Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all synonyms
Select your origin of interest
Sequencing of GUCY2D identified a novel missense mutation (c.2129C:T; p.Ala710Val) resulting in substitution of alanine by valine at position 710 changes the conformation of the regulatory segment within the kinase styk-domain of GC1 and causes loss of its helical structure, likely inhibiting phosphorylation of threonine residue within this segment, which is needed to activate the catalytic domain of the protein.
These results identify dissociable effects of blindness upon the visual pathway. Further, the relatively intact postgeniculate white matter pathway in GUCY2D-LCA is encouraging for the prospect of recovery of visual function with gene augmentation therapy.
Two novel mutations causing phenotypic LCA (show CLTA Proteins) and Alstrom syndrome in Saudi patients from consanguineous families expand the genotypic spectrum of congenital retinal dystrophies.
Data suggest that GCAP1 (guanylate cyclase activator 1A (show GUCA1A Proteins); Mg2 (show MUC7 Proteins)+ vs. Ca2 (show CA2 Proteins)+) exhibits conformational changes in Ca2 (show CA2 Proteins)+ switch helix that are important in activation of RetGC1; myristoylation of GCAP1 (show GUCA1A Proteins) is important as well in attaining activator conformation.
Gc1s/Gc1s phenotype variant of DBP and the unbound fraction of plasma RBP4 may be considered as factors related with the incidence, and possibly the risk, of IR in CHC patients.
Guanylate cyclase signaling pathway is down regulated in the pathogenesis of inflammatory bowel diseases.
Studies indicate that mutations in retinal guanylate cylase-1 (GUCY2D) are associated with a leading cause of recessive Leber congenital amaurosis (LCA1).
The GUCY2D mutations were frequent in Chinese families with autosomal dominant cone or cone-rod dystrophies. All mutations were found in exon 13.
Dimerization domain of RETGC1 is an essential part of GCAP1 (show GUCA1A Proteins) and GCAP2 (show GUCA1B Proteins) binding interface.
The GCAP1 and GCAP2 binding site(s) overlaps within the kinase homology and/or dimerization domains of retinal GC1.
The findings define a new regulatory mechanism of the ROS-GC system that affects visual transduction and is likely to affect the course of retinal diseases caused by cGMP toxicity.
The coexpression of ROS-GC1 and its activators in spermatozoa suggests that the Ca(2+)-modulated ROS-GC1 transduction system may be a part of the fertilization machinery
Mg(2 (show MCOLN1 Proteins)+) binding to GCAPs is critical for setting the actual dynamic range of RetGC regulation by GCAPs at physiological levels of free Ca(2 (show CA2 Proteins)+)
The Tyr965-Asn981 region of rod outer segment membrane guanylate cyclase type 1 (ROS-GC1) houses both the structural and functional components that mediate guanylate cyclase activating protein type 2 (GCAP2 (show GUCA1B Proteins)) regulation.
This gene encodes a retina-specific guanylate cyclase, which is a member of the membrane guanylyl cyclase family. Like other membrane guanylyl cyclases, this enzyme has a hydrophobic amino-terminal signal sequence followed by a large extracellular domain, a single membrane spanning domain, a kinase homology domain, and a guanylyl cyclase catalytic domain. In contrast to other membrane guanylyl cyclases, this enzyme is not activated by natriuretic peptides. Mutations in this gene result in Leber congenital amaurosis and cone-rod dystrophy-6 diseases.
, cone rod dystrophy 6
, guanylate cyclase 2D, retinal
, retinal guanylyl cyclase 1
, rod outer segment membrane guanylate cyclase
, guanylate cyclase E