IndraLab

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USP17L2 deubiquitinates H2AX. 9 / 9
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"Most importantly, using these purified proteins in an in vitro deubiquitination assay demonstrated that WT Dub3, but not CI, was able to deubiquitinate H2AX."
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"<span class="match term0">Dub3</span> controls DNA damage signalling by direct deubiquitination of <span class="match term1">H2AX</span>"
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"DUB3 (also known as USP17L2) directly interacts with and deubiquitylates H2AX [73]."
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"In addition, this negative control demonstrated that the decrease of H2AX ubiquitination by Dub3 wild type (WT) is unlikely to be a nonspecific effect of overexpression."
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"This effect is due to the catalytic activity of Dub3, as expression of a catalytic inactive version of Dub3 (CI, C89S) did not reduce the monoubiquitination of H2AX ( Figure 1 A)."
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"Overexpression of DUB3 decreased monoubiquitination of γH2AX in the absence of an exogenous DNA damage source as well as post-IR [33]."
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"Inhibition of Dub activity by N-ethylmaleimide (NEM) prevented deubiquitination of H2AX by Dub3 and to support the specificity of the assay, we demonstrate that USP28, an aspecific Dub, previously rep[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Given the effects of Dub3 overexpression on 53BP1 and BRCA1 focus formation, two events upstream the regulation of the DNA damage-induced cell cycle arrest, the direct interaction between Dub3 and H2A[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Moreover, Dub3 and H2AX interact and Dub3 deubiquitinates H2AX in vitro."
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