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USP7 deubiquitinates XPC. 6 / 7
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"Inhibition of USP7 increases XPC ubiquitination level, and without USP7, cells have decreased efficiency in repairing UV lesions [XREF_BIBR, XREF_BIBR]."

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"Specifically, USP7 plays crucial roles in transcription-coupled nucleotide excision repair by interacting with UVSSA ( Schwertman et al., 2012; Zhang et al., 2012 ), and it is also involved in global [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Specifically, UV induced XPC proteasomal degradation occurs without protection by USP7 which deubiquitinates XPC."

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"Both XPC and CSB also appear to be deubiquitylated by USP7 30, 39, 40 (see below) and regulated by SUMOylation 37, 41, further underscoring the analogies (Figure 2)."

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"Other proteins involved in the stabilization of XPC might be the deubiquitylating enzymes OTUD4 and USP7, which were shown to deubiquitylate XPC upon UV induced DNA damage XREF_BIBR XREF_BIBR."

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"USP7 plays an important role in DNA repair by deubiquitinating XPC, a key recognition factor of DNA damage, to avoid its degradation [43]."