The DOI matches its Crossref record; 99 of the 99 references it cites were found in a registry or an index.
Role of Intrinsic Protein Disorder in the Function and Interactions of the Transcriptional Coactivators CREB-binding Protein (CBP) and p300
Open accessAbstract
The transcriptional coactivators CREB-binding protein (CBP) and p300 undergo a particularly rich set of interactions with disordered and partly ordered partners, as a part of their ubiquitous role in facilitating transcription of genes. CBP and p300 contain a number of small structured domains that provide scaffolds for the interaction of disordered transactivation domains from a wide variety of partners, including p53, hypoxia-inducible factor 1α (HIF-1α), NF-κB, and STAT proteins, and are the targets for the interactions of disordered viral proteins that compete with cellular factors to disrupt signaling and subvert the cell cycle. The functional diversity of the CBP/p300 interactome provides an excellent example of the power of intrinsic disorder to facilitate the complexity of living systems.
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Cites
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Self-citationIntrinsically unstructured proteins: re-assessing the protein structure-function paradigm
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Self-citationIntrinsically disordered proteins in cellular signalling and regulation
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Phosphorylated CREB binds specifically to the nuclear protein CBP
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Self-citationCREB-binding Protein and p300 in Transcriptional Regulation
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Intrinsic Disorder in Transcription Factors
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Targeting transcription factors in cancer — from undruggable to reality
Bushweller, J. H. (2019) · Nature Reviews Cancer · doi:10.1038/s41568-019-0196-7 · Cited by 919
AlphaFold and Implications for Intrinsically Disordered Proteins
Ruff, K. M., & Pappu, R. V. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167208 · Cited by 635
Advances in Targeting ‘Undruggable’ transcription Factors With Small Molecules
Henley, M. J., & Koehler, A. N. (2021) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00199-0 · Cited by 409
Pioneer factors as master regulators of the epigenome and cell fate
Balsalobre, A., & Drouin, J. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00464-z · Cited by 251
Large-scale mapping and mutagenesis of human transcriptional effector domains
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Metadata
- Authors
- Dyson, H. J., & Wright, P. E.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2016-03
- Volume
- 291
- Issue
- 13
- Pages
- 6714-6722
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2294967868
- Cited by
- 317
- References
- 99
- FWCI
- 13.39
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Dyson, H. J., & Wright, P. E. (2016). Role of Intrinsic Protein Disorder in the Function and Interactions of the Transcriptional Coactivators CREB-binding Protein (CBP) and p300. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.r115.692020
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
