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PERK regulates oligodendrocyte survival during differentiation.
Data suggest the activation of PERK is part of a protective response to mutant rhodopsin (show RHO Proteins) that ultimately limits photoreceptor cell death.
Atg7 (show ATG7 Proteins) ablation mainly induced the PERK-ATF4 (show ATF4 Proteins)-CHOP (show DDIT3 Proteins) axis of the endoplasmic reticulum (ER) stress response in growth plate chondrocytes.
heme-regulated inhibitor (HRI (show EIF2AK1 Proteins)), protein kinase (show CDK7 Proteins) R (PKR (show EIF2AK2 Proteins)), PKR (show EIF2AK2 Proteins)-like endoplasmic reticulum kinase, (PERK) and general control non-depressible 2 (GCN2 (show EIF2AK4 Proteins)) are sufficient for the integrated stress response; there are no additional eIF2alpha (show EIF2A Proteins) kinases in vertebrates
these findings reveal a new crucial combined effect of the silencing of PERK and ATF4 (show ATF4 Proteins) in modulating ER stressmediated apoptosis during chondrocyte differentiation and proliferation.
Activation of the ER stress execution proteins, PERK and CHOP10 (show DDIT3 Proteins), was evaluated to determine whether this process was involved in 15d-PMJ2 cell death. 15d-PMJ2 increased the phosphorylation of PERK and expression of CHOP10 (show DDIT3 Proteins) in tumorigenic but not nontumorigenic cells
In response to endoplasmic reticulum stress, activation of PERK coordinates the integrated stress response by phosphorylating eIF2alpha (show EIF2A Proteins), which is then quickly dephosphorylated by the GADD34 (show PPP1R15A Proteins) complex. Data imply dual role of the ISR in promoting and inhibiting medulloblastoma tumorigenesis.
These findings identify DLK as a central regulator of not only JNK but also PERK stress signaling in neurons, with both pathways contributing to neurodegeneration.
PERK has a role in mediating the internal ribosome entry site-dependent translational activation of mRNAs encoding angiogenic growth factors after ischemic stress
NDRG2 is a novel ERS-responsive protein and acts as PERK co-factor to facilitate PERK branch, thereby contributing to ERS-induced apoptosis.
In this paper, we evaluate the clinical features of the patients having W522X mutation and we compare this group with other patients reported to date. Except the characteristic features as diabetes mellitus and epiphyseal dysplasia, all the WRS (show KCNQ1 Proteins) patients, including patients with W522X mutation, show extensive phenotypic variability that correlates poorly to genotype.
PERK is a master-regulator dictating pancreatic beta cell homoeostasis in development and in diabetes. (Review)
Three branches of the Unfolded Protein Response (UPR) have been described, including the activation of the inositol-requiring enzyme 1 (IRE1 (show ERN1 Proteins)), the pancreatic ER kinase (PKR (show PKLR Proteins))-like ER kinase (PERK), and the activating transcription factor 6 (ATF6 (show ATF6 Proteins)).
Our work demonstrates for the first time that the adaptation to endoplasmic reticulum(ER) stress in cancer cells produces a MDR phenotype. The PERK/Nrf2 (show GABPA Proteins)/MRP1 (show MDM4 Proteins) axis is responsible for the resistance to ER stress and chemotherapy, and may represent a good therapeutic target in aggressive and resistant tumors.
miR-204 Targets PERK and Regulates UPR Signaling and beta-Cell Apoptosis
novel findings suggest that HMGB1 (show HMGB1 Proteins) triggered EPC (show TCF21 Proteins) apoptosis in a manner of RAGE (show AGER Proteins)-mediated activation of the PERK/eIF2alpha (show EIF2A Proteins) pathway.
The present study is the first to uncover a key prosurvival modulator, Yip1A, which coordinates IRE1 signaling with PERK signaling to support the survival of HeLa and CaSki cervical cancer cells.
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