The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
p300 Functions as a Coactivator for the Peroxisome Proliferator-activated Receptor α
Open accessAbstract
The integrator protein, p300, was demonstrated to interact with mouse peroxisome proliferator-activated receptor alpha in a ligand-enhanced manner. The PPARalpha-interacting domain of p300 was mapped to amino acids 39-117 which interacted strongly with PPARalpha but did not interact with retinoic acid receptor-gamma or retinoid X receptor-alpha. Amino acids within the carboxyl terminus of PPARalpha as well as residues within the hinge region were required for ligand-dependent interaction with p300. p300 enhanced the transcriptional activation properties of PPARalpha and, therefore, can be considered a bona fide coactivator for this nuclear receptor. These observations extend the group of p300-interacting proteins to include mPPARalpha and further characterize the molecular mechanisms of PPARalpha-mediated transcriptional regulation.
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Cites
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Cited by
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Metadata
- Authors
- Dowell, P., Ishmael, J. E., Avram, D., Peterson, V. J., Nevrivy, D. J., & Leid, M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1997-12
- Volume
- 272
- Issue
- 52
- Pages
- 33435-33443
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2017153232
- Cited by
- 176
- References
- 12
- FWCI
- 5.17
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Dowell, P., Ishmael, J. E., Avram, D., Peterson, V. J., Nevrivy, D. J., & Leid, M. (1997). p300 Functions as a Coactivator for the Peroxisome Proliferator-activated Receptor α. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.272.52.33435
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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