The structure of the PERK kinase domain suggests the mechanism for its activation
about
Protein kinase R-like ER kinase and its role in endoplasmic reticulum stress-decided cell fateDangER: protein ovERload. Targeting protein degradation to treat myelomaConserved and plant-unique strategies for overcoming endoplasmic reticulum stressThe Role of the PERK/eIF2α/ATF4/CHOP Signaling Pathway in Tumor Progression During Endoplasmic Reticulum StressIdentification and validation of novel PERK inhibitors.The eIF2 kinase PERK and the integrated stress response facilitate activation of ATF6 during endoplasmic reticulum stress.Unfolded Protein Response and PERK Kinase as a New Therapeutic Target in the Pathogenesis of Alzheimer's DiseaseEnzymatic Characterization of ER Stress-Dependent Kinase, PERK, and Development of a High-Throughput Assay for Identification of PERK Inhibitors.Endoplasmic Reticulum Stress-Related Genes in Yellow Catfish Pelteobagrus fulvidraco: Molecular Characterization, Tissue Expression, and Expression Responses to Dietary Copper Deficiency and ExcessATF6 signaling is required for efficient West Nile virus replication by promoting cell survival and inhibition of innate immune responses.Membrane lipid saturation activates endoplasmic reticulum unfolded protein response transducers through their transmembrane domainsActivation of protein kinase PKR requires dimerization-induced cis-phosphorylation within the activation loop.Endoplasmic reticulum and the unfolded protein response: dynamics and metabolic integrationEndoplasmic reticulum stress response in yeast and humans.Endoplasmic reticulum stress as a novel neuronal mediator in Alzheimer's disease.The unfolded protein response in glioblastomas: targetable or trouble?The role of endoplasmic reticulum stress in neurodegenerative disease.The ER stress sensor PERK luminal domain functions as a molecular chaperone to interact with misfolded proteins.Endoplasmic Reticulum (ER) Stress and Endocrine Disorders.Fine-tuning PERK signaling for neuroprotection.Molecular dynamics reveal a novel kinase-substrate interface that regulates protein translation.Regulation of PKR by RNA: formation of active and inactive dimers.Residues required for phosphorylation of translation initiation factor eIF2α under diverse stress conditions are divergent between yeast and human.Mechanistic basis of Nek7 activation through Nek9 binding and induced dimerization.The luminal domain of the ER stress sensor protein PERK binds misfolded proteins and thereby triggers PERK oligomerization.Protective effect of 3-hydroxybutyrate against endoplasmic reticulum stress-associated vascular endothelial cell damage induced by low glucose exposure.Flaviviral regulation of the unfolded protein response: can stress be beneficial?Salidroside mitigates hypoxia/reoxygenation injury by alleviating endoplasmic reticulum stress‑induced apoptosis in H9c2 cardiomyocytesEndoplasmic reticulum (ER) stress response in Coronavirus infection
P2860
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P2860
The structure of the PERK kinase domain suggests the mechanism for its activation
description
2011 nî lūn-bûn
@nan
2011 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
The structure of the PERK kinase domain suggests the mechanism for its activation
@ast
The structure of the PERK kinase domain suggests the mechanism for its activation
@en
The structure of the PERK kinase domain suggests the mechanism for its activation
@nl
type
label
The structure of the PERK kinase domain suggests the mechanism for its activation
@ast
The structure of the PERK kinase domain suggests the mechanism for its activation
@en
The structure of the PERK kinase domain suggests the mechanism for its activation
@nl
prefLabel
The structure of the PERK kinase domain suggests the mechanism for its activation
@ast
The structure of the PERK kinase domain suggests the mechanism for its activation
@en
The structure of the PERK kinase domain suggests the mechanism for its activation
@nl
P2093
P2860
P1476
The structure of the PERK kinase domain suggests the mechanism for its activation
@en
P2093
Bingdong Sha
Jingzhi Li
Wenjun Cui
P2860
P356
10.1107/S0907444911006445
P50
P577
2011-05-01T00:00:00Z