The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Mouse Mutants Reveal that Putative Protein Interaction Sites in the p53 Proline-Rich Domain Are Dispensable for Tumor Suppression
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“supporting previous suggestions based on mutagenesis, that the domain plays a predominantly structural role (33).”
From Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain (2008) · cites this paper as [33]
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Cites
Direct Activation of Bax by p53 Mediates Mitochondrial Membrane Permeabilization and Apoptosis
Chipuk, J. E., Kuwana, T., Bouchier-Hayes, L., Droin, N. M., Newmeyer, D. D., Schuler, M., & Green, D. R. (2004) · Science · doi:10.1126/science.1092734 · Cited by 2,108
Regulating the p53 pathway: in vitro hypotheses, in vivo veritas
Toledo, F., & Wahl, G. M. (2006) · Nature reviews. Cancer · doi:10.1038/nrc2012 · Cited by 1,286
Self-citationKeeping p53 in check: essential and synergistic functions of Mdm2 and Mdm4
Marine, J.-C., Francoz, S., Maetens, M., Wahl, G., Toledo, F., & Lozano, G. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401912 · Cited by 352
Self-citationMdm4 and Mdm2 cooperate to inhibit p53 activity in proliferating and quiescent cells in vivo
Francoz, S., Froment, P., Bogaerts, S., De Clercq, S., Maetens, M., Doumont, G., Bellefroid, E., & Marine, J.-C. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508476103 · Cited by 260
Toledo, F., Krummel, K. A., Lee, C. J., Liu, C.-W., Rodewald, L.-W., Tang, M., & Wahl, G. M. (2006) · Cancer Cell · doi:10.1016/j.ccr.2006.03.014 · Cited by 199 · cited 10×
“We used homologous recombination to introduce the desired mutations into the endogenous Trp53 locus as described previously (28).”
BackgroundMethodResultInfluentialSelf-citationPhosphorylation of Serine 18 Regulates Distinct p53 Functions in Mice
Sluss, H. K., Armata, H., Gallant, J., & Jones, S. N. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.3.976-984.2004 · Cited by 152
Cell Type- and Promoter-specific Roles of Ser18 Phosphorylation in Regulating p53 Responses
Chao, C., Hergenhahn, M., Kaeser, M. D., Wu, Z., Saito, S., Iggo, R., Hollstein, M., Appella, E., & Xu, Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306938200 · Cited by 141
Defective apoptosis and B-cell lymphomas in mice with p53 point mutation at Ser 23
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Cited by
The prolyl isomerase PIN1: a pivotal new twist in phosphorylation signalling and disease
Lu, K. P., & Zhou, X. Z. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2261 · Cited by 682
Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain
Wells, M., Tidow, H., Rutherford, T. J., Markwick, P., Jensen, M. R., Mylonas, E., Svergun, D. I., Blackledge, M., & Fersht, A. R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801353105 · Cited by 434
A complex barcode underlies the heterogeneous response of p53 to stress
Murray-Zmijewski, F., Slee, E. A., & Lu, X. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2451 · Cited by 420
Brady, C. A., & Attardi, L. D. (2010) · Journal of Cell Science · doi:10.1242/jcs.064501 · Cited by 403
Prolyl isomerase Pin1 as a molecular switch to determine the fate of phosphoproteins
Liou, Y.-C., Zhou, X. Z., & Lu, K. P. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.07.001 · Cited by 326
Metadata
- Authors
- Toledo, F., Lee, C. J., Krummel, K. A., Rodewald, L.-W., Liu, C.-W., & Wahl, G. M.
- Affiliations
- Salk Institute for Biological Studies, Gene Expression Laboratory, 10010 North Torrey Pines Road, La Jolla, California 92037
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2007-02-01
- Volume
- 27
- Issue
- 4
- Pages
- 1425-1432
- ISSN
- 1098-5549
- Cited by
- 46
- References
- 9
- Language
- en
- Licence
- journals.asm.org/non-commercial-tdm-license (tdm)
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- This page
- CoChat. (2026). Citation check: Mouse Mutants Reveal that Putative Protein Interaction Sites in the p53 Proline-Rich Domain Are Dispensable for Tumor Suppression. https://app.cochat.ai/papers/10.1128/mcb.00999-06
- The paper
- Toledo, F., Lee, C. J., Krummel, K. A., Rodewald, L.-W., Liu, C.-W., & Wahl, G. M. (2007). Mouse Mutants Reveal that Putative Protein Interaction Sites in the p53 Proline-Rich Domain Are Dispensable for Tumor Suppression. Molecular and Cellular Biology. https://doi.org/10.1128/mcb.00999-06
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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.
