Evidence map›Paper›PMID 33436410›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

Ferric heme as a CO/NO sensor in the nuclear receptor Rev-Erbß by coupling gas binding to electron transfer.

Anindita Sarkar, Eric L Carter, Jill B Harland, Amy L Speelman, Nicolai Lehnert, Stephen W Ragsdale

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

13 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Gas-sensing riboceptors.RNA biology · 2024
    Article
  6. Biosynthesis of High-Active Hemoproteins by the Efficient Heme-Supply Pichia Pastoris Chassis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Article
  7. Review
  8. Molecular Mechanisms of Iron and Heme Metabolism.Annual review of nutrition · 2022
    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. Early processes in heme-based CO-sensing proteins.Frontiers in molecular biosciences · 2022
    Review
  11. Review
  12. Review
  13. 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

6 authors at 1 institution in 1 country.

Anindita SarkarDepartment of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109.ORCID 0000-0002-7947-860X
Eric L CarterDepartment of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109.ORCID 0000-0003-2877-3411
Jill B HarlandDepartment of Chemistry, University of Michigan, Ann Arbor, MI 48109.ORCID 0000-0003-0274-6722
Amy L SpeelmanDepartment of Chemistry, University of Michigan, Ann Arbor, MI 48109.
Nicolai LehnertDepartment of Chemistry, University of Michigan, Ann Arbor, MI 48109.ORCID 0000-0002-5221-5498
Stephen W RagsdaleDepartment of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109; sragsdal@umich.edu.ORCID 0000-0003-3938-8906
University of Michigan · US

Funding

Metalloenzyme structure, function and assemblyR35GM126982 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI CATHERINE L DRENNAN · 2018 to 2026
$3.4M
Metalloprotein Mechanisms of Redox Regulation and CatalysisR35GM141758 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RAGSDALE, STEPHEN WILEY · 2021 to 2025
$3.0M
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
NIGMS NIH HHS R01 GM123513NIGMS NIH HHS R35 GM126982NIGMS NIH HHS R35 GM141758
6 · The paper itself

Abstract

Rev-Erbβ is a nuclear receptor that couples circadian rhythm, metabolism, and inflammation. Heme binding to the protein modulates its function as a repressor, its stability, its ability to bind other proteins, and its activity in gas sensing. Rev-Erbβ binds Fe

Indexed as

ElectronsBinding SitesBiological TransportCarbon MonoxideCircadian RhythmElectron Spin Resonance SpectroscopyElectron TransportEscherichia coliGene ExpressionHemeHumansIronModels, BiologicalModels, MolecularNitric OxideOxidation-ReductionCarbon MonoxideHemeIronNitric OxideNR1D2 protein, humanReceptors, Cytoplasmic and NuclearRecombinant Fusion ProteinsRepressor Proteinselectro-chemical couplinghemeredoxRev-Erb

Identifiers

PMID33436410
PMCPMC7826342
OpenAlexW3120495139

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.