Results 31 to 40 of about 1,373 (155)
Pathways of arsenic uptake and efflux
Environment International, 2019 Arsenic is a non-essential, environmentally ubiquitous toxic metalloid. In response to this pervasive environmental challenge, organisms evolved mechanisms to confer resistance to arsenicals.
Luis D. Garbinski +2 more
doaj +1 more source
Diabetic Kidney Disease-Associated Pathological Angiogenesis: The Role of Aquaporin-1. [PDF]
J DiabetesHyperglycemia upregulates AQP1 expression in renal endothelial cells, promoting abnormal angiogenesis. Structurally and functionally immature vessels lead to glomerular capillary leakage, proteinuria, and progressive renal injury. Targeting AQP1 may attenuate abnormal angiogenesis in DKD and slow disease progression.
Zhang F +9 more
europepmc +2 more sources
Cells, 2021 Aquaporins are required by cells to enable fast adaptation to volume and osmotic changes, as well as microenvironmental metabolic stimuli. Aquaglyceroporins play a crucial role in supplying cancer cells with glycerol for metabolic needs.
Andreia de Almeida +5 more
doaj +1 more source
The yeast aquaglyceroporin Fps1p is a bidirectional arsenite channel [PDF]
FEBS Letters, 2009 The stress‐activated kinase Hog1p mediates arsenic tolerance by decreasing arsenite influx through the aquaglyceroporin Fps1p in Saccharomyces cerevisiae. Unexpectedly, we found that overexpression of FPS1 increased arsenite tolerance suggesting a physiological role of Fps1p in arsenic detoxification.
Maciaszczyk-Dziubinska, Ewa +4 more
openaire +2 more sources
Pathogens, 2022 Ornithodoros moubata transmits African swine fever and human relapsing fever in Africa. The elimination of O. moubata populations from anthropic environments is expected to improve the prevention and control of these diseases.
Ricardo Pérez-Sánchez +3 more
doaj +1 more source
Anionic Lipids Modulate the Activity of the Aquaglyceroporin GlpF [PDF]
Biophysical Journal, 2015 The structure and composition of a biological membrane can severely influence the activity of membrane-embedded proteins. Here, we show that the E. coli aquaglyceroporin GlpF has only little activity in lipid bilayers formed from native E. coli lipids. Thus, at first glance, GlpF appears to not be optimized for its natural membrane environment. In fact,
Klein, Noreen +2 more
openaire +2 more sources
Predicting the functionality of major intrinsic proteins: An in silico analysis in Musa [PDF]
Trends in Pharmaceutical Sciences, 2016 Major intrinsic proteins (MIPs) are tetrameric complexs with six transmembrane domains. MIPs which are involved in water and nutrient permeability have been called aquaporins and aquaglyceroporins respectivly.
Shiva Hemmati
doaj +2 more sources
Computational Modeling on Aquaporin-3 as Skin Cancer Target: A Virtual Screening Study
Frontiers in Chemistry, 2020 Aquaporin-3 (AQP3) is one of the aquaglyceroporins, which is expressed in the basolateral layer of the skin membrane. Studies have reported that human skin squamous cell carcinoma overexpresses AQP3 and inhibition of its function may alleviate skin ...
Dharmendra Kumar Yadav +4 more
doaj +1 more source
Arsenite transport by mammalian aquaglyceroporins AQP7 and AQP9 [PDF]
Proceedings of the National Academy of Sciences, 2002 Much is known about the transport of arsenite and antimonite into microbes, but the identities of mammalian transport proteins are unknown. The Saccharomyces cerevisiae FPS1 gene encodes a membrane protein homologous to the bacterial aquaglyceroporin GlpF and to mammalian aquaglyceroporins ...
Rosen, Barry P. +5 more
openaire +2 more sources
The gating mechanism of the human aquaporin 5 revealed by molecular dynamics simulations. [PDF]
PLoS ONE, 2013 Aquaporins are protein channels located across the cell membrane with the role of conducting water or other small sugar alcohol molecules (aquaglyceroporins). The high-resolution X-ray structure of the human aquaporin 5 (HsAQP5) shows that HsAQP5, as all
Lorant Janosi, Matteo Ceccarelli
doaj +1 more source