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Honeder, SE; Tomin, T; Schinagl, M; Pfleger, R; Hoehlschen, J; Darnhofer, B; Schittmayer, M; Birner-Gruenberger, R.
Research Advances Through Activity-Based Lipid Hydrolase Profiling
ISR J CHEM. 2023;
Doi: 10.1002/ijch.202200078
Web of Science
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- Führende Autor*innen der Med Uni Graz
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Birner-Grünberger Ruth
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Honeder Sophie
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Schittmayer-Schantl Matthias
- Co-Autor*innen der Med Uni Graz
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Darnhofer Barbara
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Schinagl Maximilian
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Tomin Tamara
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- Abstract:
- Activity-based proteomic profiling (ABPP) enables the functional study of enzymes by employing small molecule probes that bind covalently to the active site of an enzyme. Activity-based probes can penetrate cells and tissues and thereby allow enzymes to be targeted/labelled in their native state. Probes can be designed to target individual enzymes or whole enzyme groups, which makes ABPP a versatile protein profiling technique. In this review, we give an overview of research advances through ABPP in the context of lipid hydrolase research. We report of lipid hydrolases that were discovered and characterized through ABPP, and aim to give an overview of commonly used probes as well as inhibitors that were discovered and characterized by competitive ABPP. Lastly, this review aims to raise caveats and current limitations of this protein profiling technique.
- Find related publications in this database (Keywords)
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ABPP
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functional proteomics
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lipid hydrolase
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serine hydrolase