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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.
the impaired working memory in forebrain-specific Perk knockout mice may stem from altered Gq protein-coupled intracellular Ca(2 (show CA2 Proteins)+) dynamics in cortical pyramidal neurons.
Overall, these data demonstrate that hypoxia can suppress adiponectin expression and activate the PERK and IRE1 signaling pathways in differentiated adipocytes, and this two pathways are involved in the suppression of adiponectin expression induced by hypoxia.
Free CNPY2 (show CNPY2 Proteins) then engages protein kinase (show CDK7 Proteins) R-like endoplasmic reticulum kinase (PERK) to induce expression of the transcription factor C/EBP homologous protein (CHOP (show DDIT3 Proteins)), thereby initiating the unfolded protein response.
Therefore, our study suggests that CREB and PSD95 are novel substrates of PERK, so inhibition of PERK phosphorylation using GSK2656157 would be beneficial against memory impairment after TBI.
regulates both Ca2 (show CA2 Proteins)+ -dependent working memory and protein synthesis-dependent memory flexibility
SLC30A10 (show SLC30A10 Proteins) has a protective role in 1-methyl-4-phenylpyridinium-induced toxicity via PERK-ATF4 (show ATF4 Proteins) pathway.
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.
To illustrate the mechanism by which the PERK luminal domain interacts with misfolded proteins, the crystal structure of the human PERK luminal domain was determined to 3.2 A resolution. Two dimers of the PERK luminal domain constitute a tetramer in the asymmetric unit.
These results indicated that dual targeting of PI3K and PERK pathways might improve clinical prognosis and enhance the treatment of ESCC patients.
The role of neutrophil elastase (show ELANE Proteins) in the activation of unfolded protein response effector molecules via PERK and CHOP (show DDIT3 Proteins) is reported.
High PERK expression is associated with gastrointestinal neuroendocrine tumors.
The PERK-eIF2alpha (show EIF2A Proteins)-ATF4 (show ATF4 Proteins)-CHOP (show DDIT3 Proteins) signaling pathway has a critical role in tumor progression during endoplasmic reticulum stress. (Review)
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