Evidence map›Paper›PMID 23265640›Full record

ReviewCurrent opinion in structural biology2013

Take home lessons from studies of related proteins.

Adrian A Nickson, Beth G Wensley, Jane Clarke

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Determinants of Protein Folding Pathways: Lessons from Metamorphic Proteins.International journal of molecular sciences · 2026
    Review
  2. Review
  3. Templated folding of intrinsically disordered proteins.The Journal of biological chemistry · 2020
    Review
  4. Shared unfolding pathways of unrelated immunoglobulin-like β-sandwich proteins.Protein engineering, design & selection : PEDS · 2019
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Evolutionary trend toward kinetic stability in the folding trajectory of RNases H.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  10. Knotting and unknotting of a protein in single molecule experiments.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  11. Review
  12. Microscopic interpretation of folding ϕ-values using the transition path ensemble.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Even with nonnative interactions, the updated folding transition states of the homologs Proteins G & L are extensive and similar.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  18. Article
  19. Review
  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.

Adrian A NicksonDepartment of Chemistry, University of Cambridge, Lensfield Rd, Cambridge CB2 1EW, UK. aan23@cam.ac.uk
Beth G Wensley
Jane Clarke

Funding

Wellcome Trust 095195Wellcome Trust WT064417
6 · The paper itself

Abstract

The 'Fold Approach' involves a detailed analysis of the folding of several topologically, structurally and/or evolutionarily related proteins. Such studies can reveal determinants of the folding mechanism beyond the gross topology, and can dissect the residues required for folding from those required for stability or function. While this approach has not yet matured to the point where we can predict the native conformation of any polypeptide chain in silico, it has been able to highlight, amongst others, the specific residues that are responsible for nucleation, pathway malleability, kinetic intermediates, chain knotting, internal friction and Paracelsus switches. Some of the most interesting discoveries have resulted from the attempt to explain differences between homologues.

Indexed as

Protein FoldingComputational BiologyKineticsProteinsProteins

Identifiers

PMID23265640
PMCPMC3578095

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.