Reversible phosphorylation of eukaryotic initiation factor 2 alpha in response to endoplasmic reticular signaling.
about
Growth arrest and DNA damage-inducible protein GADD34 targets protein phosphatase 1 alpha to the endoplasmic reticulum and promotes dephosphorylation of the alpha subunit of eukaryotic translation initiation factor 2Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinaseFeedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alphaTranslation of 5' leaders is pervasive in genes resistant to eIF2 repressionLimited effects of an eIF2αS51A allele on neurological impairments in the 5xFAD mouse model of Alzheimer's disease.17alpha-Hydroxylase/17,20 lyase inhibitor VN/124-1 inhibits growth of androgen-independent prostate cancer cells via induction of the endoplasmic reticulum stress response.The unfolded protein response triggers selective mRNA release from the endoplasmic reticulum.Cellular stress response pathways and ageing: intricate molecular relationshipsThe small molecule C-6 is selectively cytotoxic against breast cancer cells and its biological action is characterized by mitochondrial defects and endoplasmic reticulum stressVaricella-Zoster virus IE63, a major viral latency protein, is required to inhibit the alpha interferon-induced antiviral responseAttenuating the endoplasmic reticulum stress response improves functional recovery after spinal cord injury.Vapb/Amyotrophic lateral sclerosis 8 knock-in mice display slowly progressive motor behavior defects accompanying ER stress and autophagic response.Translation regulation by eukaryotic initiation factor-2 kinases in the development of latent cysts in Toxoplasma gondii.Using natural variation in Drosophila to discover previously unknown endoplasmic reticulum stress genes.Endoplasmic reticulum stress induces PRNP prion protein gene expression in breast cancer.Translational repression mediates activation of nuclear factor kappa B by phosphorylated translation initiation factor 2Regulatory crosstalk within the mammalian unfolded protein response.Crosstalk Between Endoplasmic Reticulum Stress, Oxidative Stress, and Autophagy: Potential Therapeutic Targets for Acute CNS Injuries.Herp coordinates compartmentalization and recruitment of HRD1 and misfolded proteins for ERAD.Molecular mechanisms of mTOR regulation by stressInhibition of palmitate-induced GADD34 expression augments apoptosis in mouse insulinoma cells (MIN6).Stress-induced gene expression requires programmed recovery from translational repression.Effects of a Sublethal and Transient Stress of the Endoplasmic Reticulum on the Mitochondrial Population.Ubiquitination-mediated regulation of biosynthesis of the adhesion receptor SHPS-1 in response to endoplasmic reticulum stress.Analysis of the endoplasmic reticular Ca2+ requirement for alpha1-antitrypsin processing and transport competence.Borrelidin Induces the Unfolded Protein Response in Oral Cancer Cells and Chop-Dependent Apoptosis.Complementary Roles of GADD34- and CReP-Containing Eukaryotic Initiation Factor 2α Phosphatases during the Unfolded Protein Response.Internal ribosome entry site-mediated translation of a mammalian mRNA is regulated by amino acid availability.Inhibition of translational initiation by activators of the glucose-regulated stress protein and heat shock protein stress response systems. Role of the interferon-inducible double-stranded RNA-activated eukaryotic initiation factor 2alpha kinase.Activation of the double-stranded RNA-regulated protein kinase by depletion of endoplasmic reticular calcium stores.PERK (eIF2alpha kinase) is required to activate the stress-activated MAPKs and induce the expression of immediate-early genes upon disruption of ER calcium homoeostasis.Endoplasmic Reticulum Stress Instigates the Rotenone Induced Oxidative Apoptotic Neuronal Death: a Study in Rat Brain.Ribosome profiling uncovers selective mRNA translation associated with eIF2 phosphorylation in erythroid progenitors.Melatonin protects brain against ischemia/reperfusion injury by attenuating endoplasmic reticulum stress.Cross-compartment proteostasis regulation during redox imbalance induced ER stressBrefeldin A inhibits protein synthesis through the phosphorylation of the α-subunit of eukaryotic initiation factor-2
P2860
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P2860
Reversible phosphorylation of eukaryotic initiation factor 2 alpha in response to endoplasmic reticular signaling.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
@zh
1993年论文
@zh-cn
name
Reversible phosphorylation of ...... doplasmic reticular signaling.
@en
type
label
Reversible phosphorylation of ...... doplasmic reticular signaling.
@en
prefLabel
Reversible phosphorylation of ...... doplasmic reticular signaling.
@en
P2093
P356
P1476
Reversible phosphorylation of ...... doplasmic reticular signaling.
@en
P2093
C O Brostrom
C R Prostko
M A Brostrom
P2888
P304
P356
10.1007/BF01076776
P478
P577
1993-11-01T00:00:00Z