Cysteines, as one of the most intrinsically nucleophilic amino acids, play important roles in proteins involved in diverse biological processes. They are also targets of covalent drugs for treating cancers and other diseases. Understanding the cysteine reactivity towards different types of electrophilic reactive groups will contribute to design of cysteine-reactive probes and facilitate the development of cysteine-based covalent drugs. In this study, we systematically evaluated the cysteinome reactivity toward two common electrophilic probes that are based on nucleophilic substitution and Michael addition, respectively, using chemical proteomic strategies. Our profiling results showed that each probe had its own preferential reactivity towa...
Our laboratory focuses on chemical proteomics-enabled discovery of new cysteine-reactive small molec...
Reversible covalency, achieved with, for instance, highly electron-deficient olefins, offers a compe...
In this thesis, we develop a new mass spectrometry-based chemoproteomic method that allows detection...
Proteomic profiling using bioorthogonal chemical probes that selectively react with certain amino ac...
Covalent drug discovery, in particular targeting reactive cysteines, has undergone a resurgence over...
Covalent inhibitors have numerous applications as drugs, as tools for drug discovery, and as probes ...
Covalent inactivation of proteins by small molecules is experiencing an increasing trend in pharmace...
Targeted covalent inhibitors have emerged as a powerful approach in the drug discovery pipeline. Key...
Targeted covalent inhibitors have become an integral part of a number of therapeutic protocols and a...
Summary: Differential amino acid reactivity with chemical probes can provide valuable information on...
Cysteine-directed chemoproteomic profiling methods yield high-throughput inventories of redox-sensit...
Targeted covalent inhibition and the use of irreversible chemical probes are important strategies in...
There is a resurging interest in compounds that engage their target through covalent interactions. C...
Cysteine is the most intrinsically nucleophilic amino acid in proteins, where its reactivity is tune...
Cysteine is the most intrinsically nucleophilic amino acid in proteins, where its reactivity is tune...
Our laboratory focuses on chemical proteomics-enabled discovery of new cysteine-reactive small molec...
Reversible covalency, achieved with, for instance, highly electron-deficient olefins, offers a compe...
In this thesis, we develop a new mass spectrometry-based chemoproteomic method that allows detection...
Proteomic profiling using bioorthogonal chemical probes that selectively react with certain amino ac...
Covalent drug discovery, in particular targeting reactive cysteines, has undergone a resurgence over...
Covalent inhibitors have numerous applications as drugs, as tools for drug discovery, and as probes ...
Covalent inactivation of proteins by small molecules is experiencing an increasing trend in pharmace...
Targeted covalent inhibitors have emerged as a powerful approach in the drug discovery pipeline. Key...
Targeted covalent inhibitors have become an integral part of a number of therapeutic protocols and a...
Summary: Differential amino acid reactivity with chemical probes can provide valuable information on...
Cysteine-directed chemoproteomic profiling methods yield high-throughput inventories of redox-sensit...
Targeted covalent inhibition and the use of irreversible chemical probes are important strategies in...
There is a resurging interest in compounds that engage their target through covalent interactions. C...
Cysteine is the most intrinsically nucleophilic amino acid in proteins, where its reactivity is tune...
Cysteine is the most intrinsically nucleophilic amino acid in proteins, where its reactivity is tune...
Our laboratory focuses on chemical proteomics-enabled discovery of new cysteine-reactive small molec...
Reversible covalency, achieved with, for instance, highly electron-deficient olefins, offers a compe...
In this thesis, we develop a new mass spectrometry-based chemoproteomic method that allows detection...