Evidence map›Paper›PMID 20112293›Full record

ReviewJournal of cellular physiology2010

Coactivator recruitment: a new role for PAS domains in transcriptional regulation by the bHLH-PAS family.

Carrie L Partch, Kevin H Gardner

Abstract readReview
In one paragraph

Review in Journal of cellular physiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed.

  1. Aryl hydrocarbon receptor nuclear translocator 2: a forgotten per-ARNT-Sim transcription factor.Toxicological sciences : an official journal of the Society of Toxicology · 2026
    Review
  2. Context-dependent variability of HIF heterodimers influences interactions with macromolecular and small molecule partners.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. bHLH-PAS Proteins: Their Structure and Intrinsic Disorder.International journal of molecular sciences · 2019
    Review
  12. Article
  13. Review
  14. Formation of a repressive complex in the mammalian circadian clock is mediated by the secondary pocket of CRY1.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Small molecule modifiers of circadian clocks.Cellular and molecular life sciences : CMLS · 2013
    Review
  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

2 authors.

Carrie L PartchDepartment of Biochemistry, University of Texas Southwestern Medical Center at Dallas, Dallas, Texas 75390-8816, USA.
Kevin H Gardner

Funding

Structural studies of PAS domain signaling mechanismsR01GM081875 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI GARDNER, KEVIN H · 2007 to 2010
$1.2M
Molecular basis of selectivity for coactivator recruitment by ARNT PAS domainsF32CA130441 · NCI · UT SOUTHWESTERN MEDICAL CENTER · PI PARTCH, CARRIE L · 2007 to 2009
$148k
NCI NIH HHS CA130441NCI NIH HHS F32 CA130441NIGMS NIH HHS GM081875NIGMS NIH HHS R01 GM081875
6 · The paper itself

Abstract

Transcriptional regulation is dependent on layers of interactions between transcription factors and coactivators, controlling the specificity, temporal regulation, and extent to which transcriptional programs are executed. A key issue in the field of transcriptional regulation is to identify structural mechanisms by which transcription factors and coactivators build hierarchical protein assemblies. The basic helix-loop-helix Per-ARNT-Sim domain (bHLH-PAS) family of transcriptional regulators comprises both transcription factors and coactivators, which have different functions despite conserved domain architecture. Within this family, the tandem PAS domains typically mediate dimerization of the transcription factors, while C-terminal transactivation domains facilitate the dynamic interplay between transcription factors and coactivators. However, recent studies have shown that the modular PAS domains play an important role in regulating coactivator recruitment and oligomerization status. In this study, we provide a brief overview of the structural and functional studies that have identified a novel protein interaction interface on PAS domains utilized by both transcription factors and coactivators within the bHLH-PAS family.

Indexed as

Gene Expression RegulationTranscription, GeneticAnimalsBasic Helix-Loop-Helix ProteinsHumansProtein BindingProtein Structure, TertiaryTrans-ActivatorsBasic Helix-Loop-Helix ProteinsTrans-Activators

Identifiers

PMID20112293
PMCPMC2872778

What OpenQuestion holds

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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.