Ubiquitylation in innate and adaptive immunity
By V. Bhoj, Zhijian J. Chen. Nature, 2009
633 citations recorded by the source corpus.
Subfields: Cancer Research, Immunology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/b8654faa6a3325d7578120d4dd3f8235e4d0ad5a
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Citations in the corpus
- The role of pattern-recognition receptors in innate immunity: update on Toll-like receptors (2010, background): “Thus, the K63 polyubiquitin chains might be responsible for recruiting TAK1 to form a complex with IKK, thus allowing TAK1 to phosphorylate IKKβ through its close proximity to the IKK complex, which leads to NF-κB activation via phosphorylation and subsequent degradation of IκB protein”
- The outs and the ins of sphingosine-1-phosphate in immunity (2011, neutral): “This liberates NF-κB (a dimeric transcription factor consisting of p65 and p50 subunits), which then enters the nucleus and regulates the transcription of its target gene”
- A Proteome-wide, Quantitative Survey of In Vivo Ubiquitylation Sites Reveals Widespread Regulatory Roles (2011, background): “(57), and about 100 deubiquitylases reverse this modifica-”
- IAPs: from caspase inhibitors to modulators of NF-κB, inflammation and cancer (2010, background): “Importantly, both these pathways are Ub-dependent signal transduction cascades in which Ub ligases, Ub receptors and deubiquitylating enzymes (DUBs) build up, recognize and remove Ub signals, allowing the temporally controlled assembly of protein complexes that lead to the activation of kinases that”
- SPHINGOSINE-1-PHOSPHATE: A MISSING COFACTOR FOR THE E3 UBIQUITIN LIGASE TRAF2 (2010, neutral): “One of the best characterized examples is the non-degradative Lys 63 polyubiquitination of RIP1 that serves as a scaffold to recruit proteins containing specific ubiquitin binding domains, resulting in recruitment and phosphorylation of the IKK complex leading to the activation of NF-κ B 5,14,15.”
- Toll-like receptors in antiviral innate immunity (2013, background): “Ubiquitination, especially that promotes the formation of Lys63-linked ubiquitin chains, plays an important role in activating immune signaling pathways including those through the TLRs [211].”
- Type I interferon inhibits interleukin-1 production and inflammasome activation. (2011, background): “As seen with TRIM25, the ubiquitination system plays an important role in the regulation of IFN signal transduction (Bhoj and Chen, 2009).”