Evidence map›Paper›PMID 8896449›Full record

ArticleThe EMBO journal1996

The inducible elongin A elongation activation domain: structure, function and interaction with the elongin BC complex.

T Aso, D Haque, R J Barstead, R C Conaway, J W Conaway

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
16.1field-weighted citation impact, top 1% 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

37 citing papers in PubMed, 100 citations in OpenAlex.

  1. Article
  2. Structure of the transcribing RNA polymerase II-Elongin complex.Nature structural & molecular biology · 2023
    Article
  3. Science advances · 2023
    Article
  4. Article
  5. Review
  6. Elongin functions as a loading factor for Mediator at ATF6α-regulated ER stress response genes.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  7. Lysine methylation signaling of non-histone proteins in the nucleus.Cellular and molecular life sciences : CMLS · 2019
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

5 authors at 1 institution in 1 country.

T AsoProgram in Molecular and Cell Biology, Oklahoma Medical Research Foundation, Oklahoma City 73104, USA.
D Haque
R J Barstead
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

The elongin (SIII) complex strongly stimulates the rate of elongation by RNA polymerase II by suppressing transient pausing by polymerase at many sites along the DNA. Elongin (SIII) is composed of a transcriptionally active A subunit and two small regulatory B and C subunits, which bind stably to each other to form a binary complex that interacts with elongin A and strongly induces its transcriptional activity. The elongin (SIII) complex is a potential target for negative regulation by the von Hippel-Lindau (VHL) tumor suppressor protein, which is capable of binding stably to the elongin BC complex and preventing it from activating elongin A. Here, we identify an elongin A domain sufficient for activation of elongation and demonstrate that it is a novel type of inducible activator that targets the RNA polymerase II elongation complex and is evolutionarily conserved in species as distantly related as Caenorhabditis elegans and man. In addition, we demonstrate that both the elongin A elongation activation domain and the VHL tumor suppressor protein interact with the elongin BC complex through a conserved elongin BC binding site motif that is essential for induction of elongin A activity by elongin BC and for tumor suppression by the VHL protein.

Indexed as

LigasesTumor Suppressor ProteinsUbiquitin-Protein LigasesAmino Acid SequenceAnimalsBinding SitesCaenorhabditis elegansCaenorhabditis elegans ProteinsConserved SequenceDNAElonginGenes, Tumor SuppressorGenomic LibraryMolecular Sequence DataProtein ConformationProteinsCaenorhabditis elegans ProteinsDNAEloa protein, ratElonginLigasesProteinsRNA Polymerase IItceb-3 protein, C elegansTranscription FactorsTumor Suppressor ProteinsUbiquitin-Protein LigasesVon Hippel-Lindau Tumor Suppressor Protein

Identifiers

PMID8896449
PMCPMC452300
OpenAlexW130301589

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.