Results 11 to 20 of about 1,538 (126)
The aquaporin genes (aqps) are widely distributed among vertebrates. In cartilaginous fish, aqp3 and aqp10 are duplicated, whereas many species have lost aqp8.
Shinichiro Hidaka +2 more
doaj +2 more sources
An Atypical Aquaporin 1 Derived From Paramecium multimicronucleatum Functions as a Multifunctional Channel That Permeates Water, Glycerol, and Urea. [PDF]
ABSTRACT Although it had been reported that the translation product of the functional aquaporin gene, aqp1, is localized to the contractile vacuole complex of Paramecium multimicronucleatum, the molecules that pass through this channel protein had not been identified. In the present study, we introduced and expressed this protein in Xenopus oocytes and
Ishida M +5 more
europepmc +2 more sources
Lactic Acid Permeability of Aquaporin-9 Enables Cytoplasmic Lactate Accumulation via an Ion Trap
(1) Background: Human aquaporin-9 (AQP9) conducts several small uncharged metabolites, such as glycerol, urea, and lactic acid. Certain brain tumors were shown to upregulate AQP9 expression, and the putative increase in lactic acid permeability was ...
Katharina Geistlinger +2 more
doaj +1 more source
Aquaporins (AQPs) are integral membrane proteins that facilitate the transport of water and small solutes across cell membranes. These proteins are vital for maintaining water homeostasis in living organisms.
Zhongkai Wang +8 more
doaj +1 more source
Lessons From Drug Discovery for Cryoprotective Agent Design: An AI-Oriented Perspective. [PDF]
Cryoprotectant design is reframed through the lens of drug discovery as a multiparameter optimization problem. This perspective highlights how AI and systematic design strategies could enable safer, more effective cryoprotectants, while identifying key limitations that currently constrain predictive progress in cryobiology. ABSTRACT Cryopreservation is
Wilczok D +4 more
europepmc +2 more sources
In this article, the Brownian dynamics fluctuation-dissipation theorem (BD-FDT) is applied to the study of transport of neutral solutes across the cellular membrane of Plasmodium berghei (Pb), a disease-causing parasite.
Liao Y. Chen
doaj +1 more source
Boric acid transport activity of human aquaporins expressed in Xenopus oocytes
Boric acid is a vital micronutrient that is toxic at high concentrations in animals. However, the mechanisms underlying boric acid transport in animal cells remain unclear.
Kazutaka Ushio +8 more
doaj +1 more source
Cope's gray treefrog, Hyla chrysoscelis, is a freeze-tolerant anuran that accumulates cryoprotective glycerol during cold acclimation. H. chrysoscelis erythrocytes express the aquaglyceroporin HC-3, which facilitates transmembrane glycerol and water ...
Venkateshwar Mutyam +4 more
doaj +1 more source
Aquaglyceroporin Modulators as Emergent Pharmacological Molecules for Human Diseases
Aquaglyceroporins, a sub-class of aquaporins that facilitate the diffusion of water, glycerol and other small uncharged solutes across cell membranes, have been recognized for their important role in human physiology and their involvement in multiple ...
Catarina Pimpão +7 more
doaj +1 more source
Boric acid transport activity of marine teleost aquaporins expressed in Xenopus oocytes
Marine teleosts ingest large amounts of seawater containing various ions, including 0.4 mM boric acid, which can accumulate at toxic levels in the body. However, the molecular mechanisms by which marine teleosts absorb and excrete boric acid are not well
Shiori Kumagai +15 more
doaj +1 more source

