NF-κB-Inducing Kinase Regulates the Processing of NF-κB2 p100

By G. Xiao, E. Harhaj, Shao-Cong Sun. 2001

787 citations recorded by the source corpus.

Subfields: Cancer Research, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/12cb0399f8d31bac5540aac6df71326cba1655a4

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cancer Research

1. S. Ghosh
2. N. Perkins
3. M. Hayden
4. M. Karin
5. J. Moscat
6. Alexander Hoffmann
7. M. Diaz-Meco
8. A. Duran

In Molecular Biology

1. M. Hayden
2. S. Ghosh
3. N. Perkins
4. M. Karin
5. D. Vučić
6. Bruce J. Aronow
7. Anil G. Jegga
8. J. Moscat

Citations in the corpus

• The NF-κB pathway (2005, background): “These receptors cause the sequential activation of NF- B-inducing kinase (NIK) and IKK (Xiao et al., 2001).”
• NF-κB and the immune response (2006, background): “TRAF3 negatively regulates NIK, and undergoes signal-dependent degradation resulting in the activation of the non-canonical pathway (Liao et al., 2004).”
• BAFF-induced NEMO-independent processing of NF-κB2 in maturing B cells (2002, background): “Ubiquitin-dependent processing of p100 is reported to be dependent on NI”
• Activation of IKKα target genes depends on recognition of specific κB binding sites by RelB:p52 dimers (2004, background): “Recently, a second NF-kB activation pathway based on regulated processing of the NF-kB2/p100 precursor protein was identified (Senftleben et al, 2001; Xiao et al, 2001 ).”
• Essential role of RelA Ser311 phosphorylation by ζPKC in NF‐κB transcriptional activation (2003, background): “…or B cells with BAFF, the IKKa subunit of the IKK complex phosphorylates p100, triggering its processing and the release of the RelB±p52 complex that now is free to enter the nucleus (Senftleben et al., 2001; Xiao et al., 2001; Claudio et al., 2002; Dejardin et al., 2002; Kayagaki et al., 2002).”
• Signaling via the NFκB system (2016, background): “Processing is tightly controlled by a processing-suppressive region in the C-terminal portion of the p100 protein and disruption of this domain leads to constitutive p100 processing.(82,92) p100 that does not form p52 is free to form highermolecular-weight inhibitors of NFκB (IκBδ), and therefore ti”