<div class="csl-bib-body">
<div class="csl-entry">Honeder, S. E., Tomin, T., Schinagl, M., Pfleger, R., Hoehlschen, J., Darnhofer, B., Schittmayer, M., & Birner‐Gruenberger, R. (2023). Research Advances Through Activity‐Based Lipid Hydrolase Profiling. <i>Israel Journal of Chemistry</i>, Article e202200078. https://doi.org/10.1002/ijch.202200078</div>
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dc.identifier.issn
0021-2148
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dc.identifier.uri
http://hdl.handle.net/20.500.12708/153266
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dc.description.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.
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dc.description.sponsorship
FWF Fonds zur Förderung der wissenschaftlichen Forschung (FWF)
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dc.language.iso
en
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dc.publisher
Wiley
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dc.relation.ispartof
Israel Journal of Chemistry
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dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
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dc.subject
ABPP
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dc.subject
functional proteomics
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dc.subject
lipid hydrolase
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dc.subject
serine hydrolase
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dc.title
Research Advances Through Activity‐Based Lipid Hydrolase Profiling