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Pre-mRNA splicing occurs in 2 sequential transesterification steps. Additionally we are shipping and many more products for this protein.
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Within early haematopoiesis, myeloid differentiation is impaired, suggesting Prpf8 is required for haematopoietic development.
We show that PRP31 (show PRPF31 Antibodies), a component of U4 snRNP (show LSM2 Antibodies), is modified with K63-linked ubiquitin chains by the PRP19 (show PRPF19 Antibodies) complex and deubiquitinated by USP15 (show USP15 Antibodies) and its substrate targeting factor SART3 (show SART3 Antibodies). USP15SART3 makes a complex with USP4 (show USP4 Antibodies) and this ternary complex serves as a platform to deubiquitinate PRP31 (show PRPF31 Antibodies) and PRP3 (show CLCA4 Antibodies)
HSP90 (show HSP90 Antibodies)/R2TP chaperone system promotes the assembly of a key module of U5 snRNP (show LSM2 Antibodies) while assuring the quality control of PRPF8. The proteomics data further reveal new interactions between R2TP and the tuberous sclerosis complex, pointing to a potential link between growth signals and the assembly of key cellular machines.
influenza A virus upregulates cellular PRPF8 gene expression through viral NS1 protein and influenza virus polymerase basic protein 1 to increase virus production.
Our findings exemplify the regulatory potential of changes in the core spliceosome machinery, which may be relevant to slow-onset human genetic diseases linked to PRPF8 deficiency
Most importantly between Prp8 and nucleotides at the exon-intron junction.
A mutation in a splicing factor (show SLU7 Antibodies) PRPF8 that causes retinitis pigmentosa has a transcriptome-wide effect on mRNA splicing.
Data suggest Enterovirus 3DPol (RNA-dependent RNA polymerase) enters nucleus via nuclear localization signal, targets pre-mRNA processing factor 8 (Prp8) to block pre-mRNA splicing/mRNA synthesis, and shuts off cellular transcription/translation.
In the cytoplasm, Prp8 forms a precursor complex with U5 snRNA
these data show how a Ski2 (show SKIV2L Antibodies)-like RNA helicase (show DDX46 Antibodies) Brr2 (show SNRNP200 Antibodies) can be reversibly inhibited by a protein cofactor Prp8 that directly competes with RNA substrate binding.
This is the first report of marked intrafamilial variability associated with mutations in the PRPF8 gene, including incomplete penetrance. PRPF8 mutations should be suspected in patients with autosomal dominant retinitis pigmentosa.
The mouse retinal pigment epithelium (RPE (show RPE Antibodies))is the primary cell affected by mutations in the RNA splicing factors (PRPF3 (show PRPF3 Antibodies), PRPF8, and PRPF31 (show PRPF31 Antibodies)), and these changes occur at an early age.
found that PRP31 (show PRPF31 Antibodies) and PRPC8 as well as snRNAs are highly expressed in retinal cells
The finding of similar degenerative changes in RPE (show RPE Antibodies) cells of all three mouse models suggests that the retinal pigment epithelium may be the primary cell type affected in the RNA splicing factor (show SLU7 Antibodies) forms of retinitis pigmentosa.
Pre-mRNA splicing occurs in 2 sequential transesterification steps. The protein encoded by this gene is a component of both U2- and U12-dependent spliceosomes, and found to be essential for the catalytic step II in pre-mRNA splicing process. It contains several WD repeats, which function in protein-protein interactions. This protein has a sequence similarity to yeast Prp8 protein. This gene is a candidate gene for autosomal dominant retinitis pigmentosa.
PRP8 pre-mRNA processing factor 8 homolog
, pre-mRNA-processing-splicing factor 8
, 220 kDa U5 snRNP-specific protein
, PRP8 homolog
, U5 snRNP-specific protein (220 kD), ortholog of S. cerevisiae Prp8p
, apoptosis-regulated protein 1
, apoptosis-regulated protein 2
, precursor mRNA processing protein
, splicing factor Prp8