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| Chaperones are a class of conserved cellular proteins who function as a quality control system in living cells which assist non-native proteins' folding to functional native conformation correctly and efficiently. In yeast, the chaperones are divided into eight categories including small heat shock protein, AAA+ family, the CCT/TRiC complex, the prefoldin/GimC complex, Hsp40, Hsp60, Hsp70, and Hsp90. |
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Proteomic and genetic techniques, especially the recent powerful
experiment method such as high affinity purification mass
spectrum, Yeast Two Hybrid, Synthetic Genetic Array are useful
to explore the function of the chaperones from different
perspectives.
ChaperoneDB is a comprehensive collection of yeast chaperone interactions both from our previous work and BIOGRID, and it contents all the interaction information including chaperone type, number of chaperone interactors or substrates interactors, experiment method, mostly all these chaperone and substrates can be linked to popular databases like SGD, Entrez-Gene, GeneDB, Germ Online, Raw TAP data, BIOGRID. And the intuitive interaction map from SVG file is easy for users to interpreter. |
