The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.
The role of mutant p53 in human cancer
Open accessAbstract
Mutations in the TP53 (p53) gene are present in a large fraction of human tumours, which frequently express mutant p53 proteins at high but heterogeneous levels. The clinical significance of this protein accumulation remains clouded. Mouse models bearing knock‐in mutations of p53 have established that the mutant p53 proteins can drive tumour formation, invasion and metastasis through dominant negative inhibition of wild‐type p53 as well as through gain of function or ‘neomorphic’ activities that can inhibit or activate the function of other proteins. These models have also shown that mutation alone does not confer stability, so the variable staining of mutant proteins seen in human cancers reflects tumour‐specific activation of p53‐stabilizing pathways. Blocking the accumulation and activity of mutant p53 proteins may thus provide novel cancer therapeutic and diagnostic targets, but their induction by chemotherapy may paradoxically limit the effectiveness of these treatments. Copyright © 2010 Pathological Society of Great Britain and Ireland. Published by John Wiley & Sons, Ltd.
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Citations
Cites
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BackgroundMutant p53 gain of function in two mouse models of Li-Fraumeni syndrome
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Self-citationp53 isoforms can regulate p53 transcriptional activity
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Cited by
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Targeting p53 pathways: mechanisms, structures, and advances in therapy
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The miR-29 family: genomics, cell biology, and relevance to renal and cardiovascular injury
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Therapeutic targeting of p53: all mutants are equal, but some mutants are more equal than others
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HDAC6 deacetylates p53 at lysines 381/382 and differentially coordinates p53-induced apoptosis
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Regulation of the p53 Family Proteins by the Ubiquitin Proteasomal Pathway
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Disruptive chemicals, senescence and immortality
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Metadata
- Authors
- Goh, A. M., Coffill, C. R., & Lane, D. P.
- Venue
- The Journal of Pathology
- Publisher
- Wiley
- Published
- 2010-10-25
- Volume
- 223
- Issue
- 2
- Pages
- 116-126
- ISSN
- 0022-3417 (ISSN-L)
- 1096-9896
- OpenAlex
- W2078989706
- Cited by
- 398
- References
- 17
- FWCI
- 17.67
- Type
- journal article
- Language
- en
- Open access
- bronze
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