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"During the course of our studies, we observed that mutating theUSP4 catalytic cysteine to alanine (C311A) to render USP4 enzymatically inactive (" catalytic-dead " [CD]), almost totally abrogated its interactions with CtIP and MRN (XREF_FIG A; note that binding of USP4 to CtIP and RAD50 was not abrogated by the DNA intercalating agent ethidium bromide (EtBr), suggesting that interaction was not mediated by DNA bridging."

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