Evidence map›Paper›PMID 23671331›Full record

ArticleNucleic acids research2013

EvoDesign: De novo protein design based on structural and evolutionary profiles.

Pralay Mitra, David Shultis, Yang Zhang

Abstract read
In one paragraph

Article in Nucleic acids research, 2013. 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. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. A general-purpose protein design framework based on mining sequence-structure relationships in known protein structures.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Computational approaches forBioscience reports · 2017
    Review
  14. An Evolution-Based Approach to De Novo Protein Design.Methods in molecular biology (Clifton, N.J.) · 2017
    Article
  15. Article
  16. Article
  17. Preface.Methods in enzymology · 2016
    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

3 authors.

Pralay MitraDepartment of Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, MI 48109 USA.
David Shultis
Yang Zhang

Funding

I-TASSER based atomic-level protein structure predictionR01GM083107 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ZHANG, YANG · 2008 to 2019
$3.5M
Atomic-level, large-scale structure prediction of G protein-coupled receptorsR01GM084222 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ZHANG, YANG · 2009 to 2012
$1.3M
NIGMS NIH HHS GM083107NIGMS NIH HHS GM084222NIGMS NIH HHS R01 GM083107NIGMS NIH HHS R01 GM084222
6 · The paper itself

Abstract

Protein design aims to identify new protein sequences of desirable structure and biological function. Most current de novo protein design methods rely on physics-based force fields to search for low free-energy states following Anfinsen's thermodynamic hypothesis. A major obstacle of such approaches is the inaccuracy of the force field design, which cannot accurately describe the atomic interactions or distinguish correct folds. We developed a new web server, EvoDesign, to design optimal protein sequences of given scaffolds along with multiple sequence and structure-based features to assess the foldability and goodness of the designs. EvoDesign uses an evolution-profile-based Monte Carlo search with the profiles constructed from homologous structure families in the Protein Data Bank. A set of local structure features, including secondary structure, torsion angle and solvation, are predicted by single-sequence neural-network training and used to smooth the sequence motif and accommodate the physicochemical packing. The EvoDesign algorithm has been extensively tested in large-scale protein design experiments, which demonstrate enhanced foldability and structural stability of designed sequences compared with the physics-based designing methods. The EvoDesign server is freely available at http://zhanglab.ccmb.med.umich.edu/EvoDesign.

Indexed as

SoftwareEvolution, MolecularInternetMonte Carlo MethodProtein ConformationProtein EngineeringSequence Analysis, Protein

Identifiers

PMID23671331
PMCPMC3692067

What OpenQuestion holds

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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.