Evidence map›Paper›PMID 31294862›Full record

ArticleProteins2019

CASP13 target classification into tertiary structure prediction categories.

Lisa N Kinch, Andriy Kryshtafovych, Bohdan Monastyrskyy, Nick V Grishin

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 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
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  5. Easy Not Easy: Comparative Modeling with High-Sequence Identity Templates.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  6. Article
  7. Article
  8. Ultrafast end-to-end protein structure prediction enables high-throughput exploration of uncharacterized proteins.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Deep template-based protein structure prediction.PLoS computational biology · 2021
    Article
  14. Article
  15. Article
  16. Article
  17. Article
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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

4 authors.

Lisa N KinchDepartments of Biophysics and Biochemistry, Howard Hughes Medical Institute, University of Texas Southwestern Medical Center at Dallas, Dallas, Texas.ORCID 0000-0003-3041-2615
Andriy KryshtafovychGenome Center, University of California, Davis, California.ORCID 0000-0001-5066-7178
Bohdan MonastyrskyyGenome Center, University of California, Davis, California.
Nick V GrishinDepartments of Biophysics and Biochemistry, Howard Hughes Medical Institute, University of Texas Southwestern Medical Center at Dallas, Dallas, Texas.

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
Computational methods for structural-functional studies of proteinsR01GM094575 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI GRISHIN, NICK V. · 2010 to 2017
$2.4M
Computational analysis of proteinsR35GM127390 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI GRISHIN, NICK V. · 2018 to 2022
$1.5M
Computations of Fold Changes in Evolution of ProteinsR01GM067165 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI GRISHIN, NICK V. · 2003 to 2006
$1.1M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM067165NIGMS NIH HHS R01 GM094575NIGMS NIH HHS R01 GM100482NIGMS NIH HHS R35 GM127390NIH HHS GM094575NIH HHS GM100482NIH HHS GM127390
6 · The paper itself

Abstract

Protein target structures for the Critical Assessment of Structure Prediction round 13 (CASP13) were split into evaluation units (EUs) based on their structural domains, the domain organization of available templates, and the performance of servers on whole targets compared to split target domains. Eighty targets were split into 112 EUs. The EUs were classified into categories suitable for assessment of high accuracy modeling (or template-based modeling [TBM]) and topology (or free modeling [FM]) based on target difficulty. Assignment into assessment categories considered the following criteria: (a) the evolutionary relationship of target domains to existing fold space as defined by the Evolutionary Classification of Protein Domains (ECOD) database; (b) the clustering of target domains using eight objective sequence, structure, and performance measures; and (c) the placement of target domains in a scatter plot of target difficulty against server performance used in the previous CASP. Generally, target domains with good server predictions had close template homologs and were classified as TBM. Alternately, targets with poor server predictions represent a mixture of fast evolving homologs, structure analogs, and new folds, and were classified as FM or FM/TBM overlap.

Indexed as

Computational BiologyAmino Acid SequenceDatabases, ProteinModels, MolecularProtein ConformationProtein FoldingProteinsProtein Structure, TertiarySequence AlignmentProteinsCASP13classificationfold spacefree modelingprotein structuresequence homologsstructure analogsstructure predictiontemplate-based modeling

Identifiers

PMID31294862
PMCPMC6851465

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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.