IndraLab

Statements


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sparser
"In addition to USP1, two other DUBs, USP12 and USP46 interact with UAF1 [ xref ], but the UAF1-binding sites in these DUBs have not yet been mapped."

sparser
"In C. elegans , USP46 and USP12 both bind to USP1-associated factor 1 (UAF1/WDR48) and the binding dramatically enhances the activity of USP12 and USP46 ( xref , xref ; xref )."

sparser
"UAF1 also binds and activates two other DUBs, USP12 and USP46 ( xref ), and studies that reveal how UAF1 binds and activates USP12 and USP46 suggest that UAF1 will bind to USP1 in an analogous manner ( xref , xref )."

sparser
"WDR20 forms a unique ternary complex with WDR48 and either USP12 or USP46 (Sowa et al., 2009; Kee et al., 2010) and further enhances their catalytic activity in vitro (Kee et al., 2010; Faesen et al., 2011)."

sparser
"UAF1 also interacts with DUBs USP12 and USP46 ( García-Santisteban et al., 2013 ) and, thus, both genes also could be involved in senescence."

sparser
"Recent crystallographic studies demonstrate that UAF1 binds to a distinct site on USP12 or USP46 and, through an allosteric interaction, stimulates DUB activity ( xref ; xref )."

sparser
"The mode of interaction of USP12 and USP46 with UAF1 is still unclear."

sparser
"Recent structural work revealed how the WD-repeat protein UAF1 interacted with the catalytic domain of USP46 and USP12, which is facilitated predominantly through the “fingers” subdomain of the USP core, mediating long-range allosteric interactions eventually leading to enhanced enzyme efficiency ( xref , xref )."

sparser
"P65 interacted with USP12, USP46 and UAF1 in both resting and LPS-stimulated macrophages, but exhibited no association with USP1 (Fig.  xref )."