Student or educator? Sign up with your school email and get 6 months of Pro free.
Cited by 306

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

The Med proteins of yeast and their function through the RNA polymerase II carboxy-terminal domain

Open access
Myers, Lawrence C., Gustafsson, Claes M., Bushnell, David A., Lui, Mary, Erdjument-Bromage, Hediye, Tempst, Paul, Kornberg, Roger D.·1998·Genes & Development

Abstract

Mediator was resolved from yeast as a multiprotein complex on the basis of its requirement for transcriptional activation in a fully defined system. Three groups of mediator polypeptides could be distinguished: the products of five SRB genes, identified as suppressors of carboxy-terminal domain (CTD)-truncation mutants; products of four genes identified as global repressors; and six members of a new protein family, termed Med, thought to be primarily responsible for transcriptional activation. Notably absent from the purified mediator were Srbs 8, 9, 10, and 11, as well as members of the SWI/SNF complex. The CTD was required for function of mediator in vitro, in keeping with previous indications of involvement of the CTD in transcriptional activation in vivo. Evidence for human homologs of several mediator proteins, including Med7, points to similar mechanisms in higher cells.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1101/gad.12.1.45

Cites

2 of 2 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 2 references

Cited by

See all 306

Metadata

Authors
Myers, L. C., Gustafsson, C. M., Bushnell, D. A., Lui, M., Erdjument-Bromage, H., Tempst, P., & Kornberg, R. D.
Venue
Genes & Development
Published
1998-01-01
Volume
12
Issue
1
Pages
45-54
ISSN
  • 0890-9369 (ISSN-L)
  • 1549-5477
OpenAlex
W2135992596
Cited by
306
References
2
Type
posted content
Language
en
Open access
diamond

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: The Med proteins of yeast and their function through the RNA polymerase II carboxy-terminal domain. https://app.cochat.ai/papers/10.1101/gad.12.1.45
The paper
Myers, L. C., Gustafsson, C. M., Bushnell, D. A., Lui, M., Erdjument-Bromage, H., Tempst, P., & Kornberg, R. D. (1998). The Med proteins of yeast and their function through the RNA polymerase II carboxy-terminal domain. Genes & Development. https://doi.org/10.1101/gad.12.1.45

Data sources

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.