The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Protein methylation at the surface and buried deep: thinking outside the histone box
Open accessAbstract
Methylated lysine and arginine residues on histones represent a crucial part of the histone code and their recognition by protein interaction domains modulates transcription. While some methylating enzymes appear to be specific for histones, many can modify both histone and non-histone substrates, and an increasing number are specific for non-histone substrates. Although some of the non-histone substrates can also be involved in transcription, a distinct subset of protein methylation reactions occurs at residues deeply buried in ribosomal proteins that may function in protein-RNA interactions rather than protein-protein interactions. Additionally, recent work has identified enzymes catalyzing protein methylation reactions on new sites in ribosomal and other proteins, including modifications of histidine and cysteine residues as well as the N terminus.
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Citations
Cites
Regulation of chromatin by histone modifications
Bannister, A. J., & Kouzarides, T. (2011) · Cell Research · doi:10.1038/cr.2011.22 · Cited by 6,012
Histone methylation: a dynamic mark in health, disease and inheritance
Greer, E. L., & Shi, Y. (2012) · Nature Reviews Genetics · doi:10.1038/nrg3173 · Cited by 2,241
Many paths to methyltransfer: a chronicle of convergence
Schubert, H. L., Blumenthal, R. M., & Cheng, X. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(03)00090-2 · Cited by 876
Protein lysine methyltransferase G9a acts on non-histone targets
Rathert, P., Dhayalan, A., Murakami, M., Zhang, X., Tamas, R., Jurkowska, R., Komatsu, Y., Shinkai, Y., Cheng, X., & Jeltsch, A. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.88 · Cited by 347
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
Cited by
Advances in Fmoc solid‐phase peptide synthesis
Behrendt, R., White, P., & Offer, J. (2016) · Journal of Peptide Science · doi:10.1002/psc.2836 · Cited by 760
Wiederstein, J. L., Nolte, H., Günther, S., Piller, T., Baraldo, M., Kostin, S., Bloch, W., Schindler, N., Sandri, M., Blaauw, B., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.03.136 · Cited by 52
Metadata
- Authors
- Clarke, S. G.
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2013-05
- Volume
- 38
- Issue
- 5
- Pages
- 243-252
- ISSN
- 0968-0004 (ISSN-L)
- OpenAlex
- W1974077096
- Cited by
- 191
- References
- 5
- FWCI
- 1.54
- Type
- journal article
- Language
- en
- Open access
- green
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