Evidence map›Paper›PMID 9420330›Full record

ArticleGenes & development1998

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

L C Myers, C M Gustafsson, D A Bushnell, M Lui, H Erdjument-Bromage, P Tempst, R D Kornberg

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 126 papers.

0numbers the graph read from it
0cells of the map it votes in
126citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

126 citing papers in PubMed, 308 citations in OpenAlex.

  1. Article
  2. Article
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  4. Article
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  6. Article
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  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Assembly of RNA polymerase II transcription initiation complexes.Current opinion in structural biology · 2022
    Review
  14. Article
  15. Structural basis for CDK7 activation by MAT1 and Cyclin H.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  16. The cryoelectron microscopy structure of the human CDK-activating kinase.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  17. Review
  18. Twenty years of Mediator complex structural studies.Biochemical Society transactions · 2019
    Review
  19. Ser7 of RNAPII-CTD facilitates heterochromatin formation by linking ncRNA to RNAi.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  20. Article

66 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

L C MyersDepartment of Structural Biology, Stanford University School of Medicine, Stanford, California 94305-5400, USA.
C M Gustafsson
D A Bushnell
M Lui
H Erdjument-Bromage
P Tempst
R D Kornberg
Stanford University · USMemorial Sloan Kettering Cancer Center · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Nicholas D Socci · 1985 to 2026
$347.4M
RNA POLYMERASE II TRANSCRIPTION SYSTEM FROM YEASTR01GM036659 · NIGMS · STANFORD UNIVERSITY · PI KORNBERG, ROGER D · 1986 to 2016
$4.7M
RNA POLYMERASE II TRANSCRIPTION SYSTEM FROM YEASTR37GM036659 · NIGMS · STANFORD UNIVERSITY · PI KORNBERG, ROGER D · 1998 to 2008
$4.6M
NCI NIH HHS 5 P30 CA08748NCI NIH HHS P30 CA008748NIGMS NIH HHS GM36659NIGMS NIH HHS R01 GM036659NIGMS NIH HHS R37 GM036659
6 · The paper itself

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.

Indexed as

Saccharomyces cerevisiae ProteinsAmino Acid SequenceBase SequenceBinding SitesDNA, ComplementaryFungal ProteinsHumansMacromolecular SubstancesMediator ComplexMolecular Sequence DataMultiprotein ComplexesRNA Polymerase IISaccharomyces cerevisiaeSequence Homology, Amino AcidTrans-ActivatorsTranscription FactorsDNA, ComplementaryFungal ProteinsMacromolecular SubstancesMED7 protein, S cerevisiaeMediator ComplexMultiprotein ComplexesRNA Polymerase IISaccharomyces cerevisiae ProteinsTrans-ActivatorsTranscription Factors

Identifiers

PMID9420330
PMCPMC316402
OpenAlexW2135992596

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.