Difference between revisions of "Cysteinome:About"

From Cysteinome
Jump to: navigation, search
 
(32 intermediate revisions by the same user not shown)
Line 1: Line 1:
−
'''Cysteine''' is a unique amino acid with the thiol side chain serving as an intrinsic nucleophile and often participating in various enzymatic reactions.
+
The covalent modification of intrinsically nucleophilic cysteine in proteins is crucial for diverse biochemical events. Bioinformatics approaches may prove useful in the design and discovery of covalent molecules targeting the cysteine in proteins to tune their functions and activities. <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/>
 
−
'''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 and PubChem.
 
  
 +
'''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. In this database it compiles over '''400 proteins''' with targetable cysteine along with more than '''1200 covalent modulators''' curated from existing literatures. Proteins are annotated with a detailed description of protein families, biological process and related diseases. In addition, covalent modulators are carefully annotated with chemical name, chemical structure, binding affinity, physicochemical properties, molecule type and related diseases etc.<br/>
  
−
In Cysteinome, users could start by two ways:
+
The Cysteinome database serve as a useful platform for the identification of crucial proteins with targetable cysteine in certain cellular context. Furthermore, it may help biologists and chemists for the design and discovery of covalent chemical probes or inhibitors homing at functional cysteine of critical protein targets implicated in various physiological or disease process.<br/>
−
#From the Target List, it could be found that the proteins are classified by the species. During these catalogues, the “Animal” is the biggest one, which contains the targets from Human, Mouse, Rat, Bovine, some Insects and so on. Besides, in Cysteinome there are “Bacteria”, “Virus”, “Parasite” and “Plant”.
 
−
#From the Search, users can start by searching the name and UNP ID of the protein, or the name and PubChem cid of the ligands (most of the ligands possess a PubChem cid).
 
−
::Taken “Streptopain” as an example, from the entry, users could easily overview the target and get access to the other databases convenient:
 
−
::Taken “Oxacillin” as the example of ligand:
 
  
−
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.
+
==Developers==
 +
'''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.<br/>
  
−
'''Cysteinome''' is developed by Center for Molecular Medicine, School of Life Science and Biotechnology, Dalian University of Technology, China, and now maintained by College of Pharmacy, Ohio State University, USA.
+
:'''Sijin Wu''', Ph.D. , Professor (Assistant) at Academy of Pharmacy, Xi'an Jiaotong-Liverpool University (Email: sijin.wu84 AT gmail.com).<br/>
−
 
+
:'''Yongliang Yang''', Ph.D. , Professor at Center for Molecular Medicine, School of Life Science and Biotechnology, DLUT (Email: everbright99 AT gmail.com).
−
==People==
 
−
:'''Sijin Wu''', Ph.D. : Postdoctoral researcher at Division of Medicinal Chemistry & Pharmacognosy, College of Pharmacy, OSU (Email: wu.3857 AT osu.edu).<br/>
 
−
:'''Yongliang Yang''', Ph.D. : Associate professor at Center for Molecular Medicine, School of Life Science and Biotechnology, DLUT (Email: everbright99 AT gmail.com).
 

Latest revision as of 03:01, 30 September 2023

The covalent modification of intrinsically nucleophilic cysteine in proteins is crucial for diverse biochemical events. Bioinformatics approaches may prove useful in the design and discovery of covalent molecules targeting the cysteine in proteins to tune their functions and activities.

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. In this database it compiles over 400 proteins with targetable cysteine along with more than 1200 covalent modulators curated from existing literatures. Proteins are annotated with a detailed description of protein families, biological process and related diseases. In addition, covalent modulators are carefully annotated with chemical name, chemical structure, binding affinity, physicochemical properties, molecule type and related diseases etc.

The Cysteinome database serve as a useful platform for the identification of crucial proteins with targetable cysteine in certain cellular context. Furthermore, it may help biologists and chemists for the design and discovery of covalent chemical probes or inhibitors homing at functional cysteine of critical protein targets implicated in various physiological or disease process.

Developers

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.

Sijin Wu, Ph.D. , Professor (Assistant) at Academy of Pharmacy, Xi'an Jiaotong-Liverpool University (Email: sijin.wu84 AT gmail.com).
Yongliang Yang, Ph.D. , Professor at Center for Molecular Medicine, School of Life Science and Biotechnology, DLUT (Email: everbright99 AT gmail.com).
Retrieved from "http://173.199.123.204/Cysteinome/index.php?title=Cysteinome:About&oldid=2239"