The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Regulation of p53 activity by its interaction with homeodomain-interacting protein kinase-2
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Citations
Cites
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
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 2×
“c, GST–p53(1-80) or a point mutant of this fusion protein containing a Ser 46 to alanine exchange were employed as substrate proteins, typical autoradiograms are displayed.”
MethodMomand, J., Zambetti, G. P., Olson, D. C., George, D., & Levine, A. J. (1992) · Cell · doi:10.1016/0092-8674(92)90644-r · Cited by 3,113
DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
Shieh, S.-Y., Ikeda, M., Taya, Y., & Prives, C. (1997) · Cell · doi:10.1016/s0092-8674(00)80416-x · Cited by 2,100
Self-citationDNA damage activates p53 through a phosphorylation–acetylation cascade
Sakaguchi, K., Herrera, J. E., Saito, S., Miki, T., Bustin, M., Vassilev, A., Anderson, C. W., & Appella, E. (1998) · Genes & Development · doi:10.1101/gad.12.18.2831 · Cited by 1,204
Delerive, P., De Bosscher, K., Besnard, S., Vanden Berghe, W., Peters, J. M., Gonzalez, F. J., Fruchart, J.-C., Tedgui, A., Haegeman, G., & Staels, B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.45.32048 · Cited by 1,089
Shieh, S.-Y., Ahn, J., Tamai, K., Taya, Y., & Prives, C. (2000) · Genes & Development · doi:10.1101/gad.14.3.289 · Cited by 972
Self-citationp53 Sites Acetylated In Vitro by PCAF and p300 Are Acetylated In Vivo in Response to DNA Damage
Liu, L., Scolnick, D. M., Trievel, R. C., Zhang, H. B., Marmorstein, R., Halazonetis, T. D., & Berger, S. L. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.2.1202 · Cited by 776
Cited by
Blinded by the Light: The Growing Complexity of p53
Vousden, K. H., & Prives, C. (2009) · Cell · doi:10.1016/j.cell.2009.04.037 · Cited by 3,163
NRF2 and the Hallmarks of Cancer
Rojo de la Vega, M., Chapman, E., & Zhang, D. D. (2018) · Cancer Cell · doi:10.1016/j.ccell.2018.03.022 · Cited by 1,672
Post-translational modification of p53 in tumorigenesis
Bode, A. M., & Dong, Z. (2004) · Nature Reviews Cancer · doi:10.1038/nrc1455 · Cited by 1,270
DNA damage and the balance between survival and death in cancer biology
Roos, W. P., Thomas, A. D., & Kaina, B. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2015.2 · Cited by 1,189
The multiple mechanisms that regulate p53 activity and cell fate
Hafner, A., Bulyk, M. L., Jambhekar, A., & Lahav, G. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0110-x · Cited by 1,129
Metadata
- Authors
- Hofmann, T. G., Möller, A., Sirma, H., Zentgraf, H., Taya, Y., Dröge, W., Will, H., & Schmitz, M. L.
- Venue
- Nature Cell Biology
- Published
- 2001-12-10
- Volume
- 4
- Issue
- 1
- Pages
- 1-10
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- OpenAlex
- W2063822655
- Cited by
- 592
- References
- 8
- FWCI
- 11.13
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Regulation of p53 activity by its interaction with homeodomain-interacting protein kinase-2. https://app.cochat.ai/papers/10.1038/ncb715
- The paper
- Hofmann, T. G., Möller, A., Sirma, H., Zentgraf, H., Taya, Y., Dröge, W., Will, H., & Schmitz, M. L. (2002). Regulation of p53 activity by its interaction with homeodomain-interacting protein kinase-2. Nature Cell Biology. https://doi.org/10.1038/ncb715
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.