TRIM for Tissue Specificity

Hartmann, MD

doi:10.1021/acsmedchemlett.3c00504

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TRIM for Tissue Specificity

Hartmann, M. (2024). TRIM for Tissue Specificity. ACS Medicinal Chemistry Letters, 15(1), 4-5. doi:10.1021/acsmedchemlett.3c00504.

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Item Permalink: https://hdl.handle.net/21.11116/0000-000E-1772-8 Version Permalink: https://hdl.handle.net/21.11116/0000-000E-4046-B

Genre: Journal Article

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Hartmann, MD^{1, 2}, Author

Affiliations:
1Molecular Recognition and Catalysis Group, Department Protein Evolution, Max Planck Institute for Biology Tübingen, Max Planck Society, ou_3477391
2Department Protein Evolution, Max Planck Institute for Biology Tübingen, Max Planck Society, Max-Planck-Ring 5, 72076 Tübingen, DE, ou_3371683

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Abstract: Tissue-specific manipulation of proteins is a long-standing objective in the field of targeted protein degradation, but still a distant prospect. Currently, the most successfully employed E3 ubiquitin ligases belong to the most ubiquitously expressed representatives. Unlocking of the TRIM58 ligase might represent a promising step toward tissue-specific PROTACs and molecular glue degraders.

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Dates: Published Online: 2023-12Date issued: 2024-01

Publication Status: Issued

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Identifiers: DOI: 10.1021/acsmedchemlett.3c00504
PMID: 38229746

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Title: ACS Medicinal Chemistry Letters

Source Genre: Journal

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Publ. Info: Washington, DC : ACS

Pages: - Volume / Issue: 15 (1) Sequence Number: - Start / End Page: 4 - 5 Identifier: ISSN: 1948-5875
CoNE: https://pure.mpg.de/cone/journals/resource/1948-5875