IndraLab

Statements

YOD1 binds NLRP3. 18 / 18
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"YOD1 interacted with NLRP3."
38789414
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"To verify the MS results and determine whether YOD1 interacted with other NLRP3 inflammasome molecules, we overexpressed Myc-tagged YOD1 with Flag-tagged NLRP3 or Flag-tagged Caspase-1 or Flag-tagged ASC in HEK293T cells, respectively (Figs. xref and xref )."
38789414
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"Deubiquitinase YOD1 interacts with NLRP3, leading to the inhibition of NLRP3 inflammasome activation by removing a specific ubiquitin chain [ xref ]."
39201704
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"As expected, the interaction between YOD1 and NLRP3 remained robust after mutation (Fig. 7B, C)."
38789414
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"Our previous results demonstrated that YOD1 specially interacted with NLRP3 and inhibited NLRP3 inflammasome activation, however, the functional relationship between YOD1, NLRP3 inflammasome and blood clotting remained unknown."
38789414
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"As expected, the interaction between YOD1 and NLRP3 remained robust after mutation (Fig. xref )."
38789414
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"Using MS, co-IP and co-immunofluorescence data, we identified NLRP3 as a putative target protein and YOD1 specifically interacted with NLRP3, but not with ASC and Caspase-1."
38789414
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"In our study, we showed that YOD1 interacted with NLRP3 and suppressed the NLRP3 inflammasome activation."
38789414
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"YOD1 interacted with NLRP3 to remove K33-linked ubiquitination of NLRP3 based on its deubiquitinating enzyme activity and specifically inhibited expression of NLRP3 as well as activation of NLRP3 inflammasome."
38789414
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"Although the mutation of YOD1 could interact with NLRP3, we found that the effect of YOD1 on NLRP3 ubiquitination was dependent on the deubiquitinase catalytic activity."
38789414
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"In methicillin-resistant Staphylococcus aureus (MRSA)-induced sepsis, YOD1 interacts with the NLRP3 inflammasome to remove K33-linked ubiquitin chains, effectively inhibiting inflammasome activation and reducing disseminated intravascular coagulation (DIC) and inflammatory responses, thereby providing a protective mechanism [ xref ]."
40555982
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"YOD1, a deubiquitinating enzyme, interacts with NLRP3 and specifically inhibits its expression and the activation of the NLRP3 inflammasome."
40766066
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"In vitro co-IP experiments indicated that YOD1 only interacted with NLRP3, but not with Caspase-1 and ASC."
38789414
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"Mechanically, upon methicillin-resistant Staphylococcus aureus (MRSA) infection in macrophages, YOD1 interacted with NLRP3 to specifically remove its K33-linked ubiquitination, subsequently inhibiting NLRP3 inflammasome activation and coagulation."
38789414
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"Furthermore, endogenous co-IP showed that YOD1 and NLRP3 formed a complex in both BMDMs and PMs after MRSA infection (Figs. xref and xref )."
38789414
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"These findings indicated that YOD1 specifically interacted with NLRP3."
38789414
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"Taken together, these results showed that NLRP3 interacted with YOD1 through its NACHT and LRR domains."
38789414
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"Although YOD1 interacted with NLRP3, the functional relationship between YOD1 and NLRP3 inflammasome remains unknown."
38789414