function have not been elucidated. localization at the plasma membrane and results in R578Q displaying a higher apparent molecular weight in comparison to wild-type receptor. We used the glycosidase endoglycosidase H to determine that this difference in mass is due in part to the R578Q mutant possessing a larger mass of oligosaccharides, indicative of improper N-linked glycosylation addition and/or trimming. Chemical cross-linking experiments were also performed and suggest that the R578Q variant also does not form trimers as well as wild-type receptor, a function required for its full activity. activity and localization at the plasma membrane
N-Glycosylation affects the function of ion channels at the level of multisubunit assembly, protein ...
N-glycosylation of membrane receptors is important for a wide variety of cellular processes. In the ...
P2X7 is the largest member of the P2X subfamily of purinergic receptors. A typical feature is the ca...
function have not been elucidated. localization at the plasma membrane and results in R578Q display...
The P2X7 receptor binds extracellular ATP to mediate numerous inflammatory responses and is consider...
Background: The P2X7 receptor binds extracellular ATP to mediate numerous inflammatory responses and...
N-Glycosylation affects the function of ion channels at the level of multisubunit assembly, protein ...
N-Glycosylation affects the function of ion channels at the level of multisubunit assembly, protein ...
N-Glycosylation affects the function of ion channels at the level of multisubunit assembly, protein ...
N-Glycosylation affects the function of ion channels at the level of multisubunit assembly, protein ...
N-Glycosylation affects the function of ion channels at the level of multisubunit assembly, protein ...
N-Glycosylation affects the function of ion channels at the level of multisubunit assembly, protein ...
The P2X7 receptor is a trimeric ion channel gated by extracellular adenosine 50-triphosphate. The re...
<p><b>A,</b> HEK293 stable cell lines were treated with the broad-spectrum protease proteinase K to ...
<p><b>A,</b> HEK293 cells were treated with the cell-permeable chemical cross-linker DSS to demonstr...
N-Glycosylation affects the function of ion channels at the level of multisubunit assembly, protein ...
N-glycosylation of membrane receptors is important for a wide variety of cellular processes. In the ...
P2X7 is the largest member of the P2X subfamily of purinergic receptors. A typical feature is the ca...
function have not been elucidated. localization at the plasma membrane and results in R578Q display...
The P2X7 receptor binds extracellular ATP to mediate numerous inflammatory responses and is consider...
Background: The P2X7 receptor binds extracellular ATP to mediate numerous inflammatory responses and...
N-Glycosylation affects the function of ion channels at the level of multisubunit assembly, protein ...
N-Glycosylation affects the function of ion channels at the level of multisubunit assembly, protein ...
N-Glycosylation affects the function of ion channels at the level of multisubunit assembly, protein ...
N-Glycosylation affects the function of ion channels at the level of multisubunit assembly, protein ...
N-Glycosylation affects the function of ion channels at the level of multisubunit assembly, protein ...
N-Glycosylation affects the function of ion channels at the level of multisubunit assembly, protein ...
The P2X7 receptor is a trimeric ion channel gated by extracellular adenosine 50-triphosphate. The re...
<p><b>A,</b> HEK293 stable cell lines were treated with the broad-spectrum protease proteinase K to ...
<p><b>A,</b> HEK293 cells were treated with the cell-permeable chemical cross-linker DSS to demonstr...
N-Glycosylation affects the function of ion channels at the level of multisubunit assembly, protein ...
N-glycosylation of membrane receptors is important for a wide variety of cellular processes. In the ...
P2X7 is the largest member of the P2X subfamily of purinergic receptors. A typical feature is the ca...