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a novel, positive role for PKR activation and eIF2alpha phosphorylation in human globin mRNA splicing, is reported.
Clustered regularly interspaced short palindromic repeat (CRISPR)/Cas9-mediated ablation of double-stranded RNA (dsRNA)-activated protein kinase (show CDK7 Proteins) R (PKR (show PKLR Proteins)) restored p53 (show TP53 Proteins) responses while boosting hepatitis C virus replication, showing that p53 (show TP53 Proteins) inhibition results directly from viral activation of PKR (show PKLR Proteins).
Gene silencing studies showed that the suppression of immunoproteasome induction is essentially dependent on protein kinase (show CDK7 Proteins) R (PKR (show PKLR Proteins)). Indeed, the generation of a strictly immunoproteasome-dependent cytotoxic T lymphocyte epitope was impaired in in vitro processing experiments using isolated 20S proteasomes from HCV-infected cells and was restored by the silencing of PKR (show PKLR Proteins) expression.
data provide the first evidence that KSHV ORF57 plays a role in modulating PKR (show PKLR Proteins)/eIF2alpha (show EIF2A Proteins)/SG axis and enhances virus production during virus lytic infection.
The PKR (show PKLR Proteins) is a key constituent of the metaflammasome and interacts directly with several inflammatory kinases, such as inhibitor kappaB (IkappaB) kinase (show CHUK Proteins) (IKK (show CHUK Proteins)) and c-Jun N-terminal kinase (JNK), insulin receptor substrate 1 (IRS1 (show IRS1 Proteins)), and component of the translational machinery such as eIF2alpha (show EIF2A Proteins).
infection with New World arenaviruses JUNV and MACV, but not OW LASV, activated PKR (show PKLR Proteins), concomitant with elevated phosphorylation of the translation initiation factor (show TIF1 Proteins) alpha subunit (show POLG Proteins) of eukaryotic initiation factor (show EIF4G1 Proteins) 2
The stem-loop of noncoding RNA 886 is structural feature not only critical for inhibiting PKR (show PKLR Proteins) autophosphorylation, but also the phosphorylation of its cellular substrate, EIF-2alpha (show EIF2S1 Proteins).
Protein kinase (show CDK7 Proteins) R (PKR (show PKLR Proteins)) was required for induction of stress granules (SGs (show FBN1 Proteins)) by mumps virus (MuV) infection and regulated type III IFN (IFN-lambda1) mRNA stability.
data establish a model in which the Influenza A virus NS1 (show PTPN11 Proteins) N-terminal domain engages in a binding interaction to inhibit activation of PKR (show PKLR Proteins) and ensure efficient viral propagation and virulence
It was established in this report that interactions between PACT (show RBBP6 Proteins), ADAR1 (show ADAR Proteins) and HIV-1-encoded Tat (show TAT Proteins) protein diminish the activation of PKR (show PKLR Proteins) in response to HIV-1 infection.
PKR activation is an essential part of the molecular switch from adaptation to inflammation in response to hyperosmotic stress.
We therefore concluded that in osteoblasts, P. gingivalis activated PKR, which in turn increased NLRP3 (show NLRP3 Proteins) expression by activating NF-kappaB (show NFKB1 Proteins). Our results suggest that PKR modulates inflammation by regulating the expression of the NLRP3 (show NLRP3 Proteins) inflammasome through the NF-kappaB (show NFKB1 Proteins) pathway in periodontal diseases.
identify iNOS (show NOS2 Proteins)/NO as an integral component of IFN-beta (show IFNB1 Proteins) production in response to dsRNA in hepatocytes in a pathway that involves the coordinated activities of TLR3 (show TLR3 Proteins)/Trif (show RNF138 Proteins) and PKR
The data predicts that PKR diminishes inflammasome activity by controlling protein translation to repress the induction of factors that are critical for the activity of the cryopyrin (show NLRP3 Proteins) inflammasome.
This study provides insight into the molecular pathology of Cornelia de Lange syndrome by establishing a relationship between NIPBL (show NIPBL Proteins) and HDAC8 (show HDAC8 Proteins) mutations and PKR activation.
Deletion of PKR does not affect HFD-induced obesity, hepatic steatosis or glucose metabolism, and only modestly affects adipose tissue inflammation.
results show that ceramide acts at two distinct levels of the insulin (show INS Proteins) signaling pathway (IRS1 (show IRS1 Proteins) and Akt (show AKT1 Proteins)). PKR, which is induced by both inflammation signals and ceramide, could play a major role in the development of insulin (show INS Proteins) resistance in muscle cells.
Data (including data from studies in transgenic/knockout mice) suggest that PACT/RAX (protein activator of protein kinase (show CDK7 Proteins) R) functions as negative regulator of PKR/Eif2ak2 (protein kinase (show CDK7 Proteins) R) in development of postnatal anterior pituitary tissue.
Data indicate increasing expression of PKR during TNF-a (show TNF Proteins)-induced osteoclast formation. Its inhibition prevents TNF-a (show TNF Proteins)-induced bone destruction in vivo and can be then considered as new therapeutic target for bone disease.
The authors show that Murine cytomegalovirus m142 and m143 knockout mutants attain organ titers equivalent to those attained by wild-type virus in Pkr knockout mice.
The protein encoded by this gene is a serine/threonine protein kinase that is activated by autophosphorylation after binding to dsRNA. The activated form of the encoded protein can phosphorylate translation initiation factor EIF2S1, which in turn inhibits protein synthesis. This protein is also activated by manganese ions and heparin. Three transcript variants encoding two different isoforms have been found for this gene.
double-stranded RNA-activated protein kinase
, interferon-induced, double-stranded RNA-activated protein kinase
, p68 kinase
, P1/eIF-2A protein kinase
, interferon-inducible RNA-dependent protein kinase
, IFN-stimulated dsRNA-activated eIF2-alpha kinase 2
, double-stranded RNA activated protein kinase
, eukaryotic translation initiation factor 2-alpha kinase 2
, double stranded RNA activated protein kinase
, eIF-2A protein kinase 2
, interferon-inducible elF2alpha kinase
, protein kinase, interferon-inducible double stranded RNA dependent
, tyrosine-protein kinase EIF2AK2
, IFN- type I-induced and dsRNA-activated kinase
, IFN-induced and double-stranded RNA-activated kinase
, T-cell viral integration site
, dsRNA-activated kinase
, eIF-2 alpha
, eukaryotic translation initiation factor 2 alpha kinase 2
, protein kinase RNA-activated
, protein kinase, interferon inducible double stranded RNA dependent
, serine/threonine-protein kinase TIK
, Protein kinase, interferon-inducible double stranded RNA dependent