IndraLab

Statements


| 3

sparser
"As shown in Supplementary Fig. xref , only the full‐length (FL) and the M4 (717–942aa) and M5 (811–942aa) mutants of USP33, but not other mutants, interacted with SIN1."

sparser
"First, our mass spectrometry analysis identified USP33 as a bona fide deubiquitinase of SIN1, showing that USP33 directly interacts with SIN1 and reduces its ubiquitination, thereby stabilizing SIN1 (Fig. xref and Supplementary Fig. xref )."

sparser
"Third, CDK1-mediated phosphorylation was essential for USP33 binding to SIN1 and promoting tumor progression (Fig. xref )."