Evidence map›Paper›PMID 36008970›Full record

ReviewBiomolecules2022

Detergent-Free Isolation of Membrane Proteins and Strategies to Study Them in a Near-Native Membrane Environment.

Bankala Krishnarjuna, Ayyalusamy Ramamoorthy

Open access · goldAbstract readReview
In one paragraph

Review in Biomolecules, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

29 citing papers in PubMed, 57 citations in OpenAlex.

  1. Molecular Mechanisms Governing Peptide Nanodisc Assembly and Stability.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Article
  4. OrthogonalApplied and environmental microbiology · 2025
    Article
  5. Article
  6. Article
  7. Advances in native cell membrane nanoparticles system.Current opinion in structural biology · 2025
    Review
  8. Review
  9. Article
  10. Design of a water-soluble CD20 antigen with computational epitope scaffolding.Protein science : a publication of the Protein Society · 2025
    Article
  11. Article
  12. Article
  13. Structures of methane and ammonia monooxygenases in native membranes.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  14. Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. 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

2 authors at 1 institution in 1 country.

Bankala KrishnarjunaDepartment of Chemistry and Biophysics, Biomedical Engineering, Macromolecular Science and Engineering, Michigan Neuroscience Institute, The University of Michigan, Ann Arbor, MI 48109-1055, USA.ORCID 0000-0002-4575-0011
Ayyalusamy RamamoorthyDepartment of Chemistry and Biophysics, Biomedical Engineering, Macromolecular Science and Engineering, Michigan Neuroscience Institute, The University of Michigan, Ann Arbor, MI 48109-1055, USA.ORCID 0000-0003-1964-1900
University of Michigan · US

Funding

Development of biophysical approaches to investigate high-resolution structure and dynamics of membrane proteinsR35GM139573 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Ayyalusamy Ramamoorthy · 2021 to 2026
$2.0M
NIGMS NIH HHS R35 GM139573NIH HHS R35GM139573
6 · The paper itself

Abstract

Atomic-resolution structural studies of membrane-associated proteins and peptides in a membrane environment are important to fully understand their biological function and the roles played by them in the pathology of many diseases. However, the complexity of the cell membrane has severely limited the application of commonly used biophysical and biochemical techniques. Recent advancements in NMR spectroscopy and cryoEM approaches and the development of novel membrane mimetics have overcome some of the major challenges in this area. For example, the development of a variety of lipid-nanodiscs has enabled stable reconstitution and structural and functional studies of membrane proteins. In particular, the ability of synthetic amphipathic polymers to isolate membrane proteins directly from the cell membrane, along with the associated membrane components such as lipids, without the use of a detergent, has opened new avenues to study the structure and function of membrane proteins using a variety of biophysical and biological approaches. This review article is focused on covering the various polymers and approaches developed and their applications for the functional reconstitution and structural investigation of membrane proteins. The unique advantages and limitations of the use of synthetic polymers are also discussed.

Indexed as

Membrane ProteinsNanostructuresLipid BilayersMembranesPolymersLipid BilayersMembrane ProteinsPolymerscryoEMdetergent-free membrane protein isolationionic and non-ionic polymerslipid-nanodiscmembrane protein stability and structureNMR

Identifiers

PMID36008970
PMCPMC9406181
OpenAlexW4289985743

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.