Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all species
Show all synonyms
Select your species
a recurrent missense mutation (c.403C > T, p.R135W) in the rhodopsin (RHO) gene cosegregated with all retinitis pigmentosa affected individuals in the family.
Autosomal recessive retinitis pigmentosa with homozygous rhodopsin mutation E150K and non-coding cis-regulatory variants in CRX-binding regions of SAMD7.
Functional role of positively selected amino acid substitutions in mammalian rhodopsin evolution has been uncovered for a large number of mammalian species.
Our study shows that RHO mutations are a major cause of adRP (show PLIN2 ELISA Kits) in this cohort and are responsible for 28% of adRP (show PLIN2 ELISA Kits) families.
analysis of the crystal structure of the rhodopsin-arrestin (show SAG ELISA Kits) complex
A whole-exome sequencing approach led to identification of a deletion in RHO through detection of a new linked variant in COL6A6 in autosomal dominant retinitis pigmentosa.
These insights into the dynamics of the ground states and the early photocycle stages enhance our understanding of the channel function of Channel rhodopsin.
Studies indicate that misfolding of rhodopsin can result in disruptions in cellular protein homeostasis, or proteostasis.
FIP3 (RAB11 (show RAB11FIP3 ELISA Kits)-FIP3 (show RAB11FIP3 ELISA Kits)) promotes the activity of Rab11a (show RAB11A ELISA Kits) and the ASAP1 (show ASAP1 ELISA Kits) in the Arf4 (show ARF4 ELISA Kits)-dependent ciliary transport of the sensory receptor rhodopsin.
Similar vacuolization in photoreceptor outer segment discs of transgenic mice expressing human rhodopsin with a T17M mutation or non-glycosylated form of rhodopsin was found. Non-glycosylated rhodopsin is unstable and is regulated via ubiquitin pathway
The authors elucidated this dependency by showing that guanylate cyclase-1 is a novel rhodopsin-binding protein.
Eliminating Cngb1 and reducing RDS leads to additive defects in RDS expression levels and rod electroretinogram (ERG) function, (e.g., Cngb1-/-/rds+/- versus rds+/- or Cngb1-/-) but not to additive defects in rod ultrastructure.
These findings reveal that an early and significant pathophysiologic effect of endoplasmic reticulum stress in photoreceptors is the highly efficient elimination of misfolded rhodopsin protein.
Data show that G90D1 ribozyme efficiently and specifically cleaved the mutant transcript of the G90D mutation in the rhodopsin gene while G90D2 ribozyme cleaved both WT and mutant transcript.
Data show that misfolded opsin mutants form aggregates in the endoplasmic reticulum.
Data show that the step-like responses of serine-only rhodopsin reflect slow and stochastic arrestin (show SAG ELISA Kits) binding.
Data indicate that genomic sequences from the rhodopsin gene can improve the efficacy of rhodopsin gene therapy in the rhodopsin knockout (RKO) mouse model of retinitis pigmentosa (RP).
Peripherin-2 (show PRPH2 ELISA Kits) links CNGB1 to the light-detector rhodopsin in outer segments of rod photoreceptors.
p27(kip1 (show CDKN1B ELISA Kits)) promotes mesenchymal migration and hinders amoeboid migration upstream of the Rho/ROCK pathway.
Data indicate that the number of nanodomains present in a single disc was dependent on the number of rhodopsin molecules incorporated into the membrane.
Retinitis pigmentosa is an inherited progressive disease which is a major cause of blindness in western communities. It can be inherited as an autosomal dominant, autosomal recessive, or X-linked recessive disorder. In the autosomal dominant form,which comprises about 25% of total cases, approximately 30% of families have mutations in the gene encoding the rod photoreceptor-specific protein rhodopsin. This is the transmembrane protein which, when photoexcited, initiates the visual transduction cascade. Defects in this gene are also one of the causes of congenital stationary night blindness.
opsin 2, rod pigment
, L opsin
, LWS opsin
, Long Wavelength Sensitive opsin
, Red Opsin
, Rod Opsin
, opsin 2
, Rhodopsin (retinitis pigmentosa 4, autosomal dominant)