Manipulating Tyrosine Phosphorylation by Heterobifunctional Small Molecules

Both allosteric and kinase inhibitors can be converted into bifunctional molecules to control tyrosine phosphorylation of targeted proteins.

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Bibliographic Details
Published inACS central science Vol. 9; no. 8; pp. 1512 - 1514
Main Authors Meng, Xianke, Qi, Jun
Format Journal Article
LanguageEnglish
Published Washington American Chemical Society 23.08.2023
Subjects
Allosteric properties
Binding sites
Biology
Cancer
Cell death
Chemistry
Enzymes
Epidermal growth factor
First Reactions
Kinases
Labeling
Phosphorylation
Proteins
Tyrosine
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Summary:Both allosteric and kinase inhibitors can be converted into bifunctional molecules to control tyrosine phosphorylation of targeted proteins.
Bibliography:SourceType-Other Sources-1
ObjectType-News-1
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ISSN:2374-7943
2374-7951
DOI:10.1021/acscentsci.3c00836