IndraLab

Statements


USP4 binds UBL and DUSP. 4 / 4
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sparser
"The binding of USP4 N-terminal DUSP-Ubl domain promotes a change of a switching loop near the active site, and hence enhances ubiquitin dissociation and makes it achieve full catalytic activity xref ."

sparser
"The crystal structure of USP4 DUSP-UBL shows a dimer formation where the subunits are packed against each other in an antiparallel orientation ( xref ) ( xref )."

sparser
"Indeed, surface plasmon resonance (SPR) shows an interaction of DUSPUbl with immobilized USP4 CD ( xref )."

sparser
"By binding to the linker between the DUSP and UBL domain of USP4, SART3 can shuttle USP4 to the nucleus from the cytosol through its NLS."