ReviewIUCrJ2026
Structural physiology of distinctive water channels elucidated by cryo-EM.
Review in IUCrJ, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
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.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aquaporins (AQPs) are membrane channel proteins that facilitate the transport of water and related solutes, playing indispensable roles across a wide range of organisms. Extensive structural studies using X-ray crystallography and electron crystallography have provided fundamental insights into the physiological functions of various AQPs. Recent advances in the structural analysis using single-particle cryo-electron microscopy, which bypasses the requirement for crystallization, have profoundly enhanced our understanding of AQP mechanisms. In this review, we summarize recent progress in AQP biology, providing a comparative analysis of orthodox, glycerol-permeable and unorthodox AQPs.
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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.