ArticleNature communications2015
Making water-soluble integral membrane proteins in vivo using an amphipathic protein fusion strategy.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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
22 citing papers in PubMed, 40 citations in OpenAlex.
- Lipochaperoning folding of water-soluble functional membrane protein in genetically and biosynthetically tuned EscherichiaiScience · 2026Article
- Beyond Small Molecules: Orchestrating Cell Fate with Engineered Water-Soluble Membrane Proteins.Biomolecules · 2026Article
- Topological reprogramming transforms an integral membrane oligosaccharyltransferase into a water-soluble glycosylation catalyst.bioRxiv : the preprint server for biology · 2026Article
- CW ESR spectroscopy and protein spin labeling in membrane biology.Physical biology · 2025Review
- Structural basis of apoptosis induction by the mitochondrial voltage-dependent anion channel.Nature communications · 2025Article
- BloodProST: prediction of blood-secretory proteins through self-training.Briefings in bioinformatics · 2025Article
- Solubilization of Membrane Proteins using designed protein WRAPS.bioRxiv : the preprint server for biology · 2025Article
- Design of a water-soluble transmembrane receptor kinase with intact molecular function by QTY code.Nature communications · 2024Article
- Engineered Chimera Protein Constructs to Facilitate the Production of Heterologous Transmembrane Proteins inInternational journal of molecular sciences · 2024Review
- A synthetic cell-free 36-enzyme reaction system for vitamin BNature communications · 2023Article
- A modular vaccine platform enabled by decoration of bacterial outer membrane vesicles with biotinylated antigens.Nature communications · 2023Article
- A universal glycoenzyme biosynthesis pipeline that enables efficient cell-free remodeling of glycans.Nature communications · 2022Article
- Protein Design: From the Aspect of Water Solubility and Stability.Chemical reviews · 2022Review
- Biophysical Characterization of Membrane Proteins Embedded in Nanodiscs Using Fluorescence Correlation Spectroscopy.Membranes · 2022Review
- Biomimetic Silica Encapsulation of Lipid Nanodiscs and β-Sheet-Stabilized Diacylglycerol Kinase.Bioconjugate chemistry · 2021Article
- Membrane Protein Production and Purification from Escherichia coli and Sf9 Insect Cells.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Smoothing membrane protein structure determination by initial upstream stage improvements.Applied microbiology and biotechnology · 2019Review
- Biomimetic Membranes with Transmembrane Proteins: State-of-the-Art in Transmembrane Protein Applications.International journal of molecular sciences · 2019Review
- A water-soluble DsbB variant that catalyzes disulfide-bond formation in vivo.Nature chemical biology · 2017Article
- Protein engineering: Redirecting membrane machinery.Nature chemical biology · 2017Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
Integral membrane proteins (IMPs) play crucial roles in all cells and represent attractive pharmacological targets. However, functional and structural studies of IMPs are hindered by their hydrophobic nature and the fact that they are generally unstable following extraction from their native membrane environment using detergents. Here we devise a general strategy for in vivo solubilization of IMPs in structurally relevant conformations without the need for detergents or mutations to the IMP itself, as an alternative to extraction and in vitro solubilization. This technique, called SIMPLEx (solubilization of IMPs with high levels of expression), allows the direct expression of soluble products in living cells by simply fusing an IMP target with truncated apolipoprotein A-I, which serves as an amphipathic proteic 'shield' that sequesters the IMP from water and promotes its solubilization.
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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.