Evidence map›Paper›PMID 32152224›Full record

ArticleThe Journal of biological chemistry2020

The heme-regulatory motifs of heme oxygenase-2 contribute to the transfer of heme to the catalytic site for degradation.

Angela S Fleischhacker, Amanda L Gunawan, Brent A Kochert, Liu Liu, Thomas E Wales, Maelyn C Borowy, John R Engen, Stephen W Ragsdale

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

15 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Heme Oxygenase-1 and Its Role in Colorectal Cancer.Antioxidants (Basel, Switzerland) · 2023
    Review
  8. Article
  9. Review
  10. Regulation of protein function and degradation by heme, heme responsive motifs, and CO.Critical reviews in biochemistry and molecular biology · 2022
    Review
  11. Review
  12. Review
  13. Review
  14. Article
  15. 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

8 authors at 2 institutions in 1 country.

Angela S FleischhackerDepartment of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109-0606.
Amanda L GunawanDepartment of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109-0606.
Brent A KochertDepartment of Chemistry and Chemical Biology, Northeastern University, Boston, Massachusetts 02115.
Liu LiuDepartment of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109-0606.
Thomas E WalesDepartment of Chemistry and Chemical Biology, Northeastern University, Boston, Massachusetts 02115.
Maelyn C BorowyDepartment of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109-0606.
John R EngenDepartment of Chemistry and Chemical Biology, Northeastern University, Boston, Massachusetts 02115.
Stephen W RagsdaleDepartment of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109-0606. Electronic address: sragsdal@umich.edu.
University of Michigan · USNortheastern University · 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
NIGMS NIH HHS R01 GM123513
6 · The paper itself

Abstract

Heme-regulatory motifs (HRMs) are present in many proteins that are involved in diverse biological functions. The C-terminal tail region of human heme oxygenase-2 (HO2) contains two HRMs whose cysteine residues form a disulfide bond; when reduced, these cysteines are available to bind Fe

Indexed as

Catalytic DomainHemeHeme Oxygenase (Decyclizing)HumansHydrogen Deuterium Exchange-Mass SpectrometryIronMolecular Dynamics SimulationHemeheme oxygenase-2Heme Oxygenase (Decyclizing)Ironconformational changeenzyme kineticsenzyme mechanismheme-binding siteheme oxygenaseheme-regulatory motifhydrogen-deuterium exchange mass spectrometry (HDX-MS)hydrogen exchange mass spectrometryintramolecular interactionmembrane proteinmetalloproteinprotein dynamicsprotein-protein interaction

Identifiers

PMID32152224
PMCPMC7170523
OpenAlexW3009832291

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.