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PKR is an interferon-inducible serine/threonine specific protein kinase. It is widely expressed in eukaryotic organisms and activated by double stranded RNA. Activation of PKR by dsRNAs leads to autophosphorylation at multiple sites. Phosphorylation of Thr446 and Thr451 in the PKR activation loop is required in vivo and in vitro for high level kinase activity. PKR phosphorylates its natural substrate, the alpha subunit of eukaryotic protein synthesis initiation factor 2 (EIF2 alpha), leading
Protein Kinase c alpha (PKC alpha) is an 77 kDa member of the conventional group (cPKCs: sensitive to calcium, diacylglycerol, phosphatidylserine and phorbol esters) of the PKC family of serine/ threonine kinases that are involved in a wide range of physiological processes including mitogenesis, cell survival and transcriptional regulation. PKC alpha is an ubiquitously expressed PKC isozyme that has been implicated in the regulation of a broad range of cellular functions including proliferati
This gene encodes a tumor suppressor protein containing transcriptional activation, DNA binding, and oligomerization domains. The encoded protein responds to diverse cellular stresses to regulate expression of target genes, thereby inducing cell cycle arrest, apoptosis, senescence, DNA repair, or changes in metabolism. Mutations in this gene are associated with a variety of human cancers, including hereditary cancers such as Li-Fraumeni syndrome. Alternative splicing of this gene and the use
This gene encodes a tumor suppressor protein containing transcriptional activation, DNA binding, and oligomerization domains. The encoded protein responds to diverse cellular stresses to regulate expression of target genes, thereby inducing cell cycle arrest, apoptosis, senescence, DNA repair, or changes in metabolism. Mutations in this gene are associated with a variety of human cancers, including hereditary cancers such as Li-Fraumeni syndrome. Alternative splicing of this gene and the use
This gene encodes a tumor suppressor protein containing transcriptional activation, DNA binding, and oligomerization domains. The encoded protein responds to diverse cellular stresses to regulate expression of target genes, thereby inducing cell cycle arrest, apoptosis, senescence, DNA repair, or changes in metabolism. Mutations in this gene are associated with a variety of human cancers, including hereditary cancers such as Li-Fraumeni syndrome. Alternative splicing of this gene and the use
NF-kappa-B is a ubiquitous transcription factor involved in several biological processes. It is held in the cytoplasm in an inactive state by specific inhibitors. Upon degradation of the inhibitor, NF-kappa-B moves to the nucleus and activates transcription of specific genes. NF-kappa-B is composed of NFKB1 or NFKB2 bound to either REL, RELA, or RELB. The most abundant form of NF-kappa-B is NFKB1 complexed with the product of this gene, RELA. Four transcript variants encoding different isoform