ArticleProceedings of the National Academy of Sciences of the United States of America2010
Electrostatics of aquaporin and aquaglyceroporin channels correlates with their transport selectivity.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed, 52 citations in OpenAlex.
- Structural and functional characterization of aquaporin 4 from the freshwater gastropod Pomacea canaliculata under temperature stress.Molecular biology reports · 2026Article
- SARS-CoV-2 ORF3a accessory protein is a water-permeable channel that induces lysosome swelling.Communications biology · 2025Article
- dbAQP-SNP: a database of missense single-nucleotide polymorphisms in human aquaporins.Database : the journal of biological databases and curation · 2023Article
- Water channel pore size determines exclusion properties but not solute selectivity.Scientific reports · 2019Article
- Multiscale Simulations of Biological Membranes: The Challenge To Understand Biological Phenomena in a Living Substance.Chemical reviews · 2019Article
- Review
- Aquaporin-graphene interface: relevance to point-of-care device for renal cell carcinoma and desalination.Interface focus · 2018Review
- Structural Basis for Mutations of Human Aquaporins Associated to Genetic Diseases.International journal of molecular sciences · 2018Article
- Article
- Pancreatic Aquaporin-7: A Novel Target for Anti-diabetic Drugs?Frontiers in chemistry · 2018Review
- Structure, Dynamics, and Substrate Specificity of the OprO Porin from Pseudomonas aeruginosa.Biophysical journal · 2015Article
- Pore waters regulate ion permeation in a calcium release-activated calcium channel.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Glycerol modulates water permeation through Escherichia coli aquaglyceroporin GlpF.Biochimica et biophysica acta · 2013Article
- Multiscale simulations reveal conserved patterns of lipid interactions with aquaporins.Structure (London, England : 1993) · 2013Article
- In silico study of human aquaporin AQP11 and AQP12 channels.Protein science : a publication of the Protein Society · 2013Article
- Single-file water in nanopores.Physical chemistry chemical physics : PCCP · 2011Article
- Functional Annotation Analytics of Rhodopseudomonas palustris Genomes.Bioinformatics and biology insights · 2011Article
- Physiologic upper limits of pore size of different blood capillary types and another perspective on the dual pore theory of microvascular permeability.Journal of angiogenesis research · 2010Article
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 3 institutions in 2 countries.
Funding
Abstract
Aquaporins are homotetrameric channel proteins, which allow the diffusion of water and small solutes across biological membranes. According to their transport function, aquaporins can be divided into "orthodox aquaporins", which allow the flux of water molecules only, and "aquaglyceroporins", which facilitate the diffusion of glycerol and other small solutes in addition to water. The contribution of individual residues in the pore to the selectivity of orthodox aquaporins and aquaglyceroporins is not yet fully understood. To gain insights into aquaporin selectivity, we focused on the sequence variation and electrostatics of their channels. The continuum Poisson-Boltzmann electrostatic potential along the channel was calculated and compared for ten three-dimensional-structures which are representatives of different aquaporin subfamilies, and a panel of functionally characterized mutants, for which high-accuracy three-dimensional-models could be derived. Interestingly, specific electrostatic profiles associated with the main selectivity to water or glycerol could be identified. In particular: (i) orthodox aquaporins showed a distinctive electrostatic potential maximum at the periplasmic side of the channel around the aromatic/Arg (ar/R) constriction site; (ii) aquaporin-0 (AQP0), a mammalian aquaporin with considerably low water permeability, had an additional deep minimum at the cytoplasmic side; (iii) aquaglyceroporins showed a rather flat potential all along the channel; and (iv) the bifunctional protozoan PfAQP had an unusual all negative profile. Evaluation of electrostatics of the mutants, along with a thorough sequence analysis of the aquaporin pore-lining residues, illuminated the contribution of specific residues to the electrostatics of the channels and possibly to their selectivity.
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.