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The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.

Mapping of the p53 and mdm-2 interaction domains.

Open access
Chen, J, Marechal, V, Levine, A J·1993·Molecular and Cellular Biology

Abstract

The 90-kDa cellular protein encoded by the mouse mdm-2 oncogene binds to the p53 protein in vivo and inhibits its transactivation function (J. Momand, G. P. Zambetti, D. C. Olson, D. George, and A. J. Levine, Cell 69:1237-1245, 1992). cDNA clones encoding the human homolog of the mdm-2 protein (also called hdm-2) were isolated from a HeLa cell cDNA library. A series of monoclonal antibodies have been generated against human mdm-2 protein, and the epitopes recognized by these antibodies have been mapped. By construction of a series of deletion mutants, the region of the mdm-2 protein that is critical for complex formation with the p53 protein has been mapped to the N-terminal portion of the human mdm-2 protein. Interestingly, a monoclonal antibody with an epitope located in this same region failed to immunoprecipitate the mdm-2-p53 complex and appeared to recognize only free mdm-2 protein. The domain of the p53 protein that is sufficient for interaction with human mdm-2 protein has been mapped to the N-terminal 52 amino acid residues of the p53 protein. This region contains the transactivation domain of p53, suggesting that mdm-2 may inhibit p53 function by disrupting its interaction with the general transcription machinery.

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Metadata

Authors
Chen, J., Marechal, V, & Levine, A. J.
Venue
Molecular and Cellular Biology
Published
1993-07
Volume
13
Issue
7
Pages
4107-4114
ISSN
  • 0270-7306 (ISSN-L)
  • 1098-5549
OpenAlex
W1822460389
Cited by
689
References
7
FWCI
7.14
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Mapping of the p53 and mdm-2 interaction domains. https://app.cochat.ai/papers/10.1128/mcb.13.7.4107
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Chen, J., Marechal, V, & Levine, A. J. (1993). Mapping of the p53 and mdm-2 interaction domains. Molecular and Cellular Biology. https://doi.org/10.1128/mcb.13.7.4107

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