IndraLab

Statements


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"Taken together, these data suggest that USP38 inhibits type I IFN signaling by removing K33-linked and promoting K48-linked poly-ubiquitination chains of TBK1 at Lys670.Since both NLRP4 and USP38 degr[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"USP38 is an almost uncharacterized DUB with only one functional report showing that USP38 inhibits TBK1-mediated type 1 interferon signaling in macrophages (Lin et al., 2016)."

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"Thus, it is critical to elucidate its molecular mechanisms for a better understanding of how dynamic ubiquitin editing shapes TBK1 function as well as antiviral responses.Our findings show that USP38 [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Ubiquitin-specific peptidase 38 (USP38), a member of the ubiquitin specific processing enzyme family, has been reported to inhibit type I interferon signaling during viral infection (Lin et al., 2016)."

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"These results suggest that USP38 inhibits type I IFN signaling by interacting with TBK1 after viral infection.Next we sought to determine the molecular mechanisms of how USP38 inhibits type I IFN sign[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"