Evidence map›Paper›PMID 28833563›Full record

ArticleProteins2018

Assessment of model accuracy estimations in CASP12.

Andriy Kryshtafovych, Bohdan Monastyrskyy, Krzysztof Fidelis, 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 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing 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

30 citing papers in PubMed.

  1. Article
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  10. Using physical features of protein core packing to distinguish real proteins from decoys.Protein science : a publication of the Protein Society · 2020
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  12. Article
  13. Review
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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, California.ORCID 0000-0001-5066-7178
Bohdan MonastyrskyyGenome Center, University of California, Davis, California.
Krzysztof FidelisGenome Center, University of California, Davis, California.
Torsten SchwedeBiozentrum, University of Basel, Basel, Switzerland.
Anna TramontanoDepartment of Physics, Sapienza University of Rome, Rome, 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

The record high 42 model accuracy estimation methods were tested in CASP12. The paper presents results of the assessment of these methods in the whole-model and per-residue accuracy modes. Scores from four different model evaluation packages were used as the "ground truth" for assessing accuracy of methods' estimates. They include a rigid-body score-GDT_TS, and three local-structure based scores-LDDT, CAD and SphereGrinder. The ability of methods to identify best models from among several available, predict model's absolute accuracy score, distinguish between good and bad models, predict accuracy of the coordinate error self-estimates, and discriminate between reliable and unreliable regions in the models was assessed. Single-model methods advanced to the point where they are better than clustering methods in picking the best models from decoy sets. On the other hand, consensus methods, taking advantage of the availability of large number of models for the same target protein, are still better in distinguishing between good and bad models and predicting local accuracy of models. The best accuracy estimation methods were shown to perform better with respect to the frozen in time reference clustering method and the results of the best method in the corresponding class of methods from the previous CASP. Top performing single-model methods were shown to do better than all but three CASP12 tertiary structure predictors when evaluated as model selectors.

Indexed as

Models, MolecularProtein ConformationCluster AnalysisComputational BiologyDatabases, ProteinHumansProteinsSequence AlignmentSequence Analysis, ProteinProteinsCASPEMAestimation of model accuracymodel quality assessmentprotein structure modelingprotein structure predictionQA

Identifiers

PMID28833563
PMCPMC5816721

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.