Difference between revisions of "Cysteinome:About"
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'''Cysteine''' is an unique amino acid with the thiol side chain serving as an intrinsic nucleophile and often participating in various enzymatic reactions. | '''Cysteine''' is an unique amino acid with the thiol side chain serving as an intrinsic nucleophile and often participating in various enzymatic reactions. | ||
In recent years, covalent probes or inhibitors homing at a cysteine thiol group present in the target proteins have attracted significant attention. But the lack of systematic information for proteins with targetable cysteine has hindered the design and discovery of covalent modulators of protein functions and activities. Therefore, a comprehensive database with an analysis system dedicated to proteins with targetable cysteine can be very useful. Cysteinome, the first online database that provides a rich resource for the display, search and analysis of structure, function and related annotation for proteins with targetable cysteine as well as their covalent modulators. <br/> | In recent years, covalent probes or inhibitors homing at a cysteine thiol group present in the target proteins have attracted significant attention. But the lack of systematic information for proteins with targetable cysteine has hindered the design and discovery of covalent modulators of protein functions and activities. Therefore, a comprehensive database with an analysis system dedicated to proteins with targetable cysteine can be very useful. Cysteinome, the first online database that provides a rich resource for the display, search and analysis of structure, function and related annotation for proteins with targetable cysteine as well as their covalent modulators. <br/> | ||
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'''Cysteinome''' will contribute to the understanding of how protein targets is covalently modified by chemical probes homing at cysteine residue and will serve as a useful resource for the development of covalent inhibitors | '''Cysteinome''' will contribute to the understanding of how protein targets is covalently modified by chemical probes homing at cysteine residue and will serve as a useful resource for the development of covalent inhibitors | ||
Cysteinome is able to provide considerably more information about proteins and ligands by hyperlinking to the particular databases, such as UniProt, KEGG, PDB, Pfam and PubChem.<br/> | Cysteinome is able to provide considerably more information about proteins and ligands by hyperlinking to the particular databases, such as UniProt, KEGG, PDB, Pfam and PubChem.<br/> | ||
Revision as of 05:42, 21 January 2020
Cysteine is an unique amino acid with the thiol side chain serving as an intrinsic nucleophile and often participating in various enzymatic reactions.
In recent years, covalent probes or inhibitors homing at a cysteine thiol group present in the target proteins have attracted significant attention. But the lack of systematic information for proteins with targetable cysteine has hindered the design and discovery of covalent modulators of protein functions and activities. Therefore, a comprehensive database with an analysis system dedicated to proteins with targetable cysteine can be very useful. Cysteinome, the first online database that provides a rich resource for the display, search and analysis of structure, function and related annotation for proteins with targetable cysteine as well as their covalent modulators.
Cysteinome will contribute to the understanding of how protein targets is covalently modified by chemical probes homing at cysteine residue and will serve as a useful resource for the development of covalent inhibitors
Cysteinome is able to provide considerably more information about proteins and ligands by hyperlinking to the particular databases, such as UniProt, KEGG, PDB, Pfam and PubChem.
We hope that Cysteinome will contribute to the understanding of how protein targets is covalently modified by chemical probes homing at cysteine residue and will serve as a useful resource for the development of covalent inhibitors.
Cysteinome is developed by Center for Molecular Medicine, School of Life Science and Biotechnology, Dalian University of Technology, China, and now maintained by Sijin Wu at College of Pharmacy, The Ohio State University, USA.
Developers
- Sijin Wu, Ph.D. , Postdoctoral researcher at Division of Medicinal Chemistry & Pharmacognosy, College of Pharmacy, OSU (Email: wu.3857 AT osu.edu).
- Yongliang Yang, Ph.D. , Associate professor at Center for Molecular Medicine, School of Life Science and Biotechnology, DLUT (Email: everbright99 AT gmail.com).
