The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Lysine 2-hydroxyisobutyrylation is a widely distributed active histone mark
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Citations
Cites
The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis
Maxwell, P. H., Wiesener, M. S., Chang, G.-W., Clifford, S. C., Vaux, E. C., Cockman, M. E., Wykoff, C. C., Pugh, C. W., Maher, E. R., & Ratcliffe, P. J. (1999) · Nature · doi:10.1038/20459 · Cited by 5,180
Heintzman, N. D., Stuart, R. K., Hon, G., Fu, Y., Ching, C. W., Hawkins, R. D., Barrera, L. O., Van Calcar, S., Qu, C., Ching, K. A., et al. (2007) · Nature Genetics · doi:10.1038/ng1966 · Cited by 3,398
Self-citationThe complex language of chromatin regulation during transcription
Berger, S. L. (2007) · Nature · doi:10.1038/nature05915 · Cited by 2,768
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
Self-citationIdentification of lysine succinylation as a new post-translational modification
Zhang, Z., Tan, M., Xie, Z., Dai, L., Chen, Y., & Zhao, Y. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.495 · Cited by 1,027
Self-citationSIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways
Park, J., Chen, Y., Tishkoff, D. X., Peng, C., Tan, M., Dai, L., Xie, Z., Zhang, Y., Zwaans, B. M. M., Skinner, M. E., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.06.001 · Cited by 1,000
Self-citationInfluence of Metabolism on Epigenetics and Disease
Kaelin, W. G., & McKnight, S. L. (2013) · Cell · doi:10.1016/j.cell.2013.03.004 · Cited by 920
Lysine propionylation and butyrylation are novel post-translational modifications in histones
Chen, Y., Sprung, R., Tang, Y., Ball, H., Sangras, B., Kim, S. C., Falck, J. R., Peng, J., Gu, W., & Zhao, Y. (2007) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m700021-mcp200 · Cited by 764
Self-citationLysine succinylation and lysine malonylation in histones
Xie, Z., Dai, J., Dai, L., Tan, M., Cheng, Z., Wu, Y., Boeke, J. D., & Zhao, Y. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.015875 · Cited by 613
Self-citationCooperative binding of two acetylation marks on a histone tail by a single bromodomain
Morinière, J., Rousseaux, S., Steuerwald, U., Soler-López, M., Curtet, S., Vitte, A.-L., Govin, J., Gaucher, J., Sadoul, K., Hart, D. J., et al. (2009) · Nature · doi:10.1038/nature08397 · Cited by 469
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Cited by
Class I histone deacetylases (HDAC1–3) are histone lysine delactylases
Moreno-Yruela, C., Zhang, D., Wei, W., Bæk, M., Liu, W., Gao, J., Danková, D., Nielsen, A. L., Bolding, J. E., Yang, L., et al. (2022) · Science Advances · doi:10.1126/sciadv.abi6696 · Cited by 841
Self-citationMetabolic Regulation of Gene Expression by Histone Lysine β-Hydroxybutyrylation
Xie, Z., Zhang, D., Chung, D., Tang, Z., Huang, H., Dai, L., Qi, S., Li, J., Colak, G., Chen, Y., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.03.036 · Cited by 744
Self-citationIntracellular Crotonyl-CoA Stimulates Transcription through p300-Catalyzed Histone Crotonylation
Sabari, B. R., Tang, Z., Huang, H., Yong-Gonzalez, V., Molina, H., Kong, H. E., Dai, L., Shimada, M., Cross, J. R., Zhao, Y., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.02.029 · Cited by 659
Self-citationZhong, 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-citationSnapShot: histone modifications
Huang, H., Sabari, B. R., Garcia, B. A., Allis, C. D., & Zhao, Y. (2014) · Cell · doi:10.1016/j.cell.2014.09.037 · Cited by 439
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Metadata
- Authors
- Dai, L., Peng, C., Montellier, E., Lu, Z., Chen, Y., Ishii, H., Debernardi, A., Buchou, T., Rousseaux, S., Jin, F., Sabari, B. R., Deng, Z., Allis, C. D., Ren, B., Khochbin, S., & Zhao, Y.
- Venue
- Nature Chemical Biology
- Published
- 2014-03-30
- Volume
- 10
- Issue
- 5
- Pages
- 365-370
- ISSN
- 1552-4450 (ISSN-L)
- 1552-4469
- OpenAlex
- W2046301798
- Cited by
- 455
- References
- 13
- FWCI
- 11.68
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Lysine 2-hydroxyisobutyrylation is a widely distributed active histone mark. https://app.cochat.ai/papers/10.1038/nchembio.1497
- The paper
- Dai, L., Peng, C., Montellier, E., Lu, Z., Chen, Y., Ishii, H., Debernardi, A., Buchou, T., Rousseaux, S., Jin, F., Sabari, B. R., Deng, Z., Allis, C. D., Ren, B., Khochbin, S., & Zhao, Y. (2014). Lysine 2-hydroxyisobutyrylation is a widely distributed active histone mark. Nature Chemical Biology. https://doi.org/10.1038/nchembio.1497
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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.
