Evidence map›Paper›PMID 31325340›Full record

ArticleProteins2019

High-accuracy refinement using Rosetta in CASP13.

Hahnbeom Park, Gyu Rie Lee, David E Kim, Ivan Anishchenko, Qian Cong, David Baker

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 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Article
  2. Contact-Assisted Threading in Low-Homology Protein Modeling.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  3. Article
  4. Article
  5. Using metagenomic data to boost protein structure prediction and discovery.Computational and structural biotechnology journal · 2022
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Improved protein structure prediction using predicted interresidue orientations.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  16. Homology modeling in the time of collective and artificial intelligence.Computational and structural biotechnology journal · 2020
    Review
  17. 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.

Hahnbeom ParkDepartment of Biochemistry and Institute for Protein Design, University of Washington, Seattle, Washington.ORCID 0000-0002-7129-1912
Gyu Rie LeeDepartment of Biochemistry and Institute for Protein Design, University of Washington, Seattle, Washington.
David E KimDepartment of Biochemistry and Institute for Protein Design, University of Washington, Seattle, Washington.
Ivan AnishchenkoDepartment of Biochemistry and Institute for Protein Design, University of Washington, Seattle, Washington.
Qian CongDepartment of Biochemistry and Institute for Protein Design, University of Washington, Seattle, Washington.
David BakerDepartment of Biochemistry and Institute for Protein Design, University of Washington, Seattle, Washington.

Funding

High resolution structure modeling with RosettaR01GM092802 · NIGMS · UNIVERSITY OF WASHINGTON · PI BAKER, DAVID · 2010 to 2017
$2.3M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM092802NIH HHS R01GM092802
6 · The paper itself

Abstract

Because proteins generally fold to their lowest free energy states, energy-guided refinement in principle should be able to systematically improve the quality of protein structure models generated using homologous structure or co-evolution derived information. However, because of the high dimensionality of the search space, there are far more ways to degrade the quality of a near native model than to improve it, and hence, refinement methods are very sensitive to energy function errors. In the 13th Critial Assessment of techniques for protein Structure Prediction (CASP13), we sought to carry out a thorough search for low energy states in the neighborhood of a starting model using restraints to avoid straying too far. The approach was reasonably successful in improving both regions largely incorrect in the starting models as well as core regions that started out closer to the correct structure. Models with GDT-HA over 70 were obtained for five targets and for one of those, an accuracy of 0.5 å backbone root-mean-square deviation (RMSD) was achieved. An important current challenge is to improve performance in refining oligomers and larger proteins, for which the search problem remains extremely difficult.

Indexed as

Protein ConformationProtein FoldingAlgorithmsComputational BiologyModels, MolecularProteinsReproducibility of ResultsThermodynamicsProteinsenergy functionhomology modelingprotein conformational searchrotein structure prediction

Identifiers

PMID31325340
PMCPMC6851472

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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.