Results 41 to 50 of about 1,989 (206)

Aquaglyceroporin PbAQP during intraerythrocytic development of the malaria parasite Plasmodium berghei [PDF]

open access: yes, 2007
The malaria parasite can use host plasma glycerol for lipid biosynthesis and membrane biogenesis during the asexual intraerythrocytic development. The molecular basis for glycerol uptake into the parasite is undefined.
King, Landon S.   +5 more
core   +1 more source

Aquaporin 2 mutations in Trypanosoma brucei gambiense field isolates correlate with decreased susceptibility to pentamidine and melarsoprol [PDF]

open access: yes, 2013
The predominant mechanism of drug resistance in African trypanosomes is decreased drug uptake due to loss-of-function mutations in the genes for the transporters that mediate drug import. The role of transporters as determinants of drug susceptibility is
Kaiser Marcel   +40 more
core   +1 more source

The AQP2 mutation V71M causesnephrogenic diabetes insipidus in humans but does not impair the function of a bacterial homolog

open access: yesFEBS Open Bio, 2015
Several point mutations have been identified in human aquaporins, but their effects on the function of the respective aquaporins are mostly enigmatic. We analyzed the impact of the aquaporin 2 mutation V71M, which causesnephrogenic diabetes insipidus in ...
Noreen Klein   +3 more
doaj   +1 more source

Down-regulation of TORC2-Ypk1 signaling promotes MAPK-independent survival under hyperosmotic stress

open access: yeseLife, 2015
In eukaryotes, exposure to hypertonic conditions activates a MAPK (Hog1 in Saccharomyces cerevisiae and ortholog p38 in human cells). In yeast, intracellular glycerol accumulates to counterbalance the high external osmolarity. To prevent glycerol efflux,
Alexander Muir   +4 more
doaj   +1 more source

A region within the third extracellular loop of rat Aquaporin 6 precludes trafficking to plasma membrane in a heterologous cell line

open access: yesScientific Reports, 2021
The inability to over-express Aquaporin 6 (AQP6) in the plasma membrane of heterologous cells has hampered efforts to further characterize the function of this aquaglyceroporin membrane protein at atomic detail using crystallographic approaches. Using an
D. C. Soler   +7 more
doaj   +1 more source

Pore selectivity analysis of an aquaglyceroporin by stopped-flow spectrophotometry on bacterial cell suspensions [PDF]

open access: yes, 2005
International audienceBackground information. Transport of water and small neutral solutes across plasma membranes is facilitated by AQP (aquaporin) and aquaglyceroporin channels, which belong to the MIP (major intrinsic protein) family.
Duchesne, L.   +5 more
core   +1 more source

Aquaporin-10 represents an alternative pathway for glycerol efflux from human adipocytes. [PDF]

open access: yesPLoS ONE, 2013
BACKGROUND: Glycerol outflow from adipocytes has been considered for a decade to be mediated by aquaporin-7, an aquaglyceroporin highly expressed in the adipose tissue. Its involvement in glycerol metabolism has been widely studied also in humans. Recent
Umberto Laforenza   +2 more
doaj   +1 more source

Aquaglyceroporin-3’s Expression and Cellular Localization Is Differentially Modulated by Hypoxia in Prostate Cancer Cell Lines

open access: yesCells, 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

Replication Data for "Aquaglyceroporin AQP7’s affinity for its substrate glycerol---Have we reached convergence in the computed values of glycerol-aquaglyceroporin affinity?" [PDF]

open access: yes
The parameters, the coordinates, and the scripts for setting up the model systems, running the simulations, and analyzing the data used in Falato et al (2021) "Aquaglyceroporin AQP7’s affinity for its substrate glycerol---Have we reached convergence in ...
Chen, Liao
core   +1 more source

Aquaporins with anion/monocarboxylate permeability: mechanisms, relevance for pathogen-host interactions

open access: yesFrontiers in Pharmacology, 2014
Classically, aquaporins are divided based on pore selectivity into water specific, orthodox aquaporins and solute-facilitating aquaglyceroporins, which conduct e.g. glycerol and urea.
Janis eRambow   +3 more
doaj   +1 more source

Home - About - Disclaimer - Privacy