Gene Ontology annotation through association of InterPro records with GO terms
Discovery of 1H-pyrazol-3(2H)-ones as potent and selective inhibitors of protein kinase R-like endoplasmic reticulum kinase (PERK).
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Structure-based design of ATP-competitive 1H-pyrazol-3(2H)-one inhibitors bound in the PERK kinase domain ATP pocket (PDB 4X7H, 4X7J, 4X7K, 4X7L, 4X7N, 4X7O) yielded a potent, selective PERK tool compound. The cached record is abstract-only and does not state the ATP-pocket/kinase-domain detail verbatim, so no exact-substring supporting quote is attached.
Characterization of a mutant pancreatic eIF-2alpha kinase, PEK, and co-localization with somatostatin in islet delta cells.
Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational control.
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Combined Automated Annotation using Multiple IEA Methods
Annotation inferences using phylogenetic trees
Pancreatic eukaryotic initiation factor-2alpha kinase (PEK) homologues in humans, Drosophila melanogaster and Caenorhabditis elegans that mediate translational control in response to endoplasmic reticulum stress.
Dimerization and release of molecular chaperone inhibition facilitate activation of eukaryotic initiation factor-2 kinase in response to endoplasmic reticulum stress.
Loss of kinase activity in a patient with Wolcott-Rallison syndrome caused by a novel mutation in the EIF2AK3 gene.
p58IPK is an inhibitor of the eIF2α kinase GCN2 and its localization and expression underpin protein synthesis and ER processing capacity.
Crystal structures reveal transient PERK luminal domain tetramerization in endoplasmic reticulum stress signaling.
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Transient tetramerization of the PERK luminal domain promotes PERK and eIF2alpha phosphorylation during UPR activation.
"Additionally, PERK mutants reduce tetramer formation in vitro and reduce PERK and eIf2a phosphorylation in cells."
ER and Nutrient Stress Promote Assembly of Respiratory Chain Supercomplexes through the PERK-eIF2α Axis.
PERK-ATAD3A interaction provides a subcellular safe haven for protein synthesis during ER stress.
Automatic Gene Ontology annotation based on Rhea mapping
Gene Ontology annotation based on Enzyme Commission mapping
TBL2 is a novel PERK-binding protein that modulates stress-signaling and cell survival during endoplasmic reticulum stress.
TMEM33: a new stress-inducible endoplasmic reticulum transmembrane protein and modulator of the unfolded protein response signaling.
Compounds Triggering ER Stress Exert Anti-Melanoma Effects and Overcome BRAF Inhibitor Resistance.
PARP16 is a tail-anchored endoplasmic reticulum protein required for the PERK- and IRE1α-mediated unfolded protein response.
H2S-Induced sulfhydration of the phosphatase PTP1B and its role in the endoplasmic reticulum stress response.
The ER stress sensor PERK luminal domain functions as a molecular chaperone to interact with misfolded proteins.
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
The unfolded protein response induces the angiogenic switch in human tumor cells through the PERK/ATF4 pathway.
Electronic Gene Ontology annotations created by ARBA machine learning models
Essential role of the unfolded protein response regulator GRP78/BiP in protection from neuronal apoptosis.
Role of SERCA1 truncated isoform in the proapoptotic calcium transfer from ER to mitochondria during ER stress.
The endoplasmic reticulum stress response in aging and age-related diseases.
Ursolic acid induces ER stress response to activate ASK1-JNK signaling and induce apoptosis in human bladder cancer T24 cells.
Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase.
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PERK is an ER-resident eIF2alpha kinase activated by ER stress to attenuate translation.
"ER stress increases PERK's protein-kinase activity and PERK phosphorylates eIF2alpha on serine residue 51, inhibiting translation of messenger RNA into protein."
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
The unfolded protein response: integrating stress signals through the stress sensor IRE1α.
Dissociation of PERK:BiP Heterodimer
EIF2AK3 (PERK) phosphorylates EIF2S1 (eIF2-alpha)Phosphorylation of eIF2-alpha by PERK
ALK mutants bind type I TKIs
Defining the membrane proteome of NK cells.
Coordination between Two Branches of the Unfolded Protein Response Determines Apoptotic Cell Fate.
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PERK attenuates the IRE1 branch of the UPR through RPAP2-dependent regulation.
"Here, we report that PERK governs IRE1's attenuation through a phosphatase known as RPAP2 (RNA polymerase II-associated protein 2)."
Curator notes for EIF2AK3 literature and PN review
Falcon deep research report for EIF2AK3
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Falcon research supports EIF2AK3/PERK as an ER-membrane stress sensor kinase that phosphorylates EIF2S1/eIF2alpha at Ser51 to attenuate translation and activate the PERK arm of the UPR/ISR.
"PERK's primary enzymatic function is to phosphorylate eukaryotic translation initiation factor 2 subunit alpha (eIF2alpha; gene EIF2S1) at Ser51."
Modulation of the eukaryotic initiation factor 2 alpha-subunit kinase PERK by tyrosine phosphorylation.
OpenScientist focused report on EIF2AK3/PERK nuclear localization
UniProt entry for EIF2AK3