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JmjC-domain-containing proteins and histone demethylation
Abstract
Histone methylation has important roles in regulating gene expression and forms part of the epigenetic memory system that regulates cell fate and identity. Enzymes that directly remove methyl marks from histones have recently been identified, revealing a new level of plasticity within this epigenetic modification system. Here we analyse the evolutionary relationship between Jumonji C (JmjC)-domain-containing proteins and discuss their cellular functions in relation to their potential enzymatic activities.
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“whilst several epigenetic therapies targeting the prototypical oncogene MYC through transcriptional repression generated much excitement, it is now clear that this is only transiently effective as cancer cells evolve multiple adaptive responses to retain MYC expression 184-186 .”
From The roles of DNA, RNA and histone methylation in ageing and cancer (2019) · cites this paper as [185]
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“Preclinical modelling of resistance mechanisms has shown that resistance to these therapies largely emerge through cellular reprogramming and transcriptional plasticity 184-186 .”
From The roles of DNA, RNA and histone methylation in ageing and cancer (2019) · cites this paper as [185]
Citations
Cites
MrBayes 3: Bayesian phylogenetic inference under mixed models
Ronquist, F., & Huelsenbeck, J. P. (2003) · Bioinformatics · doi:10.1093/bioinformatics/btg180 · Cited by 29,194
MRBAYES: Bayesian inference of phylogenetic trees.
Huelsenbeck, J. P., & Ronquist, F. (2001) · Bioinformatics · doi:10.1093/bioinformatics/17.8.754 · Cited by 21,937
The Pfam Protein Families Database
Bateman, A. G. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.1.276 · Cited by 14,075
MEGA3: Integrated software for Molecular Evolutionary Genetics Analysis and sequence alignment
Kumar, S. (2004) · Briefings in Bioinformatics · doi:10.1093/bib/5.2.150 · Cited by 11,674
Multiple sequence alignment with hierarchical clustering.
Corpet, F. (1988) · Nucleic Acids Research · doi:10.1093/nar/16.22.10881 · Cited by 5,575
Multiple sequence alignment with the Clustal series of programs
Chenna, R. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg500 · Cited by 4,905
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
SMART, a simple modular architecture research tool: Identification of signaling domains
Schultz, J., Milpetz, F., Peer Bork, B., & Ponting, C. P. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.5857 · Cited by 3,577
The Pfam protein families database
Bateman, A. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh121 · Cited by 3,127
Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain
Bannister, A. J., Zegerman, P., Partridge, J. F., Miska, E. A., Thomas, J. O., Allshire, R. C., & Kouzarides, T. (2001) · Nature · doi:10.1038/35065138 · Cited by 2,903
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Sundar, I. K., Yao, H., & Rahman, I. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4863 · Cited by 201
Dietrich, N., Bracken, A. P., Trinh, E., Schjerling, C. K., Koseki, H., Rappsilber, J., Helin, K., & Hansen, K. H. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601632 · Cited by 187
Targeting histone lysine demethylases — Progress, challenges, and the future
Thinnes, C. C., England, K. S., Kawamura, A., Chowdhury, R., Schofield, C. J., & Hopkinson, R. J. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.05.009 · Cited by 198
Gan, E., Xu, Y., Wong, J. Y., Goh, J. G., Sun, B., Wee, W.-Y., Huang, J., & Ito, T. (2014) · Nature Communications · doi:10.1038/ncomms6098 · Cited by 186
Targeting Histone Demethylases: A New Avenue for the Fight against Cancer
Rotili, D., & Mai, A. (2011) · Genes & Cancer · doi:10.1177/1947601911417976 · Cited by 201
The Genomes of Three Uneven Siblings: Footprints of the Lifestyles of Three Trichoderma Species
Schmoll, M., Dattenböck, C., Carreras-Villaseñor, N., Mendoza‐Mendoza, A., Tisch, D., Alemán-Duarte, M. I., Baker, S., Brown, C. M., Cervantes-Badillo, M. G., Cetz-Chel, J. E., et al. (2016) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00040-15 · Cited by 197
Recent Progress in Histone Demethylase Inhibitors
McAllister, T. E., England, K. S., Hopkinson, R. J., Brennan, P. E., Kawamura, A., & Schofield, C. J. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01758 · Cited by 192
A Systematic Review of Histone Lysine‐Specific Demethylase 1 and Its Inhibitors
Zheng, Y., Ma, J., Wang, Z., Li, J., Jiang, B., Zhou, W., Shi, X., Wang, X., Zhao, W., & Liu, H. (2015) · Medicinal Research Reviews · doi:10.1002/med.21350 · Cited by 196
Targeting histone lysine methylation in cancer
McGrath, J. P., & Trojer, P. (2015) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2015.01.002 · Cited by 190
Demethylation of trimethylated histone H3 Lys4 in vivo by JARID1 JmjC proteins
Seward, D. J., Cubberley, G., Kim, S., Schonewald, M., Zhang, L., Tripet, B., & Bentley, D. L. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1200 · Cited by 185
A Histone Methylation Network Regulates Transgenerational Epigenetic Memory in C. elegans
Greer, E. L., Beese‐Sims, S. E., Brookes, E., Spadafora, R., Zhu, Y., Rothbart, S. B., Aristizábal-Corrales, D., Chen, S., Badeaux, A. I., Jin, Q., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.02.044 · Cited by 192
Obesity and metabolic syndrome in histone demethylase JHDM2a‐deficient mice
Inagaki, T., Tachibana, M., Magoori, K., Kudo, H., Tanaka, T., Okamura, M., Naito, M., Kodama, T., Shinkai, Y., & Sakai, J. (2009) · Genes to Cells · doi:10.1111/j.1365-2443.2009.01326.x · Cited by 183
Protein Hydroxylation Catalyzed by 2-Oxoglutarate-dependent Oxygenases
Markolovic, S., Wilkins, S. E., & Schofield, C. J. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.662627 · Cited by 181
Klein, B. J., Piao, L., Xi, Y., Rincón‐Arano, H., Rothbart, S. B., Peng, D., Wen, H., Larson, C., Zhang, X., Xia, Z., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2013.12.021 · Cited by 181
de Groote, M. L., Verschure, P. J., & Rots, M. G. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks863 · Cited by 180
Structural insights into histone lysine demethylation
Hou, H., & Yu, H. (2010) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2010.09.006 · Cited by 179
Functional coupling between writers, erasers and readers of histone and DNA methylation
Torres, I. O., & Fujimori, D. G. (2015) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2015.09.007 · Cited by 185
The Role of DNA Methylation in the Central Nervous System and Neuropsychiatric Disorders
Feng, J., & Fan, G. (2009) · International review of neurobiology · doi:10.1016/s0074-7742(09)89004-1 · Cited by 179
Reprogramming of cell fate: epigenetic memory and the erasure of memories past
Nashun, B., Hill, P. W. S., & Hájková, P. (2015) · The EMBO Journal · doi:10.15252/embj.201490649 · Cited by 184
Hillringhaus, L., Yue, W. W., Rose, N. R., Ng, S. S., Gileadi, C., Loenarz, C., Bello, S. H., Bray, J. E., Schofield, C. J., & Oppermann, U. C. T. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.283689 · Cited by 183
Labbé, D. P., Zadra, G., Yang, M., Reyes, J. M., Lin, C. Y., Cacciatore, S., Ebot, E. M., Creech, A. L., Giunchi, F., Fiorentino, M., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-12298-z · Cited by 174
Histone modifications and chromatin dynamics: a focus on filamentous fungi
Brosch, G., Loidl, P., & Graessle, S. (2008) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2007.00100.x · Cited by 180
Connections between metabolism and epigenetics in cancers
Thakur, C., & Chen, F. (2019) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2019.06.006 · Cited by 176
The Emerging Therapeutic Potential of Histone Methyltransferase and Demethylase Inhibitors
Spannhoff, A., Hauser, A., Heinke, R., Sippl, W., & Jung, M. (2009) · ChemMedChem · doi:10.1002/cmdc.200900301 · Cited by 177
Succinate inhibition of α-ketoglutarate-dependent enzymes in a yeast model of paraganglioma
Smith, E. H., Janknecht, R., & Maher, L. J. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm275 · Cited by 169
Epigenetic Regulation by Lysine Demethylase 5 (KDM5) Enzymes in Cancer
Blair, L. P., Cao, J. P., Zou, M. R., Sayegh, J., & Yan, Q. (2011) · Cancers · doi:10.3390/cancers3011383 · Cited by 172
Pfannenstiel, B. T., & Keller, N. P. (2019) · Biotechnology Advances · doi:10.1016/j.biotechadv.2019.02.001 · Cited by 176
Lysine Demethylase KDM6A in Differentiation, Development, and Cancer
Tran, N., Broun, A., & Ge, K. (2020) · Molecular and Cellular Biology · doi:10.1128/mcb.00341-20 · Cited by 170
Hamada, S., Suzuki, T., Mino, K., Koseki, K., Oehme, F., Flamme, I., Ozasa, H., Itoh, Y., Ogasawara, D., Komaarashi, H., et al. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm1003655 · Cited by 166
The Roles of Jumonji-Type Oxygenases in Human Disease
Johansson, C., Tumber, A., Che, K., Cain, P., Nowak, R. P., Gileadi, C., & Oppermann, U. C. T. (2014) · Epigenomics · doi:10.2217/epi.13.79 · Cited by 167
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Han, P., Hang, C. T., Yang, J., & Chang, C. (2011) · Circulation Research · doi:10.1161/circresaha.110.224287 · Cited by 168
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Seok, H., Chen, J., Kataoka, M., Huang, Z., Ding, J., Yan, J., Hu, X., & Wang, D.-Z. (2014) · Circulation Research · doi:10.1161/circresaha.114.303784 · Cited by 167
Epigenetic Regulation by Histone Demethylases in Hypoxia
Hancock, R. L., Dunne, K., Walport, L. J., Flashman, E., & Kawamura, A. (2015) · Epigenomics · doi:10.2217/epi.15.24 · Cited by 162
Kaelin, W. G. (2011) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2011.76.010975 · Cited by 161
The control of histone methylation and gene expression by oxidative stress, hypoxia, and metals
Chervona, Y., & Costa, M. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.07.020 · Cited by 163
Sinha, K. M., Yasuda, H., Coombes, M. M., Dent, S., & Crombrugghe, B. D. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.332 · Cited by 160
KDM7 is a dual demethylase for histone H3 Lys 9 and Lys 27 and functions in brain development
Tsukada, Y.-I., Ishitani, T., & Nakayama, K. I. (2010) · Genes & Development · doi:10.1101/gad.1864410 · Cited by 158
The role of phosphatidylserine recognition receptors in multiple biological functions
Naeini, M. B., Bianconi, V., Pirro, M., & Sahebkar, A. (2020) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-020-00214-z · Cited by 163
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Cvekl, A., & Duncan, M. K. (2007) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2007.07.002 · Cited by 162
Two SET domain containing genes link epigenetic changes and aging in Caenorhabditis elegans
Ni, Z., Ebata, A., Alipanahiramandi, E., & Lee, S. S. (2011) · Aging Cell · doi:10.1111/j.1474-9726.2011.00785.x · Cited by 155
Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans
Ge, W., Wolf, A., Feng, T., Ho, C.-H., Sekirnik, R., Zayer, A., Granatino, N., Cockman, M. E., Loenarz, C., Loik, N. D., et al. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.1093 · Cited by 154
Gene expression in the placenta: maternal stress and epigenetic responses
Gheorghe, C. P., Goyal, R., Mittal, A., & Longo, L. D. (2009) · The International Journal of Developmental Biology · doi:10.1387/ijdb.082770cg · Cited by 156
Wen, H., Li, J., Song, T., Lu, M., Kan, P., Lee, M. G., Sha, B., & Shi, X. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.c109.097667 · Cited by 160
Oxidative Stress Under Ambient and Physiological Oxygen Tension in Tissue Culture
Jagannathan, L., Cuddapah, S., & Costa, M. (2016) · Current Pharmacology Reports · doi:10.1007/s40495-016-0050-5 · Cited by 161
Understanding histone H3 lysine 36 methylation and its deregulation in disease
Li, J., Ahn, J. H., & Wang, G. G. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03144-y · Cited by 155
Characterization of human epigenomes
Wang, Z., Schones, D. E., & Zhao, K. (2009) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2009.02.001 · Cited by 160
Highly selective inhibition of histone demethylases by de novo macrocyclic peptides
Kawamura, A., Münzel, M., Kojima, T., Yapp, C., Bhushan, B., Goto, Y., Tumber, A., Katoh, T., King, O. N. F., Passioura, T., et al. (2017) · Nature Communications · doi:10.1038/ncomms14773 · Cited by 153
Khoury-Haddad, H., Guttmann‐Raviv, N., Ipenberg, I., Huggins, D. J., Jeyasekharan, A. D. D., & Ayoub, N. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1317585111 · Cited by 148
Histone lysine methyltransferases and demethylases in Plasmodium falciparum
Cui, L., Fan, Q., Cui, L., & Miao, J. (2008) · International Journal for Parasitology · doi:10.1016/j.ijpara.2008.01.002 · Cited by 158
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Burchfield, J. S., Li, Q., Wang, H. Y., & Wang, R. (2015) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2015.07.006 · Cited by 160
Rose, N. R., Woon, E. C. Y., Kingham, G. L., King, O. N. F., Mecinović, J., Clifton, I. J., Ng, S. S., Talib-Hardy, J., Oppermann, U. C. T., McDonough, M. A., et al. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm901680b · Cited by 148
Lysine Demethylases Inhibitors
Suzuki, T., & Miyata, N. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm201048w · Cited by 146
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Breathing-in epigenetic change with vitamin C
Monfort, A., & Wutz, A. (2013) · The EMBO Reports · doi:10.1038/embor.2013.29 · Cited by 140
FLC or not FLC: the other side of vernalization
Alexandre, C. M., & Hennig, L. (2008) · Journal of Experimental Botany · doi:10.1093/jxb/ern070 · Cited by 140
Deveson, I. W., Holleley, C. E., Blackburn, J., Marshall Graves, J. A., Mattick, J. S., Waters, P. D., & Georges, A. (2017) · Science Advances · doi:10.1126/sciadv.1700731 · Cited by 132
“K. Williams, J. Christensen, J. Rappsilber, A. L. Nielsen, J. V. Johansen, K. Helin, The histone lysine demethylase JMJD3/KDM6B is recruited to p53 bound promoters and enhancer elements in a p53 dependent manner.”
BackgroundInfluentialA plant-specific histone H3 lysine 4 demethylase represses the floral transition in Arabidopsis
Yang, W., Jiang, D., Jiang, J., & He, Y. (2010) · The Plant Journal · doi:10.1111/j.1365-313x.2010.04182.x · Cited by 136
Salminen, A., Kauppinen, A., Hiltunen, M. O., & Kaarniranta, K. (2014) · Ageing Research Reviews · doi:10.1016/j.arr.2014.05.004 · Cited by 145
Germ cell specification in mice: signaling, transcription regulation, and epigenetic consequences
Saitou, M., & Yamaji, M. (2010) · Reproduction · doi:10.1530/rep-10-0043 · Cited by 140
Mould, D. P., McGonagle, A. E., Wiseman, D. H., Williams, E. L., & Jordan, A. M. (2014) · Medicinal Research Reviews · doi:10.1002/med.21334 · Cited by 138
Daskalaki, M., Tsatsanis, C., & Kampranis, S. C. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.26497 · Cited by 139
Understanding the interplay between CpG island-associated gene promoters and H3K4 methylation
Hughes, A. L., Kelley, J. R., & Klose, R. J. (2020) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2020.194567 · Cited by 139
Self-citationControl of Cyclin D1 and Breast Tumorigenesis by the EglN2 Prolyl Hydroxylase
Zhang, Q. H., Gu, J., Li, L., Liu, J., Luo, B., Cheung, H.-W., Boehm, J. S., Ni, M., Geisen, C., Root, D. E., et al. (2009) · Cancer Cell · doi:10.1016/j.ccr.2009.09.029 · Cited by 141
Buffet, A., Morin, A., Castro‐Vega, L. J., Habarou, F., Lussey‐Lepoutre, C., Letouzé, É., Lefèbvre, H., Guilhem, I., Haissaguerre, M., Raingeard, I., et al. (2018) · Cancer Research · doi:10.1158/0008-5472.can-17-2463 · Cited by 137
Autocatalytic differentiation of epigenetic modifications within the Arabidopsis genome
Inagaki, S., Miura-Kamio, A., Nakamura, Y., Lu, F., Cui, X., Cao, X., Kimura, H., Saze, H., & Kakutani, T. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.227 · Cited by 145
Frescas, D., Guardavaccaro, D., Kuchay, S., Kato, H., Poleshko, A. S., Basrur, V., Elenitoba‐Johnson, K. S. J., Katz, R. A., & Pagano, M. (2008) · Cell Cycle · doi:10.4161/cc.7.22.7062 · Cited by 135
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Carr, A. C., & Cook, J. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.01182 · Cited by 133
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Sun, X.-J., Xu, P.-F., Zhou, T., Hu, M., Fu, C.-T., Zhang, Y., Jin, Y., Chen, Y., Chen, S.-J., Huang, Q.-H., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001499 · Cited by 127
Self-citationYeast Jhd2p is a histone H3 Lys4 trimethyl demethylase
Liang, G., Klose, R. J., Gardner, K. E., & Zhang, Y. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1204 · Cited by 131
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Chen, X., Hu, Y., & Zhou, D. (2011) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2011.03.004 · Cited by 137
Chatting histone modifications in mammals
Izzo, A., & Schneider, R. (2010) · Briefings in Functional Genomics · doi:10.1093/bfgp/elq024 · Cited by 136
Yang, H., Han, Z., Cao, Y., Fan, D., Li, H., Mo, H., Feng, Y., Liu, L., Zheng, W., Yue, Y., et al. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002664 · Cited by 129
Teven, C. M., Liu, X., Hu, N., Tang, N., Kim, S. H., Huang, E., Yang, K., Li, M., Gao, J., Liu, H., et al. (2011) · Stem Cells International · doi:10.4061/2011/201371 · Cited by 130
Histone lysine demethylase (KDM) subfamily 4: structures, functions and therapeutic potential.
Labbe, R. M., Holowatyj, A., & Yang, Z.-Q. (2013) · Europe PMC (PubMed Central) · Cited by 127
Pharmacological targeting of the HIF hydroxylases – A new field in medicine development
Chan, M. C., Holt‐Martyn, J. P., Schofield, C. J., & Ratcliffe, P. J. (2016) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2016.01.001 · Cited by 128
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Pereira, F., Barbáchano, A., Singh, P. K., Campbell, M. J., Múñoz, A., & Larriba, M. J. (2012) · Cell Cycle · doi:10.4161/cc.11.6.19508 · Cited by 121
Dutta, A., Choudhary, P., Caruana, J. C., & Raina, R. (2017) · The Plant Journal · doi:10.1111/tpj.13623 · Cited by 124
Searle, I. R., Pontes, O., Melnyk, C. W., Smith, L. M., & Baulcombe, D. C. (2010) · Genes & Development · doi:10.1101/gad.579910 · Cited by 124
Confining euchromatin/heterochromatin territory: jumonji crosses the line
Tamaru, H. (2010) · Genes & Development · doi:10.1101/gad.1941010 · Cited by 118
Gan, Q., Chepelev, I., Wei, G., Tarayrah, L., Cui, K., Zhao, K., & Chen, X. (2010) · Cell Research · doi:10.1038/cr.2010.64 · Cited by 123
Toh, J. D. W., Sun, L., Lau, L. Z. M., Tan, J., Low, J. J. A., Tang, C. W. Q., Cheong, E. J. Y., Tan, M. J. H., Chen, Y., Hong, W., et al. (2014) · Chemical Science · doi:10.1039/c4sc02554g · Cited by 125
Shevchenko, A., Roguev, A., Schaft, D., Buchanan, L., Habermann, B. H., Şakalar, Ç., Thomas, H., Krogan, N. J., Shevchenko, A., & Stewart, A. F. (2008) · Genome biology · doi:10.1186/gb-2008-9-11-r167 · Cited by 129
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Xhabija, B., & Kidder, B. L. (2018) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2018.11.001 · Cited by 120
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Huang, C., Xiang, Y., Wang, Y., Li, X., Xu, L., Zhu, Z., Zhang, T., Zhu, Q., Zhang, K., Jing, N., et al. (2010) · Cell Research · doi:10.1038/cr.2010.5 · Cited by 123
JMJD3 in the regulation of human diseases
Zhang, X., Liu, L., Yuan, X., Wei, Y., & Wei, X. (2019) · Protein & Cell · doi:10.1007/s13238-019-0653-9 · Cited by 123
Redox Control in Mammalian Embryo Development
Ufer, C., Wang, C. C., Borchert, A., Heydeck, D., & Kühn, H. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.3044 · Cited by 121
Reprogramming the epigenome with vitamin C
Lee Chong, T., Ahearn, E. L., & Cimmino, L. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00128 · Cited by 120
Epigenetic regulation: methylation of histone and non-histone proteins
Lan, F., & Shi, Y. (2009) · Science in China Series C Life Sciences · doi:10.1007/s11427-009-0054-z · Cited by 130
PHF8 Targets Histone Methylation and RNA Polymerase II To Activate Transcription
Fortschegger, K., de Graaf, P., Outchkourov, N. S., van Schaik, F. M. A., Timmers, H. T. M., & Shiekhattar, R. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01520-09 · Cited by 119
Pfau, R., Tzatsos, A., Kampranis, S. C., Serebrennikova, O. B., Bear, S. E., & Tsichlis, P. N. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711865105 · Cited by 119
Structural and Functional Coordination of DNA and Histone MethylationPreprint
Cheng, X. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a018747 · Cited by 125
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Metadata
- Authors
- Klose, R. J., Kallin, E. M., & Zhang, Y.
- Affiliations
- University of North Carolina at Chapel Hill (US)
- Corresponding author
- Zhang, Yi
- Venue
- Nature Reviews Genetics
- Published
- 2006-09
- Volume
- 7
- Issue
- 9
- Pages
- 715-727
- ISSN
- 1471-0056 (ISSN-L)
- 1471-0064
- OpenAlex
- W1982409009
- Cited by
- 1,290
- References
- 106
- Citations by year
- 2026: 40 · 2025: 47 · 2024: 53 · 2023: 69 · 2022: 57 · 2021: 83 · 2020: 64 · 2019: 73 · 2018: 84 · 2017: 58 · 2016: 66 · 2015: 83 · 2014: 80 · 2013: 57 · 2012: 68
- FWCI
- 4.01
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Genetics (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer-related gene regulation
- Keywords
- Jumonji C domain, histone demethylation, histone methylation, chromatin modification, epigenetic inheritance, protein evolution, gene expression regulation
- MeSH terms
- Histone Methyltransferases, Amino Acid Sequence, Animals, Gene Expression Regulation, Histones, Humans, Molecular Sequence Data, Nuclear Proteins, Oxidoreductases, N-Demethylating, Phylogeny, Histone-Lysine N-Methyltransferase, Protein Methyltransferases, Transcription, Genetic, Sequence Alignment, Protein Structure, Tertiary, Amino Acid Motifs, Epigenesis, Genetic
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