PRKRA Antibody, Biotin conjugated

1. Low PACT expression is associated with Arenaviral infections. PMID: 29669840
2. phenotype of our patients overlaps that of previouslyreported DYT16 patients PMID: 26990861
3. this study shows that PACT is an essential coactivator of the MDA5-dependent type I IFN response to viral RNA PMID: 28760879
4. High PRKRA mRNA expression is associated with colorectal cancer. PMID: 27859935
5. It was established in this report that interactions between PACT, ADAR1 and HIV-1-encoded Tat protein diminish the activation of PKR in response to HIV-1 infection. PMID: 28167698
6. 5 genomic variants in GSC, HOXA2 and PRKRA were identified through mutational analysis in Chinese patients with microtia. PMID: 28109504
7. MicroRNA-122 Inhibits the Production of Inflammatory Cytokines by Targeting the PKR Activator PACT in Human Hepatic Stellate Cells. PMID: 26636761
8. The interferon-induced protein kinase(PACT) partially rescued defects of interferon-beta1 and chemokine (C-C motif) ligand 5/RANTES (regulated on activation normal T cell expressed and secreted) induction in DDX3-knockdown HEK293 cells. PMID: 26454002
9. These findings support a model in which a measles virus defective interfering RNA is sensed by PACT and RIG-I to initiate an innate antiviral response via activation of interferon-beta production. PMID: 26608320
10. this study demonstrates for the first time that OV20.0 of Orf virus is also able to interact with the dsRNA binding domain of PACT and that the presence of dsRNA strengthened the interaction of these two molecules. PMID: 26355092
11. the affinity of PACT-PACT and PACT-PKR interactions is enhanced in dystonia patient lymphoblasts, thereby leading to intensified PKR activation and enhanced cellular death. PMID: 26231208
12. Altered PRKRA signalling and C / EBPbeta expression is associated with HLA-B27 expression in monocytic cells. PMID: 21988375
13. This stuidy provides the first independent replication of the DYT16 locus at 2q31.2 and strongly confirms the causal contribution of the PRKRA gene to DYT16. Our data suggest worldwide involvement of PRKRA in dystonia. PMID: 25142429
14. NS1 prevents PACT from interacting with an essential component of the virus. PMID: 24899174
15. PKR is activated in uninfected cells, specifically during mitosis, by binding to dsRNAs formed by inverted Alu repeats (IRAlus). PMID: 24939934
16. In contrast to its previously described activity, PACT contributes to PKR dephosphorylation during HIV-1 replication. PMID: 24020926
17. MERS-CoV 4a protein interacted with PACT in an RNA-dependent manner but not with RIG-I or MDA5. PMID: 24522921
18. Ebola virus VP35 inhibits PACT-induced RIG-I ATPase activity in a dose-dependent manner. PMID: 23870315
19. Herpes simplex virus 1 Us11 suppresses host interferon beta1 production through the inhibition of the PACT. PMID: 24067967
20. Protein kinase R modulates c-Fos and c-Jun signaling to promote proliferation of hepatocellular carcinoma with hepatitis C virus infection. PMID: 23844083
21. in vitro binding patterns of human TRBP and PACT to siRNA PMID: 23658827
22. The results show that PACT and TRBP have distinct effects on Dicer-mediated dsRNA processing. PMID: 23661684
23. RISC proteins PACT, TRBP, and Dicer, together with PKR, are steroid receptor RNA activator-binding nuclear receptor coregulators that are recruited to the promoters of hormone-regulated genes and regulate the expression of downstream target genes. PMID: 23550157
24. PACT may be associated with the plasma cell function and eosinophilic inflammation in CRSwNP. PMID: 22961479
25. DGCR8, AGO1, AGO2, PACT, and TARBP1 expression levels were significantly higher in the epithelial skin cancer groups than the healthy controls (P > 0.05). PMID: 22025453
26. The PACT-protein kinase PKR pathway represents a potential link between Abeta accumulation, PKR activation and tau phosphorylation. PMID: 21790829
27. Data demonstrate that PACT-PACT interaction is essential for efficient PKR activation. PMID: 22473766
28. NF-kappa-B is involved in the protein activator of PKR-RNA-dependent protein kinase interaction and the production of pro-inflammatory cytokines in periodontitis. PMID: 21882225
29. show that PACT physically binds to the C-terminal repression domain of RIG-I and potently stimulates RIG-I-induced type I interferon production PMID: 21501829
30. though mutation analysis demonstrated no mutation of PACT in the patients of microtia in the present study, suggest that PACT may play an essential role in mammalian ear development PMID: 21595004
31. results demonstrate for the first time that stress-induced PACT phosphorylation functions to free PACT from the inhibitory interaction with TRBP and also to enhance its interaction with PKR PMID: 21526770
32. The C-terminal, third conserved motif of the protein activator PACT plays an essential role in the activation of double-stranded-RNA-dependent protein kinase PMID: 11985496
33. Us11 protein of herpes simplex virus type 1 can block PKR activation by PACT both in vitro and in vivo PMID: 12368348
34. RAX, the cellular activator of PKR, has a novel role in synergistically stimulating SV40 large T antigen-dependent gene expression PMID: 12874289
35. The interaction with Dicer involves the third dsRNA-binding domain (dsRBD) of PACT and the N-terminal region of Dicer containing the helicase motif. Like TRBP, PACT is not required for the pre-microRNA (miRNA) cleavage reaction step. PMID: 16424907
36. RAX (PRKRA) may function as a negative regulator of growth that is required to activate PKR in response to a broad range of apoptosis-inducing stress. PMID: 16861340
37. The underlying biochemical mechanism of the activation of PKR via PACT phosphorylation at specific activation domain residues is reported as the major mode of transmission of cellular stress response to PKR. PMID: 16982605
38. Results show that PACT is expressed ubiquitously in different cell types at varying abundance, and Sp1 is the major transcription factor responsible for PACT promoter activity. PMID: 17125937
39. Results indicate that human TRBP and PACT directly interact with each other and associate with Dicer to stimulate the cleavage of double-stranded or short hairpin RNA to siRNA. PMID: 17452327
40. DYT16, a novel young-onset dystonia-parkinsonism disorder, identification of a segregating mutation in the stress-response protein PRKRA. PMID: 18243799
41. A heterozygous frameshift mutation in PRKRA (DYT16) associated with generalised dystonia in a German patient. PMID: 18420150
42. TRBP controls PACT activation of PKR, an activity that is reversed by stress. PMID: 18936160
43. writer's cramp as presenting symptom is not associated with mutations in DYT11, DYT16, but it can be the sole manifestation of DYT1 GAG deletion mutation carriers. PMID: 19441135
44. Strong protein kinase R (PKR) binding is needed for PACT-mediated PKR activation and phosphorylation in vivo. PMID: 19580324
45. RAX phosphorylation is required for PKR activation, full protein synthesis inhibition, and rapid apoptosis following stress. PMID: 15299031

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HGNC: 9438

OMIM: 603424

KEGG: hsa:8575

STRING: 9606.ENSP00000318176

UniGene: Hs.570274