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anti-Human RHO Antibodies:
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Human Monoclonal RHO Primary Antibody for IF, WB - ABIN968300
Brandt, Gimona, Hillmann, Haller, Mischak: Protein kinase C induces actin reorganization via a Src- and Rho-dependent pathway. in The Journal of biological chemistry 2002
Show all 5 references for ABIN968300
Our study shows that RHO mutations are a major cause of adRP (show PLIN2 Antibodies) in this cohort and are responsible for 28% of adRP (show PLIN2 Antibodies) families.
analysis of the crystal structure of the rhodopsin-arrestin (show SAG Antibodies) 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 Antibodies)-FIP3 (show RAB11FIP3 Antibodies)) promotes the activity of Rab11a (show RAB11A Antibodies) and the ASAP1 (show ASAP1 Antibodies) in the Arf4 (show ARF4 Antibodies)-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
show that although the basic activation pathways of human and bovine rhodopsin are similar, structural deviations exist in the inactive conformation and during receptor activation, even between closely related rhodopsins
Rer1p regulates the ER retention of immature or misfolded rhodopsin and modulates its intracellular trafficking through the early secretory pathway.
crystal structure of a constitutively active form of human rhodopsin bound to a pre-activated form of the mouse visual arrestin (show SAG Antibodies), determined by serial femtosecond X-ray laser crystallography
The authors elucidated this dependency by showing that guanylate cyclase-1 is a novel rhodopsin-binding protein.
Eliminating Cngb1 (show CNGB1 Antibodies) and reducing RDS (show PRPH2 Antibodies) leads to additive defects in RDS (show PRPH2 Antibodies) expression levels and rod electroretinogram (ERG (show ERG Antibodies)) function, (e.g., Cngb1 (show CNGB1 Antibodies)-/-/rds (show PRPH2 Antibodies)+/- versus rds (show PRPH2 Antibodies)+/- or Cngb1 (show CNGB1 Antibodies)-/-) 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 Antibodies) 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 Antibodies) links CNGB1 (show CNGB1 Antibodies) to the light-detector rhodopsin in outer segments of rod photoreceptors.
p27(kip1 (show CDKN1B Antibodies)) 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)