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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
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Human Polyclonal RHO Primary Antibody for IHC, WB - ABIN350722
Carninci, Kasukawa, Katayama, Gough, Frith, Maeda, Oyama, Ravasi, Lenhard, Wells, Kodzius, Shimokawa, Bajic, Brenner, Batalov, Forrest, Zavolan, Davis, Wilming, Aidinis, Allen, Ambesi-Impiombato et al.: The transcriptional landscape of the mammalian genome. ... in Science (New York, N.Y.) 2005
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Human Polyclonal RHO Primary Antibody for IHC, WB - ABIN350720
Munemitsu, Innis, Clark, McCormick, Ullrich, Polakis: Molecular cloning and expression of a G25K cDNA, the human homolog of the yeast cell cycle gene CDC42. in Molecular and cellular biology 1990
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Data suggest that retinitis pigmentosa-associated mutation G51A behaves differently in human rhodopsin compared to bovine rhodopsin; human rhodopsin is more thermally stable than ancestral ancestrally reconstructed mammalian rhodopsin.
The metformin-rescued P23H rhodopsin was still intrinsically unstable and led to increased structural instability of the rod outer segments. These data suggest that improving the traffic of misfolding rhodopsin mutants is unlikely to be a practical therapy, but also highlights the potential of altering translation through AMPK (show PRKAA1 Antibodies) to improve protein function in other protein misfolding diseases
Study reports an X-ray free electron laser crystal structure of the rhodopsin-arrestin (show SAG Antibodies) complex, in which the phosphorylated C terminus of rhodopsin forms an extended intermolecular beta sheet with the N-terminal beta strands of arrestin (show SAG Antibodies). Phosphorylation was detected at rhodopsin C-terminal tail residues T336 and S338.
results suggest that nonsense-mediated mRNA decay modulates the severity of retinitis pigmentosa in patients with nonsense mutations in the rhodopsin gene
both the charged G90D(2.57) and the hydrophobic T94I(2.61) mutation alter the dark state by weakening the interaction between the Schiff base (SB) and its counterion E113(3.28) We propose that this interference with the tight regulation of the dim light photoreceptor rhodopsin increases background noise in the visual system and causes the loss of night vision characteristic for CSNB (show CSN2 Antibodies) patients.
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 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
Rab8a (show RAB8A Antibodies) and Rab11a (show RAB11A Antibodies) Are Dispensable for Rhodopsin Transport in Mouse Photoreceptors
This study demonstrated that Rhodopsin Phosphorylation on Dark Adaptation in Mouse Rods.
Findings indicate that Rho and ROCK knockout may improve the behavior of mice and prevent MPTP (show PTPN2 Antibodies)-induced dopaminergic neurons damage by regulating Sema3A (show SEMA3A Antibodies), PlexinA and NRP-1 (show NRP1 Antibodies) in a mouse model of Parkinson's disease.
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.
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)