Evidence map›Paper›PMID 29082672›Full record

ArticleProteins2018

Critical assessment of methods of protein structure prediction (CASP)-Round XII.

John Moult, Krzysztof Fidelis, Andriy Kryshtafovych, Torsten Schwede, Anna Tramontano

Abstract read
In one paragraph

Article in Proteins, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 139 papers.

0numbers the graph read from it
0cells of the map it votes in
139citing 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

139 citing papers in PubMed.

  1. Article
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  5. Article
  6. Review
  7. The physics-AI dialogue in drug design.RSC medicinal chemistry · 2025
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Learnable Filters for Geometric Scattering Modules.IEEE transactions on signal processing : a publication of the IEEE Signal Processing Society · 2024
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

79 more citing papers are in PubMed but not listed here.

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

5 authors.

John MoultInstitute for Bioscience and Biotechnology Research and Department of Cell Biology and Molecular Genetics, University of Maryland, 9600 Gudelsky Drive, Rockville, Maryland, 20850.ORCID 0000-0002-3012-2282
Krzysztof FidelisGenome Center, University of California, Davis, 451 Health Sciences Drive, Davis, California, 95616.ORCID 0000-0002-8061-412X
Andriy KryshtafovychGenome Center, University of California, Davis, 451 Health Sciences Drive, Davis, California, 95616.ORCID 0000-0001-5066-7178
Torsten SchwedeUniversity of Basel, Biozentrum & SIB Swiss Institute of Bioinformatics, Basel, Switzerland.ORCID 0000-0003-2715-335X
Anna TramontanoDepartment of Physics and Istituto Pasteur - Fondazione Cenci Bolognetti, Sapienza University of Rome, P.le Aldo Moro, 5, Rome, 00185, Italy.

Funding

Prospective analysis to determine model accuracy performance and boundaries in the post-AlphaFold2 environmentR01GM100482 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI FIDELIS, KRZYSZTOF A · 2012 to 2025
$11.1M
NIGMS NIH HHS R01 GM100482
6 · The paper itself

Abstract

This article reports the outcome of the 12th round of Critical Assessment of Structure Prediction (CASP12), held in 2016. CASP is a community experiment to determine the state of the art in modeling protein structure from amino acid sequence. Participants are provided sequence information and in turn provide protein structure models and related information. Analysis of the submitted structures by independent assessors provides a comprehensive picture of the capabilities of current methods, and allows progress to be identified. This was again an exciting round of CASP, with significant advances in 4 areas: (i) The use of new methods for predicting three-dimensional contacts led to a two-fold improvement in contact accuracy. (ii) As a consequence, model accuracy for proteins where no template was available improved dramatically. (iii) Models based on a structural template showed overall improvement in accuracy. (iv) Methods for estimating the accuracy of a model continued to improve. CASP continued to develop new areas: (i) Assessing methods for building quaternary structure models, including an expansion of the collaboration between CASP and CAPRI. (ii) Modeling with the aid of experimental data was extended to include SAXS data, as well as again using chemical cross-linking information. (iii) A team of assessors evaluated the suitability of models for a range of applications, including mutation interpretation, analysis of ligand binding properties, and identification of interfaces. This article describes the experiment and summarizes the results. The rest of this special issue of PROTEINS contains papers describing CASP12 results and assessments in more detail.

Indexed as

Models, StatisticalProtein ConformationComputational BiologyHumansModels, MolecularProteinsX-Ray DiffractionProteinsCASPcommunity wide experimentprotein structure prediction

Identifiers

PMID29082672
PMCPMC5897042

What OpenQuestion holds

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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.