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Human Monoclonal PRKRA Primary Antibody for IHC (p), IP - ABIN563706
Surova, Akbar, Zhivotovsky: Knock-down of core proteins regulating microRNA biogenesis has no effect on sensitivity of lung cancer cells to ionizing radiation. in PLoS ONE 2012
Cow (Bovine) Polyclonal PRKRA Primary Antibody for IHC, WB - ABIN2778859
Lee, Hur, Park, Kim, Suh, Kim: The role of PACT in the RNA silencing pathway. in The EMBO journal 2006
Show all 2 Pubmed References
TARBP2, but not PRKRA, functions in miRNA biogenesis of a subclass of miRNAs, and suggesting that functional redundancy between TARBP2 and PRKRA does not involve miRNA biogenesis.
PKR knock-out alleviates abnormal brain signaling and body weight gain in experimental obesity.
PACT interacts with LGP2 and this interaction is enhanced by encephalomyocarditis virus (EMCV) infection. In vitro interaction analyses using purified recombinant proteins confirmed that the single-stranded Theiler's murine encephalitis virus genome enhanced the interaction between LGP2 and PACT.
Data (including data from studies in transgenic/knockout mice) suggest that PACT/RAX (protein activator of protein kinase R) functions as negative regulator of PKR/Eif2ak2 (protein kinase R) in development of postnatal anterior pituitary tissue.
Deficiency of PKR diminished peripheral inflammatory responses following E. coli
These findings demonstrated a novel function of PACT/RAX in the regulation of neuronal migration.
The protein kinase PKR is critical for LPS-induced iNOS production but is dispensable for inflammasome activation in macrophages.
These observations identified a specific mutation that reduces steady-state levels of RAX protein and disrupts the dsRNA binding function of the protein, demonstrating the importance of the Prkra gene in various aspects of mouse development.
RAX phosphorylation at serine 18 is required for PKR activation and consequent translation inhibition
Study demonstrated an essential role of PACT in mammalian ear development and produced the first animal model.
The role of PACT in mediating gene induction, PKR activation, and apoptosis in response to diverse stimuli
TRBP controls PACT activation of PKR, an activity that is reversed by stress.
The authors demonstrate for the first time that PACT is phosphorylated in response to tunicamycin and is responsible for PKR activation by direct interaction.
Study revealed a physiologically significant role for PACT in cell proliferation and an essential role of a dsRNA-binding protein in mammalian pituitary expansion.
The antiviral activity of PACT is mediated primarily via its interaction with and inhibition of IAV polymerase.
Low PACT expression is associated with Arenaviral infections.
phenotype of our patients overlaps that of previouslyreported DYT16 patients
this study shows that PACT is an essential coactivator of the MDA5-dependent type I IFN response to viral RNA
High PRKRA mRNA expression is associated with colorectal cancer.
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.
5 genomic variants in GSC, HOXA2 and PRKRA were identified through mutational analysis in Chinese patients with microtia.
MicroRNA-122 Inhibits the Production of Inflammatory Cytokines by Targeting the PKR Activator PACT in Human Hepatic Stellate Cells.
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.
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.
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.
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.
Altered PRKRA signalling and C / EBPbeta expression is associated with HLA-B27 expression in monocytic cells.
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.
NS1 prevents PACT from interacting with an essential component of the virus.
PKR is activated in uninfected cells, specifically during mitosis, by binding to dsRNAs formed by inverted Alu repeats (IRAlus).
In contrast to its previously described activity, PACT contributes to PKR dephosphorylation during HIV-1 replication.
MERS-CoV 4a protein interacted with PACT in an RNA-dependent manner but not with RIG-I or MDA5.
Ebola virus VP35 inhibits PACT-induced RIG-I ATPase activity in a dose-dependent manner.
Herpes simplex virus 1 Us11 suppresses host interferon beta1 production through the inhibition of the PACT.
Tumour necrosis factor alpha up-regulates protein kinase R (PKR)-activating protein (PACT, PRKRA) and increases phosphorylation of PKR and eukaryotic initiation factor 2-alpha in articular chondrocytes.
This gene encodes a protein kinase activated by double-stranded RNA which mediates the effects of interferon in response to viral infection. Mutations in this gene have been associated with dystonia. Alternative splicing results in multiple transcript variants.
protein kinase, interferon-inducible double stranded RNA dependent activator
, interferon-inducible double stranded RNA-dependent protein kinase activator A-like
, PKR-associated protein X
, PKR-associating protein X
, interferon-inducible double stranded RNA-dependent protein kinase activator A
, protein activator of the interferon-induced protein kinase
, protein kinase, interferon-inducible double stranded RNA-dependent activator
, interferon-inducible double stranded RNA-dependent protein kinase activator A homolog
, double-stranded RNA-binding protein A
, interferon-inducible double stranded RNA-dependent protein kinase activator A homolog A
, interferon-inducible double stranded RNA-dependent protein kinase activator A homolog B