Evidence map›Paper›PMID 28510063›Full record

ReviewBiophysical reviews2011

Structural gymnastics of multifunctional metamorphic proteins.

Sophia C Goodchild, Paul M G Curmi, Louise J Brown

Abstract readReview
In one paragraph

Review in Biophysical reviews, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Shining light on the dark proteome with unstructural biology.Current research in structural biology · 2026
    Article
  2. Article
  3. Biomolecules · 2023
    Article
  4. Article
  5. Metamorphic Protein Folding Encodes Multiple Anti-Pathogens (Basel, Switzerland) · 2021
    Article
  6. Article
  7. Article
  8. Functional and Regulatory Roles of Fold-Switching Proteins.Structure (London, England : 1993) · 2021
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Extant fold-switching proteins are widespread.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  17. MinE conformational switching confers robustness on self-organized Min protein patterns.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  18. Review
  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

3 authors.

Sophia C GoodchildDepartment of Chemistry and Biomolecular Sciences, Macquarie University, Sydney, New South Wales, 2109, Australia.
Paul M G CurmiSchool of Physics, University of New South Wales, Sydney, New South Wales, 2052, Australia.
Louise J BrownDepartment of Chemistry and Biomolecular Sciences, Macquarie University, Sydney, New South Wales, 2109, Australia. Louise.Brown@mq.edu.au.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The classic structure-function paradigm holds that a protein exhibits a single well-defined native state that gives rise to its biological function. Nonetheless, over the past few decades, numerous examples of proteins exhibiting biological function arising from multiple structural states of varying disorder have been identified. Most recently, several examples of 'metamorphic proteins', able to interconvert between vastly different native-like topologies under physiological conditions, have been characterised with multiple functions. In this review, we look at the concept of protein metamorphosis in relation to the current understanding of the protein structure-function landscape. Although structural dynamism observed for metamorphic proteins provides a novel source of functional versatility, the dynamic nature of the metamorphic proteins generally makes them difficult to identify and probe using conventional protein structure determination methods. However, as the existence of metamorphic proteins has now been established and techniques enabling the analysis of multiple protein conformers are improving, it is likely that this class will continue to grow in number.

Indexed as

CLIC1LymphotactinMad2Metamorphic proteins

Identifiers

PMID28510063
PMCPMC5425669

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.