The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.
Mammalian mediator of transcriptional regulation and its possible role as an end-point of signal transduction pathways
Open accessAbstract
A multiprotein complex isolated from murine cells is identified as a counterpart of the yeast Mediator of transcriptional regulation on the basis of the following: homologs of two subunits of yeast Mediator, Srb7 and Med7, copurify with the complex; peptide sequencing reveals, in addition, homologs of the yeast Mediator subunits Rgr1 and Med6; as with yeast Mediator, the mouse complex binds to the RNA polymerase II C-terminal domain (CTD) and stimulates phosphorylation of the CTD by TFIIH. Peptide sequencing also identifies a component of mouse Mediator as a relative of Ring-3 protein, a mitogen-activated nuclear protein kinase, raising the possibility of Mediator as an end point of signal transduction pathways.
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Metadata
- Authors
- Jiang, Y. W., Veschambre, P., Erdjument-Bromage, H., Tempst, P., Conaway, J. W., Conaway, R. C., & Kornberg, R. D.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1998-07-21
- Volume
- 95
- Issue
- 15
- Pages
- 8538-8543
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2080910217
- Cited by
- 305
- References
- 40
- FWCI
- 6.42
- Type
- journal article
- Language
- en
- Open access
- green
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- Jiang, Y. W., Veschambre, P., Erdjument-Bromage, H., Tempst, P., Conaway, J. W., Conaway, R. C., & Kornberg, R. D. (1998). Mammalian mediator of transcriptional regulation and its possible role as an end-point of signal transduction pathways. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.95.15.8538
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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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