The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
The screening of the second‐site suppressor mutations of the common p53 mutants
Abstract
Second‐site suppressor (SSS) mutations in p53 found by random mutagenesis have shown to restore the inactivated function of some tumor‐derived p53. To screen novel SSS mutations against common mutant p53s, intragenic second‐site (SS) mutations were introduced into mutant p53 cDNA in a comprehensive manner by using a p53 missense mutation library. The resulting mutant p53s with background and SS mutations were assayed for their ability to restore the p53 transactivation function in both yeast and human cell systems. We identified 12 novel SSS mutations including H178Y against a common mutation G245S. Surprisingly, the G245S phenotype is rescued when coexpressed with p53 bearing the H178Y mutation. This result indicated that there is a possibility that intragenic suppressor mutations might restore the protein function in an intermolecular manner. The intermolecular mechanism may lead to novel strategies for restoring inactivated p53 function and tumor suppression in cancer treatment. © 2007 Wiley‐Liss, Inc.
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.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Second site suppressor mutations could help correct the conformation of mutant p53, improve the stability of p53-DNA binding, and provide a theoretical basis for the reactivation of mutant p53 (Table 4).531–545”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [533]
In the citing paper
“Second site suppressor mutations could help correct the conformation of mutant p53, improve the stability of p53-DNA binding, and provide a theoretical basis for the reactivation of mutant p53 (Table 4).531–545”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [533]
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
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 1×
“The structure of the core DNA-binding domain has been resolved by X-ray crystallographic analysis.(2) The p53 forms a homotetramer through the tetramerization domain and the p53 tetramer forms a sequence-specific DNA-binding interface.”
MethodThe IARC TP53 database: new online mutation analysis and recommendations to users
Olivier, M., Eeles, R., Hollstein, M., Khan, M. A., Harris, C. C., & Hainaut, P. (2002) · Human Mutation · doi:10.1002/humu.10081 · Cited by 1,248
Walker, 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
Isolation of Temperature-sensitive p53 Mutations from a Comprehensive Missense Mutation Library
Shiraishi, K., Kato, S., Han, S.-Y., Liu, W., Otsuka, K., Sakayori, M., Ishida, T., Takeda, M., Kanamaru, R., Ohuchi, N., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310815200 · Cited by 96
Self-citation
Research works printed but not linked: 37
- Arrowsmith CH, 1996, New insights into p53 function from structural studies, Oncogene, 12, 1379
- 10.1126/science.7878474 · DOI · Paper page
- 10.1126/science.2144363 · DOI · Paper page
- 10.1126/science.2144364 · DOI · Paper page
- 10.1126/science.7878469 · DOI · Paper page
- Soussi T, 1990, Structural aspects of the p53 protein in relation to gene evolution, Oncogene, 5, 945
- 10.1016/S0092-8674(00)80540-1 · DOI · Paper page
- 10.1038/nm0798-839 · DOI · Paper page
- Greenblatt MS, 1994, Mutations in the p53 tumor suppressor gene: clues to cancer etiology and molecular pathogenesis, Cancer Res, 54, 4855
- Hollstein M, 1994, Database of p53 gene somatic mutations in human tumors and cell lines, Nucleic Acids Res, 22, 3551
- 10.1002/humu.10032 · DOI
- 10.1002/(SICI)1098-1004(200001)15:1<105::AID-HUMU19>3.0.CO;2-G · DOI · Paper page
- 10.1073/pnas.1431692100 · DOI · Paper page
- 10.1158/0008-5472.CAN-04-2935 · DOI
- 10.1093/emboj/17.7.1847 · DOI · Paper page
- 10.1093/emboj/19.3.370 · DOI · Paper page
- 10.1038/nm1096-1143 · DOI
- 10.1093/nar/30.7.1563 · DOI
- 10.1073/pnas.0401162101 · DOI
- 10.1074/jbc.M500179200 · DOI · Paper page
- 10.1038/35094077 · DOI · Paper page
- Shimada A, 1999, The transcriptional activities of p53 and its homologue p51/p63: similarities and differences, Cancer Res, 59, 2781
- 10.1038/ng1093-124 · DOI · Paper page
- Ishioka C, 1995, Mutational analysis of the carboxy‐terminal portion of p53 using both yeast and mammalian cell assays in vivo, Oncogene, 10, 1485
- 10.1006/bbrc.1997.6216 · DOI
- 10.1038/sj.onc.1208839 · DOI
- 10.1002/elps.1150181505 · DOI · Paper page
- 10.1038/sj.onc.1203434 · DOI · Paper page
- 10.1074/jbc.M107516200 · DOI · Paper page
- 10.1016/S0022-2836(02)00326-1 · DOI · Paper page
- Shortle D, 1985, Genetic analysis of staphylococcal nuclease: identification of three intragenic “global” suppressors of nuclease‐minus mutations, Genetics, 110, 539, 10.1093/genetics/110.4.539 · DOI · Paper page
- 10.1016/S0021-9258(18)47105-0 · DOI
- Yamaguchi A, 1993, Second‐site mutation of Ala‐220 to Glu or Asp suppresses the mutation of Asp‐285 to Asn in the transposon Tn10‐encoded metal‐tetracycline/H+ antiporter of Escherichia coli, J Biol Chem, 268, 26990, 10.1016/S0021-9258(19)74208-2 · DOI
- 10.1016/0005-2728(92)90108-E · doi:10.1016/0005-2728(92)90108-e
- 10.1016/0005-2736(91)90390-T · DOI
- Iwamoto A, 1991, Mutations in Ser174 and the glycine‐rich sequence (Gly149, Gly150, and Thr156) in the beta subunit of Escherichia coli H(+)‐ATPase, J Biol Chem, 266, 16350, 10.1016/S0021-9258(18)55304-7 · DOI
- Kuo PH, 2000, Intragenic and intergenic suppression of the Escherichia coli ATP synthase subunit a mutation of Gly‐213 to Asn: functional interactions between residues in the proton transport site, Biochem J, 347, 797, 10.1042/bj3470797 · doi:10.1042/bj3470797
Cited by
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 Therapies for the p53 Protein in Cancer Treatments
Levine, A. J. (2019) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-030518-055455 · Cited by 84
Metadata
- Authors
- Otsuka, K., Kato, S., Kakudo, Y., Mashiko, S., Shibata, H., & Ishioka, C.
- Venue
- International Journal of Cancer
- Publisher
- Wiley
- Published
- 2007-05-25
- Volume
- 121
- Issue
- 3
- Pages
- 559-566
- ISSN
- 0020-7136
- 1097-0215
- Cited by
- 23
- References
- 4
- Language
- en
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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: The screening of the second‐site suppressor mutations of the common p53 mutants. https://app.cochat.ai/papers/10.1002/ijc.22724
- The paper
- Otsuka, K., Kato, S., Kakudo, Y., Mashiko, S., Shibata, H., & Ishioka, C. (2007). The screening of the second‐site suppressor mutations of the common p53 mutants. International Journal of Cancer. https://doi.org/10.1002/ijc.22724
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.
