Evidence map›Paper›PMID 12801412›Full record

ArticleGenome biology2003

A phylogenetic study of cytochrome b561 proteins.

Wim Verelst, Han Asard

Open access · goldAbstract readComparative Study
In one paragraph

Article in Genome biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.4field-weighted citation impact, top 8% 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

27 citing papers in PubMed, 63 citations in OpenAlex.

  1. DVL, a Lectin fromAntibiotics (Basel, Switzerland) · 2025
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  4. Iron Homeostasis in Insects.Annual review of entomology · 2023
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  8. Review
  9. ZIP13: A Study ofFrontiers in genetics · 2017
    Review
  10. Article
  11. Structure and mechanism of a eukaryotic transmembrane ascorbate-dependent oxidoreductase.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  12. Article
  13. Dihydrolipoic acid reduces cytochrome b561 proteins.European biophysics journal : EBJ · 2013
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Mining Cytochrome b561 proteins from plant genomes.International journal of bioinformatics research and applications · 2010
    Article
  20. 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 at 2 institutions in 2 countries.

Wim VerelstLaboratory of Plant Physiology, Department of Biology, University of Antwerp, Groenenborgerlaan 171, B-2020 Antwerp, Belgium. wverelst@ruca.ua.ac.be
Han Asard
University of Antwerp · BEUniversity of Nebraska–Lincoln · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundAs an antioxidant and cofactor to numerous metabolic enzymes, ascorbate has an essential role in plants and animals. Cytochromes b561 constitute a class of intrinsic membrane proteins involved in ascorbate regeneration. Despite their importance in ascorbate metabolism, no evolutionary analysis has been presented so far on this newly described protein family.

resultsCytochromes b561 have been identified in a large number of phylogenetically distant species, but are absent in fungi and prokaryotes. Most species contain three or four cytochrome b561 paralogous proteins, and the encoding genes usually have four or five exons. At the protein level, sequence similarities are rather low between cytochromes b561 within a single species (34-45% identity), and among phylogenetically distant species (around 30% identity). However, particular structural features characterizing this protein family are well conserved in members from all species investigated. These features comprise six transmembrane helices, four strictly conserved histidine residues, probably coordinating the two heme molecules, and putative ascorbate and monodehydro-ascorbate (MDHA) substrate-binding sites. Analysis of plant cytochromes b561 shows a separation between those from monocotyledonous and dicotyledonous species in a phylogenetic tree.

conclusionsAll cytochromes b561 have probably evolved from a common ancestral protein before the separation of plants and animals. Their phyletic distribution mirrors the use of ascorbate as primary antioxidant, indicating their role in ascorbate homeostasis and antioxidative defense. In plants, the differentiation into four cytochrome b561 isoforms probably occurred before the separation between monocots and dicots.

Indexed as

AnimalsArabidopsisArabidopsis ProteinsCaenorhabditis elegansCaenorhabditis elegans ProteinsCattleCiona intestinalisCraterostigmaCytochrome b GroupDrosophila melanogasterDrosophila ProteinsGenomeGenome, PlantHumansMiceOryzaArabidopsis ProteinsCaenorhabditis elegans Proteinscytochrome b561Cytochrome b GroupDrosophila ProteinsPlant ProteinsXenopus Proteins

Identifiers

PMID12801412
PMCPMC193617
OpenAlexW1596520144

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.