Results 11 to 20 of about 1,989 (206)

The Important Role of Aquaglyceroporin 7 in Health and Disease [PDF]

open access: yesBiomolecules
Aquaporins (AQPs) are highly conserved small transmembrane proteins that facilitate the transport of water and small solutes across cell membranes. Aquaglyceroporin 7 (AQP7), a significant member of the AQP family, is widely distributed throughout the ...
Jing Liu   +7 more
doaj   +4 more sources

Implications of Aquaglyceroporin 7 in Energy Metabolism [PDF]

open access: yesInternational Journal of Molecular Sciences, 2018
The aquaglyceroporin AQP7 is a pore-forming transmembrane protein that facilitates the transport of glycerol across cell membranes. Glycerol is utilized both in carbohydrate and lipid metabolism. It is primarily stored in white adipose tissue as part of the triglyceride molecules.
Lebeck, Janne; id_orcid 0000-0003-1716-0417   +1 more
openaire   +4 more sources

The yeast aquaglyceroporin Fps1p is a bidirectional arsenite channel [PDF]

open access: yesFEBS 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   +4 more sources

Anionic Lipids Modulate the Activity of the Aquaglyceroporin GlpF [PDF]

open access: yesBiophysical 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   +4 more sources

Targeted deletion of the aquaglyceroporin AQP9 is protective in a mouse model of Parkinson's disease. [PDF]

open access: yesPLoS ONE, 2018
More than 90% of the cases of Parkinson's disease have unknown etiology. Gradual loss of dopaminergic neurons of substantia nigra is the main cause of morbidity in this disease. External factors such as environmental toxins are believed to play a role in
Katja Stahl   +12 more
doaj   +4 more sources

Acyrthosiphon pisum AQP2: A multifunctional insect aquaglyceroporin [PDF]

open access: yesBiochimica et Biophysica Acta (BBA) - Biomembranes, 2012
Annotation of the recently sequenced genome of the pea aphid (Acyrthosiphon pisum) identified a gene ApAQP2 (ACYPI009194, Gene ID: 100168499) with homology to the Major Intrinsic Protein/aquaporin superfamily of membrane channel proteins. Phylogenetic analysis suggests that ApAQP2 is a member of an insect-specific clade of this superfamily.
Wallace, Ian S.   +6 more
openaire   +3 more sources

Regulatory mechanisms of Leishmania Aquaglyceroporin AQP1 [PDF]

open access: yes, 2017
Pentavalent antimonials [Sb(V)] are the primary drug of choice against all forms of leishmaniasis. Emergence of antimony unresponsiveness is a major issue. There is a dire need of understanding antimony resistance mechanisms in Leishmania.
Sharma, Mansi
openaire   +3 more sources

Functional characterization of a microbial aquaglyceroporin [PDF]

open access: yesMicrobiology, 2001
The major intrinsic proteins (MIPs) constitute a widespread membrane channel family essential for osmotic cell equilibrium. The MIPs can be classified into three functional subgroups: aquaporins, glycerol facilitators and aquaglyceroporins. Bacterial MIP genes have been identified in archaea as well as in Gram-positive and Gram-negative eubacteria ...
Alexandrine, Froger   +9 more
openaire   +2 more sources

Role of Aquaglyceroporin (AQP1) Gene and Drug Uptake in Antimony-resistant Clinical Isolates of Leishmania donovani [PDF]

open access: yes, 2008
Antimonial-containing drugs are the first line of treatment against Leishmaniasis. Resistance to antimonials in Leishmania is proposed to be due to reduced uptake of trivalent antimony (SbIII) through the aquaglyceroporin (AQP1).
Singh, Sushma   +3 more
core   +6 more sources

Aquaglyceroporins: ancient channels for metalloids [PDF]

open access: yesJournal of Biology, 2008
The identification of aquaglyceroporins as uptake channels for arsenic and antimony shows how these toxic elements can enter the food chain, and suggests that food plants could be genetically modified to exclude arsenic while still accumulating boron and silicon.
Bhattacharjee, Hiranmoy   +3 more
openaire   +2 more sources

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