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A statistically significant association with the risk of AD was observed with the CT genotype for rs784567 on the TARBP2 gene. on controlling for age and sex, we found that for the TARBP2-RNASEN (show DROSHA Proteins) association with AD the age variation was a risk factor for AD risk (P<0.001; OR=1.104; 95% CI, 1.059-1.151).
TRBP is a novel transcriptional coactivator of the Notch (show NOTCH1 Proteins) signaling pathway, playing an important role in neural stem cell regulation during mammalian brain development
TRBP is required for normal antiviral responses to Cardiovirus infection.
Experimental and computational techniques were employed to examine the hypothesis that TRBP-double-stranded RNA-binding domain (dsRBD) 2 binding by a 20-mer (show MERTK Proteins) dsRNA is coupled with RNA bending, results suggest that this particular dsRBD-dsRNA interaction produces little to no change in the A-form geometry of dsRNA in solution
We propose that the S6K2 (show RPS6KB2 Proteins)/TRBP node controls miRNA biogenesis in HDLECs and provides a molecular link between the mTOR (show FRAP1 Proteins) pathway and the miRNA biogenesis machinery.
TARBP2 silencing inhibits in vitro invasion and migration of NCIH1299 nonsmall cell lung cancer cell via the JNK (show MAPK8 Proteins)/STAT3 (show STAT3 Proteins)/AKT (show AKT1 Proteins) pathway. TARBP2 silencing does not significantly affect cell growth.
TARBP2 has roles in tumor development and progression [review]
SUMOylation of TARBP2 is required for regulating siRNA efficiency.
HIV-1 Rev-response element RNA acts as an RNA silencing suppressor by competing with TRBP-bound siRNAs.
the role of TRBP and unveils negative feedback regulation of PKR through TRBP phosphorylation.
TARBP2, but not PRKRA (show PRKRA Proteins), functions in miRNA biogenesis of a subclass of miRNAs, and suggesting that functional redundancy between TARBP2 and PRKRA (show PRKRA Proteins) does not involve miRNA biogenesis.
study demonstrated that Trbp participates in the regulation of muscle differentiation and regeneration
These data indicate that the association between PKR and TRBP integrates metabolism with translational control and inflammatory signaling and plays important roles in metabolic homeostasis and disease.
Trbp (Tarbp2), an RNA-binding protein, is required for normal heart function.
The mammalian Dicer-partner TRBP, a Loqs-PB homolog, tunes where Dicer cleaves pre-miR-132. [TRBP]
Results show the crystal structure of the interface between microRNA biogenesis proteins Dicer (show DICER1 Proteins) and TRBP. Mutations in this interface prevent recruitment of TRBP to Dicer (show DICER1 Proteins).
Tarbp2 binding to TRPC4 (show TRPC4 Proteins) promotes changes of cytosolic Ca(2 (show CA2 Proteins)+) and, thereby, leads to a dynamic regulation of Dicer (show DICER1 Proteins) activity, essentially at low endogenous Dicer (show DICER1 Proteins) concentrations.
TRBP controls PACT (show RBBP6 Proteins) activation of PKR (show EIF2AK2 Proteins), an activity that is reversed by stress.
Binding of Dicer to TRBP is critical for RNAi function.
HIV-1, the causative agent of acquired immunodeficiency syndrome (AIDS), contains an RNA genome that produces a chromosomally integrated DNA during the replicative cycle. Activation of HIV-1 gene expression by the transactivator Tat is dependent on an RNA regulatory element (TAR) located downstream of the transcription initiation site. The protein encoded by this gene binds between the bulge and the loop of the HIV-1 TAR RNA regulatory element and activates HIV-1 gene expression in synergy with the viral Tat protein. Alternative splicing results in multiple transcript variants encoding different isoforms. This gene also has a pseudogene.
TAR (HIV-1) RNA binding protein 2
, RISC-loading complex subunit tarbp2
, RISC-loading complex subunit TARBP2
, TAR (HIV) RNA binding protein 2
, TAR (HIV) RNA-binding protein 2
, TAR (HIV) RNA-binding protein TRBP1
, TAR RNA binding protein 2
, TAR RNA-binding protein 2
, trans-activation responsive RNA-binding protein
, trans-activation-responsive RNA-binding protein
, PRM-1 RNA-binding protein
, protamine-1 RNA-binding protein