1. Vision using multiple distinct rod opsins in deep-sea fishes
The nucleophilic thiol group allows cysteines to undergo a broad range of chemical modifications. Thiol-based protein oxidation (S-sulfenylation, S-sulfinylation, S-Glutathionylation, etc.) by exogenous and endogenous reactive oxygen
species (ROS) is a crucial mechanism in cell signaling. To gain a better understanding of how these thiol modifications affect protein functions in normal or stressed biological systems, we should first know which cysteinyl thiols
on a protein can be oxidized or modified. In other words, identification of protein targets of thiol oxidation is crucial to understanding of their roles in biology and disease. Our research programs develop two complementary site-centric
chemoproteomic strategies to systematically quantify thiol reactivities and to globally map distinct types of thiol oxidation in native proteomes (Fig. 1). With these tools in hand, we redefine the hydrogen peroxide-dependent redoxome
in human cells and generate the first site-centric S-sulfenylome and S-sulfinylome datasets. We also develop the first web portal database, called OXID, for sharing and integrating redox proteomics. These works not only expand
the landscape of thiol redox proteome in human cells, but also suggest novel redox mechanisms of several proteins with key biological functions, such as SIRT6 and APIP. In collaboration with a diverse group of biologists worldwide,
now we are applying our chemoproteomic toolbox to various model organisms, including M. musculus, C. elegans, D. melanogaster, and A. thaliana, and to study cysteine-mediated redox regulation in a range of physiological processes
and adaptive responses.
Fig. 3 develop new tools for studying protein-protein interactions
To gain a better understanding of how these thiol modifications affect protein functions in normal or stressed biological systems, we should first know which cysteinyl thiols on a protein can be oxidized or modified.
2. Chemical Epigenetics: To explore the biological significance of novel histone PTMs
The nucleophilic thiol group allows cysteines to undergo a broad range of chemical modifications. Thiol-based protein oxidation (S-sulfenylation, S-sulfinylation, S-Glutathionylation, etc.) by exogenous and endogenous reactive oxygen
species (ROS) is a crucial mechanism in cell signaling. To gain a better understanding of how these thiol modifications affect protein functions in normal or stressed biological systems, we should first know which cysteinyl thiols
on a protein can be oxidized or modified. In other words, identification of protein targets of thiol oxidation is crucial to understanding of their roles in biology and disease. Our research programs develop two complementary site-centric
chemoproteomic strategies to systematically quantify thiol reactivities and to globally map distinct types of thiol oxidation in native proteomes (Fig. 1). With these tools in hand, we redefine the hydrogen peroxide-dependent redoxome
in human cells and generate the first site-centric S-sulfenylome and S-sulfinylome datasets. We also develop the first web portal database, called OXID, for sharing and integrating redox proteomics. These works not only expand
the landscape of thiol redox proteome in human cells, but also suggest novel redox mechanisms of several proteins with key biological functions, such as SIRT6 and APIP. In collaboration with a diverse group of biologists worldwide,
now we are applying our chemoproteomic toolbox to various model organisms, including M. musculus, C. elegans, D. melanogaster, and A. thaliana, and to study cysteine-mediated redox regulation in a range of physiological processes
and adaptive responses.
Fig. 3 develop new tools for studying protein-protein interactions
To gain a better understanding of how these thiol modifications affect protein functions in normal or stressed biological systems, we should first know which cysteinyl thiols on a protein can be oxidized or modified.
3. Article Three Article Three Article Three Article Three Article Three Article Three Article Three
The nucleophilic thiol group allows cysteines to undergo a broad range of chemical modifications. Thiol-based protein oxidation (S-sulfenylation, S-sulfinylation, S-Glutathionylation, etc.) by exogenous and endogenous reactive oxygen
species (ROS) is a crucial mechanism in cell signaling. To gain a better understanding of how these thiol modifications affect protein functions in normal or stressed biological systems, we should first know which cysteinyl thiols
on a protein can be oxidized or modified. In other words, identification of protein targets of thiol oxidation is crucial to understanding of their roles in biology and disease. Our research programs develop two complementary site-centric
chemoproteomic strategies to systematically quantify thiol reactivities and to globally map distinct types of thiol oxidation in native proteomes (Fig. 1). With these tools in hand, we redefine the hydrogen peroxide-dependent redoxome
in human cells and generate the first site-centric S-sulfenylome and S-sulfinylome datasets. We also develop the first web portal database, called OXID, for sharing and integrating redox proteomics. These works not only expand
the landscape of thiol redox proteome in human cells, but also suggest novel redox mechanisms of several proteins with key biological functions, such as SIRT6 and APIP. In collaboration with a diverse group of biologists worldwide,
now we are applying our chemoproteomic toolbox to various model organisms, including M. musculus, C. elegans, D. melanogaster, and A. thaliana, and to study cysteine-mediated redox regulation in a range of physiological processes
and adaptive responses.
Fig. 3 develop new tools for studying protein-protein interactions
To gain a better understanding of how these thiol modifications affect protein functions in normal or stressed biological systems, we should first know which cysteinyl thiols on a protein can be oxidized or modified.
