IndraLab

Statements

OTUB1 binds K48-Ub 2. 3 / 3
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"To probe further the binding between hOtu1 and K48-Ub 2, we measured the substrate concentration dependence of the cleavage rate."
19211026
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"The K m was determined to be 78 +/- 15 muM, which suggests that binding between hOtu1 and K48-Ub 2 is relatively weak and is consistent with the results of the NMR titrations."
19211026
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"To examine further the binding between hOtu1 and K48-Ub 2, we measured the NMR chemical shift perturbations that resulted from titration of catalytically-inactive hOtu1C91S into 15 N labeled K48-Ub 2."
19211026