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Schmidinger, H; Hermetter, A; Birner-Gruenberger, R.
Activity-based proteomics: enzymatic activity profiling in complex proteomes.
Amino Acids. 2006; 30(4): 333-350. Doi: 10.1007/s00726-006-0305-2
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Führende Autor*innen der Med Uni Graz
Birner-Grünberger Ruth
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Abstract:
In the postgenomic era new technologies are emerging for global analysis of protein function. The introduction of active site-directed chemical probes for enzymatic activity profiling in complex mixtures, known as activity-based proteomics has greatly accelerated functional annotation of proteins. Here we review probe design for different enzyme classes including serine hydrolases, cysteine proteases, tyrosine phosphatases, glycosidases, and others. These probes are usually detected by their fluorescent, radioactive or affinity tags and their protein targets are analyzed using established proteomics techniques. Recent developments, such as the design of probes for in vivo analysis of proteomes, as well as microarray technologies for higher throughput screenings of protein specificity and the application of activity-based probes for drug screening are highlighted. We focus on biological applications of activity-based probes for target and inhibitor discovery and discuss challenges for future development of this field.
Find related publications in this database (using NLM MeSH Indexing)
Animals -
Drug Evaluation, Preclinical -
Enzyme Activation -
Enzymes - chemistry
Humans - chemistry
Peptides - chemistry
Protein Array Analysis - methods
Proteomics - trends
Sensitivity and Specificity - trends
Structure-Activity Relationship - trends

Find related publications in this database (Keywords)
activity-based proteomics
functional proteomics
enzymatic activity profiling
active site-directed chemical probes
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