IndraLab

Statements

TRAF2 binds OTUD7B. 8 / 8
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"Deletion of the UBA domain resulted in complete loss of interaction between OTUD7b and TRAF2."
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"In addition, loss of the active catalytic site C194 showed reduction in binding of OTUD7b to TRAF2 upon TNF stimulation, presumably by disruption of the TRAF binding region spanning the catalytic domain of OTUD7b."
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"Immunoprecipitation experiments showed that the interaction between TRAF2 and OTUD7b was completely abolished by deletion of the N-terminal UBA domain."
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"Deletion of the UBA domain resulted in complete loss of interaction between OTUD7b and TRAF2."
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"Our co-immunoprecipitation experiments showed induced interaction of OTUD7b with TRAF2 upon TNF stimulation (Fig. xref ), Since proteasomal degradation of the substrate is mediated either by K11- or K48-linked polyubiquitin chains, we next determined K48- and K11-linked polyubiquitin chains on TRAF2."
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"In addition, loss of the active catalytic site C194 showed reduction in binding of OTUD7b to TRAF2 upon TNF stimulation, presumably by disruption of the TRAF binding region spanning the catalytic domain of OTUD7b.The in vivo function of OTUD7b in infectious diseases has been sparsely studied."
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"Immunoprecipitation experiments showed that the interaction between TRAF2 and OTUD7b was completely abolished by deletion of the N-terminal UBA domain."
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sparser
"In line with our data after long-term exposure to TNF (Fig. xref ), we observed (i) enhanced proteasomal degradation of TRAF2 (Fig. xref ), (ii) TNF-induced OTUD7b-TRAF2 interaction (Fig. xref ) (iii) increased levels of K48-linked polyubiquitin chains on TRAF2 (Fig. xref ), (iv) interaction of TRAF2 with RIPK1 and OTUD7b with RIPK1 (Fig. xref ), and consequently, (v) reduced K63-linked polyubiquitination of RIPK1 (Fig. xref )."
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