IndraLab

Statements

L-prolylglycine inhibits MYD88. 6 / 6
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"Pg - LPS stimulation led to the phosphorylation of P38 MAPK , JNK , and ERK , and MyD88 knockdown inhibited the phosphorylation of P38 MAPK and JNK but not ERK ."
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"LPS R. capsulatus PG significantly decreases the synthesis of MyD88-dependent NF-kappaB-regulated cytokines activated by LPS E. coli, Der p 2, or their combination."
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"Strikingly, Pg caused time dependent reduction in the levels of MyD88 protein but not mRNA (XREF_FIG), suggesting that Pg causes MyD88 degradation at least in vitro."
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"The ability of Pg to degrade MyD88 was completely reversed by C5aRA or anti-TLR2 (XREF_FIG), suggesting that degradation is mediated by C5aR-TLR2 crosstalk."
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"Indeed, when Smurf1 protein expression was diminished by siRNA to Smurf1, the ability of Pg to degrade MyD88 was suppressed (XREF_FIG)."
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"Importantly, Pg (but not Pam3CSK4) induced degradation of MyD88 also in vivo, as shown by examining neutrophils harvested from Pg inoculated mouse chambers (XREF_FIG)."
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