Evidence map›Paper›PMID 28402475›Full record

ArticleNucleic acids research2017

ReFOLD: a server for the refinement of 3D protein models guided by accurate quality estimates.

Ahmad N Shuid, Robert Kempster, Liam J McGuffin

Abstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Protein Structure Prediction Methods.Advances in experimental medicine and biology · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Proteomic Tools for the Analysis of Cytoskeleton Proteins.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  6. Article
  7. A NovelBiology · 2021
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Methods for the Refinement of Protein Structure 3D Models.International journal of molecular sciences · 2019
    Review
  15. Article
  16. Review
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.

Ahmad N ShuidSchool of Biological Sciences, University of Reading, Whiteknights, Reading RG6 6AS, UK.
Robert KempsterSchool of Biological Sciences, University of Reading, Whiteknights, Reading RG6 6AS, UK.
Liam J McGuffinSchool of Biological Sciences, University of Reading, Whiteknights, Reading RG6 6AS, UK.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ReFOLD is a novel hybrid refinement server with integrated high performance global and local Accuracy Self Estimates (ASEs). The server attempts to identify and to fix likely errors in user supplied 3D models of proteins via successive rounds of refinement. The server is unique in providing output for multiple alternative refined models in a way that allows users to quickly visualize the key residue locations, which are likely to have been improved. This is important, as global refinement of a full chain model may not always be possible, whereas local regions, or individual domains, can often be much improved. Thus, users may easily compare the specific regions of the alternative refined models in which they are most interested e.g. key interaction sites or domains. ReFOLD was used to generate hundreds of alternative refined models for the CASP12 experiment, boosting our group's performance in the main tertiary structure prediction category. Our successful refinement of initial server models combined with our built-in ASEs were instrumental to our second place ranking on Template Based Modeling (TBM) and Free Modeling (FM)/TBM targets. The ReFOLD server is freely available at: http://www.reading.ac.uk/bioinf/ReFOLD/.

Indexed as

Models, MolecularProtein FoldingUser-Computer InterfaceAnimalsBenchmarkingHumansInternetProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsProteinsProtein Structure, TertiaryThermodynamicsProteins

Identifiers

PMID28402475
PMCPMC5570150

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LicenceCC BY
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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.