Identification of NAP1, a Regulatory Subunit of IκB Kinase-Related Kinases That Potentiates NF-κB Signaling

By F. Fujita, Y. Taniguchi, Takashi Kato, Yasuko Narita, A. Furuya, Tatsuhiro Ogawa, H. Sakurai, T. Joh, M. Itoh, M. Delhase and 2 more. Molecular and Cellular Biology, 2003

166 citations recorded by the source corpus.

Subfields: Cancer Research, Immunology, Oncology

View Paper: https://www.semanticscholar.org/paper/fabed6fbffc72090efb6b7471eed0730bee6091e

How researchers see this paper

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In Cancer Research

1. H. Nakano
2. Lin-Feng Chen
3. W. Greene
4. N. Perkins
5. S. Ghosh
6. M. Hayden

In Immunology

1. H. Nakano
2. Lin-Feng Chen
3. W. Greene
4. N. Perkins
5. S. Ghosh
6. M. Hayden

In Oncology

1. Lin-Feng Chen
2. W. Greene

Citations in the corpus

• Transient and Selective NF-κB p65 Serine 536 Phosphorylation Induced by T Cell Costimulation Is Mediated by IκB Kinase β and Controls the Kinetics of p65 Nuclear Import 1 (2004, background): “Serine 536 can be phosphorylated by the IKKs (29), but there is also evidence for phosphorylation by calmodulin-dependent protein kinase IV (32) or the NF- B-activating kinase/NF- B-activating kinase-associated protein 1 complex (33).”
• Shaping the nuclear action of NF-κB (2004, methodology): “NAK potentiates the NF-κB activity by phosphorylating serine 536 (Ref”