The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
A General Molecular Affinity Strategy for Global Detection and Proteomic Analysis of Lysine Methylation
Open accessAbstract
Summary Lysine methylation of histone proteins regulates chromatin dynamics and plays important roles in diverse physiological and pathological processes. However, beyond histone proteins, the proteome-wide extent of lysine methylation remains largely unknown. We have engineered the naturally occurring MBT domain repeats of L3MBTL1 to serve as a universal affinity reagent for detecting, enriching, and identifying proteins carrying a mono- or di-methylated lysine. The domain is broadly specific for methylated lysine (“pan-specific”) and can be applied to any biological system. We have used our approach to demonstrate that SIRT1 is a substrate of the methyltransferase G9a both in vitro and in cells, to perform proteome-wide detection and enrichment of novel methylated proteins, and to identify candidate in-cell substrates of G9a and the related methyltransferse GLP. Together, our results demonstrate a powerful new approach for global and quantitative analysis of methylated lysine, and they represent the first systems biology understanding of lysine methylation.
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Cox, J., & Mann, M. (2008) · Nature Biotechnology · doi:10.1038/nbt.1511 · Cited by 14,855
Regulation of chromatin by histone modifications
Bannister, A. J., & Kouzarides, T. (2011) · Cell Research · doi:10.1038/cr.2011.22 · Cited by 6,012
Ong, S.-E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., & Mann, M. (2002) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m200025-mcp200 · Cited by 5,574
Lysine acetylation targets protein complexes and co-regulates major cellular functions
Choudhary, C., Kumar, C., Gnad, F., Nielsen, M. L., Rehman, M., Walther, T. C., Olsen, J. V., & Mann, M. (2009) · Science · doi:10.1126/science.1175371 · Cited by 4,040
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
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
Cited by
Non-histone protein methylation as a regulator of cellular signalling and function
Biggar, K. K., & Li, S. S.-C. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3915 · Cited by 479
Quantitative Proteomic Analysis of Histone Modifications
Huang, H., Lin, S., Garcia, B. A., & Zhao, Y. (2015) · Chemical Reviews · doi:10.1021/cr500491u · Cited by 370
Chemical and Biochemical Perspectives of Protein Lysine Methylation
Luo, M. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00008 · Cited by 284
Discovery of an in Vivo Chemical Probe of the Lysine Methyltransferases G9a and GLP
Liu, F., Barsyte-Lovejoy, D., Li, F., Xiong, Y., Korboukh, V., Huang, X.-P., Allali-Hassani, A., Janzen, W. P., Roth, B. L., Frye, S. V., et al. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm401480r · Cited by 268
Ferry, L., Fournier, A., Tsusaka, T., Adelmant, G., Shimazu, T., Matano, S., Kirsh, O., Amouroux, R., Dohmae, N., Suzuki, T., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.07.012 · Cited by 203
Metadata
- Authors
- Moore, K. E., Carlson, S. M., Camp, N. D., Cheung, P., James, R. G., Chua, K. F., Wolf-Yadlin, A., & Gozani, O.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2013-05
- Volume
- 50
- Issue
- 3
- Pages
- 444-456
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2047552911
- Cited by
- 165
- References
- 6
- FWCI
- 9.82
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Moore, K. E., Carlson, S. M., Camp, N. D., Cheung, P., James, R. G., Chua, K. F., Wolf-Yadlin, A., & Gozani, O. (2013). A General Molecular Affinity Strategy for Global Detection and Proteomic Analysis of Lysine Methylation. Molecular Cell. https://doi.org/10.1016/j.molcel.2013.03.005
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