AbstractPDZ domains are thought to act as protein-binding modules mediating the clustering of membrane and membrane-associated proteins. The INAD protein has been shown to interact via a PDZ domain with the calcium channel TRP which contributes to capacitative calcium entry into Drosophila photoreceptor cells. We have cloned the cDNA of a human INAD-Like protein (hINADL) of 1524 amino acids in length containing at least five PDZ domains. Additionally, two truncated versions hINADLΔ304 and hINADLΔ853 were identified. hInadl transcripts of differing size are expressed in various tissues including brain, where transcripts are abundant in the cerebellum
Drosophila inactivation no afterpotential D (INAD) is a PDZ domain-containing scaffolding protein th...
PDZ domains are protein-protein interaction modules that typically bind to short peptide sequences a...
In Drosophila, phototransduction is mediated by Gq-activation of phospholipase C and is a well studi...
AbstractPDZ domains are thought to act as protein-binding modules mediating the clustering of membra...
InaD, a Drosophila photoreceptor scaffolding protein, assembles multiple signal-transducing proteins...
The vast majority of PDZ domains are known to bind to a few C-terminal tail residues of target prote...
AbstractIn Drosophila, the store-operated Ca2+ channel, TRP, is required in photoreceptor cells for ...
PDZ domains are common building blocks of scaffold proteins that enhance specificity and speed in si...
PDZ domains are protein-protein interaction modules that typically bind to short peptide sequences a...
AbstractInaDP215 is a point mutation that affects photoreceptor function in Drosophila. To understan...
PDZ domains (also known as DHR domains or GLGF repeats) are ˜90-residue repeats found in a number of...
Here, we reveal a novel feature of the dynamic organization of signaling components in Drosophila ph...
AbstractDrosophila vision involves a G protein-coupled phospholipase C-mediated signaling pathway th...
AbstractInaD, a Drosophila photoreceptor scaffolding protein, assembles multiple signal-transducing ...
AbstractPDZ domains can dimerize or bind to the carboxyl termini of unrelated proteins. Crystallogra...
Drosophila inactivation no afterpotential D (INAD) is a PDZ domain-containing scaffolding protein th...
PDZ domains are protein-protein interaction modules that typically bind to short peptide sequences a...
In Drosophila, phototransduction is mediated by Gq-activation of phospholipase C and is a well studi...
AbstractPDZ domains are thought to act as protein-binding modules mediating the clustering of membra...
InaD, a Drosophila photoreceptor scaffolding protein, assembles multiple signal-transducing proteins...
The vast majority of PDZ domains are known to bind to a few C-terminal tail residues of target prote...
AbstractIn Drosophila, the store-operated Ca2+ channel, TRP, is required in photoreceptor cells for ...
PDZ domains are common building blocks of scaffold proteins that enhance specificity and speed in si...
PDZ domains are protein-protein interaction modules that typically bind to short peptide sequences a...
AbstractInaDP215 is a point mutation that affects photoreceptor function in Drosophila. To understan...
PDZ domains (also known as DHR domains or GLGF repeats) are ˜90-residue repeats found in a number of...
Here, we reveal a novel feature of the dynamic organization of signaling components in Drosophila ph...
AbstractDrosophila vision involves a G protein-coupled phospholipase C-mediated signaling pathway th...
AbstractInaD, a Drosophila photoreceptor scaffolding protein, assembles multiple signal-transducing ...
AbstractPDZ domains can dimerize or bind to the carboxyl termini of unrelated proteins. Crystallogra...
Drosophila inactivation no afterpotential D (INAD) is a PDZ domain-containing scaffolding protein th...
PDZ domains are protein-protein interaction modules that typically bind to short peptide sequences a...
In Drosophila, phototransduction is mediated by Gq-activation of phospholipase C and is a well studi...