Evidence map›Paper›PMID 25308991›Full record

ArticleIsrael journal of chemistry2014

Learning To Fold Proteins Using Energy Landscape Theory.

N P Schafer, B L Kim, W Zheng, P G Wolynes

Abstract read
In one paragraph

Article in Israel journal of chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing 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

32 citing papers in PubMed.

  1. Article
  2. Review
  3. Generating the polymorph landscapes of amyloid fibrils using AI: RibbonFold.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Computationally exploring the mechanism of bacteriophage T7 gp4 helicase translocating along ssDNA.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Disorder Mediated Oligomerization ofThe journal of physical chemistry. B · 2019
    Article
  17. Article
  18. Forging tools for refining predicted protein structures.Proceedings of the National Academy of Sciences of the United States of America · 2019
    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

4 authors.

N P SchaferDepartment of Physics, Rice University, Houston, TX 77005, USA ; Center for Theoretical Biological Physics, Rice University, Houston, TX 77005, USA.
B L KimDepartment of Chemistry, Rice University, Houston, TX 77005, USA ; Center for Theoretical Biological Physics, Rice University, Houston, TX 77005, USA.
W ZhengDepartment of Chemistry, Rice University, Houston, TX 77005, USA ; Center for Theoretical Biological Physics, Rice University, Houston, TX 77005, USA.
P G WolynesDepartment of Physics, Rice University, Houston, TX 77005, USA ; Department of Chemistry, Rice University, Houston, TX 77005, USA ; Center for Theoretical Biological Physics, Rice University, Houston, TX 77005, USA.

Funding

STRUCTURE AND STABILITY OF IKB/NF-KB COMPLEXESP01GM071862 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI KOMIVES, ELIZABETH A. · 2006 to 2016
$14.9M
CONCEPTUAL ASPECTS OF THE PROTEIN FOLDING PROBLEMR01GM044557 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI WOLYNES, PETER GUY · 1990 to 2018
$4.2M
NIGMS NIH HHS P01 GM071862NIGMS NIH HHS R01 GM044557
6 · The paper itself

Abstract

This review is a tutorial for scientists interested in the problem of protein structure prediction, particularly those interested in using coarse-grained molecular dynamics models that are optimized using lessons learned from the energy landscape theory of protein folding. We also present a review of the results of the AMH/AMC/AMW/AWSEM family of coarse-grained molecular dynamics protein folding models to illustrate the points covered in the first part of the article. Accurate coarse-grained structure prediction models can be used to investigate a wide range of conceptual and mechanistic issues outside of protein structure prediction; specifically, the paper concludes by reviewing how AWSEM has in recent years been able to elucidate questions related to the unusual kinetic behavior of artificially designed proteins, multidomain protein misfolding, and the initial stages of protein aggregation.

Identifiers

PMID25308991
PMCPMC4189132

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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.