IndraLab

Statements


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sparser
"In addition, TMPO-AS1 has been found to facilitate the interaction between E2F1 and OTUB1."

reach
"The interactions between E2F1, OTUB1, and TMPO-AS1 were predicted via Agostini et al. introduced catRAPID (http://s.tartaglialab.com/page/catrapid_group), a server to identify the interaction of RNA and protein and Tuvshinjargal et al. developed a web server named PRIdictor (http://bclab.inha.ac.kr/pridictor) to reveal mutual binding in protein and RNA."

sparser
"Importantly, the results of co-immunoprecipitation (Co-IP) assays showed that silencing TMPO-AS1 not only increased E2F1 ubiquitination but also mitigated the interaction between OTUB1 and E2F1 ( xref ); importantly, this phenotype was rescued after the TMPO-AS1 overexpression."

sparser
"Additionally, TMPO-AS1 fueled the binding of E2F1 to OTU domain-containing ubiquitin aldehyde binding 1 (OTUB1), enhancing the deubiquitination and stability of E2F1, which unveiled a novel TMPO-AS1/E2F1/OTUB1 regulatory program ( xref )."

sparser
"Additionally, TMPO-AS1 facilitates the interaction of E2F1 with OTU domain-containing ubiquitin aldehyde binding 1 (OTUB1), leading to E2F1 deubiquitination and stabilization; therefore, TMPO-AS1 promotes BC malignant phenotypes."

sparser
"We demonstrate that E2F1 activates the transcription of TMPO-AS1, which, in turn, facilitates the interaction of E2F1 with OTU domain-containing ubiquitin aldehyde binding 1 (OTUB1), a deubiquitinase; consequently, the E2F1 protein levels are increased via stabilization, promoting BC malignant phenotypes."

reach
"Additionally, the protein interactions between E2F1 and OTUB1 were predicted using HDOCK (http://hdock.phys.hust.edu.cn)."

reach
"Importantly, the results of co-immunoprecipitation (Co-IP) assays showed that silencing TMPO-AS1 not only increased E2F1 ubiquitination but also mitigated the interaction between OTUB1 and E2F1 (XREF_FIG); importantly, this phenotype was rescued after the TMPO-AS1 overexpression."

reach
"In addition, TMPO-AS1 has been found to facilitate the interaction between E2F1 and OTUB1."