IndraLab

Statements

USP34 binds Ubiquitin. 4 / 4
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sparser
"The structure of the complex between USP34 and Ub-PA reveals a structural basis for the distal ubiquitin recognition of USP34."
35588869
sparser
"To evaluate the structural observations, we assessed the effects of a series of mutations that are suspected to disrupt USP34-Ub contacts on the deubiquitination activity of USP34."
35588869
sparser
"The interactions between USP34 and Ub-PA result in the burial of 1704 Å 2 of exposed surface area and a relatively closed conformation of the USP34 structure."
35588869
sparser
"This analysis explains why H2164 does not form the mis-aligned conformation in the ubiquitin-bound complex of USP34: the main chain of G2162 could not employ the same conformation that is required for[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
35588869