Protein folding

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Homo sapiens
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Due to the crowded envirnoment within the cell, many proteins must interact with molecular chaperones to attain their native conformation (reviewed in Young et al., 2004). Chaperones recognize and associate with proteins in their non-native state and facilitate their folding by stabilizing the conformation of productive folding intermediates. Chaperones that take part broadly in de novo protein folding, such as the Hsp70s and the chaperonins, facilitate the folding process through cycles of substrate binding and release regulated by their ATPase activity (see Young et al., 2004; Spiess et al., 2004; Bigotti and Clarke, 2008).

Literature References
PubMed ID Title Journal Year
15459659 Pathways of chaperone-mediated protein folding in the cytosol

Young, JC, Agashe, VR, Siegers, K, Hartl, FU

Nat Rev Mol Cell Biol 2004
18395510 Chaperonins: The hunt for the Group II mechanism

Bigotti, MG, Clarke, AR

Arch Biochem Biophys 2008
15519848 Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets

Spiess, C, Meyer, AS, Reissmann, S, Frydman, J

Trends Cell Biol 2004
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