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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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PubMed
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- Führende Autor*innen der Med Uni Graz
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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.
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Animals -
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Drug Evaluation, Preclinical -
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Enzyme Activation -
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Enzymes - chemistry
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Humans - chemistry
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Peptides - chemistry
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Protein Array Analysis - methods
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Proteomics - trends
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Sensitivity and Specificity - trends
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Structure-Activity Relationship - trends
- Find related publications in this database (Keywords)
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activity-based proteomics
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functional proteomics
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enzymatic activity profiling
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active site-directed chemical probes