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- W3119402092 endingPage "1732" @default.
- W3119402092 startingPage "1717" @default.
- W3119402092 abstract "Fluorescence microscopy imaging enables receptor proteins to be investigated within their biological context. A key challenge is to site-specifically incorporate reporter moieties into proteins without interfering with biological functions or cellular networks. Small peptide tags offer the opportunity to combine inducible labeling with small tag sizes that avoid receptor perturbation. Herein, we review the current state of live-cell labeling of peptide-tagged cell-surface proteins. Considering their importance as targets in medicinal chemistry, we focus on membrane receptors such as G protein-coupled receptors (GPCRs) and receptor tyrosine kinases (RTKs). We discuss peptide tags that i) are subject to enzyme-mediated modification reactions, ii) guide the complementation of reporter proteins, iii) form coiled-coil complexes, and iv) interact with metal complexes. Given our own contributions in the field, we place emphasis on peptide-templated labeling chemistry." @default.
- W3119402092 created "2021-01-18" @default.
- W3119402092 creator A5019019129 @default.
- W3119402092 creator A5053611588 @default.
- W3119402092 creator A5073399193 @default.
- W3119402092 creator A5083922106 @default.
- W3119402092 date "2021-02-26" @default.
- W3119402092 modified "2023-10-17" @default.
- W3119402092 title "Strategies for Site‐Specific Labeling of Receptor Proteins on the Surfaces of Living Cells by Using Genetically Encoded Peptide Tags" @default.
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