ReviewThe Journal of membrane biology2014
Amphipols for each season.
Review in The Journal of membrane biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
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.
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.
Who cites it
65 citing papers in PubMed, 124 citations in OpenAlex.
- Advances in Crystallography and Cryo-Electron Microscopy for the Study of Membrane Proteins.Advances in experimental medicine and biology · 2026Review
- Structures of vesicular stomatitis virus glycoprotein G alone and bound to a neutralizing antibody.PLoS pathogens · 2025Article
- Coming Clean and Avoiding Bubble Trouble-Using Detergents Wisely in the Purification of Membrane Proteins for Cryo-EM Studies.Biomolecules · 2025Review
- Aerolysin Nanopore Structures Revealed at High Resolution in a Lipid Environment.Journal of the American Chemical Society · 2025Article
- Tunable Terpolymer Series for the Systematic Investigation of Membrane Proteins.Biomacromolecules · 2025Article
- Review
- Chaperone-assisted cryo-EM structure ofbioRxiv : the preprint server for biology · 2024Article
- Structural and biophysical insights into targeting of claudin-4 by a synthetic antibody fragment.Communications biology · 2024Article
- Review
- Chaperone-assisted cryo-EM structure of P. aeruginosa PhuR reveals molecular basis for heme binding.Structure (London, England : 1993) · 2024Article
- Functional production and biochemical investigation of an integral membrane enzyme for olefin biosynthesis.Protein science : a publication of the Protein Society · 2024Article
- Overview of Membrane Protein Sample Preparation for Single-Particle Cryo-Electron Microscopy Analysis.International journal of molecular sciences · 2023Review
- Role of surfactants in electron cryo-microscopy film preparation.Biophysical journal · 2023Article
- A comparative characterisation of commercially available lipid-polymer nanoparticles formed from model membranes.European biophysics journal : EBJ · 2023Article
- G Protein-coupled Receptor (GPCR) Reconstitution and Labeling for Solution Nuclear Magnetic Resonance (NMR) Studies of the Structural Basis of Transmembrane Signaling.Molecules (Basel, Switzerland) · 2022Review
- Mechanisms of Formation, Structure, and Dynamics of Lipoprotein Discs Stabilized by Amphiphilic Copolymers: A Comprehensive Review.Nanomaterials (Basel, Switzerland) · 2022Review
- Cycloalkane-modified amphiphilic polymers provide direct extraction of membrane proteins for CryoEM analysis.Communications biology · 2021Article
- Lipid Membrane Mimetics in Functional and Structural Studies of Integral Membrane Proteins.Membranes · 2021Review
- Methods for the solubilisation of membrane proteins: the micelle-aneous world of membrane protein solubilisation.Biochemical Society transactions · 2021Review
- Biological insights from SMA-extracted proteins.Biochemical Society transactions · 2021Review
5 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Amphipols (APols) are short amphipathic polymers that can substitute for detergents at the transmembrane surface of membrane proteins (MPs) and, thereby, keep them soluble in detergent free aqueous solutions. APol-trapped MPs are, as a rule, more stable biochemically than their detergent-solubilized counterparts. APols have proven useful to produce MPs, most noticeably by assisting their folding from the denatured state obtained after solubilizing MP inclusion bodies in either SDS or urea. They facilitate the handling in aqueous solution of fragile MPs for the purpose of proteomics, structural and functional studies, and therapeutics. Because APols can be chemically labeled or functionalized, and they form very stable complexes with MPs, they can also be used to functionalize those indirectly, which opens onto many novel applications. Following a brief recall of the properties of APols and MP/APol complexes, an update is provided of recent progress in these various fields.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.