Evidence map›Paper›PMID 15576508›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

Differences in the folding transition state of ubiquitin indicated by phi and psi analyses.

Tobin R Sosnick, Robin S Dothager, Bryan A Krantz

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing 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

44 citing papers in PubMed.

  1. Article
  2. Article
  3. Structure of a transient protein-folding intermediate by pressure-jump NMR spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Effects of binding partners on thermal reversion rates of photoswitchable molecules.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. AlphaFold2bioRxiv : the preprint server for biology · 2024
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Cooperative folding near the downhill limit determined with amino acid resolution by hydrogen exchange.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  15. 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
  16. 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
  17. Review
  18. A "slow" protein folds quickly in the end.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  19. Atomic-level description of ubiquitin folding.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors.

Tobin R SosnickDepartment of Biochemistry and Molecular Biology, University of Chicago, 920 East 58th Street, Chicago, IL 60637, USA. trsosnick@midway.uchicago.edu
Robin S Dothager
Bryan A Krantz

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We compare the folding transition state (TS) of ubiquitin previously identified by using psi analysis to that determined by using analysis. Both methods attempt to identify interactions and their relative populations at the rate-limiting step for folding. The TS ensemble derived from psi analysis has an extensive native-like chain topology, with a four-stranded beta-sheet network and a portion of the major helix. According to analysis, however, the TS is much smaller and more polarized, with only a local helix/hairpin motif. We find that structured regions can have values far from unity, the canonical value for such sites, because of structural relaxation of the TS. Consequently, these sites may be incorrectly interpreted as contributing little to the structure of the TS. These results stress the need for caution when interpreting and drawing conclusions from analysis alone and highlight the need for more specific tools for examining the structure and energetics of the TS ensemble.

Indexed as

Protein FoldingComputer SimulationModels, MolecularMutagenesis, Site-DirectedMutationProtein DenaturationProtein Structure, TertiaryThermodynamicsUbiquitinUbiquitin

Identifiers

PMID15576508
PMCPMC536030

What OpenQuestion holds

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Registered trials

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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.