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The results of this investigation indicate ASK1 inhibition prolongs keratinocyte and blastemal cell activation leading to ear regeneration.
These results suggest that the platelet Ask1 plays an important role in regulation of hemostasis and thrombosis.
Lysine 29-linkage of ASK1 by Skp1-Cullin 1-Fbxo21 ubiquitin ligase complex is required for antiviral innate response.
These results demonstrate that trans-fatty acids promote extracellular ATP-induced apoptosis by targeting ASK1 and indicate novel TFA (show F3 Proteins)-associated pathways leading to inflammatory signal transduction and cell death that underlie the pathogenesis and progression of trans-fatty acids-induced atherosclerosis.
Conversely, treatment with LY294002 (a selective inhibitor of Akt1 (show AKT1 Proteins)) reversed the effects of quercetin. In conclusion, these findings highlight the important role of quercetin in protecting against cognitive deficits and inhibiting neuronal apoptosis via the Akt (show AKT1 Proteins) signaling pathway. We believe that quercetin might prove to be a useful therapeutic component in treating cerebral I/R diseases in the near future.
ASK1 MAP kinase (show MAPK1 Proteins) signaling cascade is an important regulator of chondrocyte terminal differentiation.
ASK1 mediates astrocyte activation and leads to glial scar formation after cerebral ischaemia.
ASK1 mediates 3-NP toxicity and regulates C1q level through the astrocyte TGF-beta (show TGFB1 Proteins).
ASK1 signalling regulates brown and beige adipocyte function.
blocking MPTP (show PTPN2 Proteins)-mediated TNF (show TNF Proteins) signaling through intrathecal administration of TNF (show TNF Proteins)-neutralizing antibody prevented Trx1 (show TXN Proteins) oxidation and downstream ASK1-p38 MAPK (show MAPK14 Proteins) activation
PBL27 interacts with both CERK1 and the MAPK (show MAPK1 Proteins) kinase kinase MAPKKK5 at the plasma membrane and knockout of MAPKKK5 compromise chitin-induced MAPK (show MAPK1 Proteins) kinase activation and disease resistance to Alternaria brassicicola.
AKT2 (show AKT2 Proteins) interacts with and phosphorylates ASK1 at Ser (show SIGLEC1 Proteins)-83 resulting in inhibition of its kinase activity and signaling down-stream of ASK1.
CD40 (show CD40 Proteins) activation resulted in down-regulation of Thioredoxin (Trx)-1 (show TXN Proteins) to permit ASK1 activation and apoptosis. Although soluble receptor (show IFNAR1 Proteins) agonist alone could not induce death, combinatorial treatment incorporating soluble CD40 (show CD40 Proteins) agonist and pharmacological inhibition of Trx-1 (show MLL Proteins) was functionally equivalent to the signal triggered by mCD40L
from the two catalytic cysteines of TRX1 (show MLL Proteins) the residue C32 is responsible for the high-affinity binding of TRX1 (show MLL Proteins) to the ASK1-TRX (show VAC14 Proteins)-binding domain in reducing conditions
Shotgun mass spectrometry and manual validation identified 12 distinct ASK1 phosphosites. Targeted parallel reaction monitoring assays were used to track the phosphorylation dynamics of each confirmed site in response to treatment.
phosphorus NMR and time-resolved tryptophan fluorescence measurements suggest that 14-3-3zeta (show YWHAZ Proteins) interacts with the kinase domain of ASK1 in close proximity to its active site, thus indicating this interaction might block its accessibility and/or affect its conformation.
Pretreatment by IRE1 (show ERN1 Proteins) agonist tunicamycin or JNK (show MAPK8 Proteins) agonist anisomycin attenuated the effect of psoralen on osteoporotic osteoblasts. Psoralen inhibited apoptosis of osteoporotic osteoblasts by regulating IRE1 (show ERN1 Proteins)-ASK1-JNK (show MAPK8 Proteins) pathway
Our results thus suggest that GSK-3beta is a key factor involved in ASK1 activation and reactive oxygen species-induced cell death.
the data show that miRNA-mediated down-regulation of ASK1 protects mesenchymal stem cells during post-transplantation, leading to an increase in the efficacy of MSC (show MSC Proteins)-based cell therapy.
Mitogen-activated protein kinase (MAPK) signaling cascades include MAPK or extracellular signal-regulated kinase (ERK), MAPK kinase (MKK or MEK), and MAPK kinase kinase (MAPKKK or MEKK). MAPKK kinase/MEKK phosphorylates and activates its downstream protein kinase, MAPK kinase/MEK, which in turn activates MAPK. The kinases of these signaling cascades are highly conserved, and homologs exist in yeast, Drosophila, and mammalian cells. MAPKKK5 contains 1,374 amino acids with all 11 kinase subdomains. Northern blot analysis shows that MAPKKK5 transcript is abundantly expressed in human heart and pancreas. The MAPKKK5 protein phosphorylates and activates MKK4 (aliases SERK1, MAPKK4) in vitro, and activates c-Jun N-terminal kinase (JNK)/stress-activated protein kinase (SAPK) during transient expression in COS and 293 cells\; MAPKKK5 does not activate MAPK/ERK.
, MAP/ERK kinase kinase 5
, MAPK/ERK kinase kinase 5
, MEK kinase 5
, MEKK 5
, apoptosis signal regulating kinase 1
, apoptosis signal-regulating kinase 1
, mitogen activated protein kinase kinase kinase 5
, mitogen-activated protein kinase kinase kinase 5
, mitogen-activated protein kinase kinase kinase 5 pseudogene