The DOI matches its Crossref record; 137 of the 138 references it cites were found in a registry or an index.
Non-histone protein methylation as a regulator of cellular signalling and function
Abstract
Methylation of Lys and Arg residues on non-histone proteins has emerged as a prevalent post-translational modification and as an important regulator of cellular signal transduction mediated by the MAPK, WNT, BMP, Hippo and JAK-STAT signalling pathways. Crosstalk between methylation and other types of post-translational modifications, and between histone and non-histone protein methylation frequently occurs and affects cellular functions such as chromatin remodelling, gene transcription, protein synthesis, signal transduction and DNA repair. With recent advances in proteomic techniques, in particular mass spectrometry, the stage is now set to decode the methylproteome and define its functions in health and disease.
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 effect may even be trans -acting, as exemplified by m6A in Xist RNA that is required for it to mediate transcriptional repression 40 .”
From The roles of DNA, RNA and histone methylation in ageing and cancer (2019) · cites this paper as [40]
In the citing paper
“Thus far the tumour-intrinsic mechanisms of resistance appear to be quite different to the paradigm of acquired resistance reported for other targeted therapies such as kinase inhibitors 188 .”
From The roles of DNA, RNA and histone methylation in ageing and cancer (2019) · cites this paper as [188]
Citations
Cites
The language of covalent histone modifications
Strahl, B. D., & Allis, C. D. (2000) · Nature · doi:10.1038/47412 · Cited by 8,679
Massagué, J. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.753 · Cited by 7,571
Mass spectrometry-based proteomics
Aebersold, R., & Mann, M. (2003) · Nature · doi:10.1038/nature01511 · Cited by 6,955
High-Resolution Profiling of Histone Methylations in the Human Genome
Barski, A., Cuddapah, S., Cui, K., Roh, T.-Y., Schones, D. E., Wang, Z., Wei, G., Chepelev, I., & Zhao, K. (2007) · Cell · doi:10.1016/j.cell.2007.05.009 · Cited by 6,845
Regulation of chromatin by histone modifications
Bannister, A. J., & Kouzarides, T. (2011) · Cell Research · doi:10.1038/cr.2011.22 · Cited by 6,012
The Nuclear Factor NF- B Pathway in InflammationPreprint
Lawrence, T. (2009) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a001651 · Cited by 5,126
Mdm2 promotes the rapid degradation of p53
Haupt, Y., Maya, R., Kazaz, A., & Oren, M. (1997) · Nature · doi:10.1038/387296a0 · Cited by 4,506
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
Role of Histone H3 Lysine 27 Methylation in Polycomb-Group Silencing
Cao, R., Wang, L., Wang, H., Xia, L., Erdjument-Bromage, H., Tempst, P., Jones, R. S., & Zhang, Y. (2002) · Science · doi:10.1126/science.1076997 · Cited by 3,775
Zhao, B., Wei, X., Li, W., Udan, R. S., Yang, Q., Kim, J., Xie, J., Ikenoue, T., Yu, J., Li, L., et al. (2007) · Genes & Development · doi:10.1101/gad.1602907 · Cited by 3,092
Cited by
Sorted by citations
The molecular hallmarks of epigenetic control
Allis, C. D., & Jenuwein, T. (2016) · Nature Reviews Genetics · doi:10.1038/nrg.2016.59 · Cited by 2,809
Arginine Methylation: The Coming of Age
Blanc, R. S., & Richard, S. (2017) · Molecular Cell · doi:10.1016/j.molcel.2016.11.003 · Cited by 1,054
Specificity, versatility, and control of TGF-β family signaling
Derynck, R., & Budi, E. H. (2019) · Science Signaling · doi:10.1126/scisignal.aav5183 · Cited by 785
“Various transmembraneproteins and receptors are functionally regulated by acetylation on Lys (147, 148) ormethylation on Lys orArg (149); however, these modes of posttranslational regulation are less studied than the control of protein function by phosphorylation.”
BackgroundThe 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
Morris, M., Knudsen, G. M., Maeda, S., Trinidad, J. C., Ioanoviciu, A., Burlingame, A. L., & Mucke, L. (2015) · Nature Neuroscience · doi:10.1038/nn.4067 · Cited by 472
Zhong, Q., Xiao, X., Qiu, Y., Xu, Z., Chen, C., Chong, B., Zhao, X., Hai, S., Li, S., An, Z., et al. (2023) · MedComm · doi:10.1002/mco2.261 · Cited by 442
Self-citationThe language of chromatin modification in human cancers
Zhao, S., Allis, C. D., & Wang, G. G. (2021) · Nature reviews. Cancer · doi:10.1038/s41568-021-00357-x · Cited by 420
Click Chemistry in Proteomic Investigations
Parker, C. G., & Pratt, M. R. (2020) · Cell · doi:10.1016/j.cell.2020.01.025 · Cited by 391
The post-translational modification, SUMOylation, and cancer (Review)
Han, Z., Feng, Y.-H., Gu, B.-H., Li, Y., & Chen, H. (2018) · International Journal of Oncology · doi:10.3892/ijo.2018.4280 · Cited by 358
Posttranslational mutagenesis: A chemical strategy for exploring protein side-chain diversity
Wright, T. H., Bower, B. J., Chalker, J. M., Bernardes, G. J. L., Wiewiora, R., Ng, W., Raj, R., Faulkner, S., Vallée, M. R. J., Phanumartwiwath, A., et al. (2016) · Science · doi:10.1126/science.aag1465 · Cited by 324
Chemical and Biochemical Perspectives of Protein Lysine Methylation
Luo, M. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00008 · Cited by 295
Methyltransferase SETD2-Mediated Methylation of STAT1 Is Critical for Interferon Antiviral Activity
Chen, K., Liu, J., Liu, S., Meng, X., Zhang, X., Han, D., Jiang, Y., Wang, C., & Cao, X. (2017) · Cell · doi:10.1016/j.cell.2017.06.042 · Cited by 291
Temozolomide and Other Alkylating Agents in Glioblastoma Therapy
Strobel, H., Baisch, T., Fitzel, R., Schilberg, K., Siegelin, M. D., Karpel-Massler, G., Debatin, K.-M., & Westhoff, M.-A. (2019) · Biomedicines · doi:10.3390/biomedicines7030069 · Cited by 279
Structural Biology and Regulation of Protein Import into the Nucleus
Christie, M., Chang, C.-W. M., Róna, G., Smith, K. M. L., Stewart, A. G., Takeda, A. A. S., Fontes, M. R. M., Stewart, M., Vértessy, B. G., Forwood, J. K., et al. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.10.023 · Cited by 259
Histone methylation and the DNA damage response
Gong, F., & Miller, K. M. (2017) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2017.09.003 · Cited by 265
TAK1-TABs Complex: A Central Signalosome in Inflammatory Responses
Xu, Y., & Lei, C. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2020.608976 · Cited by 245
Histone demethylases in chromatin biology and beyond
Dimitrova, E., Turberfield, A. H., & Klose, R. J. (2015) · EMBO Reports · doi:10.15252/embr.201541113 · Cited by 251
Protein Posttranslational Modifications: Roles in Aging and Age‐Related Disease
Santos, A. L., & Lindner, A. B. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/5716409 · Cited by 239
The winding path of protein methylation research: milestones and new frontiers
Murn, J., & Shi, Y. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.35 · Cited by 205
Wang, G., Long, J., Gao, Y., Zhang, W., Han, F., Xu, C. S., Sun, L., Yang, S.-C., Lan, J., Hou, Z., et al. (2019) · Nature Cell Biology · doi:10.1038/s41556-018-0266-1 · Cited by 189
Update: Post-translational protein modifications in plant metabolism
Friso, G., & van Wijk, K. J. (2015) · PLANT PHYSIOLOGY · doi:10.1104/pp.15.01378 · Cited by 186
Post-translational modifications of Hsp70 family proteins: Expanding the chaperone code
Nitika, N., Porter, C. M., Truman, A. W., & Truttmann, M. C. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.rev120.011666 · Cited by 174
Post-Translational Modifications of the TAK1-TAB Complex
Hirata, Y., Takahashi, M., Morishita, T., Noguchi, T., & Matsuzawa, A. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18010205 · Cited by 159
AKT methylation by SETDB1 promotes AKT kinase activity and oncogenic functions
Guo, J., Dai, X., Laurent, B., Zheng, N., Gan, W., Zhang, J., Guo, A., Yuan, M., Liu, P., Asara, J. M., et al. (2019) · Nature Cell Biology · doi:10.1038/s41556-018-0261-6 · Cited by 156
Hänzelmann, P., & Schindelin, H. (2017) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2017.00021 · Cited by 160
Karr, J. P., Ferrie, J. J., Tjian, R., & Darzacq, X. (2021) · Genes & Development · doi:10.1101/gad.349160.121 · Cited by 155
Methylation multiplicity and its clinical values in cancer
Dai, X., Ren, T., Zhang, Y., & Nan, N. (2021) · Expert Reviews in Molecular Medicine · doi:10.1017/erm.2021.4 · Cited by 150
Nan, Y., Wu, C., & Zhang, Y. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01758 · Cited by 146
Post‐translational regulation of antiviral innate signaling
Zhou, Y., He, C., Wang, L., & Ge, B.-X. (2017) · European Journal of Immunology · doi:10.1002/eji.201746959 · Cited by 139
A SMYD3 Small‐Molecule Inhibitor Impairing Cancer Cell Growth
Peserico, A., Germani, A., Sanese, P., Barbosa, A. J. M., Virgilio, V. D., Fittipaldi, R., Fabini, E., Bertucci, C., Varchi, G., Moyer, M. P., et al. (2015) · Journal of Cellular Physiology · doi:10.1002/jcp.24975 · Cited by 128
Nonhistone Lysine Methylation in the Regulation of Cancer PathwaysPreprint
Carlson, S. M., & Gozani, O. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026435 · Cited by 133
Bengtsson, A. A., & Rönnblom, L. (2017) · Best Practice & Research Clinical Rheumatology · doi:10.1016/j.berh.2017.10.003 · Cited by 121
The nexus between RNA-binding proteins and their effectors
He, S., Valkov, E., Cheloufi, S., & Murn, J. (2022) · Nature Reviews Genetics · doi:10.1038/s41576-022-00550-0 · Cited by 122
Jacot, D., Tosetti, N., Pires, I., Stock, J., Graindorge, A., Hung, Y.-F., Han, H., Tewari, R., Kursula, I., & Soldati‐Favre, D. (2016) · Cell Host & Microbe · doi:10.1016/j.chom.2016.10.020 · Cited by 118
Mitochondria Signaling Pathways in Allergic Asthma
Qian, L., Nasab, E. M., Athari, S. M., & Athari, S. S. (2022) · Journal of Investigative Medicine · doi:10.1136/jim-2021-002098 · Cited by 117
Hsiao, K., Zegzouti, H., & Goueli, S. A. (2016) · Epigenomics · doi:10.2217/epi.15.113 · Cited by 115
Lee, H., Li, C., Ruan, D., Powers, S., Thompson, P. A., Frohman, M. A., & Chan, C. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.08.009 · Cited by 114
SETD3 protein is the actin-specific histidine N-methyltransferase
Kwiatkowski, S., Seliga, A. K., Vertommen, D., Terreri, M., Ishikawa, T., Grabowska, I., Tiebe, M., Teleman, A. A., Jagielski, A. K., Veiga‐da‐Cunha, M., et al. (2018) · eLife · doi:10.7554/elife.37921 · Cited by 114
Interplay Among Metabolism, Epigenetic Modifications, and Gene Expression in Cancer
Huo, M., Zhang, J., Huang, W., & Wang, Y. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.793428 · Cited by 117
Lysine Methylation Regulators Moonlighting outside the Epigenome
Cornett, E. M., Ferry, L., Defossez, P., & Rothbart, S. B. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.08.026 · Cited by 113
Shi, R., Dai, X., Li, W., Lü, F., Liu, Y., Qu, H., Li, H., Chen, Q., Tian, H., Wu, E., et al. (2017) · ACS Nano · doi:10.1021/acsnano.7b05328 · Cited by 112
Pharmacological inhibition of PRMT7 links arginine monomethylation to the cellular stress response
Szewczyk, M. M., Ishikawa, Y., Organ, S. L., Sakai, N., Li, F., Halabelian, L., Ackloo, S. Z., Couzens, A. L., Eram, M. S., Dilworth, D., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16271-z · Cited by 109
Repression of hypoxia-inducible factor α signaling by Set7-mediated methylation
Liu, X., Chen, Z., Xu, C., Leng, X., Cao, H., Ouyang, G., & Xiao, W. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv379 · Cited by 112
The emerging role of lysine methyltransferase SETD8 in human diseases
Milite, C., Feoli, A., Viviano, M., Rescigno, D., Cianciulli, A., Balzano, A. L., Mai, A., Castellano, S., & Sbardella, G. (2016) · Clinical Epigenetics · doi:10.1186/s13148-016-0268-4 · Cited by 105
Beyond histones – the expanding roles of protein lysine methylation
Wu, Z., Connolly, J., & Biggar, K. K. (2017) · FEBS Journal · doi:10.1111/febs.14056 · Cited by 110
Self-citationGoing beyond Polycomb: EZH2 functions in prostate cancer
Park, S. H., Fong, K.-W., Mong, E. F., Martin, M. C., Schiltz, G. E., & Yu, J. (2021) · Oncogene · doi:10.1038/s41388-021-01982-4 · Cited by 113
Yang, Y., Wen, R., Yang, N., Zhang, T., & Liu, C. (2023) · Molecular Medicine · doi:10.1186/s10020-023-00684-9 · Cited by 107
Cause and consequences of the activated type I interferon system in SLE
Eloranta, M., & Rönnblom, L. (2016) · Journal of Molecular Medicine · doi:10.1007/s00109-016-1421-4 · Cited by 98
Chemical Proteomic Profiling of Human Methyltransferases
Horning, B. D., Suciu, R. M., Ghadiri, D. A., Ulanovskaya, O. A., Matthews, M. L., Lum, K. M., Backus, K. M., Brown, S. J., Rosen, H., & Cravatt, B. F. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b07830 · Cited by 97
Targeting epigenetic regulatory machinery to overcome cancer therapy resistance
Guo, L., Lee, Y., Zhou, Y., & Huang, Y. (2021) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2020.12.022 · Cited by 101
Zhao, Y., Lu, Q., Li, C., Wang, X., Jiang, L., Huang, L. F., Wang, C., & Chen, H. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1595-0 · Cited by 95
Preserving genome integrity and function: the DNA damage response and histone modifications
Kim, J. J., Lee, S. Y., & Miller, K. M. (2019) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2019.1620676 · Cited by 96
The Deubiquitinating Enzymes UBP12 and UBP13 Positively Regulate MYC2 Levels in Jasmonate Responses
Jeong, J. S., Jung, C., Seo, J. S., Kim, J., & Chua, N. (2017) · The Plant Cell · doi:10.1105/tpc.17.00216 · Cited by 94
Regulation of EZH2 by SMYD2-Mediated Lysine Methylation Is Implicated in Tumorigenesis
Zeng, Y., Qiu, R., Yang, Y., Gao, T., Zheng, Y., Huang, W., Gao, J., Zhang, K., Liu, R., Wang, S., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.10.004 · Cited by 92
Cardiac specific PRMT1 ablation causes heart failure through CaMKII dysregulation
Pyun, J., Kim, H. J., Jeong, M., Ahn, B. Y., Vuong, T. A., Lee, D. I., Choi, S., Koo, S., Cho, H., & Kang, J.-S. (2018) · Nature Communications · doi:10.1038/s41467-018-07606-y · Cited by 89
Lysine methylation of transcription factors in cancer
Han, D. H., Huang, M., Wang, T., Li, Z., Chen, Y., Liu, C., Lei, Z., & Chu, X. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1524-2 · Cited by 93
Chemical Methods for Encoding and Decoding of Posttranslational Modifications
Chuh, K. N., Batt, A. R., & Pratt, M. R. (2016) · Cell chemical biology · doi:10.1016/j.chembiol.2015.11.006 · Cited by 90
Histone methyltransferase and drug resistance in cancers
Yang, C., Zhang, J., Ma, Y., Wu, C., Cui, W., & Wang, L. (2020) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-020-01682-z · Cited by 88
Post-translational modifications of EZH2 in cancer
Li, Z., Li, M., Wang, D., Hou, P., Chen, X., Chu, S., Chai, D., Zheng, J., & Bai, J. (2020) · Cell & Bioscience · doi:10.1186/s13578-020-00505-0 · Cited by 87
PTEN Methylation by NSD2 Controls Cellular Sensitivity to DNA Damage
Zhang, J., Lee, Y.-R., Dang, F., Gan, W., Menon, A. V., Katon, J. M., Hsu, C.-H., Asara, J. M., Tibarewal, P., Leslie, N. R., et al. (2019) · Cancer Discovery · doi:10.1158/2159-8290.cd-18-0083 · Cited by 84
Methylation of C/EBPα by PRMT1 Inhibits Its Tumor-Suppressive Function in Breast Cancer
Liu, L.-M., Sun, W.-Z., Fan, X.-Z., Xu, Y., Cheng, M.-B., & Zhang, Y. (2019) · Cancer Research · doi:10.1158/0008-5472.can-18-3211 · Cited by 83
Małecki, J., Aileni, V. K., Ho, A. Y. Y., Schwarz, J., Moen, A. R., Sørensen, V., Nilges, B. S., Jakobsson, M. E., Leidel, S. A., & Falnes, P. Ø. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx002 · Cited by 82
PRMT5 methylating SMAD4 activates TGF-β signaling and promotes colorectal cancer metastasis
Liu, A., Yu, C., Qiu, C., Wu, Q., Huang, C., Li, X., She, X., Wan, K., Liu, L., Li, M., et al. (2023) · Oncogene · doi:10.1038/s41388-023-02674-x · Cited by 80
Discovery of Potent and Selective Inhibitors for G9a-Like Protein (GLP) Lysine Methyltransferase
Xiong, Y., Li, F., Babault, N., Dong, A., Zeng, H., Wu, H., Chen, X., Arrowsmith, C. H., Brown, P. J., Liu, J., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01645 · Cited by 79
Cao, Y. (2017) · Cell & Bioscience · doi:10.1186/s13578-017-0188-9 · Cited by 78
Li, W., Wang, H., Zhao, X., Duan, H., Cheng, B., Liu, Y., Zhao, M., Shu, W., Mei, Y.-C., Wen, Z., et al. (2019) · Science Advances · doi:10.1126/sciadv.aau7566 · Cited by 77
Madreiter‐Sokolowski, C. T., Klec, C., Parichatikanond, W., Stryeck, S., Gottschalk, B., Pulido, S., Rost, R., Eroğlu, E., Hofmann, N., Bondarenko, A. I., et al. (2016) · Nature Communications · doi:10.1038/ncomms12897 · Cited by 75
Direct interrogation of the role of H3K9 in metazoan heterochromatin function
Penke, T. J. R., McKay, D. J., Strahl, B. D., Matera, A. G., & Duronio, R. J. (2016) · Genes & Development · doi:10.1101/gad.286278.116 · Cited by 74
On-Demand Targeting: Investigating Biology with Proximity-Directed Chemistry
Long, M. J. C., Poganik, J. R., & Aye, Y. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.5b12608 · Cited by 73
Lee, S. W., Oh, Y. M., Lu, Y.-L., Kim, W. K., & Yoo, A. S. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.06.007 · Cited by 77
Fu, L., Wu, H., Cheng, S. Y., Gao, D., Zhang, L., & Zhao, Y. (2016) · eLife · doi:10.7554/elife.15690 · Cited by 72
SETDB2 Links Glucocorticoid to Lipid Metabolism through Insig2a Regulation
Roqueta‐Rivera, M., Esquejo, R. M., Phelan, P. E., Sándor, K., Dániel, B., Foufelle, F., Ding, J., Li, X., Khorasanizadeh, S., & Osborne, T. F. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.07.025 · Cited by 72
The methyltransferase PRMT6 attenuates antiviral innate immunity by blocking TBK1–IRF3 signaling
Zhang, H., Han, C., Li, T., Li, N., & Cao, X. (2018) · Cellular and Molecular Immunology · doi:10.1038/s41423-018-0057-4 · Cited by 71
A Biocatalytic Cascade for Versatile One‐Pot Modification of mRNA Starting from Methionine Analogues
Muttach, F., & Rentmeister, A. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201507577 · Cited by 71
NSD2 promotes tumor angiogenesis through methylating and activating STAT3 protein
Song, D., Lan, J., Chen, Y., Liu, A., Wu, Q., Zhao, C., Feng, Y., Wang, J., Luo, X., Cao, Z., et al. (2021) · Oncogene · doi:10.1038/s41388-021-01747-z · Cited by 70
Hartel, N. G., Chew, B. T. L., Qin, J., Xu, J., & Graham, N. A. (2019) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra119.001625 · Cited by 69
Jmjd6, a JmjC Dioxygenase with Many Interaction Partners and Pleiotropic Functions
Kwok, J., O’Shea, M. F., Hume, D. A., & Lengeling, A. (2017) · Frontiers in Genetics · doi:10.3389/fgene.2017.00032 · Cited by 70
Methylation of Elongation Factor 1A: Where, Who, and Why?
Hamey, J. J., & Wilkins, M. R. (2018) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2018.01.004 · Cited by 69
KMT5A-methylated SNIP1 promotes triple-negative breast cancer metastasis by activating YAP signaling
Yu, B., Su, J., Shi, Q., Liu, Q., Ma, J., Ru, G., Zhang, L., Zhang, J., Hu, X., & Tang, J. (2022) · Nature Communications · doi:10.1038/s41467-022-29899-w · Cited by 67
PD-L1 methylation restricts PD-L1/PD-1 interactions to control cancer immune surveillance
Huang, C., Ren, S., Chen, Y., Liu, A., Wu, Q., Jiang, T., Lv, P., Song, D., Hu, F., Lan, J., et al. (2023) · Science Advances · doi:10.1126/sciadv.ade4186 · Cited by 67
Milite, C., Feoli, A., Horton, J. R., Rescigno, D., Cipriano, A., Pisapia, V., Viviano, M., Pepe, G., Amendola, G., Novellino, E., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b02008 · Cited by 65
Luo, F., Zhang, M., Sun, B., Xu, C., Yang, Y., Zhang, Y., Li, S., Chen, G., Chen, C., Li, Y., et al. (2024) · Molecular Cancer · doi:10.1186/s12943-024-01975-3 · Cited by 65
Self-citationMolecular mechanisms of ethanol-associated oro-esophageal squamous cell carcinoma
Liu, Y., Chen, H., Sun, Z., & Chen, X. L. (2015) · Cancer Letters · doi:10.1016/j.canlet.2015.03.006 · Cited by 66
Sun, Q., Fang, L., Tang, X., Lu, S., Tamm, M., Stolz, D., & Roth, M. (2018) · The Journal of Immunology · doi:10.4049/jimmunol.1800782 · Cited by 63
Samsulrizal, N., Goh, Y. M., Hafandi, A., Dom, S. M., Syimal’ain, A. N., Zin, N. S. N. M., & Ebrahimi, M. M. (2017) · Journal of Traditional and Complementary Medicine · doi:10.1016/j.jtcme.2017.05.006 · Cited by 62
Epigenetic Regulation of Biological Rhythms: An Evolutionary Ancient Molecular Timer
Stevenson, T. J. (2017) · Trends in Genetics · doi:10.1016/j.tig.2017.11.003 · Cited by 66
Harman, J. J., Dobnikar, L., Chappell, J., Stokell, B. G., Dalby, A., Foote, K., Finigan, A. J., Freire-Pritchett, P., Taylor, A. L., Worssam, M. D., et al. (2019) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.119.312765 · Cited by 66
The methyltransferase NSD3 promotes antiviral innate immunity via direct lysine methylation of IRF3
Wang, C., Wang, Q., Xu, X., Xie, B., Zhao, Y. B., Li, N., & Cao, X. (2017) · The Journal of Experimental Medicine · doi:10.1084/jem.20170856 · Cited by 61
Resolving DNA Damage: Epigenetic Regulation of DNA Repair
Karakaidos, P., Karagiannis, D., & Rampias, T. N. (2020) · Molecules · doi:10.3390/molecules25112496 · Cited by 64
The Oviductal Extracellular Vesicles’ RNA Cargo Regulates the Bovine Embryonic Transcriptome
Bauersachs, S., Mermillod, P., & Almiñana, C. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21041303 · Cited by 60
Liu, L., Zhang, X., Ding, H., Liu, X., Cao, D., Liu, Y., Liu, J., Lin, C., Zhang, N., Wang, G., et al. (2021) · Oncogene · doi:10.1038/s41388-021-01785-7 · Cited by 60
Sun, Q., Liu, L., Mandal, J., Molino, A., Stolz, D., Tamm, M., Lu, S., & Roth, M. (2016) · Cellular Signalling · doi:10.1016/j.cellsig.2016.01.004 · Cited by 60
PRMT1-mediated PGK1 arginine methylation promotes colorectal cancer glycolysis and tumorigenesis
Liu, H., Chen, X., Wang, P., Chen, M., Deng, C., Qian, X., Bai, J., Li, Z., & Yu, X. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06544-6 · Cited by 59
The histone methyltransferase Suv39h2 contributes to nonalcoholic steatohepatitis in mice
Fan, Z., Li, L., Li, M., Zhang, X., Hao, C., Yu, L., Zeng, S., Xu, H., Fang, M., Shen, A., et al. (2017) · Hepatology · doi:10.1002/hep.29127 · Cited by 59
Yan, Q., Zhou, J., Gu, Y., Huang, W., Ruan, M., Zhang, H., Wang, T., Wei, P., Chen, G., Wan, L., et al. (2024) · Cell Death and Differentiation · doi:10.1038/s41418-024-01327-0 · Cited by 58
Tyrosine kinase 2 – Surveillant of tumours and bona fide oncogene
Leitner, N. R., Witalisz‐Siepracka, A., Strobl, B., & Müller, M. M. (2015) · Cytokine · doi:10.1016/j.cyto.2015.10.015 · Cited by 59
Lysine methylation signaling of non-histone proteins in the nucleus
Levy, D. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03142-0 · Cited by 56
HSP90 is necessary for the ACK1-dependent phosphorylation of STAT1 and STAT3
Mahendrarajah, N., Borisova, M. E., Reichardt, S., Godmann, M., Sellmer, A., Mahboobi, S., Haitel, A., Schmid, K., Kenner, L., Heinzel, T., et al. (2017) · Cellular Signalling · doi:10.1016/j.cellsig.2017.07.014 · Cited by 55
A glutamate/aspartate switch controls product specificity in a protein arginine methyltransferase
Debler, E., Jain, K., Warmack, R. A., Feng, Y., Clarke, S. G., Blobel, G., & Stavropoulos, P. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1525783113 · Cited by 54
Song, H., Feng, X., Zhang, M., Jin, X., Xu, X., Wang, L., Ding, X., Luo, Y., Lin, F., Wu, Q., et al. (2018) · Autophagy · doi:10.1080/15548627.2017.1389357 · Cited by 54
Metadata
- Authors
- Biggar, K. K., & Li, S. S.-C.
- Affiliations
- Western University (CA)
- Corresponding author
- Li, Shawn S.-C.
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2014-12-10
- Volume
- 16
- Issue
- 1
- Pages
- 5-17
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W2037215281
- Cited by
- 479
- References
- 138
- Citations by year
- 2026: 25 · 2025: 29 · 2024: 35 · 2023: 39 · 2022: 44 · 2021: 31 · 2020: 51 · 2019: 56 · 2018: 46 · 2017: 46 · 2016: 54 · 2015: 21 · 2014: 1
- FWCI
- 3.83
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Canadian Institutes of Health Research
- 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 › Genomics and Chromatin Dynamics
- Keywords
- non-histone protein methylation, lysine methylation, arginine methylation, post-translational modification crosstalk, histone methylation, MAPK signaling, Wnt signaling, BMP signaling, Hippo signaling pathway, JAK/STAT signaling, signal transduction, DNA repair, chromatin remodeling, gene transcription, proteomics
- MeSH terms
- Hippo Signaling Pathway, Animals, DNA Repair, Humans, Methylation, Transcription, Genetic, Protein Biosynthesis, Protein Serine-Threonine Kinases, MAP Kinase Signaling System, Chromatin Assembly and Disassembly, Extracellular Signal-Regulated MAP Kinases, STAT Transcription Factors, Wnt Proteins, Wnt Signaling Pathway
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