ArticleBiophysical chemistry2015
Kinetics of lipid mixing between bicelles and nanolipoprotein particles.
Article in Biophysical chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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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.
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- Approaches to Heterogeneity in Native Mass Spectrometry.Chemical reviews · 2022Review
- Transfer mechanism of cell-free synthesized membrane proteins into mammalian cells.Frontiers in bioengineering and biotechnology · 2022Article
- Distinct classes of multi-subunit heterogeneity: analysis using Fourier Transform methods and native mass spectrometry.The Analyst · 2020Article
- Measuring Lipid Transfer Protein Activity Using Bicelle-Dilution Model Membranes.Analytical chemistry · 2020Article
- Lipid and Protein Transfer between Nanolipoprotein Particles and Supported Lipid Bilayers.Langmuir : the ACS journal of surfaces and colloids · 2019Article
- Cell-Free Co-Translational Approaches for Producing Mammalian Receptors: Expanding the Cell-Free Expression Toolbox Using Nanolipoproteins.Frontiers in pharmacology · 2019Review
- Cell-free production of a functional oligomeric form of aThe Journal of biological chemistry · 2017Article
- Nanodiscs in Membrane Biochemistry and Biophysics.Chemical reviews · 2017Review
- From Nanodiscs to Isotropic Bicelles: A Procedure for Solution Nuclear Magnetic Resonance Studies of Detergent-Sensitive Integral Membrane Proteins.Structure (London, England : 1993) · 2016Article
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Authors and funding
3 authors at 3 institutions in 2 countries.
Funding
Abstract
Nanolipoprotein particles (NLPs), also known as nanodiscs, are lipid bilayers bounded by apolipoprotein. Lipids and membrane proteins cannot exchange between NLPs. However, the addition of bicelles opens NLPs and transfers their contents to bicelles, which freely exchange lipids and proteins. NLP-bicelle interactions may provide a new method for studying membrane protein oligomerization. The interaction mechanism was investigated by stopped flow fluorometry. NLPs with lipids having fluorescence resonance energy transfer (FRET) donors and acceptors were mixed with a 200-fold molar excess of dihexanoyl phosphatidylcholine (DHPC)/dimyristoyl phosphatidylcholine (DMPC) bicelles, and the rate of lipid transfer was monitored by the disappearance of FRET. Near or below the DMPC phase transition temperature, the kinetics were sigmoidal. Free DHPC and apolipoprotein were ruled out as participants in autocatalytic mechanisms. The NLP-bicelle mixing rate showed a strong temperature dependence (activation energy = 28 kcal/mol). Models are proposed for the NLP-bicelle mixing, including one involving fusion pores.
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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.