Evidence map›Paper›PMID 24047990›Full record

ArticleBiophysical journal2013

Lipid bilayer composition can influence the orientation of proteorhodopsin in artificial membranes.

Ramya Tunuguntla, Mangesh Bangar, Kyunghoon Kim, Pieter Stroeve, Caroline M Ajo-Franklin, Aleksandr Noy

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.7field-weighted citation impact, top 18% of its field
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

33 citing papers in PubMed, 68 citations in OpenAlex.

  1. Improving cell-free metabolism through direct integration of artificial respiratory chains.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Photocatalytic Biohybrid Vesicles.Chemical reviews · 2026
    Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. In vitro reconstitution of transition metal transporters.The Journal of biological chemistry · 2024
    Review
  8. Article
  9. Oriented Insertion of ESR-Containing Hybrid Proteins in Proteoliposomes.International journal of molecular sciences · 2023
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Rapid Estimation of Membrane Protein Orientation in Liposomes.Chembiochem : a European journal of chemical biology · 2022
    Article
  17. Review
  18. Review
  19. How bilayer properties influence membrane protein folding.Protein science : a publication of the Protein Society · 2020
    Review
  20. Cryo-EM analysis of a membrane protein embedded in the liposome.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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

6 authors at 4 institutions in 1 country.

Ramya TunuguntlaDepartment of Chemical Engineering and Materials Science, University of California, Davis, Davis, California; Materials Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, California; Physics and Life Sciences Directorate, Lawrence Livermore National Laboratory, Livermore, California.
Mangesh Bangar
Kyunghoon Kim
Pieter Stroeve
Caroline M Ajo-Franklin
Aleksandr Noy
Lawrence Berkeley National Laboratory · USLawrence Livermore National Laboratory · USUniversity of California, Berkeley · USUniversity of California, Davis · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Artificial membrane systems allow researchers to study the structure and function of membrane proteins in a matrix that approximates their natural environment and to integrate these proteins in ex vivo devices such as electronic biosensors, thin-film protein arrays, or biofuel cells. Given that most membrane proteins have vectorial functions, both functional studies and applications require effective control over protein orientation within a lipid bilayer. In this work, we explored the role of the bilayer surface charge in determining transmembrane protein orientation and functionality during formation of proteoliposomes. We reconstituted a model vectorial ion pump, proteorhodopsin, in liposomes of opposite charges and varying charge densities and determined the resultant protein orientation. Antibody-binding assay and proteolysis of proteoliposomes showed physical evidence of preferential orientation, and functional assays verified the vectorial nature of ion transport in this system. Our results indicate that the manipulation of lipid composition can indeed control orientation of an asymmetrically charged membrane protein, proteorhodopsin, in liposomes.

Indexed as

Membranes, ArtificialBiological TransportLightLipid BilayersProteolipidsProteolysisProton PumpsProtonsRhodopsinRhodopsins, MicrobialSurface PropertiesLipid BilayersMembranes, ArtificialProteolipidsproteoliposomesproteorhodopsinProton PumpsProtonsRhodopsinRhodopsins, Microbial

Identifiers

PMID24047990
PMCPMC3785883
OpenAlexW2023346969

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.