IndraLab

Statements

USP16 binds IKBKB. 11 / 11
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"Depletion of the NBD disrupted the interaction of USP16 with both IKKbeta and IKKalpha (XREF_FIG), which further suggests that USP16 and NEMO may competitively bind to IKKbeta and IKKalpha."
| PMC
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"Co-IP indicated that the UBP14 domain is indispensable for USP16 binding to IKKbeta (XREF_FIG)."
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sparser
"Under TNF-α stimulation, coimmunoprecipitation (co-IP) assays demonstrated that USP16 physically associated with IKKβ but not with p105 or IκBα in cotransfected HEK293T cells ( xref )."
| PMC
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"Under TNF-alpha stimulation, coimmunoprecipitation (co-IP) assays demonstrated that USP16 physically associated with IKKbeta but not with p105 or IkappaBalpha in cotransfected HEK293T cells (XREF_FIG)."
| PMC
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"In transfected HEK293T cells, the results of co-IP revealed that the association between IKKbeta and USP16 was dependent on the NBD of IKKbeta (XREF_FIG)."
| PMC
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"USP16 selectively interacts with IKKbeta and IKKalpha."
| PMC
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"To further confirm the interaction between endogenous USP16 and IKKbeta, we generated USP16 fl mice and crossed them with Lyz2-Cre mice to delete USP16 in myeloid cells, producing myeloid cell specific USP16-KO (USP16 MKO) mice."
| PMC
sparser
"Co-IP indicated that the UBP14 domain is indispensable for USP16 binding to IKKβ ( xref )."
| PMC
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"By comparison with NEMO, we identified five conserved amino acids that are important for binding between USP16 and IKKbeta, as suggested by the disappearance of the signal upon deletion of the sequence (XREF_FIG)."
| PMC
sparser
"To further confirm the interaction between endogenous USP16 and IKKβ, we generated USP16 fl mice and crossed them with Lyz2 -Cre mice to delete USP16 in myeloid cells, producing myeloid cell–specific USP16-KO (USP16 MKO ) mice (fig."
| PMC
sparser
"The co-IP results revealed continuous interaction between endogenous USP16 and IKKβ in BMDMs, and LPS stimulation did not promote or suppress this association ( xref )."
| PMC