Evidence map›Paper›PMID 29159950›Full record

ArticleProteins2018

Evaluation of the template-based modeling in CASP12.

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

Abstract readEvaluation Study
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 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing 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

39 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Illuminating the "Twilight Zone": Advances in Difficult Protein Modeling.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Toward the solution of the protein structure prediction problem.The Journal of biological chemistry · 2021
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Redefining PTB domain into independently functional dual cores.Biochemical and biophysical research communications · 2020
    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 KryshtafovychProtein Structure Prediction Center, Genome Center, University of California, Davis, California.ORCID 0000-0001-5066-7178
Bohdan MonastyrskyyProtein Structure Prediction Center, Genome Center, University of California, Davis, California.
Krzysztof FidelisProtein Structure Prediction Center, Genome Center, University of California, Davis, California.ORCID 0000-0002-8061-412X
John MoultInstitute for Bioscience and Biotechnology Research and Department of Cell Biology and Molecular Genetics, University of Maryland, Maryland.ORCID 0000-0002-3012-2282
Torsten SchwedeBiozentrum, University of Basel, Basel, Switzerland.ORCID 0000-0003-2715-335X
Anna TramontanoDepartment of Biochemical Sciences, Sapienza - University of Rome, P. le A. Moro, 5, Rome, 00185.

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 describes results of numerical evaluation of CASP12 models submitted on targets for which structural templates could be identified and for which servers produced models of relatively high accuracy. The emphasis is on analysis of details of models, and how well the models compete with experimental structures. Performance of contributing research groups is measured in terms of backbone accuracy, all-atom local geometry, and the ability to estimate local errors in models. Separate analyses for all participating groups and automatic servers were carried out. Compared with the last CASP, two years ago, there have been significant improvements in a number of areas, particularly the accuracy of protein backbone atoms, accuracy of sequence alignment between models and available structures, increased accuracy over that which can be obtained from simple copying of a closest template, and accuracy of modeling of sub-structures not present in the closest template. These advancements are likely associated with more effective strategies to build non-template regions of the targets ab initio, better algorithms to combine information from multiple templates, enhanced refinement methods, and better methods for estimating model accuracy.

Indexed as

Models, MolecularModels, StatisticalProtein ConformationComputational BiologyDatabases, ProteinHumansProteinsSequence AlignmentSequence Analysis, ProteinProteinsCASPhigh accuracy modelsnumerical evaluation measuresprotein structure predictiontemplate-based protein modeling

Identifiers

PMID29159950
PMCPMC5877821

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.