Evidence map›Paper›PMID 26344049›Full record

ArticleProteins2016

Methods of model accuracy estimation can help selecting the best models from decoy sets: Assessment of model accuracy estimations in CASP11.

Andriy Kryshtafovych, Alessandro Barbato, Bohdan Monastyrskyy, Krzysztof Fidelis, Torsten Schwede, Anna Tramontano

Abstract read
In one paragraph

Article in Proteins, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing 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

44 citing papers in PubMed.

  1. Article
  2. Article
  3. Recent advances and challenges in protein complex model accuracy estimation.Computational and structural biotechnology journal · 2024
    Review
  4. Article
  5. Article
  6. Article
  7. Accurate protein stability predictions from homology models.Computational and structural biotechnology journal · 2023
    Article
  8. Article
  9. Article
  10. Using physical features of protein core packing to distinguish real proteins from decoys.Protein science : a publication of the Protein Society · 2020
    Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. 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

6 authors.

Andriy KryshtafovychGenome Center, University of California, Davis, California. akryshtafovych@ucdavis.edu.
Alessandro BarbatoBiozentrum, University of Basel, Basel, Switzerland.
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 article presents assessment of the model accuracy estimation methods participating in CASP11. The results of the assessment are expected to be useful to both-developers of the methods and users who way too often are presented with structural models without annotations of accuracy. The main emphasis is placed on the ability of techniques to identify the best models from among several available. Bivariate descriptive statistics and ROC analysis are used to additionally assess the overall correctness of the predicted model accuracy scores, the correlation between the predicted and observed accuracy of models, the effectiveness in distinguishing between good and bad models, the ability to discriminate between reliable and unreliable regions in models, and the accuracy of the coordinate error self-estimates. A rigid-body measure (GDT_TS) and three local-structure-based scores (LDDT, CADaa, and SphereGrinder) are used as reference measures for evaluating methods' performance. Consensus methods, taking advantage of the availability of several models for the same target protein, perform well on the majority of tasks. Methods that predict accuracy on the basis of a single model perform comparably to consensus methods in picking the best models and in the estimation of how accurate is the local structure. More groups than in previous experiments submitted reasonable error estimates of their own models, most likely in response to a recommendation from CASP and the increasing demand from users. Proteins 2016; 84(Suppl 1):349-369. © 2015 Wiley Periodicals, Inc.

Indexed as

BenchmarkingModels, MolecularModels, StatisticalSoftwareAlgorithmsComputational BiologyHumansInternetProtein FoldingProteinsProtein Structure, SecondaryProtein Structure, TertiaryROC CurveThermodynamicsProteinsCASPEMAestimation of model accuracymodel quality assessmentprotein structure modelingprotein structure predictionQA

Identifiers

PMID26344049
PMCPMC4781682

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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.