ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2018
Proteoliposome Engineering with Cell-Free Membrane Protein Synthesis: Control of Membrane Protein Sorting into Liposomes by Chaperoning Systems.
Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 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
13 citing papers in PubMed, 32 citations in OpenAlex.
- Bottom-Up Synthesis and Purification of Extracellular Vesicle Mimetics.Journal of extracellular vesicles · 2025Article
- Cell-Free Expression of Nipah Virus Transmembrane Proteins for Proteoliposome Vaccine Design.ACS nano · 2025Article
- SARS-CoV-2 virus-like-particlesNanoscale advances · 2023Article
- Lipid packing is disrupted in copolymeric nanodiscs compared with intact membranes.Biophysical journal · 2023Article
- Extracellular Vesicle-Based SARS-CoV-2 Vaccine.Vaccines · 2023Review
- Methods to study folding of alpha-helical membrane proteins in lipids.Open biology · 2022Review
- Single-component nanodiscsChemical science · 2022Article
- Synthetic cells in biomedical applications.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2022Review
- Cell-Free Synthesis Strategies to Probe Co-translational Folding of Proteins Within Lipid Membranes.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Cotranslational recruitment of ribosomes in protocells recreates a translocon-independent mechanism of proteorhodopsin biogenesis.iScience · 2021Article
- Preparation of cationic proteoliposomes using cell-free membrane protein synthesis: the chaperoning effect of cationic liposomes.RSC advances · 2020Article
- Tumors and Their Microenvironment Dual-Targeting Chemotherapy with Local Immune Adjuvant Therapy for Effective Antitumor Immunity against Breast Cancer.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2019Article
- Proteoliposome Engineering with Cell-Free Membrane Protein Synthesis: Control of Membrane Protein Sorting into Liposomes by Chaperoning Systems.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Integral membrane proteins (IMPs) modulate key cellular processes; their dysfunctions are closely related to disease. However, production of IMPs in active conformations for further study is hindered by aggregation and toxicity in living expression systems. IMPs are therefore produced in cell-free systems employing liposome chaperoning, but membrane integration of the nascent IMPs is suboptimal and orientation of the integrated proteins remains uncontrollable. Thus, an artificial membrane protein sorting system is developed, based on polyhistidine/nickel-chelate affinity, combined with cell-free membrane protein synthesis. Its proof of concept is demonstrated with a N-terminal hexahistadine-fused conexin-43 (NHis-Cx43) model IMP. Nickel-chelating liposomes efficiently incorporate twofold newly synthesized NHis-Cx43 compared with Cx43. NHis-Cx43, when synthesized in this system, forms dye-permeable hemichannels, similar to plasma membrane pores formed by Cx43 in cells. The topology of incorporated NHis-Cx43 indicates two orientations in the liposomal membranes. However, NHis-Cx43 orientation is controlled, resulting in single topology, by combination of the natural molecular chaperone DnaKJE. Successful synthesis and at least 4.5-fold increase lipid incorporation are also achieved with three other NHis-fused IMPs, including α-helix and β-barrel IMPs. Overall, this simple membrane protein sorting system is usable combined with molecular chaperones to prepare proteoliposomes for many applications.
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.