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Cited by 349

The DOI matches its Crossref record; 51 of the 51 references it cites were found in a registry or an index.

Physical and Functional Interaction of SMADs and p300/CBP

Open access
Pouponnot, Celio, Jayaraman, Lata, Massagué, Joan·1998·Journal of Biological Chemistry

Abstract

SMADs are transforming growth factor beta (TGF-beta) receptor substrates and mediators of TGF-beta transcriptional responses. Here we provide evidence that the coactivators p300 and CBP interact with Smads 1 through 4. The biological relevance of this interaction is shown in vivo by overexpression of the adenovirus E1A protein and mutant forms of E1A that lack p300-binding sites. Wild-type E1A, but not the mutants, inhibits SMAD-dependent transcriptional responses to TGF-beta. E1A also inhibits the intrinsic transactivating function of the Smad4 MH2 domain. In addition, overexpression of p300 enhances SMAD-dependent transactivation. Our results suggest a role for p300/CBP in SMAD-mediated transcriptional activation and provide an explanation for the observed ability of E1A to interfere with TGF-beta action.

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Metadata

Authors
Pouponnot, C., Jayaraman, L., & Massagué, J.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1998-09
Volume
273
Issue
36
Pages
22865-22868
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2026436579
Cited by
349
References
51
FWCI
11.14
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Physical and Functional Interaction of SMADs and p300/CBP. https://app.cochat.ai/papers/10.1074/jbc.273.36.22865
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Pouponnot, C., Jayaraman, L., & Massagué, J. (1998). Physical and Functional Interaction of SMADs and p300/CBP. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.273.36.22865

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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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