A covalent BTK ternary complex compatible with targeted protein degradation
Bridging covalent ligand discovery with chimeric degrader design has emerged as a mechanism to target proteins that lack enzymatic activity or are intractable. Here, the authors use biochemical and cellular tools to deconvolute the role of covalent modification in targeted protein degradation using...
| Main Authors: | , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2023-03-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-023-36738-z |
| _version_ | 1797864223803441152 |
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| author | James Schiemer Andrew Maxwell Reto Horst Shenping Liu Daniel P. Uccello Kris Borzilleri Nisha Rajamohan Matthew F. Brown Matthew F. Calabrese |
| author_facet | James Schiemer Andrew Maxwell Reto Horst Shenping Liu Daniel P. Uccello Kris Borzilleri Nisha Rajamohan Matthew F. Brown Matthew F. Calabrese |
| author_sort | James Schiemer |
| collection | DOAJ |
| description | Bridging covalent ligand discovery with chimeric degrader design has emerged as a mechanism to target proteins that lack enzymatic activity or are intractable. Here, the authors use biochemical and cellular tools to deconvolute the role of covalent modification in targeted protein degradation using Bruton’s tyrosine kinase. |
| first_indexed | 2024-04-09T22:48:17Z |
| format | Article |
| id | doaj.art-8332ec11fd3e488aa9daf64205146e29 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-04-09T22:48:17Z |
| publishDate | 2023-03-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-8332ec11fd3e488aa9daf64205146e292023-03-22T11:43:27ZengNature PortfolioNature Communications2041-17232023-03-0114111210.1038/s41467-023-36738-zA covalent BTK ternary complex compatible with targeted protein degradationJames Schiemer0Andrew Maxwell1Reto Horst2Shenping Liu3Daniel P. Uccello4Kris Borzilleri5Nisha Rajamohan6Matthew F. Brown7Matthew F. Calabrese8Discovery Sciences, Pfizer Worldwide Research and DevelopmentDiscovery Sciences, Pfizer Worldwide Research and DevelopmentDiscovery Sciences, Pfizer Worldwide Research and DevelopmentDiscovery Sciences, Pfizer Worldwide Research and DevelopmentDiscovery Sciences, Pfizer Worldwide Research and DevelopmentDiscovery Sciences, Pfizer Worldwide Research and DevelopmentDiscovery Sciences, Pfizer Worldwide Research and DevelopmentDiscovery Sciences, Pfizer Worldwide Research and DevelopmentDiscovery Sciences, Pfizer Worldwide Research and DevelopmentBridging covalent ligand discovery with chimeric degrader design has emerged as a mechanism to target proteins that lack enzymatic activity or are intractable. Here, the authors use biochemical and cellular tools to deconvolute the role of covalent modification in targeted protein degradation using Bruton’s tyrosine kinase.https://doi.org/10.1038/s41467-023-36738-z |
| spellingShingle | James Schiemer Andrew Maxwell Reto Horst Shenping Liu Daniel P. Uccello Kris Borzilleri Nisha Rajamohan Matthew F. Brown Matthew F. Calabrese A covalent BTK ternary complex compatible with targeted protein degradation Nature Communications |
| title | A covalent BTK ternary complex compatible with targeted protein degradation |
| title_full | A covalent BTK ternary complex compatible with targeted protein degradation |
| title_fullStr | A covalent BTK ternary complex compatible with targeted protein degradation |
| title_full_unstemmed | A covalent BTK ternary complex compatible with targeted protein degradation |
| title_short | A covalent BTK ternary complex compatible with targeted protein degradation |
| title_sort | covalent btk ternary complex compatible with targeted protein degradation |
| url | https://doi.org/10.1038/s41467-023-36738-z |
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