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The protein encoded by DBR1 is an RNA lariat debranching enzyme that hydrolyzes 2'-5' prime branched phosphodiester bonds. Additionally we are shipping DBR1 Proteins (13) and many more products for this protein.
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saturation mutagenesis of DBR1 and Gal4 (show LGALS4 Antibodies) and show that the experimental phenotypes for over 80% of the mutations correlate well with predicted effects of mutations on protein stability and RNA binding affinity.
Results of protein-protein interaction between human Dbr1 and factors found in the Intron Large complex identify Xab2 (show XAB2 Antibodies) and a novel protein CWF19L1 as specific interactors of DBR1.
Inhibition of DBR1 caused a significant reduction in the formation of intermediate and full-length HIV-1 cDNA.
Dbr1 protein cleaves the 2'-5' phosphodiester bond of intron lariats, necessary for subsequent intron degradation that follows pre-mRNA splicing.
Lariat RNAs localized in nuclear bodies, and partially co-localize with HYL1 (show EPHX1 Antibodies), and both DCL1 (show CD302 Antibodies) and HYL1 (show EPHX1 Antibodies) were mis (show AMH Antibodies)-localized in dbr1-2... we thus propose that lariat RNAs, as decoys, inhibit miRNA processing, suggesting a hitherto unknown layer of regulation in miRNA biogenesis.
The protein encoded by this gene is an RNA lariat debranching enzyme that hydrolyzes 2'-5' prime branched phosphodiester bonds. The encoded protein specifically targets the bonds at the branch point of excised lariat intron RNA, converting them to linear molecules that are then degraded. This protein may also be involved in retroviral replication.
lariat debranching enzyme
, debranching enzyme homolog 1 (S. cerevisiae)
, lariat debranching enzyme-like
, RNA lariat debranching enzyme
, debranching enzyme homolog 1