Evidence map›Paper›PMID 27273630›Full record

ArticleNature structural & molecular biology2016

Toward high-resolution computational design of the structure and function of helical membrane proteins.

Patrick Barth, Alessandro Senes

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Article
  5. One-shot design elevates functional expression levels of a voltage-gated potassium channel.Protein science : a publication of the Protein Society · 2024
    Article
  6. Review
  7. Article
  8. Article
  9. Membrane Protein Engineering with Rosetta.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Designing minimalist membrane proteins.Biochemical Society transactions · 2019
    Review
  15. Article
  16. Article
  17. Reprogramming G protein coupled receptor structure and function.Current opinion in structural biology · 2018
    Review
  18. Review
  19. Cyclic oligomer design with de novo αβ-proteins.Protein science : a publication of the Protein Society · 2017
    Article
  20. Review
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

2 authors.

Patrick BarthStructural and Computational Biology and Molecular Biophysics Graduate Program, Baylor College of Medicine, Houston, Texas, USA.
Alessandro SenesDepartment of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin, USA.

Funding

EXPLORING STRUCTURE AND SEQUENCE SPACES OF G PROTEIN-COUPLED RECEPTOR SIGNALINGR01GM097207 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI BARTH, PATRICK DANIEL, WENSEL, THEODORE G · 2012 to 2020
$2.8M
Structural study of transmembrane interactions in the bacterial divisomeR01GM099752 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI SENES, ALESSANDRO · 2013 to 2017
$1.7M
NIGMS NIH HHS R01 GM097207NIGMS NIH HHS R01 GM099752
6 · The paper itself

Abstract

The computational design of α-helical membrane proteins is still in its infancy but has already made great progress. De novo design allows stable, specific and active minimal oligomeric systems to be obtained. Computational reengineering can improve the stability and function of naturally occurring membrane proteins. Currently, the major hurdle for the field is the experimental characterization of the designs. The emergence of new structural methods for membrane proteins will accelerate progress.

Indexed as

Computer-Aided DesignProtein EngineeringCalcium-Transporting ATPasesEscherichia coliEscherichia coli ProteinsHumansModels, MolecularMonosaccharide Transport ProteinsProtein StabilityProtein Structure, SecondaryResearch DesignSymportersThermodynamicsCalcium-Transporting ATPasesEscherichia coli ProteinsLacY protein, E coliMonosaccharide Transport ProteinsSymporters

Identifiers

PMID27273630
PMCPMC4962061

What OpenQuestion holds

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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.