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The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.

Interaction and functional collaboration of p300/CBP and bHLH proteins in muscle and B-cell differentiation.

Open access
Eckner, R, Yao, T P, Oldread, E, Livingston, D M·1996·Genes & Development

Abstract

Differentiation of skeletal muscle cells and B lymphocytes is regulated by basic helix-loop-helix (bHLH) proteins. Both differentiation programs are inhibited by the adenovirus E1A oncoprotein. Analysis of E1A mutants has implicated two of its cellular-binding proteins, p300 and CBP, in controlling certain aspects of differentiation. We find that p300 can cooperate with tissue-specific bHLH proteins in activating target genes and requires only the bHLH domain of such proteins to stimulate E box-directed transcription. Importantly, the ability of bHLH proteins to activate transcription correlates with the presence of p300/CBP in E box-dependent DNA-binding complexes, because both phenomena require at least two adjacent E-box motifs. Microinjection of p300/CBP antibodies into myoblasts blocks terminal differentiation, cell fusion, and transcriptional activity of myogenic bHLH proteins. These results suggest that the function of p300/CBP is essential for the execution of key aspects of cellular differentiation.

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Metadata

Authors
Eckner, R., Yao, T. P., Oldread, E., & Livingston, D. M.
Venue
Genes & Development
Published
1996-10-01
Volume
10
Issue
19
Pages
2478-2490
ISSN
  • 0890-9369 (ISSN-L)
  • 1549-5477
OpenAlex
W2115034716
Cited by
362
References
5
Type
posted content
Language
en
Open access
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CoChat. (2026). Citation check: Interaction and functional collaboration of p300/CBP and bHLH proteins in muscle and B-cell differentiation. https://app.cochat.ai/papers/10.1101/gad.10.19.2478
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Eckner, R., Yao, T. P., Oldread, E., & Livingston, D. M. (1996). Interaction and functional collaboration of p300/CBP and bHLH proteins in muscle and B-cell differentiation. Genes & Development. https://doi.org/10.1101/gad.10.19.2478

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