The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Impact of low-frequency hotspot mutation R282Q on the structure of p53 DNA-binding domain as revealed by crystallography at 1.54 Å resolution
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“The crystal structure (PDB:2PCX) 20 reveals that interactions with T118, T125 and E286 are lost upon mutation, while Q282 forms a new interaction with the backbone of S127 instead of its side chain and with S116 (Fig. 2 Bii).”
From Combined Point Mutation in a Single Allele of the TP53 Gene Potentiates the Oncogenic and Transcriptional Properties of TP53 in Lung Cancer (2026) · cites this paper as [20]
In the citing paper
“Additionally, the rotation of H115 may affect overall protein folding 20.”
From Combined Point Mutation in a Single Allele of the TP53 Gene Potentiates the Oncogenic and Transcriptional Properties of TP53 in Lung Cancer (2026) · cites this paper as [20]
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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 8×
“Thus, the flexibility of L1 may be important for the DNA-binding activity of p53 because residue Lys120, which is located at the apex of L1, is involved in the sequence-specific central recognition of DNA (Cho et al., 1994; Kitayner et al., 2006).”
BackgroundInfluentialThe 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
Cited by
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
Metadata
- Authors
- Tu, C., Tan, Y.-H., Shaw, G., Zhou, Z., Bai, Y., Luo, R., & Ji, X.
- Venue
- Acta Crystallographica Section D Biological Crystallography
- Published
- 2008-04-19
- Volume
- 64
- Issue
- 5
- Pages
- 471-477
- ISSN
- 0907-4449
- Cited by
- 8
- References
- 2
- Licence
- journals.iucr.org/services/copyrightpolicy.html (vor)
- journals.iucr.org/services/copyrightpolicy.html#TDM (tdm)
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- CoChat. (2026). Citation check: Impact of low-frequency hotspot mutation R282Q on the structure of p53 DNA-binding domain as revealed by crystallography at 1.54 Å resolution. https://app.cochat.ai/papers/10.1107/s0907444908003338
- The paper
- Tu, C., Tan, Y.-H., Shaw, G., Zhou, Z., Bai, Y., Luo, R., & Ji, X. (2008). Impact of low-frequency hotspot mutation R282Q on the structure of p53 DNA-binding domain as revealed by crystallography at 1.54 Å resolution. Acta Crystallographica Section D Biological Crystallography. https://doi.org/10.1107/s0907444908003338
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.
