Evidence map›Paper›PMID 26335199›Full record

ArticleeLife2015

Large-scale determination of previously unsolved protein structures using evolutionary information.

Sergey Ovchinnikov, Lisa Kinch, Hahnbeom Park, Yuxing Liao, Jimin Pei, David E Kim, Hetunandan Kamisetty, Nick V Grishin, David Baker

Abstract read
In one paragraph

Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 133 papers.

0numbers the graph read from it
0cells of the map it votes in
133citing 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

133 citing papers in PubMed.

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  7. Insights into DNA cleavage by MutL homologs from analysis of conserved motifs in eukaryotic Mlh1.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Article
  8. Blind assessment of monomeric AlphaFold2 protein structure models with experimental NMR data.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2023
    Article
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73 more citing papers are in PubMed but not listed here.

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

9 authors.

Sergey OvchinnikovDepartment of Biochemistry, University of Washington, Seattle, United States.
Lisa KinchHoward Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, United States.
Hahnbeom ParkDepartment of Biochemistry, University of Washington, Seattle, United States.
Yuxing LiaoDepartment of Biophysics, Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, United States.
Jimin PeiHoward Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, United States.
David E KimDepartment of Biochemistry, University of Washington, Seattle, United States.
Hetunandan KamisettyFacebook Inc., Seattle, United States.
Nick V GrishinHoward Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, United States.
David BakerDepartment of Biochemistry, University of Washington, Seattle, United States.

Funding

TRAINING IN MOLECULAR AND CELLULAR BIOLOGYT32GM007270 · NIGMS · UNIVERSITY OF WASHINGTON · PI RAIBLE, DAVID W · 1985 to 2020
$21.0M
Computational methods for structural-functional studies of proteinsR01GM094575 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI GRISHIN, NICK V. · 2010 to 2017
$2.4M
High resolution structure modeling with RosettaR01GM092802 · NIGMS · UNIVERSITY OF WASHINGTON · PI BAKER, DAVID · 2010 to 2017
$2.3M
Howard Hughes Medical InstituteNIGMS NIH HHS GM094575NIGMS NIH HHS R01 GM092802NIGMS NIH HHS R01GM092802NIGMS NIH HHS R01 GM094575NIGMS NIH HHS T32 GM007270
6 · The paper itself

Abstract

The prediction of the structures of proteins without detectable sequence similarity to any protein of known structure remains an outstanding scientific challenge. Here we report significant progress in this area. We first describe de novo blind structure predictions of unprecendented accuracy we made for two proteins in large families in the recent CASP11 blind test of protein structure prediction methods by incorporating residue-residue co-evolution information in the Rosetta structure prediction program. We then describe the use of this method to generate structure models for 58 of the 121 large protein families in prokaryotes for which three-dimensional structures are not available. These models, which are posted online for public access, provide structural information for the over 400,000 proteins belonging to the 58 families and suggest hypotheses about mechanism for the subset for which the function is known, and hypotheses about function for the remainder.

Indexed as

Evolution, MolecularBacterial ProteinsComputational BiologyModels, MolecularProtein ConformationBacterial ProteinsbiophysicsB. subtilisco-evolutionE. colievolutionary biologygenomicsH. salinarumprotein familyprotein foldS. solfataricusstructural biologystructure prediction

Identifiers

PMID26335199
PMCPMC4602095

What OpenQuestion holds

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LicenceCC BY
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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.