IndraLab

Statements

GBP2 binds OTUD5. 23 / 23
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"However, the interaction between GBP2 and OTUD5 in HPMECs was partially inhibited by PD ( xref H)."
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"This reduces GBP2's interaction with OTUD5 and its inhibitory effect on OTUD5."
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"Furthermore, the precise mechanism by which PD affects the GBP2-OTUD5 interaction remains unclear and requires further investigation."
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"Second, although this study confirmed the regulatory interaction between GBP2 and OTUD5 in endothelial cells, the possibility that GBP2 modulates ferroptosis through interactions with endothelial cell receptors cannot be entirely excluded."
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"The mechanism by which GBP2 binds directly to OTUD5 and promotes GPX4 ubiquitination was elucidated using RNA interference, adeno-associated virus transfection, and endothelial-specific Gpx4 knockout mice."
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"PD treatment inhibited the interaction between GBP2 and OTUD5, leading to a reduction in GPX4 ubiquitination."
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"We further found that PD treatment inhibits the interaction between GBP2 and OTUD5 in HPMECs, reducing GPX4 ubiquitination."
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"Protein-protein docking analysis was performed to predicted the interaction between GBP2 and OTUD5, which revealed a binding energy of −67.42 kcal/mol, indicating a significant probability of interaction (Fig. 8D)."
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"Mechanistically, GBP2 interacts with OTU deubiquitinase 5 (OTUD5) in endothelial cells, promoting the ubiquitination of GPX4, thereby increasing sensitivity to ferroptosis and compromising the endothelial barrier."
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"GBP2 and OTUD5 interaction promotes the ubiquitination and degradation of GPX4 in HPMECs."
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"PD treatment inhibited the interaction between GBP2 and OTUD5, leading to a reduction in GPX4 ubiquitination."
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"The mechanism by which GBP2 binds directly to OTUD5 and promotes GPX4 ubiquitination was elucidated using RNA interference, adeno-associated virus transfection, and endothelial-specific Gpx4 knockout mice."
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"After co-culturing SMφ-EVs with HPMECs, co-immunoprecipitation confirmed the direct binding of GBP2 to OTUD5 in HPMECs."
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"Protein-protein docking analysis was performed to predicted the interaction between GBP2 and OTUD5, which revealed a binding energy of −67.42 kcal/mol, indicating a significant probability of interaction ( xref D)."
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"After co-culturing SMφ-EVs with HPMECs, co-immunoprecipitation confirmed the direct binding of GBP2 to OTUD5 in HPMECs."
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"However, the interaction between GBP2 and OTUD5 in HPMECs was partially inhibited by PD (Fig. 9H)."
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"We further found that PD treatment inhibits the interaction between GBP2 and OTUD5 in HPMECs, reducing GPX4 ubiquitination."
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"The results indicate that PD inhibits GPX4 ubiquitination and disrupts the interaction between GBP2 and OTUD5, independent of GBP2 activity.3.10 Combined treatment of GBP2 blockade and PD showed additive pulmonary-protective effects in CLP mice."
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"This reduces GBP2's interaction with OTUD5 and its inhibitory effect on OTUD5."
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"Second, although this study confirmed the regulatory interaction between GBP2 and OTUD5 in endothelial cells, the possibility that GBP2 modulates ferroptosis through interactions with endothelial cell receptors cannot be entirely excluded."
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"The results indicate that PD inhibits GPX4 ubiquitination and disrupts the interaction between GBP2 and OTUD5, independent of GBP2 activity."
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"Our study found that GBP2 interacts with OTUD5 in endothelial cells, leading to increased GPX4 ubiquitination."
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"These findings support our conclusion that GBP2-OTUD5 interactions mediate increased GPX4 ubiquitination, though further studies are required to fully elucidate the underlying mechanism."
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