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Human Interaction Network Ontology
| Preferred Name | Protein folding | |
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| Definitions |
Reviewed: Cowan, NJ, 2009-01-21 16:47:24 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). Edited: Matthews, L, 2009-02-21 04:38:35 Authored: Matthews, L, 2008-12-01 04:46:41 |
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| ID |
http://purl.obolibrary.org/obo/HINO_0016752 |
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| comment |
Reviewed: Cowan, NJ, 2009-01-21 16:47:24 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). Edited: Matthews, L, 2009-02-21 04:38:35 Authored: Matthews, L, 2008-12-01 04:46:41
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| definition source |
Pubmed15459659 Pubmed15519848 Reactome, http://www.reactome.org Pubmed18395510
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| label |
Protein folding
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| prefixIRI |
HINO:0016752
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| prefLabel |
Protein folding
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| seeAlso |
ReactomeREACT_16952 GENE ONTOLOGYGO:0051084 Reactome Database ID Release 43391251
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