ArticleScientific reports2017
Purification and functional comparison of nine human Aquaporins produced in Saccharomyces cerevisiae for the purpose of biophysical characterization.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 45 citations in OpenAlex.
- A pan-vertebrate signaling motif controls the molecular function of intracellular AQP12.The Journal of cell biology · 2026Article
- A Semi-Quantitative Yeast Complementation Platform for Characterizing Urea and Ammonia Transport by Membrane Channels.Current protocols · 2026Article
- Characterization of Aquaporin Z proteoliposome structure and functionality via microscopy and scattering methods.European biophysics journal : EBJ · 2025Article
- Yeast Complementation Assays Demonstrating the Importance of the Affinity Tag Position in Membrane Protein Purification, as Exemplified bySmall science · 2025Article
- Fine-tuning the yeast GAL10 promoter and growth conditions for efficient recombinant membrane protein production and purification.Protein science : a publication of the Protein Society · 2025Article
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- Efficient generation of a stable CHO-K1 cell line overexpressing the human water channel aquaporin-5 as tool to generate therapeutic antibodies.Scientific reports · 2024Article
- An Enzymatic and Proteomic Analysis ofJournal of fungi (Basel, Switzerland) · 2024Article
- Diverse roles of the metal binding domains and transport mechanism of copper transporting P-type ATPases.Nature communications · 2024Article
- Aquaporins and Ion Channels as Dual Targets in the Design of Novel Glioblastoma Therapeutics to Limit Invasiveness.Cancers · 2023Review
- Application of polymersomes in membrane protein study and drug discovery: Progress, strategies, and perspectives.Bioengineering & translational medicine · 2023Review
- pXOOY: A dual-function vector for expression of membrane proteins in Saccharomyces cerevisiae and Xenopus laevis oocytes.PloS one · 2023Article
- Modification of Morphology and Glycan Pattern of the Oviductal Epithelium of BaboonAnimals : an open access journal from MDPI · 2022Article
- Production of an Active, Human Membrane Protein inInternational journal of molecular sciences · 2022Article
- Aquaglyceroporin Modulators as Emergent Pharmacological Molecules for Human Diseases.Frontiers in molecular biosciences · 2022Review
- Novel Ion Channel Targets and Drug Delivery Tools for Controlling Glioblastoma Cell Invasiveness.International journal of molecular sciences · 2021Review
- Order and disorder-An integrative structure of the full-length human growth hormone receptor.Science advances · 2021Article
- Targeting Aquaporins in Novel Therapies for Male and Female Breast and Reproductive Cancers.Cells · 2021Review
- Article
- Cyclohexyl-α maltoside as a highly efficient tool for membrane protein studies.Current research in structural biology · 2021Article
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Authors and funding
11 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The sparse number of high-resolution human membrane protein structures severely restricts our comprehension of molecular physiology and ability to exploit rational drug design. In the search for a standardized, cheap and easily handled human membrane protein production platform, we thoroughly investigated the capacity of S. cerevisiae to deliver high yields of prime quality human AQPs, focusing on poorly characterized members including some previously shown to be difficult to isolate. Exploiting GFP labeled forms we comprehensively optimized production and purification procedures resulting in satisfactory yields of all nine AQP targets. We applied the obtained knowledge to successfully upscale purification of histidine tagged human AQP10 produced in large bioreactors. Glycosylation analysis revealed that AQP7 and 12 were O-glycosylated, AQP10 was N-glycosylated while the other AQPs were not glycosylated. We furthermore performed functional characterization and found that AQP 2, 6 and 8 allowed flux of water whereas AQP3, 7, 9, 10, 11 and 12 also facilitated a glycerol flux. In conclusion, our S. cerevisiae platform emerges as a powerful tool for isolation of functional, difficult-to-express human membrane proteins suitable for biophysical characterization.
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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.