Evidence map›Paper›PMID 33176159›Full record

ReviewStructure (London, England : 1993)2021

Functional and Regulatory Roles of Fold-Switching Proteins.

Allen K Kim, Lauren L Porter

Open access · bronzeAbstract readReview
In one paragraph

Review in Structure (London, England : 1993), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
3.8field-weighted citation impact, top 5% 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

49 citing papers in PubMed, 91 citations in OpenAlex.

  1. Fold-Switching Proteins.Annual review of biophysics · 2026
    Review
  2. Article
  3. A dramatic protein fold switch powers a bactericidal nanomachine.bioRxiv : the preprint server for biology · 2026
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. AlphaFold2's training set powers its predictions of some fold-switched conformations.Protein science : a publication of the Protein Society · 2025
    Article
  11. Review
  12. 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
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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 1 institution in 1 country.

Allen K KimNational Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA; National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Lauren L PorterNational Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA; National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA. Electronic address: lauren.porter@nih.gov.
National Institutes of Health · US

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 respond to cellular stimuli by remodeling their secondary structures and changing their functions. Whereas several previous reviews have focused on various structural, physical-chemical, and evolutionary aspects of this newly emerging class of proteins, this minireview focuses on how fold switching modulates protein function and regulates biological processes. It first compares and contrasts fold switchers with other known types of proteins. Second, it presents examples of how various proteins can change their functions through fold switching. Third, it demonstrates that fold switchers can regulate biological processes by discussing two proteins, RfaH and KaiB, whose dramatic secondary structure remodeling events directly affect gene expression and a circadian clock, respectively. Finally, this minireview discusses how the field of protein fold switching might advance.

Indexed as

Signal TransductionBacterial ProteinsCircadian Rhythm Signaling Peptides and ProteinsEscherichia coli ProteinsPeptide Elongation FactorsProtein FoldingTrans-ActivatorsBacterial ProteinsCircadian Rhythm Signaling Peptides and ProteinsEscherichia coli ProteinsKaiB protein, cyanobacteriaPeptide Elongation FactorsRfaH protein, E coliTrans-Activatorsfold-switching proteinsmetamorphic proteinsprotein foldingprotein functionprotein structure

Identifiers

PMID33176159
PMCPMC8184262
OpenAlexW3102499948

What OpenQuestion holds

Textmetadata
LicenceTDM
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.