ReviewBiochimica et biophysica acta2014
Aquaglyceroporins: generalized metalloid channels.
Review in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 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
60 citing papers in PubMed, 193 citations in OpenAlex.
- Aquaporin-9 and aquaporin-10 but not aquaporin-3 confer susceptibility to dimethylarsinic acid genotoxicity in human cells.bioRxiv : the preprint server for biology · 2026Article
- Differential Susceptibility to Antimony in Strains and Clinical Isolates ofPathogens (Basel, Switzerland) · 2026Article
- Independent divergences of the aquaporins across different genera highlight the distinct adaptation mechanisms within Mytilida.BMC genomics · 2025Article
- Review
- Research progress on the uptake and transport of antimony and arsenic in the soil-crop system.Frontiers in plant science · 2025Review
- Exploring Aquaporins in Human Studies: Mechanisms and Therapeutic Potential in Critical Illness.Life (Basel, Switzerland) · 2024Review
- Differential Selectivity of Human and Mouse ABCC4/Abcc4 for Arsenic Metabolites.Drug metabolism and disposition: the biological fate of chemicals · 2024Article
- Early Diversification of Membrane Intrinsic Proteins (MIPs) in Eukaryotes.Genome biology and evolution · 2024Article
- Genomic Insight of Leishmania Parasite: In-Depth Review of Drug Resistance Mechanisms and Genetic Mutations.ACS omega · 2024Review
- Antimony resistance and gene expression inParasitology · 2024Review
- The Functionality of Membrane-Inserting Proteins and Peptides: Curvature Sensing, Generation, and Pore Formation.The Journal of membrane biology · 2023Review
- Rapid arsenite oxidation by Paenarthrobacter nicotinovorans strain SSBW5: unravelling the role of GlpF, aioAB and aioE genes.Archives of microbiology · 2023Article
- Microbial biochemical pathways of arsenic biotransformation and their application for bioremediation.Folia microbiologica · 2023Review
- Plasma membrane-associated calcium signaling regulates arsenate tolerance in Arabidopsis.Plant physiology · 2023Article
- Proteomic Analysis of Arsenic Resistance during Cyanide Assimilation byInternational journal of molecular sciences · 2023Article
- Aquaporins as Prognostic Biomarker in Prostate Cancer.Cancers · 2023Review
- Ca Minerals and Oral Bioavailability of Pb, Cd, and As from Indoor Dust in Mice: Mechanisms and Health Implications.Environmental health perspectives · 2022Article
- The role of the glycerol transporter channel Fps1p in cellular proteostasis during enhanced proteotoxic stress.Applied microbiology and biotechnology · 2022Article
- Availability, Toxicology and Medical Significance of Antimony.International journal of environmental research and public health · 2022Review
- Genome mining to unravel potential metabolic pathways linked to gallium bioleaching ability of bacterial mine isolates.Frontiers in microbiology · 2022Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
backgroundAquaporins (AQPs), members of a superfamily of transmembrane channel proteins, are ubiquitous in all domains of life. They fall into a number of branches that can be functionally categorized into two major sub-groups: i) orthodox aquaporins, which are water-specific channels, and ii) aquaglyceroporins, which allow the transport of water, non-polar solutes, such as urea or glycerol, the reactive oxygen species hydrogen peroxide, and gases such as ammonia, carbon dioxide and nitric oxide and, as described in this review, metalloids. SCOPE OF REVIEW: This review summarizes the key findings that AQP channels conduct bidirectional movement of metalloids into and out of cells. MAJOR
conclusionsAs(OH)3 and Sb(OH)3 behave as inorganic molecular mimics of glycerol, a property that allows their passage through AQP channels. Plant AQPs also allow the passage of boron and silicon as their hydroxyacids, boric acid (B(OH)3) and orthosilicic acid (Si(OH)4), respectively. Genetic analysis suggests that germanic acid (GeO2) is also a substrate. While As(III), Sb(III) and Ge(IV) are toxic metalloids, borate (B(III)) and silicate (Si(IV)) are essential elements in higher plants. GENERAL SIGNIFICANCE: The uptake of environmental metalloids by aquaporins provides an understanding of (i) how toxic elements such as arsenic enter the food chain; (ii) the delivery of arsenic and antimony containing drugs in the treatment of certain forms of leukemia and chemotherapy of diseases caused by pathogenic protozoa; and (iii) the possibility that food plants such as rice could be made safer by genetically modifying them to exclude arsenic while still accumulating boron and silicon. This article is part of a Special Issue entitled Aquaporins.
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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.