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Statements

USP2 binds UBD. 20 / 30
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"We carried out stopped-flow fluorescence analyses of the binding of mono- and diubiquitin to an inactive USP2 mutant and unveiled interesting differences in the binding kinetics between the two substrates."
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sparser
"Binding of K48-linked IQF diubiquitin to USP2 under an equilibrium condition."
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"Binding was monitored by following the enhancement of TAMRA fluorescence upon the binding of K48-linked IQF diubiquitin substrate (25 nM) to USP2 (0-8 μM)."
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"Transient kinetics of K48-linked diubiquitin binding to USP2."
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"Stopped-flow fluorescence analysis was used to follow K48-linked IQF diubiquitin binding to USP2 under a pre-steady-state condition."
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"Based on the regression analysis of the plots of k obs,1 and k obs,2 , using xref - xref we were able to calculate each microscopic binding rate constant for a two-step process describing the binding of diubiquitin to USP2."
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"The binding interaction between USP2 and native K48-linked diubiquitin was also characterized using stopped-flow fluorescence analysis under the pre-steady-state condition."
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"This apparent dissociation constant was later used in calculating the individual microscopic binding rate constants in a proposed two-step process of diubiquitin binding to USP2 (vide infra)."
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"Transient kinetics of K48 linked diubiquitin binding to USP2."
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"Stopped-flow fluorescence analysis was used to follow K48 linked IQF diubiquitin binding to USP2 under a pre-steady-state condition."
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"Based on the regression analysis of the plots of k obs,1 and k obs,2, using equations 2-7 we were able to calculate each microscopic binding rate constant for a two-step process describing the binding of diubiquitin to USP2."
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"Due to an extremely week fluorescence signal we were unable to determine the apparent dissociation constant of native K48 linked diubiquitin binding to C276A USP2 under an equilibrium condition, which prevented us from calculating the k 2 and k -2 of native diubiquitin binding to USP2."
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"Different from monoubiquitin, we observed biphasic kinetics for the binding of diubiquitin to USP2."
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"Therefore, the biphasic binding kinetics observed for K48 linked diubiquitin can be best interpreted by the binding of the diubiquitin to USP2, followed by an additional conformational rearrangement in the USP2 and diubiquitin complex to position diubiquitin in a productive conformation for catalysis."
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"Our global fitting analysis revealed a conformational rearrangement step following the binding of the diubiquitin to USP2 catalytic core."
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"The binding of native K48-linked diubiquitin to USP2 was again clearly biphasic ( xref )."
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"Nonetheless, the good agreement in the measured k 1 , k −1 for the native K48-linked diubiquitin and the K48-linked IQF diubiquitin support that the fluorophores on K48-linked IQF diubiquitin do not adversely affect USP2’s interaction with diubiquitin."
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sparser
"Different from monoubiquitin, we observed biphasic kinetics for the binding of diubiquitin to USP2."
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sparser
"Our stopped-flow data for diubiquitin revealed that the binding of K48-linked IQF diubiquitin to USP2 is biphasic."
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"Therefore, the biphasic binding kinetics observed for K48-linked diubiquitin can be best interpreted by the binding of the diubiquitin to USP2, followed by an additional conformational rearrangement in the USP2-diubiquitin complex to position diubiquitin in a productive conformation for catalysis."
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