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AKT phosphorylates MAP3K5 on S83. 41 / 68
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"Furthermore, AKT phosphorylation of apoptosis signal regulating kinase 1 (ASK1) on Ser 83 was reduced by DPI and siNox4RNAs."

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"AKT phosphorylates ASK1 on Ser83 and this results in the inhibition of apoptosis induced by ASK1 [87] ."

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"It has been shown that SIRT1 activates Akt, which in turn can phosphorylate ASK1 at Ser-83 to maintain ASK1 in an inactive form xref ."

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"It has been reported that AKT activation phosphorylates ASK1 at Ser83 and thus inactivates ASK1 signaling leading to inhibition of apoptosis ( Misra et al., 2006 )."

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"Akt phosphorylates ASK1 at Ser83 and thus inhibits it."

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"Furthermore, AKT phosphorylation of apoptosis signal-regulating kinase 1 (ASK1) on Ser-83 was reduced by DPI and siNox4RNAs."

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"Crosstalk between these two pathways can occur via Akt-dependent phosphorylation of ASK1 on Ser83, suppressing ASK1 activity ( xref )."

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"The apoptosis signal-regulating kinase 1 (Ask1) is phosphorylated by Akt at serine 83, leading to its inhibition and a reduced activation of JNK, which under certain circumstances can promote apoptosis ( xref )."

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"Phosphorylation of ASK1 Ser83 by AKT attenuates ASK1 kinase activity ( xref )."

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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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"AKT phosphorylates ASK1 on Ser83 and this results in the inhibition of apoptosis induced by ASK1 [87] ."

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"10 AKT can phosphorylate ASK1 on Ser83 and inactivates the apoptotic function of ASK1, leading to the enhancement of cell survival."

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"Akt phosphorylates ASK1 at Ser83 and thus inhibits it."

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"As shown in XREF_FIG (top and left), Akt phosphorylates wild-type ASK1 at Ser 83 but does not phosphorylate mutant ASK1 (R89W)."

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"(3) Akt phosphorylates apoptosis signal-regulating kinase 1 (ASK1) on Ser83 and this results in the inhibition of apoptosis induced by ASK1 [170] ."

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"10 AKT can phosphorylate ASK1 on Ser83 and inactivates the apoptotic function of ASK1, leading to the enhancement of cell survival."

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"Interestingly, phosphorylation of human ASK1 Ser83 by Akt is thought to attenuate Ask1 activity and inhibit apoptosis ( xref ; xref )."

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

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"Moreover, the phosphorylation of Ask-1 at Ser 83 by Akt suppress Ask-1 activity and Ask-1 mediated apoptosis XREF_BIBR, XREF_BIBR."

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"PIM1 and Akt directly phosphorylate Ask1 at Ser83, which decreases its ability to phosphorylate and activate its substrates, JNK and p38."

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"It has been shown that SIRT1 activates Akt, which in turn can phosphorylate ASK1 at Ser 83 to maintain ASK1 in an inactive form XREF_BIBR."

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"Thus phosphorylation of ASK1 at Ser 83 by Akt or PIM1 maintains ASK1 in an inactive state and suppresses ASK1 mediated p38 and JNK downstream signaling."

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"It is known that the inhibition of Akt induces an activation of p38 and JNK, whereas active Akt directly phosphorylates ASK1 Ser83, which leads to apoptosis inhibition [XREF_BIBR]."

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"It has been reported that Akt can phosphorylate ASK1 on Ser83, which results in the inhibition of apoptosis induced by ASK1 (Kim et al., xref )."

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"As shown in xref (top and left), Akt phosphorylates wild-type ASK1 at Ser-83 but does not phosphorylate mutant ASK1 (R89W)."

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"For example, PRMT5 symmetrically dimethylates ASK1 (apoptosis signal-regulating kinase 1) at the arginine 89 residue, thereby promoting the interaction between ASK1 and Akt and phosphorylating ASK1 at the serine 83 residue to negatively regulate its activity xref ."

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"Through the PubMed database, it showed that AKT could directly regulate the protein phosphorylated residues of p27 (Thr187) ( Fujita et al., 2002 ), BAD (Ser112) ( Liu et al., 2012 ), BAD (Ser136) ( D[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Incidentally, Akt phosphorylates ASK-1 (on S83) as part of its pro survival functions, thus keeping the latter 's activation in check [XREF_BIBR - XREF_BIBR, XREF_BIBR, XREF_BIBR]."

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"AKT phosphorylates Ser83 of ASK1 which also leads to inhibition of ASK1-induce apoptosis."

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"Crosstalk between these two pathways can occur via Akt dependent phosphorylation of ASK1 on Ser83, suppressing ASK1 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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"It has been reported that Akt can phosphorylate ASK1 on Ser83, which results in the inhibition of apoptosis induced by ASK1."

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"One major mechanism by which this antiapoptotic effect is mediated is phosphorylation of Ser 83 of apoptosis signal-regulating kinase 1 (ASK1) by Akt, rendering this pro-apoptotic kinase inactive [ xref ]."

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"Moreover, Akt phosphorylates the apoptosis signalregulating kinase 1 (ASK1) at S83, leading to cell survival and inhibition of apoptosis [XREF_BIBR]."

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"AKT phosphorylates Ser83 of ASK1 which also leads to inhibition of ASK1-induce apoptosis."

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"For instance, Zhang et al. reported that AKT can phosphorylate ASK1 at site Ser83 to inhibit hydrogen peroxide-induced ASK1/p38 signaling activation in endothelial cells xref ."

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

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"Moreover, the phosphorylation of Ask-1 at Ser 83 by Akt suppress Ask-1 activity and Ask-1 mediated apoptosis xref , xref ."

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"It is known that the inhibition of Akt induces an activation of p38 and JNK, whereas active Akt directly phosphorylates ASK1 Ser83, which leads to apoptosis inhibition [ xref ]."

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"For instance, Zhang et al. reported that AKT can phosphorylate ASK1 at site Ser83 to inhibit hydrogen peroxide induced ASK1 and p38 signaling activation in endothelial cells XREF_BIBR."

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"The activated Akt on one hand phosphorylates Ask-1 at the Ser 83 site to inhibit its activation, and on the other hand it phosphorylates FoxO."