IndraLab

Statements

YOD1 binds PKM2. 7 / 7
| 7
sparser
"We demonstrate that YOD1 directly interacts with PKM2 and mediates its K63‐linked deubiquitination, thereby inhibiting the transition from tetrameric to dimeric PKM2."
40681475
sparser
"YOD1 directly bound PKM2 and reduces its ubiquitination level by removing the K63‐linked ubiquitin chain of PKM2, thereby increasing the tetramer level and reducing the dimer level of PKM2."
40681475
sparser
"YOD1 binds to PKM2 and reduces its ubiquitination level by removing the K63 ubiquitin chain of PKM2, thereby increasing the tetramer level and reducing the dimer level of PKM2."
40681475
sparser
"Together, this study demonstrates the potential of YOD1 as a novel therapeutic target for PD and provides a mechanistic foundation for developing selective inhibitors of the YOD1‐PKM2 signalling axis."
40681475
sparser
"This study reveals a new YOD1-PKM2 axis in cardiomyocytes and identifies YOD1 as a potential target for the treatment of ISO-induced cardiac remodeling and heart failure."
40500343
sparser
"These above results confirmed that PKM2 interacts with YOD1."
40681475
sparser
"This identifies a novel molecular interface regulating the YOD1‐PKM2 axis in PD pathogenesis."
40681475