Evidence map›Paper›PMID 23344058›Full record

ReviewInternational journal of molecular sciences2013

Reconstitution of membrane proteins into model membranes: seeking better ways to retain protein activities.

Hsin-Hui Shen, Trevor Lithgow, Lisa Martin

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing 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

42 citing papers in PubMed.

  1. Article
  2. Precise Regulation of Membrane Proteins: From Physical Technology to Biomolecular Strategy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. An in vitro set-up to study Pdr5-mediated substrate translocation.Protein science : a publication of the Protein Society · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Human STING is a proton channel.Science (New York, N.Y.) · 2023
    Article
  17. Review
  18. Article
  19. Oriented Insertion of ESR-Containing Hybrid Proteins in Proteoliposomes.International journal of molecular sciences · 2023
    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.

Hsin-Hui ShenDepartment of Biochemistry and Molecular Biology, Monash University, Melbourne 3800, Australia. hsin-hui.shen@monash.edu.
Trevor Lithgow
Lisa Martin

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The function of any given biological membrane is determined largely by the specific set of integral membrane proteins embedded in it, and the peripheral membrane proteins attached to the membrane surface. The activity of these proteins, in turn, can be modulated by the phospholipid composition of the membrane. The reconstitution of membrane proteins into a model membrane allows investigation of individual features and activities of a given cell membrane component. However, the activity of membrane proteins is often difficult to sustain following reconstitution, since the composition of the model phospholipid bilayer differs from that of the native cell membrane. This review will discuss the reconstitution of membrane protein activities in four different types of model membrane - monolayers, supported lipid bilayers, liposomes and nanodiscs, comparing their advantages in membrane protein reconstitution. Variation in the surrounding model environments for these four different types of membrane layer can affect the three-dimensional structure of reconstituted proteins and may possibly lead to loss of the proteins activity. We also discuss examples where the same membrane proteins have been successfully reconstituted into two or more model membrane systems with comparison of the observed activity in each system. Understanding of the behavioral changes for proteins in model membrane systems after membrane reconstitution is often a prerequisite to protein research. It is essential to find better solutions for retaining membrane protein activities for measurement and characterization in vitro.

Indexed as

Lipid BilayersLiposomesMembrane ProteinsModels, ChemicalModels, MolecularNanostructuresPhospholipidsProtein BindingProtein Structure, TertiaryUnilamellar LiposomesLipid BilayersLiposomesMembrane ProteinsPhospholipidsUnilamellar Liposomes

Identifiers

PMID23344058
PMCPMC3565336

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.