Epoxide electrophiles as activity-dependent cysteine protease profiling and discovery tools.
@article{Greenbaum2000EpoxideEA, title={Epoxide electrophiles as activity-dependent cysteine protease profiling and discovery tools.}, author={Doron C. Greenbaum and Katalin F. Medzihradszky and Alma L. Burlingame and Matthew S. Bogyo}, journal={Chemistry \& biology}, year={2000}, volume={7 8}, pages={ 569-81 } }
491 Citations
Activity Profiling of Papain-Like Cysteine Proteases in Plants1
- BiologyPlant Physiology
- 2004
Together, these results demonstrate that this technology can identify differentially activated proteases and/or characterize the activity of a particular protease within complex mixtures.
Solid‐Phase Synthesis of Double‐Headed Epoxysuccinyl Activity‐Based Probes for Selective Targeting of Papain Family Cysteine Proteases
- Biology, ChemistryChembiochem : a European journal of chemical biology
- 2005
Preliminary results involving the solid-phase synthesis of cathepsin B-specific ABPs based on the E-64 scaffold and development of a method that would allow facile attachment of diverse peptide sequences on both sides of the epoxide moiety are reported.
Activity-based probes for the proteomic profiling of metalloproteases.
- Biology, ChemistryProceedings of the National Academy of Sciences of the United States of America
- 2004
It is demonstrated that MPs can display overlapping inhibitor sensitivities despite lacking sequence homology and the need to evaluate MP inhibitors broadly across this enzyme class to develop agents with suitable target selectivities in vivo is stressed.
Activity‐Based Protein Profiling for Type I Methionine Aminopeptidase by Using Photo‐Affinity Trimodular Probes
- Biology, ChemistryChembiochem : a European journal of chemical biology
- 2007
An advanced technique is introduced, “CC-ABPP”, in which the reporter tag is attached to the probe by the bio-orthogonal copper(I)-catalyzed azide and alkyne cycloaddition reaction following covalent labeling of the protein target, and a similar strategy for the design and chemical synthesis of a trimodular affinity probe is reported.
In-cell Selectivity Profiling of Serine Protease Inhibitors by Activity-based Proteomics*S
- Biology, ChemistryMolecular & Cellular Proteomics
- 2008
This novel ABP was shown to label the active site of several serine proteases with greater efficiency than a previously reported fluorophosphonate probe and open new perspectives for safety profiling studies in uncovering potential cellular “side effects” of drugs (unanticipated off-target inhibition or activation) that may be overlooked by standard selectivity profiling methods.
From covalent glycosidase inhibitors to activity-based glycosidase probes.
- Biology, ChemistryChemistry
- 2014
This concept presents the current progress and future directions in the design of activity-based probes targeting retaining Glycosidases, enzymes that employ a double displacement mechanism in the hydrolysis of glycosidic bonds with overall retention.
Small Molecules as Versatile Tools for Activity-Based Protein Profiling Experiments
- Biology, Chemistry
- 2010
Protease proteomics: revealing protease in vivo functions using systems biology approaches.
- BiologyMolecular aspects of medicine
- 2008
Applications of Copper-Catalyzed Click Chemistry in Activity-Based Protein Profiling
- Biology, ChemistryMolecules
- 2014
Recent examples of CuAAC in ABPP are summarized to illustrate the contribution of bioorthogonal chemistry to advancing discoveries in this field.
Recent Advances in Activity-Based Protein Profiling of Proteases.
- BiologyCurrent topics in microbiology and immunology
- 2019
This chapter discusses several strategies to enable detection of a single active protease species and describes the different types of detection tags that facilitate the read-out possibilities including various types of imaging methods and mass spectrometry-based target identification.
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