IndraLab

Statements


| 4 11

sparser
"USP24 interacts with Beclin1."

sparser
"The interaction between USP24 and Beclin1 represents a key molecular mechanism that promotes autophagy related ferroptosis in HCC."

sparser
"It was found that Beclin1 could be co-immunoprecipitated by USP24 (Fig.  xref ), but no other autophagy proteins, such as ULK1 and Atg5 (Supplementary Fig.  xref ), indicating that USP24 could interact with Beclin1."

sparser
"Next, a reciprocal Co-IP assay was conducted to further confirm the interaction between USP24 and Beclin1 (Fig.  xref )."

sparser
"Additionally, cellular double immunofluorescence assay provided morphological evidence of the interaction between USP24 and Beclin1 protein (Fig.  xref and Supplementary Fig.  xref ) and the colocalization coefficients increased after USP24 overexpression (Fig.  xref and Supplementary Fig.  xref )."

sparser
"USP24 interacts endogenously with Beclin 1 and delays its degradation by reducing K48-linked ubiquitination."

sparser
"These results collectively confirmed the interaction between USP24 and Beclin1."

reach
"The endogenous interaction between USP24 and Beclin1 is confirmed."

reach
"Next, a reciprocal Co-IP assay was conducted to further confirm the interaction between USP24 and Beclin1 (Fig. 4B)."

sparser
"To the best of our knowledge, this is the first evidence demonstrating that USP24 interacts with Beclin1, primarily by inhibiting its K48-linked ubiquitination."

reach
"These results collectively confirmed the interaction between USP24 and Beclin1."

reach
"The interaction between USP24 and Beclin1 represents a key molecular mechanism that promotes autophagy-dependent ferroptosis."

sparser
"The interaction between USP24 and Beclin1 represents a key molecular mechanism that promotes autophagy-dependent ferroptosis."

sparser
"Targeting the USP24-Beclin1 axis may provide a therapeutic strategy for HCC."

sparser
"The endogenous interaction between USP24 and Beclin1 is confirmed."