Evidence map›Paper›PMID 20812781›Full record

ReviewAntioxidants & redox signaling2011

Thiol/Disulfide redox switches in the regulation of heme binding to proteins.

Stephen W Ragsdale, Li Yi

Abstract readReview
In one paragraph

Review in Antioxidants & redox signaling, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Regulation of protein function and degradation by heme, heme responsive motifs, and CO.Critical reviews in biochemistry and molecular biology · 2022
    Review
  5. Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Hydrogen bond donation to the heme distal ligand of Staphylococcus aureus IsdG tunes the electronic structure.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015
    Article
  16. Review
  17. Article
  18. 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.

Stephen W RagsdaleDepartment of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan 48109-0606, USA. sragsdal@umich.edu
Li Yi

Funding

Thiol/Disulfide Redox Regulation of Heme Oxygenase-2R01HL102662 · NHLBI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RAGSDALE, STEPHEN WILEY · 2010 to 2013
$2.2M
Elucidation of the Role of the Heme Regulatory Motif in Heme Oxygenase-2R21HL089837 · NHLBI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RAGSDALE, STEPHEN WILEY · 2008 to 2009
$402k
NHLBI NIH HHS R01 HL102662NHLBI NIH HHS R21 HL089837
6 · The paper itself

Abstract

This review focuses on thiol/disulfide redox switches that regulate heme binding to proteins and modulate their activities. The importance of redox switches in metabolic regulation and the general mechanism by which redox switches modulate activity are discussed. Methods are described to characterize heme-binding sites and to assess their physiological relevance. For thiol/disulfide interconversion to regulate activity of a system, the redox process must be reversible at the ambient redox potentials found within the cell; thus, methods (and their limitations) are discussed that can address the physiological relevance of a redox switch. We review recent results that define a mechanism for how thiol/disulfide redox switches that control heme binding can regulate the activities of an enzyme, heme oxygenase-2, and an ion channel, the BK potassium channel. The redox switches on these proteins are composed of different types of Cys-containing motifs that have opposite effects on heme affinity, yet have complementary effects on hypoxia sensing. Finally, a model is proposed to describe how the redox switches on heme oxygenase-2 and the BK channel form an interconnected system that is poised to sense oxygen levels in the bloodstream and to elicit the hypoxic response when oxygen levels drop below a threshold value.

Indexed as

DisulfidesHemeModels, BiologicalOxidation-ReductionProtein BindingProteinsDisulfidesHemeProteins

Identifiers

PMID20812781
PMCPMC3042308

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.