ArticleBioorganic & medicinal chemistry2014
A comparative study of ATP analogs for phosphorylation-dependent kinase-substrate crosslinking.
Article in Bioorganic & medicinal chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 19 citations in OpenAlex.
- SuFEx chemistry for nucleosides, nucleotides, and nucleic acids.RSC chemical biology · 2026Review
- 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
- Photoaffinity labelling strategies for mapping the small molecule-protein interactome.Organic & biomolecular chemistry · 2021Review
- An Affinity-Based, Cysteine-Specific ATP Analog for Kinase-Catalyzed Crosslinking.Angewandte Chemie (International ed. in English) · 2021Article
- Chemically reprogramming the phospho-transfer reaction to crosslink protein kinases to their substrates.Protein science : a publication of the Protein Society · 2019Article
- Identification of Kinases and Interactors of p53 Using Kinase-Catalyzed Cross-Linking and Immunoprecipitation.Journal of the American Chemical Society · 2018Article
- K-BILDS: A Kinase Substrate Discovery Tool.Chembiochem : a European journal of chemical biology · 2017Article
- K-CLASP: A Tool to Identify Phosphosite Specific Kinases and Interacting Proteins.ACS chemical biology · 2016Article
- A Cell-Permeable ATP Analogue for Kinase-Catalyzed Biotinylation.Angewandte Chemie (International ed. in English) · 2015Article
- Protein networks and activation of lymphocytes.Current opinion in immunology · 2015Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Kinase-catalyzed protein phosphorylation is an important post-translational modification that regulates a variety of cellular functions. Identification of the many substrates of a specific kinase is critical to fully characterize cell biology. Unfortunately, kinase-substrate interactions are often transient, which makes their identification challenging. Here, the transient kinase-substrate complex was stabilized by covalent crosslinking using γ-phosphate modified ATP analogs. Building upon prior use of an ATP-aryl azide photocrosslinking analog, we report here the creation of an ATP-benzophenone photocrosslinking analog. ATP-benzophenone displayed a higher conversion percentage but more diffuse crosslinking compared to the ATP-aryl azide analog. A docking study was also performed to rationalize the conversion and crosslinking data. In total, the photocrosslinking ATP analogs produced stable kinase-substrate complexes that are suitable for future applications characterizing cell signaling pathways.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.