Evidence map›Paper›PMID 18515799›Full record

ArticleThe Journal of biological chemistry2008

Physical and functional interactions of monoubiquitylated transactivators with the proteasome.

Chase T Archer, Lyle Burdine, Bo Liu, Anwarul Ferdous, Stephen Albert Johnston, Thomas Kodadek

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

23 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Review
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  9. Article
  10. Regulation of gene expression by the ubiquitin-proteasome system.Seminars in cell & developmental biology · 2012
    Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Ubiquitin-binding domains - from structures to functions.Nature reviews. Molecular cell biology · 2009
    Review
  18. Article
  19. Article
  20. Review
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

6 authors at 1 institution in 1 country.

Chase T ArcherDivision of Translational Research and Department of Internal Medicine, University of Texas-Southwestern Medical Center, Dallas, TX 75390-9185, USA.
Lyle Burdine
Bo Liu
Anwarul Ferdous
Stephen Albert Johnston
Thomas Kodadek
The University of Texas Southwestern Medical Center · US

Funding

Post-translational modification of activatorsR01GM071833 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI KODADEK, THOMAS J. · 2004 to 2008
$1.4M
NIGMS NIH HHS GM 71833
6 · The paper itself

Abstract

Destabilization of activator-DNA complexes by the proteasomal ATPases can inhibit transcription by limiting activator interaction with DNA. Modification of the activator by monoubiquitylation protects the activator from this destabilization activity. In this study, we probe the mechanism of this protective effect of monoubiquitylation. Using novel label transfer and chemical cross-linking techniques, we show that ubiquitin contacts the ATPase complex directly, apparently via Rpn1 and Rpt1. This interaction results in the dissociation of the activation domain-ATPase complex via an allosteric process. A model is proposed in which activator monoubiquitylation serves to limit the lifetime of the activator-ATPase complex interaction and thus the ability of the ATPases to unfold the activator and dissociate the protein-DNA complex.

Indexed as

Transcriptional ActivationAdenosine TriphosphatasesCross-Linking ReagentsDNADNA-Binding ProteinsHeLa CellsHumansHydrolysisInhibitory Concentration 50Models, ChemicalProteasome Endopeptidase ComplexProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinAdenosine TriphosphatasesCross-Linking ReagentsDNADNA-Binding ProteinsProteasome Endopeptidase ComplexRPN1 protein, S cerevisiaeRPT1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin

Identifiers

PMID18515799
PMCPMC2490782
OpenAlexW1985562398

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.