IndraLab

Statements

USP14 binds IDO1. 6 / 6
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"The interaction between USP14 and IDO1 was confirmed using endogenous reciprocal IP and glutathione-S-transferase (GST) pulldown assays (Fig.  xref , and Supplementary Fig.  xref )."
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"Thus, inhibitors targeting the UBL domain would specifically abolish the interaction between USP14 and IDO1."
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"These results indicated that USP14 interacted with IDO1 and was involved in the regulation of IDO1 protein levels in CRC."
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"Furthermore, our results demonstrate that the UBL domain of USP14 is necessary for the interaction between USP14 and IDO1."
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"Co-immunoprecipitation (Co-IP) showed that USP14 selectively interacted with IDO1 but not with other enzymes involved in TRP metabolism, including IDO2, tryptophan 2,3 dioxygenase (TDO2), and arylformamidase (AFMID) (Fig.  xref )."
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"These results suggested that USP14 interacted with IDO1 and increased the stability of IDO1 protein in CRC cells."
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