Evidence map›Paper›PMID 16116080›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2005

A funneled energy landscape for cytochrome c directly predicts the sequential folding route inferred from hydrogen exchange experiments.

Patrick Weinkam, Chenghang Zong, Peter G Wolynes

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing 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

52 citing papers in PubMed.

  1. Review
  2. Reassessing the exon-foldon correspondence using frustration analysis.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. On the role of native contact cooperativity in protein folding.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Article
  6. Dramatic Shape Changes Occur as CytochromeThe journal of physical chemistry. B · 2020
    Article
  7. Article
  8. Molecular origin of the weak susceptibility of kinesin velocity to loads and its relation to the collective behavior of kinesins.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  9. The case for defined protein folding pathways.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  10. Review
  11. Article
  12. The nature of protein folding pathways.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Review
  13. Frustration in biomolecules.Quarterly reviews of biophysics · 2014
    Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Stepwise protein folding at near amino acid resolution by hydrogen exchange and mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2013
    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.

Patrick WeinkamCenter for Theoretical Biological Physics and Department of Physics, University of California at San Diego, La Jolla, CA 92093, USA.
Chenghang Zong
Peter G Wolynes

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins fold through a variety of mechanisms. For a given protein, folding routes largely depend on the protein's stability and its native-state geometry, because the landscape is funneled. These ideas are corroborated for cytochrome c by using a coarse-grained topology-based model with a perfect funnel landscape that includes explicit modeling of the heme. The results show the importance of the heme as a nucleation site and explain the observed hydrogen exchange patterns of cytochrome c within the context of energy landscape theory.

Indexed as

Biophysical PhenomenaBiophysicsCytochromes cHemeHydrogenModels, MolecularProtein ConformationProtein FoldingThermodynamicsCytochromes cHemeHydrogen

Identifiers

PMID16116080
PMCPMC1194935

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.