ArticleNature communications2023
Cryo-EM structure supports a role of AQP7 as a junction protein.
Article in Nature communications, 2023. 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, 24 citations in OpenAlex.
- Current Advances in Cetacean Semen Cryopreservation and Their Application to Yangtze Finless Porpoise Conservation.Animals : an open access journal from MDPI · 2026Review
- Review
- Structural insights into AQP3 channel closure upon pH and redox changes reveal an autoregulatory molecular mechanism.Nature communications · 2025Article
- AQP7 deficiency drives adipose tissue remodeling and disrupts homeostasis.npj metabolic health and disease · 2025Article
- Aquaporins in lipid metabolism: functions and regulation in health and disease.Lipids in health and disease · 2025Review
- Characterization of Aquaporin Z proteoliposome structure and functionality via microscopy and scattering methods.European biophysics journal : EBJ · 2025Article
- Narrowed pore conformations of aquaglyceroporins AQP3 and GlpF.Nature communications · 2025Article
- An Unexpected Water Channel in the Light-Harvesting Complex of a Diatom: Implications for the Switch between Light Harvesting and Photoprotection.ACS physical chemistry Au · 2025Article
- Computation suggests that the cell adhesion sub-proteome is enriched for sites of pH-dependence and charge burial.PloS one · 2025Article
- Protein Structures of Urea Transporters.Sub-cellular biochemistry · 2025Review
- Urea Transport Mediated by Membrane Proteins of Non-urea-Transporters.Sub-cellular biochemistry · 2025Review
- The Important Role of Aquaglyceroporin 7 in Health and Disease.Biomolecules · 2024Review
- Molecular basis for human aquaporin inhibition.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Aquaporin water channels: roles beyond renal water handling.Nature reviews. Nephrology · 2023Review
- Aquaglyceroporins in Human Breast Cancer.Cells · 2023Article
- Review
- Anomalous Oligomerization Behavior ofInternational journal of molecular sciences · 2023Article
- Effect of guanylin peptides on pancreas steatosis and function in experimental diet-induced obesity and after bariatric surgery.Frontiers in endocrinology · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aquaglyceroporin 7 (AQP7) facilitates glycerol flux across the plasma membrane with a critical physiological role linked to metabolism, obesity, and associated diseases. Here, we present the single-particle cryo-EM structure of AQP7 determined at 2.55 Å resolution adopting two adhering tetramers, stabilized by extracellularly exposed loops, in a configuration like that of the well-characterized interaction of AQP0 tetramers. The central pore, in-between the four monomers, displays well-defined densities restricted by two leucine filters. Gas chromatography mass spectrometry (GC/MS) results show that the AQP7 sample contains glycerol 3-phosphate (Gro3P), which is compatible with the identified features in the central pore. AQP7 is shown to be highly expressed in human pancreatic α- and β- cells suggesting that the identified AQP7 octamer assembly, in addition to its function as glycerol channel, may serve as junction proteins within the endocrine pancreas.
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.