Evidence map›Paper›PMID 26199411›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Computational redesign of the lipid-facing surface of the outer membrane protein OmpA.

James A Stapleton, Timothy A Whitehead, Vikas Nanda

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. 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. The Name Is Barrel, β-Barrel.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Outer membrane protein evolution.Current opinion in structural biology · 2021
    Review
  8. De novo design of transmembrane β barrels.Science (New York, N.Y.) · 2021
    Article
  9. Review
  10. Designing minimalist membrane proteins.Biochemical Society transactions · 2019
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Outer membrane protein design.Current opinion in structural biology · 2017
    Review
  16. 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

3 authors.

James A StapletonDepartment of Chemical Engineering and Materials Science, Michigan State University, East Lansing, MI 48824; Center for Advanced Biotechnology and Medicine and the Department of Biochemistry and Molecular Biology, Robert Wood Johnson Medical School, Rutgers University, Piscataway, NJ 08854;
Timothy A WhiteheadDepartment of Chemical Engineering and Materials Science, Michigan State University, East Lansing, MI 48824; Department of Biosystems and Agricultural Engineering, Michigan State University, East Lansing, MI 48824.
Vikas NandaCenter for Advanced Biotechnology and Medicine and the Department of Biochemistry and Molecular Biology, Robert Wood Johnson Medical School, Rutgers University, Piscataway, NJ 08854; nanda@cabm.rutgers.edu.

Funding

A Computational Approach to Developing Heterochiral Peptide TherapeuticsR01GM089949 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI NANDA, VIKAS · 2010 to 2014
$1.5M
Computational design of beta-barrel membrane proteinsF32GM099291 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI STAPLETON, JAMES ALAN · 2011 to 2013
$155k
NIGMS NIH HHS F32 GM099291NIGMS NIH HHS F32-GM-099291NIGMS NIH HHS R01 GM089949NIGMS NIH HHS R01-GM-089949
6 · The paper itself

Abstract

Advances in computational design methods have made possible extensive engineering of soluble proteins, but designed β-barrel membrane proteins await improvements in our understanding of the sequence determinants of folding and stability. A subset of the amino acid residues of membrane proteins interact with the cell membrane, and the design rules that govern this lipid-facing surface are poorly understood. We applied a residue-level depth potential for β-barrel membrane proteins to the complete redesign of the lipid-facing surface of Escherichia coli OmpA. Initial designs failed to fold correctly, but reversion of a small number of mutations indicated by backcross experiments yielded designs with substitutions to up to 60% of the surface that did support folding and membrane insertion.

Indexed as

Amino Acid SequenceBacterial Outer Membrane ProteinsComputational BiologyElectrophoresis, Polyacrylamide GelEscherichia coliFlow CytometryFluorescenceLipidsModels, MolecularMolecular Sequence DataMutant ProteinsProlineProtein FoldingProtein Structure, SecondaryRecombinant ProteinsSequence AlignmentBacterial Outer Membrane ProteinsLipidsMutant ProteinsOMPA outer membrane proteinsProlineRecombinant Proteinsmembrane proteinsOmpAprotein designstatistical potentialβ-barrel

Identifiers

PMID26199411
PMCPMC4534290

What OpenQuestion holds

Textmetadata
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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.