IndraLab

Statements


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sparser
"Mechanistically, OTUB1 directly bound to RACK1 at its C-terminal domain and decreased the K48-linked ubiquitination of RACK1 through its non-canonical suppression of ubiquitination activity, which stabilized RACK1 protein levels in HCC cells."

reach
"Although the precise mechanism by which OTUB1 induces RACK1 stabilization requires further elucidation, it is very likely that the binding between OTUB1 and RACK1 as well as OTUB1’s ability to inhibit E2-conjugating enzymes recruited by the unknown E3 ligase contribute to RACK1 stabilization induced by OTUB1."

No evidence text available

No evidence text available

sparser
"Mariola et al. [ 23 ] proved that OTUB1 protein interacts with RACK1 protein from the perspective of molecular structure."

reach
"Mechanistically, OTUB1 directly bound to RACK1 at its C-terminal domain and decreased the K48-linked ubiquitination of RACK1 through its non-canonical suppression of ubiquitination activity, which stabilized RACK1 protein levels in HCC cells."

reach
"These findings suggested that the binding between OTUB1 and RACK1 is not dependent on its deubiquitinating enzyme activity, but may be related to its interaction with E2-binding enzymes."

sparser
"The collected total protein was mixed with Goat Anti-Mouse IgG (Proteintech, Wuhan, China) or indicted-IP OTUB1 antibody40 (Abcam, Massachusetts, USA) overnight at 4 °C. According to the antigen-antib[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"We also detected the expression of ubiquitin using Ubiquitin Antibody (abclonal, Wuhan, China) in the complex of OTUB1 and RACK1 protein."

No evidence text available

sparser
"It was obvious of the complex of OTUB1 protein and RACK1 protein according to the results of the CO-IP assay ( Fig. 9 e)."

sparser
"As we pointed out in the relationship between OTUB1 and RACK1, RACK1 directly interacted with the deubiquitinating enzyme OTUB1."