, Katoh R (2012) Global histone modification of histone H3 in colorectal cancer and its precursor lesions. Hum Pathol 43(6):834–842. https://doi.org/10.1016/j.humpath.2011.07.009
Ngollo M, Lebert A, Daures M, Judes G, Rifai K, Dubois L, Kemeny JL, Penault-Llorca F, Bignon YJ, Guy L, Bernard-Gallon D (2017) Global analysis of H3K27me3 as an epigenetic marker in prostate cancer progression. BMC Cancer 17(1):1–8. https://doi.org/10.1186/s12885-017-3256-y
Nguyen AT, Zhang Y (2011) The diverse functions of Dot1 and H3K79 methylationanh. Genes Dev 25(13):1345–1358. https://doi.org/10.1101/gad.2057811
Pan MR, Hsu MC, Chen LT, Hung WC (2018) Orchestration of H3K27 methylation: mechanisms and therapeutic implication. Cell Mol Life Sci 75(2):209–223. https://doi.org/10.1007/s00018-017-2596-8
Pandey V, Kumar V (2015) Stabilization of SIRT7 deacetylase by viral oncoprotein HBx leads to inhibition of growth restrictive RPS7 gene and facilitates cellular transformation. Sci Rep 5(March):1–15. https://doi.org/10.1038/srep14806
Park YS, ** MY, Kim YJ, Yook JH, Kim BS, Jang SJ (2008) The global histone modification pattern correlates with cancer recurrence and overall survival in gastric adenocarcinoma. Ann Surg Oncol 15(7):1968–1976. https://doi.org/10.1245/s10434-008-9927-9
Petty E, Pillus L (2013) Balancing chromatin remodeling and histone modifications in transcription. Trends Genet 29(11):621–629. https://doi.org/10.1016/j.tig.2013.06.006
Rajendran G, Shanmuganandam K, Bendre A, Mujumdar D, Goel A, Shiras A (2011) Epigenetic regulation of DNA methyltransferases: DNMT1 and DNMT3B in gliomas. J Neuro-Oncol 104(2):483–494. https://doi.org/10.1007/s11060-010-0520-2
Reyes DA, SarrÃa VMS, Salazar-Viedma M, D’Afonseca V (2021) Histone methyltransferases useful in gastric cancer research. Cancer Informat 20. https://doi.org/10.1177/11769351211039862
Ruthenburg AJ, Li H, Patel DJ, David Allis C (2007) Multivalent engagement of chromatin modifications by linked binding modules. Nat Rev Mol Cell Biol 8(12):983–994. https://doi.org/10.1038/nrm2298
Saidi D, Cheray M, Osman AM, Stratoulias V, Lindberg OR, Shen X, Blomgren K, Joseph B (2018) Glioma-induced SIRT1-dependent activation of hMOF histone H4 lysine 16 acetyltransferase in microglia promotes a tumor supporting phenotype. OncoImmunology 7(2):1–13. https://doi.org/10.1080/2162402X.2017.1382790
Schulte JH, Lim S, Schramm A, Friedrichs N, Koster J, Versteeg R, Ora I, Pajtler K, Klein-Hitpass L, Kuhfittig-Kulle S, Metzger E, Schüle R, Eggert A, Buettner R, Kirfel J (2009) Lysine-specific demethylase 1 is strongly expressed in poorly differentiated neuroblastoma: implications for therapy. Cancer Res 69(5):2065–2071. https://doi.org/10.1158/0008-5472.CAN-08-1735
Seligson DB, Horvath S, Shi T, Yu H, Tze S, Grunstein M, Kurdistani SK (2005) Global histone modification patterns predict risk of prostate cancer recurrence. Nature 435(7046):1262–1266. https://doi.org/10.1038/nature03672
Seligson DB, Horvath S, McBrian MA, Mah V, Yu H, Tze S, Wang Q, Chia D, Goodglick L, Kurdistani SK (2009) Global levels of histone modifications predict prognosis in different cancers. Am J Pathol 174(5):1619–1628. https://doi.org/10.2353/ajpath.2009.080874
Sheikh BN, Akhtar A (2019) The many lives of KATs – detectors, integrators and modulators of the cellular environment. Nat Rev Genet 20(1):7–23. https://doi.org/10.1038/s41576-018-0072-4
Shen X, Liu Y, Hsu YJ, Fujiwara Y, Kim J, Mao X, Yuan GC, Orkin SH (2008) EZH1 mediates methylation on histone H3 lysine 27 and complements EZH2 in maintaining stem cell identity and executing pluripotency. Mol Cell 32(4):491–502. https://doi.org/10.1016/j.molcel.2008.10.016
Shi Y, Lan F, Matson C, Mulligan P, Whetstine JR, Cole PA, Casero RA, Shi Y (2004) Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell 119(7):941–953. https://doi.org/10.1016/j.cell.2004.12.012
Sun J, Zhu Z, Li W, Shen M, Cao C, Sun Q, Guo Z, Liu L, Wu D (2020) UBE2T-regulated H2AX monoubiquitination induces hepatocellular carcinoma radioresistance by facilitating CHK1 activation. J Exp Clin Cancer Res 39(1):1–18. https://doi.org/10.1186/s13046-020-01734-4
Tzao C, Tung HJ, ** JS, Sun GH, Hsu HS, Chen BH, Yu CP, Lee SC (2009) Prognostic significance of global histone modifications in resected squamous cell carcinoma of the esophagus. Mod Pathol 22(2):252–260. https://doi.org/10.1038/modpathol.2008.172
Wagner EJ, Carpenter PB (2012) Understanding the language of Lys36 methylation at histone H3. Nat Rev Mol Cell Biol 13(2):115–126. https://doi.org/10.1038/nrm3274
Wei Y, **a W, Zhang Z, Liu J, Wang H, Adsay NV, Albarracin C, Yu D, Abbruzzese JL, Mills GB, Bast RC, Hortobagyi GN, Hung MC (2008) Loss of trimethylation at lysine 27 of histone H3 is a predictor of poor outcome in breast, ovarian, and pancreatic cancers. Mol Carcinog 47(9):701–706. https://doi.org/10.1002/mc.20413
Wu D, Qiu Y, Jiao Y, Qiu Z, Liu D (2020) Small molecules targeting HATs, HDACs, and BRDs in cancer therapy. Front Oncol 10(November):1–14. https://doi.org/10.3389/fonc.2020.560487
Yamaguchi H, Hung MC (2014) Regulation and role of EZH2 in cancer. Cancer Res Treat 46(3):209–222. https://doi.org/10.4143/crt.2014.46.3.209
Yamamoto S, Wu Z, Russnes HG, Takagi S, Peluffo G, Vaske C, Zhao X, MoenVollan HK, Maruyama R, Ekram MB, Sun H, Kim JH, Carver K, Zucca M, Feng J, Almendro V, Bessarabova M, Rueda OM, Nikolsky Y et al (2014) JARID1B is a luminal lineage-driving oncogene in breast cancer. Cancer Cell 25(6):762–777. https://doi.org/10.1016/j.ccr.2014.04.024
Ye XD, Qiu BQ, **ong D, Pei X, Jie N, Xu H, Zhu SQ, Long X, Xu Z, Wu HB, Xu JJ, Huang YS, Wu YB (2020) High level of H3K4 tri-methylation modification predicts poor prognosis in esophageal cancer. J Cancer 11(11):3256–3263. https://doi.org/10.7150/jca.36801
Yokoyama M, Chiba T, Zen Y, Oshima M, Kusakabe Y, Noguchi Y, Yuki K, Koide S, Tara S, Saraya A, Aoyama K, Mimura N, Miyagi S, Inoue M, Wakamatsu T, Saito T, Ogasawara S, Suzuki E, Ooka Y et al (2017) Histone lysine methyltransferase G9a is a novel epigenetic target for the treatment of hepatocellular carcinoma. Oncotarget 8(13):21315–21326. https://doi.org/10.18632/oncotarget.15528
Yu J, Yu J, Rhodes DR, Tomlins SA, Cao X, Chen G, Mehra R, Wang X, Ghosh D, Shah RB, Varambally S, Pienta KJ, Chinnaiyan AM (2007) A polycomb repression signature in metastatic prostate cancer predicts cancer outcome. Cancer Res 67(22):10657–10663. https://doi.org/10.1158/0008-5472.CAN-07-2498
Zhang E, Han L, Yin D, He X, Hong L, Si X, Qiu M, Xu T, De W, Xu L, Shu Y, Chen J (2017a) H3K27 acetylation activated-long non-coding RNA CCAT1 affects cell proliferation and migration by regulating SPRY4 and HOXB13 expression in esophageal squamous cell carcinoma. Nucleic Acids Res 45(6):3086–3101. https://doi.org/10.1093/nar/gkw1247
Zhang K, Wang J, Tong TR, Wu X, Nelson R, Yuan YC, Reno T, Liu Z, Yun X, Kim JY, Salgia R, Raz DJ (2017b) Loss of H2B monoubiquitination is associated with poor-differentiation and enhanced malignancy of lung adenocarcinoma. Int J Cancer 141(4):766–777. https://doi.org/10.1002/ijc.30769
Zhao Y, Ye X, Chen R, Gao Q, Zhao D, Ling C, Qian Y, Xu C, Tao M, **e Y (2020) Sirtuin 7 promotes non-small cell lung cancer progression by facilitating G1/S phase and epithelial-mesenchymal transition and activating AKT and ERK1/2 signaling. Oncol Rep 44(3):959–972. https://doi.org/10.3892/or.2020.7672
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Karim, M.F., Kabir, Y. (2023). Role of Histone Modifications in the Progression of Cancer. In: Rezaei, N. (eds) Handbook of Cancer and Immunology. Springer, Cham. https://doi.org/10.1007/978-3-030-80962-1_50-1
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