The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.
A pervasive role of ubiquitin conjugation in activation and termination of IκB kinase pathways
Open accessAbstract
The nuclear factor (NF)-kappaB pathway is a paradigm for gene expression control by ubiquitin-mediated protein degradation. In stimulated cells, phosphorylation by the IkappaB kinase (IKK) complex primes NF-kappaB-inhibiting IkappaB molecules for lysine (Lys)-48-linked polyubiquitination and subsequent destruction by the 26S proteasome. However, recent studies indicate that the ubiquitin (Ub) system controls NF-kappaB pathways at many levels. Ub ligases are activated by different upstream signalling pathways, and they function as central regulators of IKK and c-Jun amino-terminal kinase activation. The assembly of Lys 63 polyUb chains provides docking surfaces for the recruitment of IKK-activating complexes, a reaction that is counteracted by deubiquitinating enzymes. Furthermore, Ub conjugation targets upstream signalling mediators as well as nuclear NF-kappaB for post-inductive degradation to limit the duration of signalling.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Extracellular inflammatory signals including lipopolysaccharide (LPS), pro-inflammatory cytokines, reactive oxygen species, advanced glycation end products, and oxidized low-density lipoprotein trigger the phosphorylation of IKKβ, which in turn phosphorylates IκBα for ubiquitination and degradation by proteasome [13–18].”
From Edible blue-green algae reduce the production of pro-inflammatory cytokines by inhibiting NF-κB pathway in macrophages and splenocytes (2013) · cites this paper as [15]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Hayden, M. S., & Ghosh, S. (2004) · Genes & Development · doi:10.1101/gad.1228704 · Cited by 3,842
The two NF-κB activation pathways and their role in innate and adaptive immunity
Bonizzi, G., & Karin, M. (2004) · Trends in Immunology · doi:10.1016/j.it.2004.03.008 · Cited by 2,535
TAK1 is a ubiquitin-dependent kinase of MKK and IKK
Wang, C., Deng, L., Hong, M., Akkaraju, G. R., Inoue, J.-I., & Chen, Z. J. (2001) · Nature · doi:10.1038/35085597 · Cited by 2,125
De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-κB signalling
Wertz, I. E., O’Rourke, K. M., Zhou, H., Eby, M. T., Aravind, L., Seshagiri, S., Wu, P., Wiesmann, C., Baker, R. T., Boone, D. L., et al. (2004) · Nature · doi:10.1038/nature02794 · Cited by 1,889
Deng, L., Wang, C., Spencer, E., Yang, L., Braun, A., You, J., Slaughter, C., Pickart, C., & Chen, Z. J. (2000) · Cell · doi:10.1016/s0092-8674(00)00126-4 · Cited by 1,872
Failure to Regulate TNF-Induced NF-κB and Cell Death Responses in A20-Deficient Mice
Lee, E. G., Boone, D. L., Chai, S., Libby, S. L., Chien, M., Lodolce, J. P., & Ma, A. (2000) · Science · doi:10.1126/science.289.5488.2350 · Cited by 1,409
TRAF6 deficiency results in osteopetrosis and defective interleukin-1, CD40, and LPS signalingPreprint
Lomaga, M. A., Yeh, W., Sarosi, I., Duncan, G. S., Furlonger, C. L., Ho, A. P., Morony, S., Capparelli, C., Van, G. Y., Kaufman, S., et al. (1999) · Genes & Development · doi:10.1101/gad.13.8.1015 · Cited by 1,265
Ninomiya‐Tsuji, J., Kishimoto, K., Hiyama, A., Inoue, J., Cao, Z., & Matsumoto, K. (1999) · Nature · doi:10.1038/18465 · Cited by 1,187
The ubiquitin-modifying enzyme A20 is required for termination of Toll-like receptor responses
Boone, D. L., Turer, E. E., Lee, E. G., Ahmad, R., Wheeler, M. T., Tsui, C., Hurley, P. J., Chien, M., Chai, S., Hitotsumatsu, O., et al. (2004) · Nature Immunology · doi:10.1038/ni1110 · Cited by 1,104
The tumour suppressor CYLD negatively regulates NF-κB signalling by deubiquitination
Kovalenko, A., Chable-Bessia, C., Cantarella, G., Israël, A., Wallach, D., & Courtois, G. (2003) · Nature · doi:10.1038/nature01802 · Cited by 1,018
Flagged first, then by citations
Cited by
Sorted by citations
Items 101–128 of 128
Ubiquitin‐Independent Mechanisms of Substrate Recognition and Degradation by the Proteasome
Hoyt, M. A., & Coffino, P. (2007) · Wiley eBooks · doi:10.1002/9783527620234.ch5 · Cited by 2
Miao, Y., Yuan, Y., Qian, L., Yu, Y., Cui, Q., Zhang, T., Zhang, R., Zhao, Q., Li, Z., Miao, A., et al. (2026) · Cell Insight · doi:10.1016/j.cellin.2026.100322 · Cited by 1
Lee, H.-S. (2009) · Journal of Life Science · doi:10.5352/jls.2009.19.1.021 · Cited by 1
A causal role of ATM- and NEMO-dependent NF-κB activation in DNA damage-induced senescence and aging
Zhao, J. (2016) · D-Scholarship@Pitt (University of Pittsburgh) · Cited by 1
Characterization and interactions of Tbx2
Paxton, C. N. (2006) · doi:10.31274/rtd-180813-17496
Ubiquitin-Mediated Regulation of Protein Kinases in NFκB Signaling
Xu, M., & Chen, Z. J. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374145-5.00083-8
Characterization of the Ubc13-Mms2 Lysine-63-linked ubiquitin conjugating complex
Pastushok, L. (2006) · University Library - University of Saskatchewan (University of Saskatchewan)
Parkinson disease: identifying different players sharing a common principle
Farooqı, A. A., Arshad, S., Fayyaz, S., Abbas, S., & Bhatti, S. (2011) · Research in Biotechnology
Deubiquitinating Enzymes, Cell Proliferation, and Cancer
Baker, R. T. (2006) · Wiley eBooks · doi:10.1002/9783527620227.ch9
Roythorne, A. (2014) · Northumbria Research Link (Northumbria University)
Role of the COP9 signalosome and IKK complexes in atherosclerosis
Asare, Y., & Bernhagen, J. (2013) · RWTH Publications (RWTH Aachen)
The Regulatory Role of Interleukin-1 Receptor Associated Kinase M in Toll-Like Receptor Signaling
Zhou, H. (2016) · EngagedScholarship @ Cleveland State University (Cleveland State University)
Regulation of the transcription factor p63 by [beta]TrCP
Gallegos, J. R. (2008) · doi:10.6083/m4513w4d
Paul, M. (2016) · Lu Zone Ul (Laurentian University)
Ubiquitin Signaling and Cancer Pathogenesis
Haglund, K., & Đikić, I. (2007) · Wiley eBooks · doi:10.1002/9783527619320.ch1c
Deubiquitinating Enzymes, Cell Proliferation, and Cancer
Baker, R. T. (2007) · Wiley eBooks · doi:10.1002/9783527619320.ch9b
Tantoh, A. L. A. (2014) · Open University of Cape Town (University of Cape Town)
Étude de la régulation de la protéine mitochondriale MAVS au cours de l’immunité innée antivirale
Castanier, C. (2011) · theses.fr (ABES) · doi:10.70675/1ad655f2z8bf1z4a47zba70z55e456a89d8a
Le rôle de l’ubiquitination et des endomembranes dans l’activation du facteur de transcription NF-κB
Zemirli, N. (2014) · theses.fr (ABES) · doi:10.70675/098ff617z3ed6z43caz9f51z004f55dce561
Rôle oncogénique des fragments de p65/RelA Nf-kB générés par l'activité de RIPK3
Latreche-Carton, C. (2017) · theses.fr (ABES) · doi:10.70675/fc5745f5z890cz47dcz86dez3f5b29420b57
Characterization of protein-protein interactions mediated by the IKK complex
Moro, S. (2022) · theses.fr (ABES) · doi:10.70675/340a028ezd105z4e02z83b4z27f3cd5ea5eb
The role of HECT-type E3 ubiquitin ligases in inflammation
Wang, Z., Wang, P., Xie, H., You, Z., Liu, X., Cao, F., & Yao, S. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1810360
Metadata
- Authors
- Krappmann, D., & Scheidereit, C.
- Affiliations
- Max Delbrück Center (DE)
- Corresponding author
- Scheidereit, Claus
- Venue
- The EMBO Reports
- Published
- 2005-04-01
- Volume
- 6
- Issue
- 4
- Pages
- 321-326
- ISSN
- 1469-221X (ISSN-L)
- 1469-3178
- PMC
- PMC1299290
- OpenAlex
- W2169463874
- Cited by
- 128
- References
- 41
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 3 · 2023: 1 · 2022: 2 · 2021: 1 · 2020: 2 · 2019: 2 · 2017: 2 · 2016: 5 · 2015: 3 · 2014: 6 · 2013: 5 · 2012: 5
- FWCI
- 1.47
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- EMBO Reports (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Site cant be reached (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Keywords
- ubiquitin conjugation, NF-κB signaling, IκB kinase, IκB degradation, Lys63-linked polyubiquitination, E3 ubiquitin ligase, deubiquitinase, c-Jun N-terminal kinase, 26S proteasome, signal termination
- MeSH terms
- Enzyme Activation, Gene Expression Regulation, Humans, Models, Biological, Signal Transduction, NF-kappa B, Protein Serine-Threonine Kinases, Ubiquitin, I-kappa B Kinase
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
