ReviewFrontiers in bioengineering and biotechnology2020
Large Nanodiscs: A Potential Game Changer in Structural Biology of Membrane Protein Complexes and Virus Entry.
Review in Frontiers in bioengineering and biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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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.
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Who cites it
16 citing papers in PubMed.
- Understanding charged polymer-lipid interactions in model membranes revealed by EPR and solid-state NMR: Implications for membrane protein studies.Chemistry and physics of lipids · 2026Article
- Generation of Nano-Antibodies Targeting the SNMP1 Membrane Receptor ofJournal of extracellular biology · 2026Article
- Oversized nanodiscs for combined structural and functional investigation of multicomponent membrane protein systems.Scientific reports · 2025Article
- Review
- Exploring the World of Membrane Proteins: Techniques and Methods for Understanding Structure, Function, and Dynamics.Molecules (Basel, Switzerland) · 2023Review
- What's the defect? Using mass defects to study oligomerization of membrane proteins and peptides in nanodiscs with native mass spectrometry.Methods (San Diego, Calif.) · 2023Review
- Recent advances in membrane mimetics for membrane protein research.Biochemical Society transactions · 2023Review
- Self-cyclisation as a general and efficient platform for peptide and protein macrocyclisation.Communications chemistry · 2023Article
- Native-like environments afford novel mechanistic insights into membrane proteins.Trends in biochemical sciences · 2022Review
- Measurement of Residual Dipolar Couplings Using Magnetically Aligned and Flipped Nanodiscs.Langmuir : the ACS journal of surfaces and colloids · 2022Article
- The high-throughput production of membrane proteins.Emerging topics in life sciences · 2021Article
- Solid-State NMR Study to Probe the Effects of Divalent Metal Ions (CaLangmuir : the ACS journal of surfaces and colloids · 2021Article
- Review
- Expression, Purification and Crystallization of Asrij, A Novel Scaffold Transmembrane Protein.The Journal of membrane biology · 2021Article
- Changes in Membrane Protein Structural Biology.Biology · 2020Review
- Structure and Dynamics of GPCRs in Lipid Membranes: Physical Principles and Experimental Approaches.Molecules (Basel, Switzerland) · 2020Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Phospho-lipid bilayer nanodiscs have gathered much scientific interest as a stable and tunable membrane mimetic for the study of membrane proteins. Until recently the size of the nanodiscs that could be produced was limited to ~ 16 nm. Recent advances in nanodisc engineering such as covalently circularized nanodiscs (cND) and DNA corralled nanodiscs (DCND) have opened up the possibility of engineering nanodiscs of size up to 90 nm. This enables widening the application of nanodiscs from single membrane proteins to investigating large protein complexes and biological processes such as virus-membrane fusion and synaptic vesicle fusion. Another aspect of exploiting the large available surface area of these novel nanodiscs could be to engineer more realistic membrane mimetic systems with features such as membrane asymmetry and curvature. In this review, we discuss the recent technical developments in nanodisc technology leading to construction of large nanodiscs and examine some of the implicit applications.
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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.