The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.
Chemical Biology of Protein Arginine Modifications in Epigenetic Regulation
Open accessAbstract
Review article on histone citrullination (arginine deimination), histone arginine methylation, and noncanonical histone arginine modifications.
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Cites
Neutrophil Extracellular Traps Kill Bacteria
Brinkmann, V., Reichard, U., Goosmann, C., Fauler, B., Uhlemann, Y., Weiss, D. S., Weinrauch, Y., & Zychlinsky, A. (2004) · Science · doi:10.1126/science.1092385 · Cited by 10,268
p53 Mutations in Human Cancers
Hollstein, M., Sidransky, D., Vogelstein, B., & Harris, C. C. (1991) · Science · doi:10.1126/science.1905840 · Cited by 8,018
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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 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
Tan, M., Luo, H., Lee, S., Jin, F., Yang, J. S., Montellier, E., Buchou, T., Cheng, Z., Rousseaux, S., Rajagopal, N., et al. (2011) · Cell · doi:10.1016/j.cell.2011.08.008 · Cited by 1,902
PAD4 is essential for antibacterial innate immunity mediated by neutrophil extracellular traps
Li, P., Li, M., Lindberg, M. R., Kennett, M. J., Xiong, N., & Wang, Y. (2010) · Journal of Experimental Medicine · doi:10.1084/jem.20100239 · Cited by 1,495
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Cited by
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
Phase Separation of FUS Is Suppressed by Its Nuclear Import Receptor and Arginine Methylation
Hofweber, M., Hutten, S., Bourgeois, B., Spreitzer, E., Niedner-Boblenz, A., Schifferer, M., Ruepp, M.-D., Simons, M., Niessing, D., Madl, T., et al. (2018) · Cell · doi:10.1016/j.cell.2018.03.004 · Cited by 668
Global profiling of arginine reactivity and ligandability in the human proteome
Wang, Y., Hu, T., Zhu, L., Xie, S., Yang, X., Xu, C., Zhai, Y., Li, Y., Huang, X., Yang, B., et al. (2026) · Nature Chemistry · doi:10.1038/s41557-025-02012-6 · Cited by 12
Proximity-Dependent Labeling of Cysteines
Sen, S., Sultana, N., Shaffer, S. A., & Thompson, P. R. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c07069 · Cited by 11
Self-citation(2024) · doi:10.1016/j.isci.2024.109584 · Cited by 6
Metadata
- Authors
- Fuhrmann, J., Clancy, K. W., & Thompson, P. R.
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2015-05-13
- Volume
- 115
- Issue
- 11
- Pages
- 5413-5461
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W1532675490
- Cited by
- 323
- References
- 15
- FWCI
- 1.97
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Fuhrmann, J., Clancy, K. W., & Thompson, P. R. (2015). Chemical Biology of Protein Arginine Modifications in Epigenetic Regulation. Chemical Reviews. https://doi.org/10.1021/acs.chemrev.5b00003
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
