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BRCC3 deubiquitinates HMGCR. 8 / 8
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"Figure 4B shows that BRCC36 overexpression significantly inhibited the degradation of HMGCR in HepG2 and SMMC7721 cells treated with CHX, while HMGCR protein was markedly degraded after depletion of BRCC36 in Hep3B cells treated with CHX.To examine whether BRCC36 blocks the ubiquitination of HMGCR, we detected the ubiquitination level of HMGCR."
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"Figure 4D shows that overexpression of BRCC36 reduced K63‐linked ubiquitination of HMGCR without affecting other types of linkages, indicating that BRCC36 primarily removes K63‐linked polyubiquitin chains of HMGCR."
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"Moreover, the ubiquitin level of HMGCR was increased after THL treatment (Figure 7D), indicating that the ability of BRCC36 to deubiquitinate HMGCR was attenuated."
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"BRCC36 is involved in the deubiquitination of HMGCR, and its inhibition can suppress liver cancer cell proliferation [9]."
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"BRCA1/BRCA2-containing complex subunit 36 deubiquitinates HMGCR through DUB activity and inhibits ferroptosis while promoting pyroptosis (127)."
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"Recently, it was reported that BRCC36 deubiquitinates HMGCR, connecting ferroptosis with pyroptosis [25], other than that, the relationship between ferroptosis and pyroptosis is currently under-researched."
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"BRCC36 Deubiquitinates HMGCR to Regulate the Interplay Between Ferroptosis and Pyroptosis."
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"Furthermore, this study demonstrated that BRCC36 (BRCA1/BRCA2-containing complex subunit 36) deubiquitinated HMGCR in a manner dependent on deubiquitinating enzyme (DUB) activity, and inhibited ferroptosis and promoted pyroptosis."
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