ArticleChemical communications (Cambridge, England)2021
Site-selective incorporation of phosphorylated tyrosine into the p50 subunit of NF-κB and activation of its downstream gene CD40.
Article in Chemical communications (Cambridge, England), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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Who cites it
5 citing papers in PubMed, 7 citations in OpenAlex.
- Alteration of CD40 Protein Expression by Tyrosine Phosphorylation of the NF-κB p50 Subunit.Chembiochem : a European journal of chemical biology · 2026Article
- Biological Regulation StudiedAccounts of chemical research · 2025Article
- Genetic Encoding of Phosphorylated Amino Acids into Proteins.Chemical reviews · 2024Review
- Elongation Factor P Modulates the Incorporation of Structurally Diverse Noncanonical Amino Acids intoJournal of the American Chemical Society · 2023Article
- Site-Selective Tyrosine Phosphorylation in the Activation of the p50 Subunit of NF-κB for DNA Binding and Transcription.ACS chemical biology · 2023Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The NF-κB family of transcriptional activators is responsible for the expression of numerous genes that control key functions such as cell development and survival. Subunit p50 has been studied extensively and is known to include 13 tyrosines, but the extent and pattern of tyrosine phosphorylation that accompanies p50 function has not been defined in the literature, especially at the level of selectivity of gene expression. In this study, phosphorylated tyrosine (pTyr) was site-selectively incorporated into the p50 subunit using an
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Registered trials
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