The DOI matches its Crossref record; 25 of the 25 references it cites were found in a registry or an index.
Positive and Negative Regulation of IκB Kinase Activity Through IKKβ Subunit Phosphorylation
Abstract
IκB [inhibitor of nuclear factor κB (NF-κB)] kinase (IKK) phosphorylates IκB inhibitory proteins, causing their degradation and activation of transcription factor NF-κB, a master activator of inflammatory responses. IKK is composed of three subunits—IKKα and IKKβ, which are highly similar protein kinases, and IKKγ, a regulatory subunit. In mammalian cells, phosphorylation of two sites at the activation loop of IKKβ was essential for activation of IKK by tumor necrosis factor and interleukin-1. Elimination of equivalent sites in IKKα, however, did not interfere with IKK activation. Thus, IKKβ, not IKKα, is the target for proinflammatory stimuli. Once activated, IKKβ autophosphorylated at a carboxyl-terminal serine cluster. Such phosphorylation decreased IKK activity and may prevent prolonged activation of the inflammatory response.
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Cites
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Self-citationIKK-1 and IKK-2: Cytokine-Activated IκB Kinases Essential for NF-κB Activation
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Cited by
Phosphorylation meets ubiquitination: the control of NF-κB activity
Karin, M., & Ben-Neriah, Y. (2000) · Annual Review of Immunology · doi:10.1146/annurev.immunol.18.1.621 · Cited by 4,766
Self-citationShared Principles in NF-κB Signaling
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NF-κB: a key role in inflammatory diseases
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Hayden, M. S., & Ghosh, S. (2004) · Genes & Development · doi:10.1101/gad.1228704 · Cited by 3,842
Missing Pieces in the NF-κB Puzzle
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Self-citation
Metadata
- Authors
- Delhase, M., Hayakawa, M., Chen, Y., & Karin, M.
- Venue
- Science
- Published
- 1999-04-09
- Volume
- 284
- Issue
- 5412
- Pages
- 309-313
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1661180389
- Cited by
- 852
- References
- 25
- FWCI
- 24.81
- Type
- journal article
- Language
- en
- Open access
- closed
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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