The DOI matches its Crossref record; 166 of the 167 references it cites were found in a registry or an index.
Critical roles of non-histone protein lysine methylation in human tumorigenesis
Abstract
Several protein lysine methyltransferases and demethylases have been identified to have critical roles in histone modification. A large body of evidence has indicated that their dysregulation is involved in the development and progression of various diseases, including cancer, and these enzymes are now considered to be potential therapeutic targets. Although most studies have focused on histone methylation, many reports have revealed that these enzymes also regulate the methylation dynamics of non-histone proteins such as p53, RB1 and STAT3 (signal transducer and activator of transcription 3), which have important roles in human tumorigenesis. In this Review, we summarize the molecular functions of protein lysine methylation and its involvement in human cancer, with a particular focus on lysine methylation of non-histone proteins.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“The mechanisms that underpin these adaptive responses and render epigenetic therapies ineffective are varied and include tumour-intrinsic mechanisms and heterogenous cellular and molecular effects of the drugs 187 .”
From The roles of DNA, RNA and histone methylation in ageing and cancer (2019) · cites this paper as [187]
Citations
Cites
Shrestha, S., & Offer, S. M. (2016) · Medical Epigenetics · doi:10.1159/000444713 · Cited by 8,951
Mutational landscape and significance across 12 major cancer types
Kandoth, C., McLellan, M. D., Vandin, F., Ye, K., Niu, B., Lu, C., Xie, M., Zhang, Q., McMichael, J. F., Wyczalkowski, M. A., et al. (2013) · Nature · doi:10.1038/nature12634 · Cited by 4,419
Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
Shi, Y., Lan, F., Matson, C., Mulligan, P., Whetstine, J. R., Cole, P. A., Casero, R. A., & Shi, Y. (2004) · Cell · doi:10.1016/j.cell.2004.12.012 · Cited by 4,051
VEGF receptor signalling ? in control of vascular function
Olsson, A.-K., Dimberg, A., Kreuger, J., & Claesson-Welsh, L. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1911 · Cited by 3,122
Regulation of chromatin structure by site-specific histone H3 methyltransferases
Rea, S., Eisenhaber, F., O'Carroll, D., Strahl, B. D., Sun, Z.-W., Schmid, M., Opravil, S., Mechtler, K., Ponting, C. P., Allis, C. D., et al. (2000) · Nature · doi:10.1038/35020506 · Cited by 2,845
The mutational landscape of lethal castration-resistant prostate cancer
Grasso, C. S., Wu, Y.-M., Robinson, D. R., Cao, X., Dhanasekaran, S. M., Khan, A. P., Quist, M. J., Jing, X., Lonigro, R. J., Brenner, J. C., et al. (2012) · Nature · doi:10.1038/nature11125 · Cited by 2,517
HSP90 and the chaperoning of cancer
Whitesell, L., & Lindquist, S. L. (2005) · Nature Reviews Cancer · doi:10.1038/nrc1716 · Cited by 2,502
Histone demethylation by a family of JmjC domain-containing proteins
Tsukada, Y.-I., Fang, J., Erdjument‐Bromage, H., Warren, M., Borchers, C. H., Tempst, P., & Zhang, Y. (2005) · Nature · doi:10.1038/nature04433 · Cited by 2,244
EZH2 inhibition as a therapeutic strategy for lymphoma with EZH2-activating mutations
McCabe, M. T., Ott, H. M., Ganji, G., Korenchuk, S., Thompson, C., Van Aller, G. S., Liu, Y., Graves, A. P., III, A. D. P., Diaz, E., et al. (2012) · Nature · doi:10.1038/nature11606 · Cited by 1,786
The HSP70 chaperone machinery: J proteins as drivers of functional specificity
Kampinga, H. H., & Craig, E. A. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2941 · Cited by 1,760
Frequent mutation of histone-modifying genes in non-Hodgkin lymphoma
Morin, R. D., Mendez-Lago, M., Mungall, A. J., Goya, R., Mungall, K. L., Corbett, R. D., Johnson, N. A., Severson, T. M., Chiu, R., Field, M., et al. (2011) · Nature · doi:10.1038/nature10351 · Cited by 1,614
Targeting the dynamic HSP90 complex in cancer
Trepel, J. B., Mollapour, M., Giaccone, G., & Neckers, L. (2010) · Nature reviews. Cancer · doi:10.1038/nrc2887 · Cited by 1,523
Pratt, W. B., & Toft, D. O. (2003) · Experimental Biology and Medicine · doi:10.1177/153537020322800201 · Cited by 1,497
Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications
Ciocca, D. R., & Calderwood, S. K. (2005) · Cell Stress and Chaperones · doi:10.1379/csc-99r.1 · Cited by 1,420
Münger, K., Werness, B. A., Dyson, N. J., Phelps, W. C., Harlow, E. E., & Howley, P. M. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb08594.x · Cited by 1,204
Rational design of inhibitors that bind to inactive kinase conformations
Liu, Y., & Gray, N. S. (2006) · Nature Chemical Biology · doi:10.1038/nchembio799 · Cited by 1,096
Emerging roles of E2Fs in cancer: an exit from cell cycle control
Chen, H., Tsai, S., & Leone, G. W. (2009) · Nature reviews. Cancer · doi:10.1038/nrc2696 · Cited by 1,052
The retinoblastoma protein is phosphorylated during specific phases of the cell cycle
Buchkovich, K., Duffy, L. A., & Harlow, E. (1989) · Cell · doi:10.1016/0092-8674(89)90508-4 · Cited by 995
A selective jumonji H3K27 demethylase inhibitor modulates the proinflammatory macrophage response
Kruidenier, L., Chung, C.-W., Cheng, Z., Liddle, J., Che, K., Joberty, G., Bantscheff, M., Bountra, C., Bridges, A., Diallo, H., et al. (2012) · Nature · doi:10.1038/nature11262 · Cited by 950
NF-κB signaling pathways in mammalian and insect innate immunityPreprint
Silverman, N. S., & Maniatis, T. (2001) · Genes & Development · doi:10.1101/gad.909001 · Cited by 904
Methylation of H3-Lysine 79 Is Mediated by a New Family of HMTases without a SET Domain
Feng, Q. F., Wang, H., Ng, H., Erdjument‐Bromage, H., Tempst, P., Struhl, K., & Zhang, Y. (2002) · Current Biology · doi:10.1016/s0960-9822(02)00901-6 · Cited by 897
Reversal of H3K9me2 by a Small-Molecule Inhibitor for the G9a Histone Methyltransferase
Kubicek, S., O'Sullivan, R. J., August, E. M., Hickey, E. R., Zhang, Q., Teodoro, M. L., Rea, S., Mechtler, K., Kowalski, J. A., Homon, C. A., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.01.017 · Cited by 859
Regulation of p53 activity through lysine methylation
Chuikov, S., Kurash, J. K., Wilson, J. R., Xiao, B., Justin, N., Ivanov, G. S., McKinney, K. M., Tempst, P., Prives, C. L., Gamblin, S. J., et al. (2004) · Nature · doi:10.1038/nature03117 · Cited by 846
Kim, E. H., Kim, M., Woo, D., Shin, Y., Shin, J., Chang, N., Oh, Y. T., Kim, H., Rheey, J., Nakano, I., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.04.008 · Cited by 846
hDOT1L Links Histone Methylation to Leukemogenesis
Okada, Y., Feng, Q. F., Lin, Y.-H., Jiang, Q., Li, Y., Coffield, V. M., Su, L., Xu, G., & Zhang, Y. (2005) · Cell · doi:10.1016/j.cell.2005.02.020 · Cited by 835
p53 is regulated by the lysine demethylase LSD1
Huang, J. L., Sengupta, R., Espejo, A. B., Lee, M. G., Dorsey, J. A., Richter, M., Opravil, S., Shiekhattar, R., Bedford, M. T., Jenuwein, T., et al. (2007) · Nature · doi:10.1038/nature06092 · Cited by 820
Somatic mutations of the histone H3K27 demethylase gene UTX in human cancer
van Haaften, G., Dalgliesh, G. L., Davies, H., Chen, L., Bignell, G., Greenman, C., Edkins, S., Hardy, C., O'Meara, S., Teague, J., et al. (2009) · Nature Genetics · doi:10.1038/ng.349 · Cited by 784
Tachibana, M., Sugimoto, K., Fukushima, T., & Shinkai, Y. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101914200 · Cited by 784
Somatic mutations of the histone methyltransferase gene EZH2 in myelodysplastic syndromes
Nikoloski, G., Langemeijer, S. M. C., Kuiper, R. P., Knops, R., Massop, M., Tönnissen, E., van der Heijden, A., Scheele, T. N., Vandenberghe, P., de Witte, T., et al. (2010) · Nature Genetics · doi:10.1038/ng.620 · Cited by 777
A selective inhibitor of EZH2 blocks H3K27 methylation and kills mutant lymphoma cells
Knutson, S. K., Wigle, T. J., Warholic, N. M., Sneeringer, C. J., Allain, C. J., Klaus, C. R., Sacks, J. D., Raimondi, A., Majer, C. R., Song, J., et al. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.1084 · Cited by 776
Frequent mutations of chromatin remodeling genes in transitional cell carcinoma of the bladder
Gui, Y., Guo, G., Huang, Y., Hu, X., Tang, A., Gao, S., Wu, R., Chen, C., Li, X., Zhou, L., et al. (2011) · Nature Genetics · doi:10.1038/ng.907 · Cited by 759
SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells
Hamamoto, R., Furukawa, Y., Morita, M., Iimura, Y., Pittella-Silva, F., Li, M., Yagyu, R., & Nakamura, Y. (2004) · Nature Cell Biology · doi:10.1038/ncb1151 · Cited by 752
Self-citationSchenk, T., Chen, W. C., Göllner, S., Howell, L., Jin, L., Hebestreit, K., Klein, H.-U., Popescu, A. C., Burnett, A., Mills, K., et al. (2012) · Nature Medicine · doi:10.1038/nm.2661 · Cited by 672
Repression of p53 activity by Smyd2-mediated methylation
Huang, J. L., Perez-Burgos, L., Placek, B. J., Sengupta, R., Richter, M., Dorsey, J. A., Kubicek, S., Opravil, S., Jenuwein, T., & Berger, S. L. (2006) · Nature · doi:10.1038/nature05287 · Cited by 626
Bannister, A. J., Schneider, R., & Kouzarides, T. (2002) · Cell · doi:10.1016/s0092-8674(02)00798-5 · Cited by 560
Wandinger, S. K., Richter, K., & Büchner, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800007200 · Cited by 554
A chemical probe selectively inhibits G9a and GLP methyltransferase activity in cells
Vedadi, M., Baršytė-Lovejoy, D., Liu, F., Rival‐Gervier, S., Allali‐Hassani, A., Labrie, V., Wigle, T. J., DiMaggio, P. A., Wasney, G. A., Siarheyeva, A., et al. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.599 · Cited by 547
Knutson, S. K., Kawano, S., Minoshima, Y., Warholic, N. M., Huang, K., Xiao, Y., Kadowaki, T., Uesugi, M., Kuznetsov, G., Kumar, N., et al. (2014) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-13-0773 · Cited by 547
Identification of a specific inhibitor of the histone methyltransferase SU(VAR)3-9
Greiner, D., Bonaldi, T., Eskeland, R., Roemer, E., & Imhof, A. (2005) · Nature Chemical Biology · doi:10.1038/nchembio721 · Cited by 524
The Occurrence of iε-N-Methyl Lysine in Histones
Murray, K. (1964) · Biochemistry · doi:10.1021/bi00889a003 · Cited by 521
Hayami, S., Kelly, J. D., Cho, H., Yoshimatsu, M., Unoki, M., Tsunoda, T., Field, H. I., Neal, D. E., Yamaue, H., Ponder, B. A. J., et al. (2011) · International Journal of Cancer · doi:10.1002/ijc.25349 · Cited by 489
Self-citationThe mutational landscape of adenoid cystic carcinoma
Ho, A. S., Kannan, K. S., Roy, D. M., Morris, L. G. T., Ganly, I., Katabi, N., Ramaswami, D., Walsh, L. A., Eng, S., Huse, J. T., et al. (2013) · Nature Genetics · doi:10.1038/ng.2643 · Cited by 472
Modulation of p53 Function by SET8-Mediated Methylation at Lysine 382
Shi, X., Kachirskaia, I., Yamaguchi, H., West, L. E., Wen, H., Wang, E. W., Dutta, S. M., Appella, E., & Gozani, O. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.07.012 · Cited by 463
Bejar, R. L., Stevenson, K. E., Caughey, B. A., Abdel-Wahab, O. I., Steensma, D. P., Galili, N., Raza, A., Kantarjian, H. M., Levine, R. L., Neuberg, D. S., et al. (2012) · Journal of Clinical Oncology · doi:10.1200/jco.2011.40.7379 · Cited by 450
NUP98–NSD1 links H3K36 methylation to Hox-A gene activation and leukaemogenesis
Wang, G. G., Cai, L., Pasillas, M. P., & Kamps, M. P. (2007) · Nature Cell Biology · doi:10.1038/ncb1608 · Cited by 441
MMSET regulates histone H4K20 methylation and 53BP1 accumulation at DNA damage sites
Pei, H., Zhang, L. M., Luo, K., Qin, Y., Chesi, M., Fei, Y. F., Bergsagel, P. L., Wang, L., You, Z., & Lou, Z. (2011) · Nature · doi:10.1038/nature09658 · Cited by 425
SMYD3 links lysine methylation of MAP3K2 to Ras-driven cancer
Mazur, P. K., Reynoird, N., Khatri, P., Jansen, P. W. T. C., Wilkinson, A. W., Liu, S., Barbash, O., Aller, G. S. V., Huddleston, M. J., Dhanak, D., et al. (2014) · Nature · doi:10.1038/nature13320 · Cited by 410
Chemical mechanisms of histone lysine and arginine modifications
Smith, B. C., & Denu, J. M. (2009) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2008.06.005 · Cited by 390
Contrasting roles of histone 3 lysine 27 demethylases in acute lymphoblastic leukaemia
Ntziachristos, P., Tsirigos, A., Welstead, G. G., Trimarchi, T., Bakogianni, S., Xu, L., Loizou, E., Holmfeldt, L., Strikoudis, A., King, B., et al. (2014) · Nature · doi:10.1038/nature13605 · Cited by 377
Lysine Methylation Regulates E2F1-Induced Cell Death
Kontaki, H., & Talianidis, I. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.06.006 · Cited by 374
Martínez-García, E., Popovic, R., Min, D.-J., Sweet, S. M. M., Thomas, P. M., Zamdborg, L., Heffner, A., Will, C., Lamy, L., Staudt, L. M., et al. (2010) · Blood · doi:10.1182/blood-2010-07-298349 · Cited by 365
Fan, F., Wey, J. S., McCarty, M. F., Belcheva, A., Liu, W., Bauer, T. W., Somcio, R., Wu, Y. L., Hooper, A. T., Hicklin, D. J., et al. (2005) · Oncogene · doi:10.1038/sj.onc.1208246 · Cited by 350
Jankowska, A. M., Makishima, H., Tiu, R. V., Szpurka, H., Huang, Y., Traina, F., Visconte, V., Sugimoto, Y., Prince, C. J., O’Keefe, C. L., et al. (2011) · Blood · doi:10.1182/blood-2010-10-311019 · Cited by 345
Hollink, I. H. I. M., van den Heuvel‐Eibrink, M. M., Arentsen-Peters, S. T. C. J. M., Pratcorona, M., Abbas, S., Katsman-Kuipers, J. E., van Galen, J. F., Beverloo, H. B., Sonneveld, E., Kaspers, G. J. L., et al. (2011) · Blood · doi:10.1182/blood-2011-04-346643 · Cited by 341
Reversible methylation of promoter-bound STAT3 by histone-modifying enzymes
Yang, J., Huang, J., Dasgupta, M., Sears, N., Miyagi, M., Wang, B., Chance, M. R., Chen, X., Du, Y., Wang, Y., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1016147107 · Cited by 340
Dissection of a Nuclear Localization Signal
Hodel, M. R., Corbett, A. H., & Hodel, A. E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008522200 · Cited by 339
Estrogen Receptor Alpha in Human Breast Cancer: Occurrence and Significance
Ali, S., & Coombes, R. (2000) · Journal of mammary gland biology and neoplasia · doi:10.1023/a:1009594727358 · Cited by 336
Wang, L., Chang, J., Varghese, D., Dellinger, M. T., Kumar, S., Best, A. M., Ruiz, J. C., Bruick, R. K., Peña‐Llopis, S., Xu, J., et al. (2013) · Nature Communications · doi:10.1038/ncomms3035 · Cited by 328
Brown, M. A., Sims, R. J., Gottlieb, P. D., & Tucker, P. W. (2006) · Molecular Cancer · doi:10.1186/1476-4598-5-26 · Cited by 320
trans-2-Phenylcyclopropylamine Is a Mechanism-Based Inactivator of the Histone Demethylase LSD1
Schmidt, D. M. Z., & McCafferty, D. G. (2007) · Biochemistry · doi:10.1021/bi0618621 · Cited by 319
Kotake, Y., Cao, R., Viatour, P., Sage, J., Zhang, Y., & Xiong, Y. (2007) · Genes & Development · doi:10.1101/gad.1499407 · Cited by 318
Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294
Chang, Y., Zhang, X., Horton, J. R., Upadhyay, A. K., Spannhoff, A., Liu, J., Snyder, J. P., Bedford, M. T., & Cheng, X. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1560 · Cited by 317
Identification of driver genes in hepatocellular carcinoma by exome sequencing
Cleary, S. P., Jeck, W. R., Zhao, X., Chen, K., Selitsky, S. R., Savich, G. L., Tan, T. X., Wu, M. C., Getz, G. A., Lawrence, M. S., et al. (2013) · Hepatology · doi:10.1002/hep.26540 · Cited by 315
Nonhistone protein acetylation as cancer therapy targets
Singh, B. N., Zhang, G., Hwa, Y. L., Li, J., Dowdy, S. C., & Jiang, S. (2010) · Expert Review of Anticancer Therapy · doi:10.1586/era.10.62 · Cited by 315
O’Carroll, D., Scherthan, H., Peters, A. H. F. M., Opravil, S., Haynes, A. R., Laible, G., Rea, S., Schmid, M., Lebersorger, A., Jerratsch, M., et al. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.24.9423-9433.2000 · Cited by 304
Regulation of Estrogen Receptor α by the SET7 Lysine Methyltransferase
Subramanian, K., Jia, D., Kapoor-Vazirani, P., Powell, D. R., Collins, R. E., Sharma, D., Peng, J., Cheng, X., & Vertino, P. M. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.03.022 · Cited by 291
ɛ-N-Methyl-lysine in Bacterial Flagellar Protein
Ambler, R. P., & Rees, M. W. (1959) · Nature · doi:10.1038/184056b0 · Cited by 291
Regulation of NF-κB by NSD1/FBXL11-dependent reversible lysine methylation of p65
Lu, T., Jackson, M. W., Wang, B., Yang, M., Chance, M. R., Miyagi, M., Gudkov, A. V., & Stark, G. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912493107 · Cited by 286
Global chromatin profiling reveals NSD2 mutations in pediatric acute lymphoblastic leukemia
Jaffe, J. D., Wang, Y., Chan, H. M., Zhang, J., Huether, R., Kryukov, G. V., Bhang, H.-E. C., Taylor, J. E., Hu, M., Englund, N. P., et al. (2013) · Nature Genetics · doi:10.1038/ng.2777 · Cited by 284
Fiskus, W., Sharma, S., Shah, B., Portier, B. P., Devaraj, S. G. T., Liu, K., Iyer, S. P., Bearss, D., & Bhalla, K. N. (2014) · Leukemia · doi:10.1038/leu.2014.119 · Cited by 284
Enhanced SMYD3 expression is essential for the growth of breast cancer cells
Hamamoto, R., Pittella-Silva, F., Tsuge, M., Nishidate, T., Katagiri, T., Nakamura, Y., & Furukawa, Y. (2006) · Cancer Science · doi:10.1111/j.1349-7006.2006.00146.x · Cited by 282
Self-citationDOT1L, the H3K79 methyltransferase, is required for MLL-AF9–mediated leukemogenesis
Nguyen, A. T., Taranova, O., He, J., & Zhang, Y. (2011) · Blood · doi:10.1182/blood-2011-02-334359 · Cited by 280
EZH2 Generates a Methyl Degron that Is Recognized by the DCAF1/DDB1/CUL4 E3 Ubiquitin Ligase Complex
Lee, J. M., Lee, J. S., Kim, H.-K., Kim, K., Park, H., Kim, J.-Y., Lee, S. H., Kim, I. S., Kim, J., Lee, M., et al. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.09.004 · Cited by 268
Levy, D., Kuo, A. J., Chang, Y., Schaefer, U., Kitson, C., Cheung, P., Espejo, A. B., Zee, B. M., Liu, C. L., Tangsombatvisit, S., et al. (2010) · Nature Immunology · doi:10.1038/ni.1968 · Cited by 266
Human LSD2/KDM1b/AOF1 Regulates Gene Transcription by Modulating Intragenic H3K4me2 Methylation
Fang, R., Barbera, A. J., Xu, Y., Rutenberg, M. S., Leonor, T., Bi, Q., Lan, F., Mei, P., Yuan, G., Lian, C. G., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.07.008 · Cited by 264
Cho, H., Suzuki, T., Dohmae, N., Hayami, S., Unoki, M., Yoshimatsu, M., Toyokawa, G., Takawa, M., Chen, T., Kurash, J. K., et al. (2010) · Cancer Research · doi:10.1158/0008-5472.can-10-2446 · Cited by 248
Self-citationRegulation of NF-κB activity through lysine monomethylation of p65
Ea, C.-K., & Baltimore, D. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0910439106 · Cited by 239
Wang, J., Lu, F., Ren, Q., Sun, H., Xu, Z., Lan, R., Liu, Y., Ward, D. C., Quan, J., Ye, T., et al. (2011) · Cancer Research · doi:10.1158/0008-5472.can-11-0896 · Cited by 236
Methylation of the Retinoblastoma Tumor Suppressor by SMYD2
Saddic, L., West, L. E., Aslanian, A., Yates, J. R., Rubin, S. M., Gozani, O., & Sage, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.137612 · Cited by 226
Histone Lysine Methyltransferase SETD8 Promotes Carcinogenesis by Deregulating PCNA Expression
Takawa, M., Cho, H., Hayami, S., Toyokawa, G., Kogure, M., Yamane, Y., Iwai, Y., Maejima, K., Ueda, K., Masuda, A., et al. (2012) · Cancer Research · doi:10.1158/0008-5472.can-11-3701 · Cited by 217
Self-citationHayami, S., Yoshimatsu, M., Veerakumarasivam, A., Unoki, M., Iwai, Y., Tsunoda, T., Field, H. I., Kelly, J. D., Neal, D. E., Yamaue, H., et al. (2010) · Molecular Cancer · doi:10.1186/1476-4598-9-59 · Cited by 212
Self-citationRB1 Methylation by SMYD2 Enhances Cell Cycle Progression through an Increase of RB1 Phosphorylation
Cho, H., Hayami, S., Toyokawa, G., Maejima, K., Yamane, Y., Suzuki, T., Dohmae, N., Kogure, M., Kang, D., Neal, D. E., et al. (2012) · Neoplasia · doi:10.1593/neo.12656 · Cited by 209
Self-citationJARID1B Is a Luminal Lineage-Driving Oncogene in Breast Cancer
Yamamoto, S., Wu, Z., Russnes, H. G., Takagi, S., Peluffo, G., Vaske, C. J., Zhao, X., Vollan, H. K. M., Maruyama, R., Ekram, M. B., et al. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.04.024 · Cited by 209
Structural Basis of Substrate Methylation and Inhibition of SMYD2
Ferguson, A. D., Larsen, N. A., Howard, T., Pollard, H., Green, I., Grande, C., Cheung, T., Garcia-Arenas, R., Cowen, S., Wu, J., et al. (2011) · Structure · doi:10.1016/j.str.2011.06.011 · Cited by 203
Abu‐Farha, M., Lambert, J., Madhoun, A. S. A., Elisma, F., Skerjanc, I. S., & Figeys, D. (2007) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m700271-mcp200 · Cited by 199
Dubuc, A. M., Remke, M., Korshunov, A., Northcott, P. A., Zhan, S. H., Méndez-Lago, M., Kool, M., Jones, D., Unterberger, A., Morrissy, A. S., et al. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-1070-9 · Cited by 197
Takawa, M., Masuda, K., Kunizaki, M., Daigo, Y., Takagi, K., Iwai, Y., Cho, H., Toyokawa, G., Yamane, Y., Maejima, K., et al. (2011) · Cancer Science · doi:10.1111/j.1349-7006.2011.01958.x · Cited by 194
Self-citationConcurrent loss of Ezh2 and Tet2 cooperates in the pathogenesis of myelodysplastic disorders
Muto, T., Sashida, G., Oshima, M., Wendt, G. R., Mochizuki‐Kashio, M., Nagata, Y., Sanada, M., Miyagi, S., Saraya, A., Kamio, A., et al. (2013) · The Journal of Experimental Medicine · doi:10.1084/jem.20131144 · Cited by 191
Ringrose, L., Ehret, H., & Paro, R. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.10.015 · Cited by 182
PARP inhibitors: its role in treatment of cancer
Chen, A. P. (2011) · 癌症:英文版 · doi:10.5732/cjc.011.10111 · Cited by 182
Kunizaki, M., Hamamoto, R., Pittella-Silva, F., Yamaguchi, K., Nagayasu, T., Shibuya, M., Nakamura, Y., & Furukawa, Y. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-1132 · Cited by 181
Self-citationKomatsu, S., Imoto, I., Tsuda, H., Kozaki, K.-I., Muramatsu, T., Shimada, Y., Aiko, S., Yoshizumi, Y., Ichikawa, D., Otsuji, E., et al. (2009) · Carcinogenesis · doi:10.1093/carcin/bgp116 · Cited by 175
Isolation of p53‐target genes and their functional analysis
Nakamura, Y. (2004) · Cancer Science · doi:10.1111/j.1349-7006.2004.tb03163.x · Cited by 173
Self-citationThe retinoblastoma tumor-suppressor gene, the exception that proves the rule
Goodrich, D. W. (2006) · Oncogene · doi:10.1038/sj.onc.1209616 · Cited by 170
Involvement of E2F transcription factor family in cancer
Tsantoulis, P. K., & Gorgoulis, V. G. (2005) · European Journal of Cancer · doi:10.1016/j.ejca.2005.08.005 · Cited by 166
Regulation of estrogen receptor α by histone methyltransferase SMYD2-mediated protein methylation
Zhang, X., Tanaka, K. Y., Yan, J., Li, J., Peng, D., Jiang, Y., Yang, Z., Barton, M. C., Wen, H., & Shi, X. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1307959110 · Cited by 165
Ezponda, T., Popovic, R., Shah, M. Y., Martinez-Garcia, E., Zheng, Y., Min, D.-J., Will, C., Neri, A., Kelleher, N. L., Yu, J., et al. (2013) · Oncogene · doi:10.1038/onc.2012.297 · Cited by 158
The methyltransferase G9a regulates HoxA9-dependent transcription in AMLPreprint
Lehnertz, B., Pabst, C., Yi, L.-Y., Miller, M., Liu, F., Yi, L., Zhang, R., Krošl, J., Yung, E., Kirschner, J., et al. (2014) · Genes & Development · doi:10.1101/gad.236794.113 · Cited by 156
Gossage, L., Murtaza, M., Slatter, A. F., Lichtenstein, C. P., Warren, A. Y., Haynes, B., Marass, F., Roberts, I., Shanahan, S. J., Claas, A., et al. (2013) · Genes Chromosomes and Cancer · doi:10.1002/gcc.22116 · Cited by 137
Oncogenic features of the JMJD2A histone demethylase in breast cancer
Berry, W. L., Shin, S., Lightfoot, S. A., & Janknecht, R. (2012) · International Journal of Oncology · doi:10.3892/ijo.2012.1618 · Cited by 132
Structural and Functional Profiling of the Human Histone Methyltransferase SMYD3
Foreman, K. W., Brown, M., Park, F., Emtage, S., Harriss, J. V., Das, C., Zhu, L., Crew, A., Arnold, L. D., Shaaban, S. A., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0022290 · Cited by 128
Klaus, C. R., Iwanowicz, D., Johnston, D., Campbell, C. T., Smith, J. J., Moyer, M. P., Copeland, R. A., Olhava, E. J., Scott, M. P., Pollock, R. M., et al. (2014) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.114.214577 · Cited by 128
Loss of heterozygosity in 7q myeloid disorders: clinical associations and genomic pathogenesis
Jerez, A., Sugimoto, Y., Makishima, H., Verma, A. K., Jankowska, A. M., Przychodzen, B. P., Visconte, V., Tiu, R. V., O’Keefe, C. L., Mohamedali, A. M., et al. (2012) · Blood · doi:10.1182/blood-2011-12-397620 · Cited by 127
Cho, H., Kelly, J. D., Hayami, S., Toyokawa, G., Takawa, M., Yoshimatsu, M., Tsunoda, T., Field, H. I., Neal, D. E., Ponder, B. A. J., et al. (2011) · Neoplasia · doi:10.1593/neo.11512 · Cited by 126
Self-citationCho, H., Shimazu, T., Toyokawa, G., Daigo, Y., Maehara, Y., Hayami, S., Ito, A., Masuda, K., Ikawa, N., Field, H. I., et al. (2012) · Nature Communications · doi:10.1038/ncomms2074 · Cited by 122
Self-citationConcurrent Alterations in TERT , KDM6A , and the BRCA Pathway in Bladder Cancer
Nickerson, M. L., Dancik, G. M., Im, K. M., Edwards, M. G., Turan, S., Brown, J., Ruiz-Rodriguez, C., Owens, C. R., Costello, J. C., Guo, G., et al. (2014) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-0330 · Cited by 120
Set9, NF-κB, and microRNA-21 mediate berberine-induced apoptosis of human multiple myeloma cells
Hu, H., Li, K., Wang, X., Liu, Y., Lu, Z., Dong, R., Guo, H., & Zhang, M. (2012) · Acta Pharmacologica Sinica · doi:10.1038/aps.2012.161 · Cited by 119
The Mitochondrial and Autosomal Mutation Landscapes of Prostate Cancer
Lindberg, J., Mills, I. G., Klevebring, D., Liu, W., Neiman, M., Xu, J., Wikström, P., Wiklund, P. N., Wiklund, F. E., Egevad, L., et al. (2012) · European Urology · doi:10.1016/j.eururo.2012.11.053 · Cited by 117
Carr, S. M., Munro, S., Kessler, B. M., Oppermann, U. C. T., & Thangue, N. B. L. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.311 · Cited by 115
Ene, C., Edwards, L., Riddick, G., Baysan, M. S., Woolard, K., Kotliarova, S. E., Lai, C., Belova, G. I., Cam, M. C., Walling, J., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0051407 · Cited by 115
Daze, K. D., & Hof, F. A. (2012) · Accounts of Chemical Research · doi:10.1021/ar300072g · Cited by 115
Ruault, M., Brun, M.-E., Ventura, M., Roizès, G., & Sario, A. D. (2002) · Gene · doi:10.1016/s0378-1119(02)00392-x · Cited by 113
Piao, L., Kang, D., Suzuki, T., Masuda, A., Dohmae, N., Nakamura, Y., & Hamamoto, R. (2014) · Neoplasia · doi:10.1016/j.neo.2014.03.002 · Cited by 110
Self-citationCritical role of lysine 134 methylation on histone H2AX for γ-H2AX production and DNA repair
Sone, K., Piao, L., Nakakido, M., Ueda, K., Jenuwein, T., Nakamura, Y., & Hamamoto, R. (2014) · Nature Communications · doi:10.1038/ncomms6691 · Cited by 109
Self-citationSasaki, M., Yamaguchi, J., Itatsu, K., Ikeda, H., & Nakanuma, Y. (2008) · The Journal of Pathology · doi:10.1002/path.2345 · Cited by 108
Zhao, L., Li, W., Zang, W., Liu, Z., Xu, X., Yu, H., Yang, Q., & Jia, J. (2013) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-0254 · Cited by 108
The Role of C/EBPβ in Mammary Gland Development and Breast Cancer
Grimm, S. L., & Rosen, J. M. (2003) · Journal of Mammary Gland Biology and Neoplasia · doi:10.1023/a:1025900908026 · Cited by 108
G9a-mediated Lysine Methylation Alters the Function of CCAAT/Enhancer-binding Protein-β
Pleß, O., Kowenz‐Leutz, E., Knoblich, M., Lausen, J., Beyermann, M., Walsh, M. J., & Leutz, A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802132200 · Cited by 107
Abdelrahim, M., Baker, C. H., Abbruzzese, J. L., Sheikh‐Hamad, D., Liu, S., Cho, S. D., Yoon, K., & Safe, S. H. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-3831 · Cited by 107
Shimazu, T., Barjau, J., Sohtome, Y., Sodeoka, M., & Shinkai, Y. (2014) · PLoS ONE · doi:10.1371/journal.pone.0105394 · Cited by 104
Deregulated expression of selected histone methylases and demethylases in prostate carcinoma
Vieira, F. Q., Costa‐Pinheiro, P., Ramalho-Carvalho, J., Faria‐Pereira, A., Menezes, F. D., Antunes, L., Carneiro, I. C., Oliveira, J., Henrique, R., & Jerónimo, C. (2013) · Endocrine Related Cancer · doi:10.1530/erc-13-0375 · Cited by 103
Zeng, B., Li, Z., Chen, R., Guo, N., Zhou, J., Zhou, Q., Lin, Q., Cheng, D., Liao, Q., Zheng, L., et al. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.06.049 · Cited by 101
Toyokawa, G., Cho, H., Masuda, K., Yamane, Y., Yoshimatsu, M., Hayami, S., Takawa, M., Iwai, Y., Daigo, Y., Tsuchiya, E., et al. (2011) · Neoplasia · doi:10.1593/neo.11048 · Cited by 101
Self-citationHamamoto, R., Toyokawa, G., Nakakido, M., Ueda, K., & Nakamura, Y. (2014) · Cancer Letters · doi:10.1016/j.canlet.2014.05.014 · Cited by 101
Self-citationKim, J., Kee, H. J., Choe, N., Kim, S., Eom, G.-H., Baek, H. J., Kook, H. Y., Kook, H., & Seo, S. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.02130-07 · Cited by 98
Histone trimethylation by Set1 is coordinated by the RRM, autoinhibitory, and catalytic domains
Schlichter, A., & Cairns, B. R. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600607 · Cited by 98
Cho, H., Toyokawa, G., Daigo, Y., Hayami, S., Masuda, K., Ikawa, N., Yamane, Y., Maejima, K., Tsunoda, T., Field, H. I., et al. (2011) · International Journal of Cancer · doi:10.1002/ijc.26501 · Cited by 97
Self-citationPang, C. N. I., Gasteiger, E., & Wilkins, M. R. (2010) · BMC Genomics · doi:10.1186/1471-2164-11-92 · Cited by 93
Targeting Tyrosine Phosphorylation of PCNA Inhibits Prostate Cancer Growth
Zhao, H., Lo, Y., Ma, L., Waltz, S. E., Gray, J. K., Hung, M., & Wang, S. (2011) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-10-0778 · Cited by 93
hSETD1A Regulates Wnt Target Genes and Controls Tumor Growth of Colorectal Cancer Cells
Salz, T., Li, G., Kaye, F. J., Zhou, L. J., Qiu, Y., & Huang, S. (2013) · Cancer Research · doi:10.1158/0008-5472.can-13-1400 · Cited by 88
STAT3, a Poor Survival Predicator, Is Associated with Lymph Node Metastasis from Breast Cancer
Chen, Y., Wang, J., Wang, X., Liu, X., Li, H., Lv, Q., Zhu, J., Wei, B., & Tang, Y. (2013) · Journal of Breast Cancer · doi:10.4048/jbc.2013.16.1.40 · Cited by 87
Expression and significance of histone H3K27 demethylases in renal cell carcinoma
Shen, Y., Guo, X., Wang, Y., Qiu, W., Chang, Y., Zhang, A., & Duan, X. (2012) · BMC Cancer · doi:10.1186/1471-2407-12-470 · Cited by 86
Zhong, X., Chen, X., Guan, X., Zhang, H., Ma, Y., Zhang, S., Wang, E., Zhang, L., & Han, Y. (2014) · Histopathology · doi:10.1111/his.12456 · Cited by 84
Yamada, D., Kobayashi, S., Yamamoto, H., Tomimaru, Y., Noda, T., Uemura, M., Wada, H., Marubashi, S., Eguchi, H., Tanemura, M., et al. (2011) · Annals of Surgical Oncology · doi:10.1245/s10434-011-1797-x · Cited by 83
Basavapathruni, A., Olhava, E. J., Daigle, S. R., Therkelsen, C. A., Jin, L., Boriack‐Sjodin, P. A., Allain, C. J., Klaus, C. R., Raimondi, A., Scott, M. P., et al. (2014) · Biopharmaceutics & Drug Disposition · doi:10.1002/bdd.1889 · Cited by 79
Kang, D., Cho, H., Toyokawa, G., Kogure, M., Yamane, Y., Iwai, Y., Hayami, S., Tsunoda, T., Field, H. I., Matsuda, K., et al. (2012) · Genes Chromosomes and Cancer · doi:10.1002/gcc.22012 · Cited by 78
Self-citationKim, S. M., Kee, H. J., Eom, G. H., Choe, N., Kim, J. Y., Kim, Y. S., Kim, S. K., Kook, H., Kook, H. Y., & Seo, S. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.04.095 · Cited by 74
Knockdown of SMYD3 by RNA interference inhibits cervical carcinoma cell growth and invasion in vitro
Wang, S., Luo, X., Shen, J., Zou, J.-N., Lu, Y.-H., & Xi, T. (2008) · BMB Reports · doi:10.5483/bmbrep.2008.41.4.294 · Cited by 72
Toyokawa, G., Cho, H., Iwai, Y., Yoshimatsu, M., Takawa, M., Hayami, S., Maejima, K., Shimizu, N., Tanaka, H., Tsunoda, T., et al. (2011) · Cancer Prevention Research · doi:10.1158/1940-6207.capr-11-0290 · Cited by 71
Self-citationKogure, M., Takawa, M., Cho, H., Toyokawa, G., Hayashi, K., Tsunoda, T., Kobayashi, T., Daigo, Y., Sugiyama, M., Atomi, Y., et al. (2013) · Cancer Letters · doi:10.1016/j.canlet.2013.04.009 · Cited by 71
Self-citationLysine methylation of promoter-bound transcription factors and relevance to cancer
Stark, G. R., Wang, Y., & Lu, T. (2010) · Cell Research · doi:10.1038/cr.2010.174 · Cited by 69
Sponziello, M., Durante, C., Boichard, A., Dima, M., Puppin, C., Verrienti, A., Tamburrano, G., Rocco, G. D., Redler, A., Lacroix, L., et al. (2014) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2014.04.016 · Cited by 64
Pittella-Silva, F., Hamamoto, R., Kunizaki, M., Tsuge, M., Nakamura, Y., & Furukawa, Y. (2007) · Oncogene · doi:10.1038/sj.onc.1210929 · Cited by 64
Self-citationDepletion of JARID1B induces cellular senescence in human colorectal cancer
Ohta, K., Haraguchi, N., KANO, Y., Kagawa, Y., Konno, M., Nishikawa, S., Hamabe, A., Hasegawa, S., Ogawa, H., Fukusumi, T., et al. (2013) · International Journal of Oncology · doi:10.3892/ijo.2013.1799 · Cited by 61
Somatic Mutations of the Mixed-Lineage Leukemia 3 (MLL3) Gene in Primary Breast Cancers
Wang, X.-X., Fu, L., Li, X., Wu, X., Zhu, Z., Fu, L., & Dong, J.-T. (2010) · Pathology & Oncology Research · doi:10.1007/s12253-010-9316-0 · Cited by 55
The Expression of Histone Demethylase JMJD1A in Renal Cell Carcinoma
Guo, X., SHI, M., Sun, L.-G., WANG, Y., Gui, Y., Cai, Z., & DUAN, X. (2011) · Neoplasma · doi:10.4149/neo_2011_02_153 · Cited by 55
Zhang, H., Tang, H., Shao, H., Gao, C., Hylander, B. L., Repasky, E. A., Dy, G. K., Ma, W. W., Yu, C., & Adjei, A. A. (2011) · Cancer Research · doi:10.1158/1538-7445.am2011-1 · Cited by 51
JMJD2A predicts prognosis and regulates cell growth in human gastric cancer
Hu, C., Liu, Y.-C., Zhang, H., & Huang, G. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.04.126 · Cited by 49
Role of lysine methylation of NF-κB in differential gene regulation
Lu, T., Yang, M., Huang, D.-B., Han, W., Ozer, G. H., Ghosh, G., & Stark, G. R. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1311770110 · Cited by 49
Natarajan, T. G., Kallakury, B., Sheehan, C. E., Bartlett, M. B., Ganesan, N., Preet, A., Ross, J. S., & Fitzgerald, K. T. (2010) · Cancer Cell International · doi:10.1186/1475-2867-10-13 · Cited by 49
A Role for DOT1L in MLL -Rearranged Leukemias
Bernt, K. M., & Armstrong, S. A. (2011) · Epigenomics · doi:10.2217/epi.11.98 · Cited by 46
Yin, S., Yang, J., Lin, B., Deng, W., Zhang, Y., Yi, X., Shi, Y., Tao, Y., Cai, J., Wu, C., et al. (2014) · Scientific Reports · doi:10.1038/srep06036 · Cited by 42
Guo, N., Chen, R., Li, Z., Liu, Y., Cheng, D., Zhou, Q., Zhou, J., & Lin, Q. (2011) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmr021 · Cited by 41
Chen, L., Fu, L. N., Kong, X., Xu, J., Wang, Z., Ma, X., Akiyama, Y., Chen, Y., & Fang, J. (2014) · British Journal of Cancer · doi:10.1038/bjc.2013.808 · Cited by 40
Panarello, C., Rosanda, C., & Morerio, C. (2002) · Genes Chromosomes and Cancer · doi:10.1002/gcc.10119 · Cited by 39
Kogure, M., Takawa, M., Saloura, V., Sone, K., Piao, L., Ueda, K., Ibrahim, R., Tsunoda, T., Sugiyama, M., Atomi, Y., et al. (2013) · Neoplasia · doi:10.1593/neo.131436 · Cited by 38
Self-citationThe NSD3L histone methyltransferase regulates cell cycle and cell invasion in breast cancer cells
Zhou, Z., Thomsen, R., Kahns, S., & Nielsen, A. L. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.06.119 · Cited by 38
Jumonji/Arid1b (Jarid1b) protein modulates human esophageal cancer cell growth
KANO, Y., Konno, M., Ohta, K., Haraguchi, N., Nishikawa, S., Kagawa, Y., Hamabe, A., Hasegawa, S., Ogawa, H., Fukusumi, T., et al. (2013) · Molecular and Clinical Oncology · doi:10.3892/mco.2013.127 · Cited by 32
Dong, S., Zhang, H., Wang, B., Sun, P., Wang, Y.-G., & Zhang, P. (2014) · Oncology Reports · doi:10.3892/or.2014.3307 · Cited by 30
Sun, B., Fu, L. N., Wang, Y. Q., Gao, Q., Xu, J., Cao, Z. J., Chen, Y., & Fang, J. (2014) · Journal of Digestive Diseases · doi:10.1111/1751-2980.12166 · Cited by 28
Recognition of methylated histones: new twists and variations
Khorasanizadeh, S. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.10.001 · Cited by 26
Association of MLL3 expression with prognosis in gastric cancer
Li, B., Liu, H. Y., Guo, S., Sun, P., Gong, F.-M., & Jia, B. (2014) · Genetics and Molecular Research · doi:10.4238/2014.september.12.18 · Cited by 25
Xia, M., Xu, L., Leng, Y., Gao, F., Hong, X., Zhang, D., & Ding, X. (2014) · Tumor Biology · doi:10.1007/s13277-014-2616-3 · Cited by 22
Wittmann, V. (2001) · Springer eBooks · doi:10.1007/978-3-642-56874-9_54 · Cited by 21
Expression and Effects of JMJD2A Histone Demethylase in Endometrial Carcinoma
Wang, H., Liu, M., Ma, X., Fang, L., Zhang, Z., Song, T., Gao, J., Kuang, Y., Jiang, J., Li, L., et al. (2014) · Asian Pacific Journal of Cancer Prevention · doi:10.7314/apjcp.2014.15.7.3051 · Cited by 19
JARID1B Protein Expression and Prognostic Implications in Uveal Melanoma
Radberger, P., Radberger, A., Bykov, V. J. N., Seregard, S., & Economou, M. A. (2012) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.11-9296 · Cited by 18
Flagged first, then by citations
1 of the 167 references couldn’t be matched to a known paper.
Research works printed but not linked: 1
- Clarke, S. G. & Tamanoi, F. (eds) The Enzymes: Protein Methyltransferases Vol. 24 (Academic Press, 2006).
Cited by
Sorted by citations
Control of protein stability by post-translational modifications
Lee, J. M., Hammarén, H. M., Savitski, M. M., & Baek, S. H. (2023) · Nature Communications · doi:10.1038/s41467-023-35795-8 · Cited by 896
The roles of DNA, RNA and histone methylation in ageing and cancer
Michalak, E. M., Burr, M. L., Bannister, A. J., & Dawson, M. A. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0143-1 · Cited by 549
Wu, Z., Liu, G.-Q., Yang, X., & Jiang, J. (2015) · Journal of the American Chemical Society · doi:10.1021/jacs.5b01778 · Cited by 345
Regulation of the p53 response and its relationship to cancer
Meek, D. W. (2015) · Biochemical Journal · doi:10.1042/bj20150517 · Cited by 311
Lüscher, B., Bütepage, M., Eckei, L., Krieg, S., Verheugd, P., & Shilton, B. H. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00122 · Cited by 264
Metadata
- Authors
- Hamamoto, R., Saloura, V., & Nakamura, Y.
- Affiliations
- University of Chicago (US)
- Corresponding author
- Hamamoto, Ryuji
- Venue
- Nature Reviews Cancer
- Published
- 2015-01-23
- Volume
- 15
- Issue
- 2
- Pages
- 110-124
- ISSN
- 1474-175X (ISSN-L)
- 1474-1768
- OpenAlex
- W2036357556
- Cited by
- 376
- References
- 167
- Citations by year
- 2026: 14 · 2025: 20 · 2024: 27 · 2023: 29 · 2022: 36 · 2021: 30 · 2020: 39 · 2019: 38 · 2018: 33 · 2017: 38 · 2016: 49 · 2015: 22
- FWCI
- 4.69
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature reviews. Cancer (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer-related gene regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
- Keywords
- carcinogenesis, p53, RB1, STAT3, lysine methyltransferase, demethylases, cancer therapy targets, histone modifications
- MeSH terms
- Cell Transformation, Neoplastic, Chromosomal Proteins, Non-Histone, Humans, Lysine, Methylation, Histone-Lysine N-Methyltransferase, Tumor Suppressor Protein p53, Retinoblastoma Protein, STAT3 Transcription Factor
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review