The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
HSP70 mediates degradation of the p65 subunit of nuclear factor κB to inhibit inflammatory signaling
Abstract
The heat shock protein HSP70 prevents excessive inflammation in mice by mediating the degradation of an NF-κB subunit.
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BAG-1 was previously described to degrade NF-kB p65, inhibiting inflammatory signaling in dendritic cells.
“BAG-1 was previously described to degrade NF-kB p65, inhibiting inflammatory signaling in dendritic cells29.”
From TNF-alpha-induced microglia activation requires miR-342: Impact on NF-kB signaling and neurotoxicity (2020) · cites this paper as [29]
Tanaka et al. described that BAG-1, when associated with HSP70, can promote NF-kB p65 degradation in LPS-treated dendritic cells.
“Tanaka et al.29 described that BAG-1, when associated with HSP70, can promote NF-kB p65 degradation in LPS-treated dendritic cells.”
From TNF-alpha-induced microglia activation requires miR-342: Impact on NF-kB signaling and neurotoxicity (2020) · cites this paper as [29]
Mouse dendritic cells deficient in either HSP70 or BAG-1 had more nuclear p65 and produced more pro-inflammatory cytokines than wild-type dendritic cells, implicating BAG-1 as a negative regulator of pro-inflammatory NF-kB signaling in dendritic cells.
“The authors reported that mouse dendritic cells deficient in either HSP70 or BAG-1 had more nuclear p65 and produced more pro-inflammatory cytokines than did wild-type dendritic cells29, implicating BAG-1 as a negative regulator of pro-inflammatory NF-kB signaling in dendritic cells.”
From TNF-alpha-induced microglia activation requires miR-342: Impact on NF-kB signaling and neurotoxicity (2020) · cites this paper as [29]
BAG-1 was the only candidate found to meet both criteria of being downregulated and previously described as a repressor of NF-kB.
“BAG-1 was the only candidate found to meet both criteria29 (Supplementary Table 4).”
From TNF-alpha-induced microglia activation requires miR-342: Impact on NF-kB signaling and neurotoxicity (2020) · cites this paper as [29]
Citations
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Protein degradation and protection against misfolded or damaged proteins.
Goldberg, A. L. (2003) · Nature · doi:10.1038/nature02263 · Cited by 2,088
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TNF-alpha-induced microglia activation requires miR-342: Impact on NF-kB signaling and neurotoxicity
Brás, J. P., Bravo, J., Freitas, J., Barbosa, M. A., Santos, S. G., Summavielle, T., & Almeida, M. I. (2020) · Cell Death & Disease · doi:10.1038/s41419-020-2626-6 · Cited by 236
Metadata
- Authors
- Tanaka, T., Shibazaki, A., Ono, R., & Kaisho, T.
- Affiliations
- Japan Science and Technology Agency (JP)
- RIKEN Center for Integrative Medical Sciences (JP)
- Corresponding author
- Tanaka, Takashi
- Kaisho, Tsuneyasu
- Venue
- Science Signaling
- Published
- 2014-12-16
- Volume
- 7
- Issue
- 356
- Pages
- ra119-ra119
- ISSN
- 1937-9145 (ISSN-L)
- 1945-0877
- OpenAlex
- W2021125416
- Cited by
- 66
- References
- 1
- Citations by year
- 2026: 1 · 2025: 10 · 2024: 2 · 2023: 4 · 2022: 5 · 2021: 5 · 2020: 6 · 2019: 9 · 2018: 6 · 2017: 8 · 2016: 8 · 2015: 2
- FWCI
- 1.98
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science Signaling (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Japan Society for the Promotion of Science (26293106, 23590577)
- Precursory Research for Embryonic Science and Technology
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Keywords
- HSP70, PDLIM2, NF-κB p65, E3 ubiquitin ligase, proteasome, protein degradation, inflammatory signaling, dendritic cells, lipopolysaccharide, BAG-1, chaperone activity, inflammatory cytokines, bacterial infection
- MeSH terms
- Animals, Dendritic Cells, DNA-Binding Proteins, Humans, Inflammation, Lipopolysaccharides, Microfilament Proteins, Transcription Factors, Signal Transduction, Protein Folding, HSP70 Heat-Shock Proteins, Ubiquitin-Protein Ligases, Proteasome Endopeptidase Complex, Adaptor Proteins, Signal Transducing, Mice, Transcription Factor RelA, HEK293 Cells, Proteolysis, LIM Domain Proteins
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