Evidence map›Paper›PMID 23249217›Full record

ReviewAntioxidants & redox signaling2013

Cytochromes b561: ascorbate-mediated trans-membrane electron transport.

Han Asard, Raffaella Barbaro, Paolo Trost, Alajos Bérczi

Open access · greenAbstract readReview
In one paragraph

Review in Antioxidants & redox signaling, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed, 1 pooled it
2.1field-weighted citation impact, top 15% 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

67 citing papers in PubMed, 1 synthesis or guideline pooled it, 122 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Inhibition of ascorbic acid on Pseudomonas bubulae under super-chilled storage.World journal of microbiology & biotechnology · 2026
    Article
  5. Electron currents mediated by tonoplast cytochromes b561.European biophysics journal : EBJ · 2026
    Review
  6. Article
  7. Article
  8. Review
  9. DVL, a Lectin fromAntibiotics (Basel, Switzerland) · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Genetic Markers of Postmortem Brain Iron.Journal of neurochemistry · 2025
    Article
  17. Review
  18. Article
  19. Article
  20. Article

7 more citing papers are in PubMed but not listed here.

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

4 authors at 3 institutions in 3 countries.

Han AsardDepartment of Biology, University of Antwerp, Antwerp, Belgium. han.asard@ua.ac.be
Raffaella Barbaro
Paolo Trost
Alajos Bérczi
University of Bologna · ITInstitute of Biophysics · HUUniversity of Antwerp · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

significanceCytochromes b561 (CYB561s) constitute a family of trans-membrane (TM), di-heme proteins, occurring in a variety of organs and cell types, in plants and animals, and using ascorbate (ASC) as an electron donor. CYB561s function as monodehydroascorbate reductase, regenerating ASC, and as Fe³⁺-reductases, providing reduced iron for TM transport. A CYB561-core domain is also associated with dopamine β-monooxygenase redox domains (DOMON) in ubiquitous CYBDOM proteins. In plants, CYBDOMs form large protein families. Physiological functions supported by CYB561s and CYBDOMs include stress defense, cell wall modifications, iron metabolism, tumor suppression, and various neurological processes, including memory retention. CYB561s, therefore, significantly broaden our view on the physiological roles of ASC. RECENT ADVANCES: The ubiquitous nature of CYB561s is only recently being recognized. Significant advances have been made through the study of recombinant CYB561s, revealing structural and functional properties of a unique "two-heme four-helix" protein configuration. In addition, the DOMON domains of CYBDOMs are suggested to contain another heme b. CRITICAL ISSUES: New CYB561 proteins are still being identified, and there is a need to provide an insight and overview on the various roles of these proteins and their structural properties. FUTURE DIRECTIONS: Mutant studies will reveal in greater detail the mechanisms by which CYB561s and CYBDOMs participate in cell metabolism in plants and animals. Moreover, the availability of efficient heterologous expression systems should allow protein crystallization, more detailed (atomic-level) structural information, and insights into the intra-molecular mechanism of electron transport.

Indexed as

AnimalsAscorbic AcidCytochrome b GroupElectron TransportHumansOxidation-ReductionPlantsProtein Interaction Domains and MotifsStructure-Activity RelationshipAscorbic Acidcytochrome b561Cytochrome b Group

Identifiers

PMID23249217
PMCPMC3763232
OpenAlexW1969724909

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.