IndraLab

Statements


| 7

sparser
"USP35 directly interacts with ferroportin and maintain its protein stability to prevent iron overload and ferroptosis."

sparser
"Together, these data indicate that USP35 can directly interact with FPN and functions as a deubiquitinase to maintain its protein stability."

sparser
"In lung cancer cells, USP35 interacts directly with FPN1 to maintain its protein stability and prevent iron overload and ferroptosis ( xref )."

sparser
"Further studies determined that USP35 directly interacted with ferroportin (FPN) and functioned as a deubiquitinase to maintain its protein stability."

sparser
"FPN ubiquitination is required for its internalization and degradation, and Zhang et al identified the deubiquitinated role of USP35 in ovarian cancer cells. xref , xref Consistently, we found that USP35 directly interacted with FPN and functioned as a deubiquitinase to maintain its protein stability."

sparser
"Conversely, the deubiquitinating enzyme USP35 interacts with SLC40A1 to maintain the protein stability of iron transporters, preventing the onset of ferroptosis in lung cancer [ xref ]."

sparser
"First, the specific domain through which USP35 interacts with FPN remains unclear and demands further investigation."