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PPP1R15A is a member of a group of genes whose transcript levels are increased following stressful growth arrest conditions and treatment with DNA-damaging agents. Additionally we are shipping Protein Phosphatase 1, Regulatory (Inhibitor) Subunit 15A Antibodies (68) and Protein Phosphatase 1, Regulatory (Inhibitor) Subunit 15A Kits (2) and many more products for this protein.
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Sustained protein synthesis sensitized cells to pharmacological induction of the Unfolded Protein Response (UPR), and the observed decrease in cell viability was restored upon inhibition of GADD34 activity. We conclude that NMP4 (show ZNF384 Proteins) is a key regulator of ribosome biogenesis and the UPR, which together play a central role in determining cell viability during endoplasmic reticulum stress.
Through aging or a high fat diet, insulin (show INS Proteins) signaling in GADD34-deficient liver converted to be down regulated compared with WT mice.
Results show that GADD34 plays a vital role in promoting cell death following proteasome inhibition via enhancing protein synthesis involved in endoplasmic reticulum stress, reactive oxygen species production and autophagy formation.
avidity for the substrate plays an important role in imparting specificity on the PPP1R15B-PP1G-actin ternary complex.
GADD34 enhances autophagy and suppresses apoptosis stimulated by LPS (show TLR4 Proteins) combined with amino acid deprivation through regulation of mTOR (show FRAP1 Proteins) signaling pathway in macrophages.
GADD34 upregulated pro-inflammatory mediator.
GADD34 promotes cell survival and adaptation to increased extracellular osmolarity by increasing the uptake of small neutral amino acids via the amino acid transporter SNAT2 (show SLC38A2 Proteins).
GADD34 expression was upregulated in the liver of mice after exposure to a carcinogen, diethylnitrosamine (DEN). In both acute and chronic DEN treatment models, GADD34 deficiency not only decreased oncogene (show RAB1A Proteins) expression, but also reduced hepatic damage.
Thus these results indicate that GADD34 appears to suppress myofibroblast differentiation through inhibiting Smad3 (show SMAD3 Proteins)-dependent TGFbeta (show TGFB1 Proteins) signal pathway and promote its apoptosis by activating caspase-3 (show CASP3 Proteins) pathway
GADD34 works to inhibit the proliferation and differentiation of HSCs or myeloid precursor cells and maintains homeostatic differentiation of neutrophil-lineage cells to avoid early immunological senescence.
reduction of GADD34 expression significantly suppressed tumor, and resulted in decreased accumulation of MDSCs and T-cells, and inhibition of GADD34 reduced secretion of vascular epithelial growth factor alpha and transforming growth factor beta by MDSCs
ANXA11 (show ANXA11 Proteins) rs1049550 and PPP1R15A rs557806 may improve the identification of mCRC patients sensitive to bevacizumab regimens, and further validation is required in large cohorts
Data of this study strengthen the evidence of an unfolded protein response during the course of RA and provide an insight of the potential interest in GADD34 as a relevant marker for RA.
The results suggest that dephosphorylation of eIF2a (show EIF2S1 Proteins) by GADD34 plays an important role in doxorubicin resistance of MCF-7/ADR (show AKR1B1 Proteins) cells.
The reactive oxygen species-generating NADPH oxidase-4 (Nox4 (show NOX4 Proteins)) is induced downstream of ATF4 (show ATF4 Proteins), binds to a PP1 (show PPA1 Proteins)-targeting subunit GADD34 at the endoplasmic reticulum, and inhibits PP1 (show PPA1 Proteins) activity to increase eIF2alpha (show EIF2A Proteins) phosphorylation and ATF4 (show ATF4 Proteins) levels.
stress pathways lead to the induction of the protein GADD34, which appears to provide protection against the toxic effects of the secreted virulence factors in Pseudomonas aeruginosa infection
The data highlight independent interactions of PP1 (show PPA1 Proteins) and eIF2alpha (show EIF2A Proteins) with GADD34, demonstrating that GADD34 functions as a scaffold both in vitro and in cells
GADD34 may play a neuroprotective role against amyloid-beta toxicity.
GADD34 enhances autophagy and suppresses apoptosis stimulated by LPS (show IRF6 Proteins) combined with amino acid deprivation through regulation of mTOR (show FRAP1 Proteins) signaling pathway in macrophages.
Data indicate that protein phosphatase 1 (show PPP1CB Proteins) subunit GADD34 directly interacts with eukaryotic translation initiation factor 2 subunit alpha (eIF2alpha (show EIF2S1 Proteins)).
This gene is a member of a group of genes whose transcript levels are increased following stressful growth arrest conditions and treatment with DNA-damaging agents. The induction of this gene by ionizing radiation occurs in certain cell lines regardless of p53 status, and its protein response is correlated with apoptosis following ionizing radiation.
protein phosphatase 1, regulatory (inhibitor) subunit 15A
, growth arrest and DNA damage-inducible protein GADD34
, growth arrest and DNA-damage-inducible 34
, myeloid differentiation primary response gene 116
, myeloid differentiation primary response protein MyD116
, protein phosphatase 1 regulatory subunit 15A
, myeloid differentiation primary response protein MyD116 homolog
, progression elevated gene 3 protein