Evidence map›Paper›PMID 37431685›Full record

ArticleBioEssays : news and reviews in molecular, cellular and developmental biology2023

Fluid protein fold space and its implications.

Lauren L Porter

Abstract read
In one paragraph

Article in BioEssays : news and reviews in molecular, cellular and developmental biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Fold-Switching Proteins.Annual review of biophysics · 2026
    Review
  2. Article
  3. Article
  4. On the emergence of metabolism: the evolution of proteins that powered life.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  5. Article
  6. Unveiling the cold reality of metamorphic proteins.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Review
  8. Review
  9. Article
  10. Temperature-dependent fold-switching mechanism of the circadian clock protein KaiB.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Review
  12. Article
  13. Article
  14. Protein Fold Usages in Ribosomes: Another Glance to the Past.International journal of molecular sciences · 2024
    Article
  15. Metamorphic proteins and how to find them.Current opinion in structural biology · 2024
    Review
  16. SSDraw: Software for generating comparative protein secondary structure diagrams.Protein science : a publication of the Protein Society · 2023
    Article
  17. 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

1 author.

Lauren L PorterNational Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, Maryland, USA.ORCID 0000-0003-2031-8326

Funding

Predictions and experimental validation of fold-switching proteinsZIALM202011 · NLM · NATIONAL LIBRARY OF MEDICINE · PI PORTER, LAUREN · 2020 to 2025
$6.5M
Intramural NIH HHS ZIA LM202011
6 · The paper itself

Abstract

Fold-switching proteins, which remodel their secondary and tertiary structures in response to cellular stimuli, suggest a new view of protein fold space. For decades, experimental evidence has indicated that protein fold space is discrete: dissimilar folds are encoded by dissimilar amino acid sequences. Challenging this assumption, fold-switching proteins interconnect discrete groups of dissimilar protein folds, making protein fold space fluid. Three recent observations support the concept of fluid fold space: (1) some amino acid sequences interconvert between folds with distinct secondary structures, (2) some naturally occurring sequences have switched folds by stepwise mutation, and (3) fold switching is evolutionarily selected and likely confers advantage. These observations indicate that minor amino acid sequence modifications can transform protein structure and function. Consequently, proteomic structural and functional diversity may be expanded by alternative splicing, small nucleotide polymorphisms, post-translational modifications, and modified translation rates.

Indexed as

Protein FoldingProteomicsAmino Acid SequenceModels, MolecularProteinsProteinsalternative splicingmetamorphic proteinsprotein evolutionprotein foldingprotein fold switching

Identifiers

PMID37431685
PMCPMC10529699

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.