Evidence map›Paper›PMID 22031179›Full record

ArticleProtein science : a publication of the Protein Society2012

A knowledge-based potential highlights unique features of membrane α-helical and β-barrel protein insertion and folding.

Daniel Hsieh, Alexander Davis, Vikas Nanda

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing 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

24 citing papers in PubMed.

  1. Review
  2. Article
  3. General features of transmembrane beta barrels from a large database.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  4. Article
  5. Spatial arrangement of proteins in planar and curved membranes by PPM 3.0.Protein science : a publication of the Protein Society · 2022
    Article
  6. Membrane Barrels Are Taller, Fatter, Inside-Out Soluble Barrels.The journal of physical chemistry. B · 2021
    Article
  7. Article
  8. GeTFEP: A general transfer free energy profile of transmembrane proteins.Protein science : a publication of the Protein Society · 2020
    Article
  9. Article
  10. Article
  11. Article
  12. Outer membrane protein design.Current opinion in structural biology · 2017
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Computational redesign of the lipid-facing surface of the outer membrane protein OmpA.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  18. Article
  19. Life at the border: adaptation of proteins to anisotropic membrane environment.Protein science : a publication of the Protein Society · 2014
    Review
  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

3 authors.

Daniel HsiehBioMaPS Institute and the Graduate Program in Computational Biology and Molecular Biophysics, Rutgers University, Piscataway, NJ 08854, USA.
Alexander Davis
Vikas Nanda

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
NIGMS NIH HHS R01 GM089949NIGMS NIH HHS R01 GM089949-01A1
6 · The paper itself

Abstract

Outer membrane β-barrel proteins differ from α-helical inner membrane proteins in lipid environment, secondary structure, and the proposed processes of folding and insertion. It is reasonable to expect that outer membrane proteins may contain primary sequence information specific for their folding and insertion behavior. In previous work, a depth-dependent insertion potential, E(z) , was derived for α-helical inner membrane proteins. We have generated an equivalent potential for TM β-barrel proteins. The similarities and differences between these two potentials provide insight into unique aspects of the folding and insertion of β-barrel membrane proteins. This potential can predict orientation within the membrane and identify functional residues involved in intermolecular interactions.

Indexed as

Models, ChemicalProtein FoldingAmino AcidsBacterial Outer Membrane ProteinsHydrophobic and Hydrophilic InteractionsLipidsModels, MolecularProtein Interaction Domains and MotifsProtein Structure, SecondaryThermodynamicsAmino AcidsBacterial Outer Membrane ProteinsLipids

Identifiers

PMID22031179
PMCPMC3323780

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.