Add to ORKGInaD, a Drosophila photoreceptor scaffolding protein, assembles multiple signal-transducing proteins at the membrane via its five PDZ domains, enhancing speed and efficiency of vision. Extensive conservation of PDZ domains suggests that these motifs have a general role in organizing diverse signaling complexes
AbstractInaDP215 is a point mutation that affects photoreceptor function in Drosophila. To understan...
AbstractPhotoreceptors which use a phospholipase C-mediated signal transduction cascade harbor a sig...
Mammalian phospholipase C-beta isozymes are activated by a heterotrimeric GTP-binding protein linked...
AbstractInaD, a Drosophila photoreceptor scaffolding protein, assembles multiple signal-transducing ...
PDZ domains are common building blocks of scaffold proteins that enhance specificity and speed in si...
SummaryThe INAD scaffold organizes a multiprotein complex that is essential for proper visual signal...
SummaryINAD is a scaffolding protein that regulates signaling in Drosophila photoreceptors. One of i...
Here, we reveal a novel feature of the dynamic organization of signaling components in Drosophila ph...
Phototransduction in Drosophila is the fastest known G-protein coupled signalingcascade to date. Stu...
The vast majority of PDZ domains are known to bind to a few C-terminal tail residues of target prote...
Drosophila inactivation no afterpotential D (INAD) is a PDZ domain-containing scaffolding protein th...
AbstractPDZ domains are thought to act as protein-binding modules mediating the clustering of membra...
AbstractIn Drosophila, the store-operated Ca2+ channel, TRP, is required in photoreceptor cells for ...
In Drosophila, phototransduction is mediated by Gq-activation of phospholipase C and is a well studi...
Scaffold proteins allow specific protein complexes to be assembled in particular regions of the cell...
AbstractInaDP215 is a point mutation that affects photoreceptor function in Drosophila. To understan...
AbstractPhotoreceptors which use a phospholipase C-mediated signal transduction cascade harbor a sig...
Mammalian phospholipase C-beta isozymes are activated by a heterotrimeric GTP-binding protein linked...
AbstractInaD, a Drosophila photoreceptor scaffolding protein, assembles multiple signal-transducing ...
PDZ domains are common building blocks of scaffold proteins that enhance specificity and speed in si...
SummaryThe INAD scaffold organizes a multiprotein complex that is essential for proper visual signal...
SummaryINAD is a scaffolding protein that regulates signaling in Drosophila photoreceptors. One of i...
Here, we reveal a novel feature of the dynamic organization of signaling components in Drosophila ph...
Phototransduction in Drosophila is the fastest known G-protein coupled signalingcascade to date. Stu...
The vast majority of PDZ domains are known to bind to a few C-terminal tail residues of target prote...
Drosophila inactivation no afterpotential D (INAD) is a PDZ domain-containing scaffolding protein th...
AbstractPDZ domains are thought to act as protein-binding modules mediating the clustering of membra...
AbstractIn Drosophila, the store-operated Ca2+ channel, TRP, is required in photoreceptor cells for ...
In Drosophila, phototransduction is mediated by Gq-activation of phospholipase C and is a well studi...
Scaffold proteins allow specific protein complexes to be assembled in particular regions of the cell...
AbstractInaDP215 is a point mutation that affects photoreceptor function in Drosophila. To understan...
AbstractPhotoreceptors which use a phospholipase C-mediated signal transduction cascade harbor a sig...
Mammalian phospholipase C-beta isozymes are activated by a heterotrimeric GTP-binding protein linked...