Evidence map›Paper›PMID 25038785›Full record

ArticleNature chemical biology2014

Evolutionary relationship of two ancient protein superfolds.

José Arcadio Farías-Rico, Steffen Schmidt, Birte Höcker

Abstract read
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In one paragraph

Article in Nature chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing 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

40 citing papers in PubMed.

  1. The history of enzyme evolution embedded in metabolism.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Retracing the evolution of a modern periplasmic binding protein.Protein science : a publication of the Protein Society · 2023
    Article
  10. Fluid protein fold space and its implications.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Article
  11. Article
  12. Introducing creative destruction as a mechanism in protein evolution.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  13. Creative destruction: New protein folds from old.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  14. Simple mechanisms for the evolution of protein complexity.Protein science : a publication of the Protein Society · 2022
    Review
  15. Review
  16. Mechanisms of protein evolution.Protein science : a publication of the Protein Society · 2022
    Review
  17. Article
  18. Folding and Evolution of a Repeat Protein on the Ribosome.Frontiers in molecular biosciences · 2022
    Article
  19. Article
  20. Evolution, folding, and design of TIM barrels and related proteins.Current opinion in structural biology · 2021
    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

3 authors.

José Arcadio Farías-RicoMax Planck Institute for Developmental Biology, Tübingen, Germany.
Steffen SchmidtMax Planck Institute for Developmental Biology, Tübingen, Germany.
Birte HöckerMax Planck Institute for Developmental Biology, Tübingen, Germany.ORCID 0000000282509462

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins are the molecular machines of the cell that fold into specific three-dimensional structures to fulfill their functions. To improve our understanding of how the structure and function of proteins arises, it is crucial to understand how evolution has generated the structural diversity we observe today. Classically, proteins that adopt different folds are considered to be nonhomologous. However, using state-of-the-art tools for homology detection, we found evidence of homology between proteins of two ancient and highly populated protein folds, the (βα)8-barrel and the flavodoxin-like fold. We detected a family of sequences that show intermediate features between both folds and determined what is to our knowledge the first representative crystal structure of one of its members, giving new insights into the evolutionary link of two of the earliest folds. Our findings contribute to an emergent vision where protein superfolds share common ancestry and encourage further approaches to complete the mapping of structure space onto sequence space.

Indexed as

Evolution, MolecularProtein FoldingAmino Acid SequenceBiological EvolutionConserved SequenceCrystallography, X-RayFlavodoxinModels, MolecularMolecular Sequence DataPeptide MappingProteinsProtein Structure, SecondaryProtein Structure, TertiarySequence HomologyFlavodoxinProteins

Identifiers

PMID25038785

What OpenQuestion holds

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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.