Evidence map›Paper›PMID 7638163›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1995

Positive regulation of general transcription factor SIII by a tailed ubiquitin homolog.

K P Garrett, T Aso, J N Bradsher, S I Foundling, W S Lane, R C Conaway, J W Conaway

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
4.5field-weighted citation impact, top 4% of its field
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

34 citing papers in PubMed, 99 citations in OpenAlex.

  1. Nitration in cancer signaling.Redox biology · 2026
    Review
  2. Article
  3. Structure of the transcribing RNA polymerase II-Elongin complex.Nature structural & molecular biology · 2023
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
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  18. Article
  19. Activation of HIF1alpha ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complex.Proceedings of the National Academy of Sciences of the United States of America · 2000
    Article
  20. Article
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 1 institution in 1 country.

K P GarrettProgram in Molecular and Cell Biology, Oklahoma Medical Research Foundation, Oklahoma City 73104, USA.
T Aso
J N Bradsher
S I Foundling
W S Lane
R C Conaway
J W Conaway
Oklahoma Medical Research Foundation · US

Funding

BIOCHEMISTRY OF EUKARYOTIC MESSENGER RNA SYNTHESISR37GM041628 · NIGMS · STOWERS INSTITUTE FOR MEDICAL RESEARCH · PI CONAWAY, RONALD C. · 2000 to 2009
$3.8M
BIOCHEMISTRY OF EUKARYOTIC MESSENGER SYNTHESISR01GM041628 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI CONAWAY, JOAN W, CONAWAY, RONALD C. · 1989 to 2013
$1.5M
NIGMS NIH HHS GM41628
6 · The paper itself

Abstract

General transcription factor SIII, a heterotrimer composed of 110-kDa (p110), 18-kDa (p18), and 15-kDa (p15) subunits, increases the catalytic rate of transcribing RNA polymerase II by suppressing transient pausing by polymerase at multiple sites on DNA templates. Here we report molecular cloning and biochemical characterization of the SIII p18 subunit, which is found to be a member of the ubiquitin homology (UbH) gene family and functions as a positive regulatory subunit of SIII. p18 is a 118-amino acid protein composed of an 84-residue N-terminal UbH domain fused to a 34-residue C-terminal tail. Mechanistic studies indicate that p18 activates SIII transcriptional activity above a basal level inherent in the SIII p110 and p15 subunits. Taken together, these findings establish a role for p18 in regulating the activity of the RNA polymerase II elongation complex, and they bring to light a function for a UbH domain protein in transcriptional regulation.

Indexed as

Amino Acid SequenceAnimalsBase SequenceCloning, MolecularDNA, ComplementaryElonginIn Vitro TechniquesModels, MolecularMolecular Sequence DataMolecular WeightProtein ConformationRatsRNA Polymerase IISequence Homology, Amino AcidTranscription FactorsUbiquitinsDNA, ComplementaryElonginRNA Polymerase IITranscription FactorsUbiquitins

Identifiers

PMID7638163
PMCPMC41301
OpenAlexW2076665343

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.