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Human Interaction Network Ontology
Preferred Name | PDI is a chaperone for collagen peptides | |
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Authored: Jupe, S, 2010-07-20 Edited: Jupe, S, 2012-05-14 Reviewed: Canty-Laird, EG, 2012-05-24 As the collagen peptide chain is translocated across the membrane of the endoplasmic reticulum, intrachain disulfide bonds are formed within the N- and C-propeptides. This allows the triple helical domain to form a nucleation point at its C-terminal end and ensures correct alignment of the chains (Engel & Prockop 1991). Protein disulfide isomerase (P4HB) catalyzes the formation of both intra- (Bulleid & Freedman 1988) and inter-chain disulfide bonds (Koivu & Myllylä 1987). In addition, PDI acts as a molecular chaperone, interacting with monomeric collagen propeptide chains to prevent premature assembly or aggregation (Wilson et al. 1998). |
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http://purl.obolibrary.org/obo/HINO_0022390 |
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comment |
Authored: Jupe, S, 2010-07-20 Edited: Jupe, S, 2012-05-14 Reviewed: Canty-Laird, EG, 2012-05-24 As the collagen peptide chain is translocated across the membrane of the endoplasmic reticulum, intrachain disulfide bonds are formed within the N- and C-propeptides. This allows the triple helical domain to form a nucleation point at its C-terminal end and ensures correct alignment of the chains (Engel & Prockop 1991). Protein disulfide isomerase (P4HB) catalyzes the formation of both intra- (Bulleid & Freedman 1988) and inter-chain disulfide bonds (Koivu & Myllylä 1987). In addition, PDI acts as a molecular chaperone, interacting with monomeric collagen propeptide chains to prevent premature assembly or aggregation (Wilson et al. 1998).
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definition source |
Pubmed1867713 Reactome, http://www.reactome.org Pubmed9560306 Pubmed9545296 Pubmed3571251 Pubmed3173483
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label |
PDI is a chaperone for collagen peptides
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prefixIRI |
HINO:0022390
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prefLabel |
PDI is a chaperone for collagen peptides
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seeAlso |
ReactomeREACT_120881 Reactome Database ID Release 432002460
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subClassOf |
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