The DOI matches its Crossref record; 159 of the 159 references it cites were found in a registry or an index.
The code and beyond: transcription regulation by the RNA polymerase II carboxy-terminal domain
Abstract
The carboxy-terminal domain (CTD) extends from the largest subunit of RNA polymerase II (Pol II) as a long, repetitive and largely unstructured polypeptide chain. Throughout the transcription process, the CTD is dynamically modified by post-translational modifications, many of which facilitate or hinder the recruitment of key regulatory factors of Pol II that collectively constitute the 'CTD code'. Recent studies have revealed how the physicochemical properties of the CTD promote phase separation in the presence of other low-complexity domains. Here, we discuss the intricacies of the CTD code and how the newly characterized physicochemical properties of the CTD expand the function of the CTD beyond the code.
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“CDK8 inhibition by MSC2530818 did not alter the phosphorylation profile of RBP1, suggesting that our treatment did not affect basal transcriptional programs (Sup. Figure 9B)”
From CDK8 fine-tunes IL-6 transcriptional activities by limiting STAT3 resident time at the gene loci (2020) · cites this paper as Harlen and Churchman, 2017
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Liquid-Liquid Phase Separation in Biology
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A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation
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Widespread transcription at neuronal activity-regulated enhancers
Kim, T.-K., Hemberg, M., Gray, J. M., Costa, A. M., Bear, D. M., Wu, J., Harmin, D. A., Laptewicz, M., Barbara-Haley, K., Kuersten, S., et al. (2010) · Nature · doi:10.1038/nature09033 · Cited by 2,450
The economics of ribosome biosynthesis in yeast
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Promoter-proximal pausing of RNA polymerase II: emerging roles in metazoans
Adelman, K., & Lis, J. T. (2012) · Nature Reviews Genetics · doi:10.1038/nrg3293 · Cited by 1,221
Controlling the elongation phase of transcription with P-TEFb
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Histone exchange, chromatin structure and the regulation of transcription
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Metadata
- Authors
- Harlen, K. M., & Churchman, L. S.
- Affiliations
- Harvard University (US)
- Corresponding author
- Churchman, L. Stirling
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2017-03-01
- Volume
- 18
- Issue
- 4
- Pages
- 263-273
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W2594707272
- Cited by
- 499
- References
- 159
- Citations by year
- 2026: 40 · 2025: 46 · 2024: 70 · 2023: 65 · 2022: 51 · 2021: 66 · 2020: 65 · 2019: 44 · 2018: 35 · 2017: 17
- FWCI
- 4.15
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Human Genome Research Institute (R01HG007173)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Keywords
- RNA polymerase II, C-terminal domain, post-translational modification, transcriptional regulation, phase separation, low-complexity domains
- MeSH terms
- Protein Domains, Gene Expression Regulation, Humans, Phosphorylation, Protein Processing, Post-Translational, RNA Polymerase II, Transcription, Genetic
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