IndraLab

Statements

USP35 deubiquitinates FUCA1. 6 / 6
| 6
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"We found that only the catalytically active USP35 (USP35 WT), not the USP35 mutant (USP35 C450A), deubiquitinated FUCA1 (Fig. 4A)."
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"We further confirmed that FUCA1 was deubiquitinated and stabilized by USP35."
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"Overall, this study indicates that USP35 contributes to tumorigenesis and confers chemo-resistance in CRC by deubiquitinating FUCA1, unraveling a novel molecular target for CRC treatment."
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"USP35 deubiquitinates and stabilizes FUCA1."
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"Considering USP35 is a deubiquitinase, we then investigated whether FUCA1 was deubiquitinated by USP35."
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"Overall, these results demonstrate that USP35 deubiquitinates FUCA1 and increases FUCA1 stability by preventing ubiquitin-proteasome pathway-mediated degradation of FUCA1."
36864055