IndraLab

Statements

CYLD binds fbxw1. 3 / 3
| 1 2
reach
"Notably, among the four reported IKK phosphorylation sites [XREF_BIBR] (S418, S422, S432 and S436) that may create two putative beta-TRCP binding motifs, mutating both phospho-degrons of CYLD abolished the interaction between CYLD and beta-TRCP."
24961988
sparser
"Notably, among the four reported IKK phosphorylation sites [ xref ] (S418, S422, S432 and S436) that may create two putative β-TRCP binding motifs (Figure xref ), mutating both phospho-degrons of CYLD abolished the interaction between CYLD and β-TRCP (Figures xref )."
24961988
sparser
"To demonstrate that CYLD is a bona-fide substrate of SCF β-TRCP , we next examined whether the interaction of β-TRCP with CYLD is through the substrate recognition domain of β-TRCP."
24961988