SnapShot: histone modifications
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Histone proteins undergo multiple post-translational modifications that regulate chromatin structure and gene expression.
“Histone proteins undergo multiple post-translational modifications (PTMs) that regulate chromatin structure and gene expression (Huang et al., 2014).”
From Histone modifications and depression: epigenetic mechanisms, therapeutic targets, and translational outlook (2026) · cites this paper as Huang et al., 2014
Cites
Chromatin modifications and their function
Kouzarides, T. (2007) · Cell · doi:10.1016/j.cell.2007.02.005 · Cited by 10,883 · see citing works
Jenuwein, T., & Allis, C. D. (2001) · Science · doi:10.1126/science.1063127 · Cited by 9,756 · see citing works
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Self-citationLysine 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 · see citing works
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 · see citing works
Self-citationLysine 2-hydroxyisobutyrylation is a widely distributed active histone mark
Dai, L., Peng, C., Montellier, E., Lu, Z., Chen, Y., Ishii, H., Debernardi, A., Buchou, T., Rousseaux, S., Jin, F., et al. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1497 · Cited by 460 · see citing works
Self-citationQuantitative Proteomic Analysis of Post-translational Modifications of Human Histones
Beck, H. C., Nielsen, E. C., Matthiesen, R., Jensen, L. H., Sehested, M., Finn, P. W., Grauslund, M., Hansen, A. M., & Jensen, O. N. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m600007-mcp200 · Cited by 194 · see citing works
Proteomic characterization of novel histone post-translational modifications
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Self-citationChromatin as an expansive canvas for chemical biology
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The significance, development and progress of high-throughput combinatorial histone code analysis
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Molecular Coupling of Histone Crotonylation and Active Transcription by AF9 YEATS Domain
Li, Y., Sabari, B. R., Panchenko, T., Wen, H., Zhao, D., Guan, H., Wan, L., Huang, H., Tang, Z., Zhao, Y., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.03.028 · Cited by 384 · see citing works
Self-citationBiological embedding of experience: a primer on epigenetics
Aristizabal, M. J., Anreiter, I., Halldorsdottir, T., Odgers, C. L., McDade, T. W., Goldenberg, A., Mostafavi, S., Kobor, M. S., Binder, E. B., Sokolowski, M. B., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1820838116 · Cited by 268 · see citing works
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Lv, L.-Z., Wang, Z.-D., Ren, J.-J., Li, L.-H., Liu, X.-B., Li, J.-L., Zhu, H., Jiang, B., Han, Y.-P., Zhou, X.-M., et al. (2026) · Frontiers in Genetics · doi:10.3389/fgene.2025.1722453 · Cited by 7 · see citing works
“Histone proteins undergo multiple post-translational modifications (PTMs) that regulate chromatin structure and gene expression (Huang et al., 2014).”
- Authors
- Huang, H., Sabari, B. R., Garcia, B. A., Allis, C. D., & Zhao, Y.
- Affiliations
- University of Chicago (US)
- Rockefeller University (US)
- University of Pennsylvania (US)
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2014-10
- Volume
- 159
- Issue
- 2
- Pages
- 458-458.e1
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC4324475
- OpenAlex
- W2101994612
- Cited by
- 439
- References
- 10
- Citations by year
- 2026: 21 · 2025: 24 · 2024: 34 · 2023: 37 · 2022: 38 · 2021: 38 · 2020: 34 · 2019: 50 · 2018: 53 · 2017: 34 · 2016: 41 · 2015: 35
- FWCI
- 15.18
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (UL1TR000430, DP2OD007447)
- National Institute of Mental Health (P50MH096890)
- National Cancer Institute (CA160036, U24CA160036)
- National Institute of General Medical Sciences (GM105933, R01GM110174, R01GM105933)
- National Center for Research Resources (RR020839, U54RR020839)
- National Center for Advancing Translational Sciences
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
- Keywords
- histone modifications, chromatin structure, gene expression regulation, lysine acylation, post-translational modification, histone proteins
- MeSH terms
- Amino Acid Sequence, Animals, Histones, Humans, Lysine, Molecular Sequence Data, Protein Processing, Post-Translational, Histone Code, Mice, Rats
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