The DOI matches its Crossref record; 62 of the 62 references it cites were found in a registry or an index.
Structure and acetyl-lysine recognition of the bromodomain
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Citations
Cites
1 retracted
Fujiki, R., Kim, M., Sasaki, Y., Yoshimura, K., Kitagawa, H., & Kato, S. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600853 · Cited by 109
RetractedChromatin modifications and their function
Kouzarides, T. (2007) · Cell · doi:10.1016/j.cell.2007.02.005 · Cited by 10,883
Jenuwein, T., & Allis, C. D. (2001) · Science · doi:10.1126/science.1063127 · Cited by 9,756
The language of covalent histone modifications
Strahl, B. D., & Allis, C. D. (2000) · Nature · doi:10.1038/47412 · Cited by 8,679
Mdm2 promotes the rapid degradation of p53
Haupt, Y., Maya, R., Kazaz, A., & Oren, M. (1997) · Nature · doi:10.1038/387296a0 · Cited by 4,506
The Role of Chromatin during Transcription
Li, B., Carey, M., & Workman, J. L. (2007) · Cell · doi:10.1016/j.cell.2007.01.015 · Cited by 3,533
Regulation of p53 stability by Mdm2
Kubbutat, M. H. G., Jones, S. N., & Vousden, K. H. (1997) · Nature · doi:10.1038/387299a0 · Cited by 3,312 · cited 3×
“in U2OS cells is low in a resting state, due to its negative regulation by MDM2 (Haupt et al., 1997; Kubbutat et al., 1997).”
BackgroundSelective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain
Bannister, A. J., Zegerman, P., Partridge, J. F., Miska, E. A., Thomas, J. O., Allshire, R. C., & Kouzarides, T. (2001) · Nature · doi:10.1038/35065138 · Cited by 2,903
Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
Lachner, M., O'Carroll, D., Rea, S., Mechtler, K., & Jenuwein, T. (2001) · Nature · doi:10.1038/35065132 · Cited by 2,868
ACETYLATION AND METHYLATION OF HISTONES AND THEIR POSSIBLE ROLE IN THE REGULATION OF RNA SYNTHESIS
Allfrey, V. G., Faulkner, R., & Mirsky, A. E. (1964) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.51.5.786 · Cited by 2,639
Cited by
Regulation of chromatin by histone modifications
Bannister, A. J., & Kouzarides, T. (2011) · Cell Research · doi:10.1038/cr.2011.22 · Cited by 6,012
Multivalent engagement of chromatin modifications by linked binding modules
Ruthenburg, A. J., Li, H., Patel, D. J., & David Allis, C. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2298 · Cited by 1,013
Yang, X.-J., & Seto, E. (2007) · Oncogene · doi:10.1038/sj.onc.1210599 · Cited by 940
Histones: annotating chromatin
Campos, E. I., & Reinberg, D. (2009) · Annual Review of Genetics · doi:10.1146/annurev.genet.032608.103928 · Cited by 852
Chemical phylogenetics of histone deacetylases
Bradner, J. E., West, N., Grachan, M. L., Greenberg, E. F., Haggarty, S. J., Warnow, T., & Mazitschek, R. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.313 · Cited by 720
Metadata
- Authors
- Mujtaba, S., Zeng, L., & Zhou, M.-M.
- Venue
- Oncogene
- Published
- 2007-08-13
- Volume
- 26
- Issue
- 37
- Pages
- 5521-5527
- ISSN
- 0950-9232 (ISSN-L)
- 1476-5594
- OpenAlex
- W1971407164
- Cited by
- 421
- References
- 62
- FWCI
- 10.18
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Structure and acetyl-lysine recognition of the bromodomain. https://app.cochat.ai/papers/10.1038/sj.onc.1210618
- The paper
- Mujtaba, S., Zeng, L., & Zhou, M.-M. (2007). Structure and acetyl-lysine recognition of the bromodomain. Oncogene. https://doi.org/10.1038/sj.onc.1210618
Data sources
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.
