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The protein encoded by EIF2AK3 phosphorylates the alpha subunit of eukaryotic translation-initiation factor 2 (EIF2), leading to its inactivation, and thus to a rapid reduction of translational initiation and repression of global protein synthesis. Additionally we are shipping PERK Antibodies (165) and PERK Kits (19) and many more products for this protein.
Showing 8 out of 10 products:
This study demonstrated that Perk Ablation Ameliorates Myelination in S63del-Charcot-Marie-Tooth 1B Neuropathy.
Data show that EIF2AK3/PERK-mediated downregulation of miR (show MLXIP Proteins)-424(322)-503 cluster regulates optimal activation of IRE1 (show ERN1 Proteins) protein and activating transcription factor 6 (ATF6 (show ATF6 Proteins)) during conditions of endoplasmic reticulum stress.
Inhibition of eIF2alpha phosphorylation via PERK suppression and reversal of de novo protein synthesis deficits can mitigate cognitive deficits in neurodegenerative diseases.
PlGF (show PGF Proteins) inhibition attenuates PERK activation, likely by tempering hypoxia in HCC (show FAM126A Proteins) via vessel normalisation. The UPR is able to regulate PlGF (show PGF Proteins) expression, suggesting the existence of a feedback mechanism for hypoxia-mediated UPR
this study demonstrates novel roles for the endoplasmic reticulum stress-response transducer PERK and a downstream effector of its activation, CHOP (show DDIT3 Proteins), in tubule cell production of fibronectin (show FN1 Proteins)
Nck1 silencing in pancreatic beta cells promotes PERK activation and signaling to protect beta cells against pathological stresses.
Nitric oxide can S-nitrosylate the endoplasmic reticulum stress sensors IRE1alapha and PERK.
Results show that PERK-eIF2alpha (show EIF2A Proteins)-mediated translational failure is a key process leading to neuronal loss in a mouse model of frontotemporal dementia, where the misfolded protein is a form of mutant tau
whole-body or pancreas-specific Perk ablation in mice leads to an increase in IFNAR1 (show IFNAR1 Proteins) protein levels and signaling in pancreatic tissues.
PGRN (show GRN Proteins) is a key regulator of insulin (show INS Proteins) resistance and PGRN (show GRN Proteins) may mediate its effects, at least in part, by inducing ER stress via the PERK-eIF2alpha (show EIF2A Proteins) dependent pathway
EnR (show LARGE Proteins) stress assessed by expression of PERK and p-eIF2alpha (show EIF2A Proteins) was significantly associated with tumor infiltrating lymphocytes in HER2 (show ERBB2 Proteins)-positive breast cancer.
Influenza A virus downregulates the host unfolded protein response mediated by the PERK protein.
Using drugs that specifically inhibit or activate the PERK or IRE1alpha sensors, we demonstrate that signalling through the PERK axis activates this expression, through a transcriptional mechanism
Data show CGK733 induced microtubule associated protein LC3B (show MAP1LC3B Proteins) formation upstream of AMP-activated protein kinase (show PRKAA2 Proteins) and protein kinase (show CDK7 Proteins) RNA-like endoplasmic reticulum kinase/CCAAT-enhancer-binding protein homologous protein (show DDIT3 Proteins) pathways and p21 Cip1 (show CDKN1A Proteins) expression.
Data from 2 consanguineous families suggest EIF2AK3 mutations (c.1337_1338insT/p.K346*; c.3009C>T/p.R903*) account for Wolcott-Rallison syndrome; ultrastructural features of autopsy materials suggest endoplasmic reticulum dysfunction. [CASE STUDIES]
CGK733-induced intracellular calcium sequestration in pancreatic tumor cells is correlated with the PERK/CHOP (show DDIT3 Proteins) signaling pathway and may also be involved in the dysregulations of calcium-binding proteins.
Data indicated that the relative timing of IRE1 and PERK signalling determines the shift from cell survival to apoptosis.
In human alveolar epithelial A549 cells, Lipopolysaccharide induces autophagic cell death that depends on the activation of the PERK branch of the unfolded protein response upon endoplasmic reticulum (ER) stress .
In this review, we particularly focused on the novel, intriguing and complicated role of PERK in ER stress-decided cell fate, and also discussed more roles of PERK in restoring cellular homeostasis
The protein encoded by this gene phosphorylates the alpha subunit of eukaryotic translation-initiation factor 2 (EIF2), leading to its inactivation, and thus to a rapid reduction of translational initiation and repression of global protein synthesis. It is a type I membrane protein located in the endoplasmic reticulum (ER), where it is induced by ER stress caused by malfolded proteins. Mutations in this gene are associated with Wolcott-Rallison syndrome.
eukaryotic translation initiation factor 2-alpha kinase 3
, eukaryotic translation initiation factor 2-alpha kinase 3-like
, PRKR-like endoplasmic reticulum kinase
, pancreatic eIF2-alpha kinase
, eukaryotic translation initiation factor 2 alpha kinase 3
, pancreatic EIF2-alpha kinase