ArticleAngewandte Chemie (International ed. in English)2021
An Affinity-Based, Cysteine-Specific ATP Analog for Kinase-Catalyzed Crosslinking.
Article in Angewandte Chemie (International ed. in English), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 8 citations in OpenAlex.
- Gadolinium-Conjugated Lipoic Acid Hydrogels for Magnetic Resonance Imaging.ACS applied bio materials · 2025Article
- Kinase-catalyzed crosslinking: A comparison of ATP-crosslinker analogs.Bioorganic & medicinal chemistry letters · 2024Article
- Kinase-Catalyzed Biotinylation to Identify Phosphatase Substrates (K-BIPS).Methods in molecular biology (Clifton, N.J.) · 2024Article
- Affinity-Based Kinase-Catalyzed Crosslinking to Study Kinase-Substrate Pairs.Bioconjugate chemistry · 2023Article
- Kinase-Catalyzed Crosslinking and Immunoprecipitation (K-CLIP) to Explore Kinase-Substrate Pairs.Current protocols · 2022Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Kinases mediate cell signaling pathways by catalyzing protein phosphorylation. Irregularities in kinase activity are directly associated with disease conditions. Therefore, methods to identify substrates of a particular kinase are needed to understand signaling cascades in normal and diseased states. Photocrosslinking ATP analogs provide powerful tools to study kinases by covalently linking kinases with substrates. However, the involvement of UV light and nonspecific reactivity of current ATP-photocrosslinkers challenge kinase-substrate identification. We report here an affinity-based crosslinking ATP analog, ATP-methylacrylamide (ATP-MAc), that contains a cysteine-reactive acrylamide crosslinking group, which avoids the UV irradiation and non-specific reactivity of prior analogs. Using in vitro kinase assays, ATP-MAc acts as a kinase co-substrate and covalently crosslinks only kinases containing cysteines in the active site. ATP-MAc was also able to crosslink cellular proteins in lysates, documenting compatibility with cell-based studies.
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Registered trials
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