IndraLab

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"The interaction between USP15 and p66Shc may be attributed to the deubiquination of p66Shc by USP15."

sparser
"Thus, USP15 interacts with p66Shc and stabilizes p66Shc expression via its deubiquitinating activity."

No evidence text available

sparser
"USP15 interacts with p66Shc."

sparser
"We found that USP15 interacts with p66Shc in the SH2 domain that has been shown to be critical for protein-protein interactions [ xref ]."

sparser
"Using tandem affinity purification/mass spectrometry (TAP/MS) and co-immunoprecipitation (Co-IP)/MS, we identified the interaction between USP15 and p66Shc."

sparser
"Specifically, USP15 interacted with the SH2 domain of p66Shc and maintained its stabilization by removing ubiquitin."

sparser
"As shown in Fig. xref , USP15 and p66Shc efficiently interacted with each other."

sparser
"Thus, the interaction between USP15 and p66Shc mainly depends on the deubiquitylating activity of USP15."

sparser
"This study aimed to investigate the molecular mechanism of p66Shc in liver I/R and characterize the interaction between USP15 and p66Shc."

sparser
"The following study focused on the interaction between USP15 and p66Shc, and the interacting peptides between them were shown in Fig. xref ."

sparser
"Strikingly, the clinical relevance of USP15 and p66Shc was observed in patients subjected to liver transplantation, indicating a potential interaction between USP15 and p66Shc in liver I/R injury."

sparser
"Considering the interaction between USP15 and p66Shc as well as the deubiquitinating activity of USP15, USP15 may exert an effect on p66Shc deubiquitination."