| http://purl.uniprot.org/citations/1339453 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/1339453 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/1339453 | http://www.w3.org/2000/01/rdf-schema#comment | "We have studied the folding, processing, and association with two endoplasmic reticulum (ER) resident proteins of the abnormal type I procollagen molecules produced by a strain of fibroblasts harboring a 4.5 kilobase deletion in an allele of COL1A2 (Willing, M. C., Cohn, D.H., Starman, B. Holbrook, K.A., Greenberg, C.R., and Byers, P.H. (1988) J. Biol. Chem. 263, 8398-8404). By sequencing cDNA, we found that the mutant allele encodes pro alpha 2(I) chains that are shortened by 180 amino acids but retain the Gly-X-Y repeat pattern crucial for collagen triple helix formation. The type I procollagen molecules that incorporated the shortened chain were retained intracellularly and were stable. The triple helical domain in these molecules did not attain a normal conformation and remained accessible to posttranslational modifying enzymes amino-terminal to the deletion site for a prolonged period. The abnormal molecules folded into a triple helical conformation more slowly than the normal molecules, and the amino-terminal ends of the pro alpha 1(I) chains failed to become protease-resistant. While the abnormal procollagen molecules were not bound by the ER-resident protein BiP, they stably associated with protein disulfide isomerase, the beta-subunit of prolyl-4-hydroxylase. These results indicate that some mutations in type I collagen genes both transiently delay folding and permanently disrupt the structure of the triple helix and suggest that binding to prolyl-4-hydroxylase helps to retain certain abnormal procollagen molecules within the ER."xsd:string |
| http://purl.uniprot.org/citations/1339453 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(18)42578-1"xsd:string |
| http://purl.uniprot.org/citations/1339453 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(18)42578-1"xsd:string |
| http://purl.uniprot.org/citations/1339453 | http://purl.uniprot.org/core/author | "Byers P.H."xsd:string |
| http://purl.uniprot.org/citations/1339453 | http://purl.uniprot.org/core/author | "Byers P.H."xsd:string |
| http://purl.uniprot.org/citations/1339453 | http://purl.uniprot.org/core/author | "Chessler S.D."xsd:string |
| http://purl.uniprot.org/citations/1339453 | http://purl.uniprot.org/core/author | "Chessler S.D."xsd:string |
| http://purl.uniprot.org/citations/1339453 | http://purl.uniprot.org/core/date | "1992"xsd:gYear |
| http://purl.uniprot.org/citations/1339453 | http://purl.uniprot.org/core/date | "1992"xsd:gYear |
| http://purl.uniprot.org/citations/1339453 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/1339453 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/1339453 | http://purl.uniprot.org/core/pages | "7751-7757"xsd:string |
| http://purl.uniprot.org/citations/1339453 | http://purl.uniprot.org/core/pages | "7751-7757"xsd:string |
| http://purl.uniprot.org/citations/1339453 | http://purl.uniprot.org/core/title | "Defective folding and stable association with protein disulfide isomerase/prolyl hydroxylase of type I procollagen with a deletion in the pro alpha 2(I) chain that preserves the Gly-X-Y repeat pattern."xsd:string |
| http://purl.uniprot.org/citations/1339453 | http://purl.uniprot.org/core/title | "Defective folding and stable association with protein disulfide isomerase/prolyl hydroxylase of type I procollagen with a deletion in the pro alpha 2(I) chain that preserves the Gly-X-Y repeat pattern."xsd:string |
| http://purl.uniprot.org/citations/1339453 | http://purl.uniprot.org/core/volume | "267"xsd:string |
| http://purl.uniprot.org/citations/1339453 | http://purl.uniprot.org/core/volume | "267"xsd:string |
| http://purl.uniprot.org/citations/1339453 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/1339453 |
| http://purl.uniprot.org/citations/1339453 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/1339453 |
| http://purl.uniprot.org/citations/1339453 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/1339453 |
| http://purl.uniprot.org/citations/1339453 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/1339453 |
| http://purl.uniprot.org/uniprot/P08123 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/1339453 |
| http://purl.uniprot.org/uniprot/P08123#attribution-0C39961C3E263B489790FEAC88D02F79 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/1339453 |