IndraLab

Statements


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eidos
"It is interesting to note that Ile83Ala / Leu86Ala mutations targeted the SAF-A / B , Acinus , and PIAS ( SAP ) domain within Lpro [ 235 ] , and while these mutations selectively abrogate DUB activity [ 240 ] and delay nuclear translocation [ 235 ] , they do not appear to target the likely Ub-binding interface of Lpro , which has been demonstrated to be an effective means to inhibit the DUB activity of other vDUBs [ 162 ] , [ 199 ] ."

eidos
"Mutations that affect the mobility of the loop and prevent the close conformation resulted in a loss of DUB activity while conserving the protease function [ 27 ] ."

eidos
"In the case of TYMV , these two activities can be uncoupled by mutations that selectively suppress the DUB activity without altering PRO ( Jupin et al ., 2017 ) ."

eidos
"This mutation , along with others , abrogated DUB activity yet permitted polyprotein cleavage at the nsp2-3 junction , thus providing an ideal system to directly assess whether PLpro DUB activity alone disrupts cellular signaling ."

eidos
"Interestingly , this residue ( equivalent of Glu168 in SARS PLpro ) seems to play an important role in Ub1 core recognition , and mutations can cause a significant loss of DUB activity ."