The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Quantitative analysis of residual folding and DNA binding in mutant p53 core domain: definition of mutant states for rescue in cancer therapy
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
p53 Mutations in Human Cancers
Hollstein, M., Sidransky, D., Vogelstein, B., & Harris, C. C. (1991) · Science · doi:10.1126/science.1905840 · Cited by 8,018
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
Crystal Structure of a p53 Tumor Suppressor-DNA Complex: Understanding Tumorigenic Mutations
Cho, Y., Gorina, S., Jeffrey, P. D., & Pavletich, N. P. (1994) · Science · doi:10.1126/science.8023157 · Cited by 2,551 · cited 11×
“However, 95% of tumorigenic p53 mutations are simply distributed in the central core domain where they abrogate the protein fold and its sequence-speci®c DNA binding a nity (Cho et al., 1994).”
BackgroundMethodInfluential14-3-3σ is required to prevent mitotic catastrophe after DNA damage
Chan, T. A., Hermeking, H., Lengauer, C., Kinzler, K. W., & Vogelstein, B. (1999) · Nature · doi:10.1038/44188 · Cited by 895
Hot-spot mutants of p53 core domain evince characteristic local structural changes
Wong, K.-B., DeDecker, B. S., Freund, S. M. V., Proctor, M. R., Bycroft, M., & Fersht, A. R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.15.8438 · Cited by 221
Self-citationWalker, D. R., Bond, J. P., Tarone, R. E., Harris, C. C., Makalowski, W., Boguski, M. S., & Greenblatt, M. S. (1999) · Oncogene · doi:10.1038/sj.onc.1202298 · Cited by 198
Correcting temperature-sensitive protein folding defects
Brown, C. R., Hong-Brown, L. Q., & Welch, W. J. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119302 · Cited by 176
Cited by
TP53 mutations in human cancers: origins, consequences, and clinical use.
Olivier, M., Hollstein, M., & Hainaut, P. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a001008 · Cited by 2,199
The p53 pathway: positive and negative feedback loops
Harris, S. L., & Levine, A. J. (2005) · Oncogene · doi:10.1038/sj.onc.1208615 · Cited by 1,967
Restoration of the tumor suppressor function to mutant p53 by a low-molecular-weight compound
Bykov, V. J. N., Issaeva, N., Shilov, A., Hultcrantz, M., Pugacheva, E., Chumakov, P., Bergman, J., Wiman, K. G., & Selivanova, G. (2002) · Nature Medicine · doi:10.1038/nm0302-282 · Cited by 1,067
mCSM: Predicting the effects of mutations in proteins using graph-based signatures
Pires, D. E. V., Ascher, D. B., & Blundell, T. L. (2014) · Bioinformatics · doi:10.1093/bioinformatics/btt691 · Cited by 1,066
Targeting p53 pathways: mechanisms, structures, and advances in therapy
Wang, H., Guo, M., Wei, H., & Chen, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01347-1 · Cited by 1,016
Targeting mutant p53 for efficient cancer therapy
Bykov, V. J. N., Eriksson, S. E., Bianchi, J., & Wiman, K. G. (2018) · Nature Reviews Cancer · doi:10.1038/nrc.2017.109 · Cited by 889
Awakening guardian angels: drugging the p53 pathway
Brown, C. J., Lain, S., Verma, C. S., Fersht, A. R., & Lane, D. P. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2763 · Cited by 881
Self-citationTP53 mutations in human cancers: Functional selection and impact on cancer prognosis and outcomes
Petitjean, A., Achatz, M. I. W., Borresen-Dale, A. L., Hainaut, P., & Olivier, M. (2007) · Oncogene · doi:10.1038/sj.onc.1210302 · Cited by 884
Assessing TP53 status in human tumours to evaluate clinical outcome
Soussi, T., & Béroud, C. (2001) · Nature reviews. Cancer · doi:10.1038/35106009 · Cited by 659
Gain of function of mutant p53 by coaggregation with multiple tumor suppressors
Xu, J., Reumers, J., Couceiro, J. R., De Smet, F., Gallardo, R., Rudyak, S., Cornelis, A., Rozenski, J., Zwolinska, A., Marine, J.-C., et al. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.546 · Cited by 543
Gaiddon, C., Lokshin, M., Ahn, J., Zhang, T., & Prives, C. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.5.1874-1887.2001 · Cited by 464
Pathological Unfoldomics of Uncontrolled Chaos: Intrinsically Disordered Proteins and Human Diseases
Uversky, V. N., Davé, V., Iakoucheva, L. M., Malaney, P., Metallo, S. J., Pathak, R. R., & Joerger, A. C. (2014) · Chemical Reviews · doi:10.1021/cr400713r · Cited by 288
Reactivation of mutant p53: molecular mechanisms and therapeutic potential
Selivanova, G., & Wiman, K. G. (2007) · Oncogene · doi:10.1038/sj.onc.1210295 · Cited by 186
The UMD TP53 database and website: update and revisions
Hamroun, D., Kato, S., Ishioka, C., Claustres, M., Béroud, C., & Soussi, T. (2006) · Human Mutation · doi:10.1002/humu.20269 · Cited by 140
Drugs Targeting p53 Mutations with FDA Approval and in Clinical Trials
Nishikawa, S., & Iwakuma, T. (2023) · Cancers · doi:10.3390/cancers15020429 · Cited by 115
A Small Molecule Reacts with the p53 Somatic Mutant Y220C to Rescue Wild-type Thermal Stability
Guiley, K. Z., & Shokat, K. M. (2023) · Cancer Discovery · doi:10.1158/2159-8290.cd-22-0381 · Cited by 102
Degtjarik, O., Golovenko, D., Diskin-Posner, Y., Abrahmsén, L., Rozenberg, H., & Shakked, Z. (2021) · Nature Communications · doi:10.1038/s41467-021-27142-6 · Cited by 78
Translational approaches targeting the p53 pathway for anti‐cancer therapy
Essmann, F., & Schulze‐Osthoff, K. (2012) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2011.01570.x · Cited by 77
Acetylation targeting chimera enables acetylation of the tumor suppressor p53
Kabir, M., Sun, N., Hu, X., Martin, T. C., Yi, J., Zhong, Y., Xiong, Y., Kaniskan, H. Ü., Gu, W., Parsons, R., et al. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c04640 · Cited by 65
Determining Biophysical Protein Stability in Lysates by a Fast Proteolysis Assay, FASTpp
Minde, D. P., Maurice, M. M., & Rüdiger, S. G. D. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046147 · Cited by 37
Functional investigations of p53 acetylation enabled by heterobifunctional molecules
Chen, L.-Y., Singha Roy, S. J., Jadhav, A. M., Wang, W. W., Chen, P.-H., Bishop, T., Erb, M. A., & Parker, C. G. (2024) · ACS Chemical Biology · doi:10.1021/acschembio.4c00438 · Cited by 18
OPUS-Mut: Studying the Effect of Protein Mutation through Side-Chain Modeling
Xu, G., Wang, Q., & Ma, J. (2023) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.2c00847 · Cited by 12
Design, synthesis, and evaluation of p53Y220C acetylation targeting chimeras (AceTACs)
Hu, X., Kabir, M., Lin, Y., Xiong, Y., Parsons, R. E., Gu, W., & Jin, J. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c01497 · Cited by 9
Bian, S., Bian, H., Koyama, H., Kompaniiets, D., Tse, W., Shah, M. V., Al-Kali, A., Miron, A., Liu, B., & Liu, S. (2026) · International Journal of Biological Sciences · doi:10.7150/ijbs.131687
Non-hydrolyzable acetyllysine analogs to study protein acetylation in vitro and in cells
Kienle, S. M., Sigg, M., Schneider, T., Stuber, K., Lehmann, J., Jansen, J., Stengel, F., Marx, A., Kovermann, M., & Scheffner, M. (2026) · Nature Communications · doi:10.1038/s41467-026-69782-6
Metadata
- Authors
- Bullock, A. N., Henckel, J., & Fersht, A. R.
- Venue
- Oncogene
- Published
- 2000-03-02
- Volume
- 19
- Issue
- 10
- Pages
- 1245-1256
- ISSN
- 0950-9232 (ISSN-L)
- 1476-5594
- OpenAlex
- W2312641146
- Cited by
- 434
- References
- 7
- FWCI
- 5.13
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
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.