IndraLab

Statements



sparser
"Binding of WDR20 to the UAF1-USP12 complex induces multiple structural changes in the enzyme, converting it into a compact form similar to Ub-bound USP46."

reach
"Reminiscent of the Ub-bound UAF1-USP46 complex, the UAF1-USP12 structure features an L-shaped architecture, in which the elongated UAF1 protein packs perpendicularly against the DUB (Figures 2A and 2B) ."

reach
"Binding of WDR20 to the UAF1 and USP12 complex induces multiple structural changes in the enzyme, converting it into a compact form similar to Ub bound USP46."

sparser
"UAF1 activation of USP12 requires structural fine-tuning at the ubiquitin-binding site, while WDR20 directly regulates the catalytic center of the enzyme remotely, transforming USP12 into a compact structure similar to USP46-Ub [ xref ]."

sparser
"Stabilization of a malleable apo USP46 to favor an active conformation would shift the equilibrium of association and promote productive interaction between ubiquitin and USP46."

sparser
"The USP46-bound ubiquitin is closer, however, sheltered adjacent to the concave inner face of the WDR48 ancillary domain."

sparser
"In addition, WDR48 has a novel ancillary domain and a C-terminal SUMO-like domain encircling the USP46-bound ubiquitin."

reach
"Binding of WDR20 to the UAF1-USP12 complex induces multiple structural changes in the enzyme, converting it into a compact form similar to Ub-bound USP46."

sparser
"We superimposed the crystal structures of USP46 in a non-covalent complex with WDR20 and WDR48 together with the covalent USP46ubiquitin complex."

reach
"Reminiscent of the Ub bound UAF1 and USP46 complex, the UAF1-USP12 structure features an L shaped architecture, in which the elongated UAF1 protein packs perpendicularly against the DUB."

reach
"Reminiscent of the Ub bound UAF1 and USP46 complex, the UAF1-USP12 structure features an L shaped architecture, in which the elongated UAF1 protein packs perpendicularly against the DUB enzyme (XREF_FIG and XREF_FIG)."

sparser
"Furthermore, difference density indicating the missing domain clearly extended from our extant WDR48 C terminus, encircling the USP46-bound ubiquitin and approaching the thumb subdomain of USP46 over [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"