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.
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“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]
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Cites
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Research works printed but not linked: 1
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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
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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
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