IndraLab

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"In the heart, reduced Trx1, Trx2 and/or glutaredoxin1 (Grx1) bind to and negatively regulate apoptosis signal-regulating kinase 1 (ASK1), which inhibits ASK-1 from inducing apoptosis [ xref – xref ]."

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"Activation of the Akt pathway blocks the apoptotic pathway by negatively regulating the activity of BAD, a member of the Bcl2 family that binds to Bcl2 or Bcl-XL and inhibits their anti-apoptotic activity [XREF_BIBR], and the ASK1 and JNK mediated pro apoptotic pathway via phosphorylation of ASK1 at ser83 that inhibits ASK1 activity [XREF_BIBR]."

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"Phosphorylation of ASK1 Ser83 by AKT attenuates ASK1 kinase activity."

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"It has been shown by others that ASK1 can be phosphorylated at several sites which either up- or down-regulate ASK1 kinase activity."

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"On the basis of our finding that methylation of ASK1 negatively regulates H 2 O 2 -induced activation of ASK1, we next asked whether methylation of ASK1 at Arg 89 affects Ser 83 in vitro and in vivo."

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"Phosphorylation of ASK1 at S83 by Akt and PKB (protein kinase B) and dephosphorylation at S845 by protein phosphatase 5 (PP5) both decrease ASK1 activity."

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"PIM1 phosphorylation of ASK1 decreases ASK1 kinase activity."

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"Inactive IGF-1R does not phosphorylate ASK1 and subsequently does not inhibit ASK1 kinase activity."

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"Interestingly, phosphorylation of human ASK1 Ser83 by Akt is thought to attenuate Ask1 activity and inhibit apoptosis (Kim et al., 2001; Zhang et al., 2005)."

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"A Novel ASK Inhibitor AGI-1067 Inhibits TLR-4-Mediated Activation of ASK1 by Preventing Dissociation of Thioredoxin from ASK1."

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"Akt phosphorylates apoptosis signaling kinase 1 (ASK-1) at Ser 83, which attenuates ASK-1 activity and promotes cell survival, as ASK-1 transduces stress signals to the pro apoptotic jun NH2-terminal [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Our Western blot findings revealed that the expression levels of p-ASK1/ASK1 and p-JNK/JNK ratios were markedly upregulated in the penumbral cortex, whereas YZR-0.4 g and YZR-0.8 g treatments effectively reduced the p-ASK1/ASK1 and p-JNK/JNK ratios at 1 day after reperfusion."

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"We now show that PRMT1 methylates apoptosis signal regulating kinase 1 (ASK1) at arginine residues 78 and 80 and thereby negatively regulates ASK1 signaling."

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"TrxR inhibition mediated by indolin-2-one compounds led to cellular Trx oxidation, increased oxidative stress and activation of apoptosis signal regulating kinase 1 (ASK1)."

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"Mutant CARD6 that lacked the ability to interact with ASK1 could not inhibit ASK1 and failed to protect against hepatic I/R injury."

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"In our observation, 5 '-AMP attenuated the methylation of ASK1 and enhanced the ubiquitination of ASK1, which accelerate ASK1 degradation, leading to an inhibition of MAPKs cascade."

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"In this study, we observed that RASSF1A increased ASK1 mRNA and protein level but inhibited phosphorylation of ASK1 (inactivation of ASK1)."

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"This was triggered by attenuating apoptosis signal regulated kinase 1 (ASK1) methylation and increasing ubiquitination mediated ASK1 protein degradation."

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"PP5 directly dephosphorylated an essential phospho-threonine residue within the kinase domain of ASK1 and thereby inactivated ASK1 activity in vitro and in vivo."

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"Moreover, rescue experiments indicated that, in DKK3 TG mice, the activation of ASK1 using a cardiac-specific conditional ASK1 transgene reduced the functionality of DKK3 in response to pressure overload; furthermore, the inactivation of ASK1 by dominant-negative ASK1 rescued pressure overload-induced cardiac abnormalities in DKK3 KO mice."

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"On the MAP3K level, phosphorylation of ASK1 at Ser 83 by AKT reduced JNK activity in response to oxidative stress and serum starvation, and decreased ASK1 dependent apoptosis in HEK 293 and L929 cells."

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"In summary, H 2 O 2 -induced ASK1 activity can be inhibited by PRMT5 methylation of ASK1 at Arg 89, which in turn promotes interaction between ASK1 and Akt and enhances phosphorylation of ASK1 at Ser 83, which inhibits endothelial cells apoptosis."

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"GS-4497 is a small molecule that inhibits apoptosis signal regulating kinase 1 (ASK1)."

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"Phosphorylation of ASK1 on Ser83 by AKT kinase and de-phosphorylation of Ser845 by protein phosphatase 5 decreases ASK1 activity."

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"Although we show phosphorylation on Ser83 of ASK1 by PIM1 inhibits ASK1 activity, the mechanism underlying how phosphorylation on Ser83 inhibits its kinase activity remains unclear."

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"Activation of the IGF-1R leads to the tyrosine phosphorylation of ASK1 that suppresses ASK1 kinase activity (Galvan et al., 2003)."

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"Protein kinase B (PKB)-mediated phosphorylation of apoptosis signal regulating kinase 1 (ASK1), one of the MAPK kinase kinases (MAPKK-Ks), blocks ASK1 kinase activity, leading to suppression of MAPK k[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"