The DOI matches its Crossref record; 20 of the 21 references it cites were found in a registry or an index.
Ubiquitin, TAK1 and IKK: is there a connection?
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“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 [14]
Citations
Cites
Baeuerle, P. A., & Baltimore, D. (1996) · Cell · doi:10.1016/s0092-8674(00)81318-5 · Cited by 3,002
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
Self-citationDe-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
Self-citationIdentification of a Member of the MAPKKK Family as a Potential Mediator of TGF-β Signal Transduction
Yamaguchi, T., Shirakabe, K., Shibuyà, H., Irie, K., Oishi, I., Ueno, N., Taniguchi, T., Nishida, E., & Matsumoto, K. (1995) · Science · doi:10.1126/science.270.5244.2008 · Cited by 1,344
Ninomiya‐Tsuji, J., Kishimoto, K., Hiyama, A., Inoue, J., Cao, Z., & Matsumoto, K. (1999) · Nature · doi:10.1038/18465 · Cited by 1,187
The Death Domain Kinase RIP Mediates the TNF-Induced NF-κB Signal
Kelliher, M. A., Grimm, S., Ishida, Y., Kuo, F., Stanger, B. Z., & Leder, P. (1998) · Immunity · doi:10.1016/s1074-7613(00)80535-x · Cited by 1,102
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
CYLD is a deubiquitinating enzyme that negatively regulates NF-κB activation by TNFR family members
Trompouki, E., Hatzivassiliou, E., Tsichritzis, T., Farmer, H., Ashworth, A., & Mosialos, G. (2003) · Nature · doi:10.1038/nature01803 · Cited by 964
Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-κB
Brummelkamp, T. R., Nijman, S. M. B., Dirac, A. M. G., & Bernards, R. (2003) · Nature · doi:10.1038/nature01811 · Cited by 947
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Items 101–116 of 116
Zhao, H., Chen, Y., Wang, Z., Zhang, Q., & Yu, H. (2019) · Journal of Ocean University of China · doi:10.1007/s11802-019-3683-2 · Cited by 5
Xie, Y., Lei, K., He, J., & Wei, Y. (2022) · Fishes · doi:10.3390/fishes7040173 · Cited by 3
Lluis, J. M., Nachbur, U., Cook, W. D., Gentle, I. E., Moujalled, D. M., Moulin, M., Wong, W. W.-L., Khan, N. R., Chau, D., Callus, B. A., et al. (2010) · PLoS ONE · doi:10.1371/annotation/4e35cd59-c68f-4020-addb-18eb896112c5 · Cited by 2
Multiple Players in the Mechanical Control of T Cell Quiescence
Neama, A. F., Looi, C. Y., & Wong, W. F. (2017) · InTech eBooks · doi:10.5772/intechopen.68869 · Cited by 1
Regulation of HTLV-I oncoprotein Tax by PDLIM2
Yan, P. (2010) · D-Scholarship@Pitt (University of Pittsburgh)
Rotavirus NSP1 is an interferon system antagonist
Graff, J. W. (2008) · Montana State University ScholarWorks (Montana State University)
Calmodulin mediated regulation of NF-kappaB in lymphocytes
Edin, S. (2008) · KTH Publication Database DiVA (KTH Royal Institute of Technology)
Functional roles of transforming growth factor activated Kinase-1 (TAK1) in skin wound healing
Tan, S. H. (2011) · DR-NTU (Nanyang Technological University) · doi:10.32657/10356/43713
Understanding the biological functions of POPX2 phosphatase through its interactome
Kim, P. (2019) · DR-NTU (Nanyang Technological University) · doi:10.32657/10356/136952
Immune Homeostasis: Activation and Downregulation of NF-κB
De, A. (2015) · Springer theses · doi:10.1007/978-3-319-14965-3_1
Särchen, V. (2022) · Publication Server of Goethe University Frankfurt am Main (Goethe University Frankfurt) · doi:10.21248/gups.70951
A Novel Motif in HIV-1 Nef that Regulates MIP-1β Chemokine Release in Macrophages: A Dissertation
Dai, L. (2010) · eScholarship@UMassChan · doi:10.13028/gwmf-s887
Tang, M., Cao, H., Ma, Y., Yao, S., Wei, X., Tan, Y., liu, F., Peng, Y., & Fan, N. (2024) · Figshare · doi:10.6084/m9.figshare.26341926
Characterization of protein-protein interactions mediated by the IKK complex
Moro, S. (2022) · theses.fr (ABES) · doi:10.70675/340a028ezd105z4e02z83b4z27f3cd5ea5eb
Caspase-14 recognizes and processes IL-1β in epithelial cells to drive anti-bacterial IgG productionPreprint
Ma, M., Wang, L., & Ge, B. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.04.14.717951
Ajike, R. A., Olayiwola, P. A., Afolabi, O. A., Lawal, O. A., Hezekiah, O. S., Olapade, O. S., Akano, S. A., Ikotun, A. E., Adekunleoke, P. P., Oyekunle, O. S., et al. (2026) · Comparative Clinical Pathology · doi:10.1007/s00580-026-03834-7
Metadata
- Authors
- Chen, Z. J., Bhoj, V, & Seth, R. B.
- Affiliations
- Howard Hughes Medical Institute (US)
- Corresponding author
- Chen, Z J
- ORCID
- Bhoj, V
- Venue
- Cell Death & Differentiation
- Published
- 2006-02-17
- Volume
- 13
- Issue
- 5
- Pages
- 687-692
- ISSN
- 1350-9047 (ISSN-L)
- 1476-5403
- OpenAlex
- W1992744008
- Cited by
- 115
- References
- 21
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 4 · 2023: 1 · 2022: 6 · 2021: 3 · 2020: 5 · 2019: 4 · 2018: 1 · 2017: 5 · 2016: 2 · 2015: 5 · 2014: 5 · 2013: 4 · 2012: 10
- FWCI
- 0.97
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Cell Death and Differentiation (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Burroughs Wellcome Fund
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM063692, R01 GM63692)
- National Institute of Allergy and Infectious Diseases (R01-AI 60919, R01AI060919)
- 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
- NF-κB signaling, TAK1, IKK activation, ubiquitination, TRAF6, E3 ubiquitin ligase, polyubiquitin chains, IκB kinase, TNF signaling, IL-1β signaling
- MeSH terms
- MAP Kinase Kinase Kinase 7, Animals, Enzyme Activation, Gene Expression Regulation, Immunity, Active, Immunity, Innate, Interleukin-1, Models, Biological, Tumor Necrosis Factor-alpha, Signal Transduction, MAP Kinase Kinase Kinases, Ubiquitin, I-kappa B Kinase
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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.
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