Evidence map›Paper›PMID 31589781›Full record

ArticleProteins2019

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

Andriy Kryshtafovych, Torsten Schwede, Maya Topf, Krzysztof Fidelis, John Moult

Abstract read
In one paragraph

Article in Proteins, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 237 papers.

0numbers the graph read from it
0cells of the map it votes in
237citing 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

237 citing papers in PubMed.

  1. Systematic discovery of circular permutations across the protein universe using CIRPIN.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  4. Characterization ofJournal of bacteriology · 2026
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  8. Backbone double-mutant cycle analysis quantifies hydrogen-bond energies in proteins.Protein science : a publication of the Protein Society · 2026
    Article
  9. Article
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  11. Article
  12. Article
  13. Review
  14. Modernizing biomolecular NMR: The POKY suite.The Journal of biological chemistry · 2026
    Review
  15. Article
  16. Article
  17. Protein language models trained on biophysical dynamics inform mutation effects.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  18. AlphaFold3 at CASP16.Proteins · 2026
    Article
  19. Article
  20. Article

177 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.

Andriy KryshtafovychGenome Center, University of California, Davis, Davis, California.ORCID 0000-0001-5066-7178
Torsten SchwedeBiozentrum & SIB Swiss Institute of Bioinformatics, University of Basel, Basel, Switzerland.ORCID 0000-0003-2715-335X
Maya TopfInstitute of Structural and Molecular Biology, Birkbeck College, University of London, London, UK.ORCID 0000-0002-8185-1215
Krzysztof FidelisGenome Center, University of California, Davis, Davis, California.ORCID 0000-0002-8061-412X
John MoultInstitute for Bioscience and Biotechnology Research, Rockville, Maryland.ORCID 0000-0002-3012-2282

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 GM100482NIGMS NIH HHS R01GM100482
6 · The paper itself

Abstract

CASP (critical assessment of structure prediction) assesses the state of the art in modeling protein structure from amino acid sequence. The most recent experiment (CASP13 held in 2018) saw dramatic progress in structure modeling without use of structural templates (historically "ab initio" modeling). Progress was driven by the successful application of deep learning techniques to predict inter-residue distances. In turn, these results drove dramatic improvements in three-dimensional structure accuracy: With the proviso that there are an adequate number of sequences known for the protein family, the new methods essentially solve the long-standing problem of predicting the fold topology of monomeric proteins. Further, the number of sequences required in the alignment has fallen substantially. There is also substantial improvement in the accuracy of template-based models. Other areas-model refinement, accuracy estimation, and the structure of protein assemblies-have again yielded interesting results. CASP13 placed increased emphasis on the use of sparse data together with modeling and chemical crosslinking, SAXS, and NMR all yielded more mature results. This paper summarizes the key outcomes of CASP13. The special issue of PROTEINS contains papers describing the CASP13 assessments in each modeling category and contributions from the participants.

Indexed as

Computational BiologyProtein ConformationAmino Acid SequenceHumansModels, MolecularProteinsScattering, Small AngleX-Ray DiffractionProteinsCASPcommunity wide experimentprotein structure prediction

Identifiers

PMID31589781
PMCPMC6927249

What OpenQuestion holds

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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.