β-TrCP binding and processing of NF-κB2/p100 involve its phosphorylation at serines 866 and 870
By Chunyang Liang, Minying Zhang, Shao-Cong Sun. 2006
107 citations recorded by the source corpus.
Subfields: Cancer Research, Immunology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/687203090328fc2b806c7528ef4ed38e7bc66ec3
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In Cancer Research
In Immunology
In Molecular Biology
Citations in the corpus
- The Regulation of NF-κB Subunits by Phosphorylation (2016, background): “These phosphorylation events lead to recruitment of βTrCP [33,34,40] resulting in K48-linked ubiquitination of p100 on lysine 856 [41].”
- Post-translational modifications regulating the activity and function of the nuclear factor kappa B pathway (2006, methodology): “Interestingly, this same cysteine residue is also required for some natural product-mediated inhibition of IKKb (Liang et al., 2006b).”