ReviewBiochemical Society transactions2021
Detergent-free systems for structural studies of membrane proteins.
Review in Biochemical Society transactions, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 28 citations in OpenAlex.
- Differential effects of lipid composition on the thermal and functional properties of membrane associated CYP2J2.Protein science : a publication of the Protein Society · 2026Article
- Advances in native cell membrane nanoparticles system.Current opinion in structural biology · 2025Review
- Coming Clean and Avoiding Bubble Trouble-Using Detergents Wisely in the Purification of Membrane Proteins for Cryo-EM Studies.Biomolecules · 2025Review
- Improved Pendant-Bearing Glucose-Neopentyl Glycols for Membrane Protein Stability.Bioconjugate chemistry · 2025Article
- Cholesterol-dependent enzyme activity of human TSPO1.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Three-Dimensional Interaction Homology: Deconstructing Residue-Residue and Residue-Lipid Interactions in Membrane Proteins.Molecules (Basel, Switzerland) · 2024Article
- Article
- Reconstitution of the Bacterial Glutamate Receptor Channel by Encapsulation of a Cell-Free Expression System.Journal of visualized experiments : JoVE · 2024Article
- Dark nanodiscs for evaluating membrane protein thermostability by differential scanning fluorimetry.Biophysical journal · 2024Article
- Heterogenous Expression and Purification of Lipid II Flippase fromProtein and peptide letters · 2024Article
- Fabrication of membrane proteins in the form of native cell membrane nanoparticles using novel membrane active polymers.Nanoscale advances · 2023Article
- Merging cultures and disciplines to create a drug discovery ecosystem at Virginia commonwealth university: Medicinal chemistry, structural biology, molecular and behavioral pharmacology and computational chemistry.SLAS discovery : advancing life sciences R & D · 2023Review
- Cryo-EM structures of full-length integrin αIIbβ3 in native lipids.Nature communications · 2023Article
- pH-tunable membrane-active polymers, NCMNP2a-Chemical science · 2023Article
- 3D interaction homology: The hydrophobic residues alanine, isoleucine, leucine, proline and valine play different structural roles in soluble and membrane proteins.Frontiers in molecular biosciences · 2023Article
- Importance of molecular dynamics equilibrium protocol on protein-lipid interaction near channel pore.Biophysical reports · 2022Article
- Membranes under the Magnetic Lens: A Dive into the Diverse World of Membrane Protein Structures Using Cryo-EM.Chemical reviews · 2022Review
- Native-like environments afford novel mechanistic insights into membrane proteins.Trends in biochemical sciences · 2022Review
- Analysis of the oligomeric state of mycobacterial membrane protein large 3 and its interaction with SQ109 with native cell membrane nanoparticles system.Biochimica et biophysica acta. Biomembranes · 2022Article
- Cryo-EM Structure of Mechanosensitive Channel YnaI Using SMA2000: Challenges and Opportunities.Membranes · 2021Article
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Authors and funding
1 author at 1 institution in 1 country.
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Abstract
Membrane proteins play vital roles in living organisms, serving as targets for most currently prescribed drugs. Membrane protein structural biology aims to provide accurate structural information to understand their mechanisms of action. The advance of membrane protein structural biology has primarily relied on detergent-based methods over the past several decades. However, detergent-based approaches have significant drawbacks because detergents often damage the native protein-lipid interactions, which are often crucial for maintaining the natural structure and function of membrane proteins. Detergent-free methods recently have emerged as alternatives with a great promise, e.g. for high-resolution structure determinations of membrane proteins in their native cell membrane lipid environments. This minireview critically examines the current status of detergent-free methods by a comparative analysis of five groups of membrane protein structures determined using detergent-free and detergent-based methods. This analysis reveals that current detergent-free systems, such as the styrene-maleic acid lipid particles (SMALP), the diisobutyl maleic acid lipid particles (DIBMALP), and the cycloalkane-modified amphiphile polymer (CyclAPol) technologies are not better than detergent-based approaches in terms of maintenance of native cell membrane lipids on the transmembrane domain and high-resolution structure determination. However, another detergent-free technology, the native cell membrane nanoparticles (NCMN) system, demonstrated improved maintenance of native cell membrane lipids with the studied membrane proteins, and produced particles that were suitable for high-resolution structural analysis. The ongoing development of new membrane-active polymers and their optimization will facilitate the maturation of these new detergent-free systems.
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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.