Evidence map›Paper›PMID 28500133›Full record

ArticleThe Journal of biological chemistry2017

The heme-regulatory motif of nuclear receptor Rev-erbβ is a key mediator of heme and redox signaling in circadian rhythm maintenance and metabolism.

Eric L Carter, Yanil Ramirez, Stephen W Ragsdale

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. 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
1.7field-weighted citation impact, top 18% 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, 38 citations in OpenAlex.

  1. Review
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  8. Review
  9. Regulation of protein function and degradation by heme, heme responsive motifs, and CO.Critical reviews in biochemistry and molecular biology · 2022
    Review
  10. Review
  11. Review
  12. Article
  13. Review
  14. Ferric heme as a CO/NO sensor in the nuclear receptor Rev-Erbß by coupling gas binding to electron transfer.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Interplay of Heme with Macrophages in Homeostasis and Inflammation.International journal of molecular sciences · 2020
    Review
  20. Heme binding to human CLOCK affects interactions with the E-box.Proceedings of the National Academy of Sciences of the United States of America · 2019
    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

3 authors at 1 institution in 1 country.

Eric L CarterFrom the Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109.ORCID 0000-0003-2877-3411
Yanil RamirezFrom the Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109.
Stephen W RagsdaleFrom the Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109 sragsdal@umich.edu.ORCID 0000-0003-3938-8906
University of Michigan · US

Funding

Redox Regulation of Heme Oxygenase-2 and the Nuclear Receptor Rev-Erb-beta by their Heme Responsive MotifsR01GM123513 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RAGSDALE, STEPHEN WILEY · 2017 to 2020
$1.5M
Redox Modulation of Repression by Rev-erb, a Heme-Binding Nuclear ReceptorF32HL114150 · NHLBI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI CARTER, ERIC LEE · 2013 to 2016
$128k
NHLBI NIH HHS F32 HL114150NIGMS NIH HHS R01 GM123513
6 · The paper itself

Abstract

Rev-erbβ is a heme-responsive transcription factor that regulates genes involved in circadian rhythm maintenance and metabolism, effectively bridging these critical cellular processes. Heme binding to Rev-erbβ indirectly facilitates its interaction with the nuclear receptor co-repressor (NCoR1), resulting in repression of Rev-erbβ target genes. Fe

Indexed as

Circadian RhythmSignal TransductionAmino Acid MotifsHemeIronKineticsNuclear Receptor Co-Repressor 1Oxidation-ReductionProtein BindingProtein DomainsReceptors, Cytoplasmic and NuclearRepressor ProteinsSpectrophotometry, UltravioletHemeIronNCOR1 protein, humanNR1D2 protein, humanNuclear Receptor Co-Repressor 1Receptors, Cytoplasmic and NuclearRepressor ProteinsDNA-binding proteinenzyme kineticshemeligand-binding proteinnuclear receptorpre-steady-state kineticsredox regulationtranscription repressorultraviolet-visible spectroscopy (UV-visible spectroscopy)

Identifiers

PMID28500133
PMCPMC5500795
OpenAlexW2613487665

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.