| http://purl.uniprot.org/citations/7628444 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7628444 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7628444 | http://www.w3.org/2000/01/rdf-schema#comment | "Hsp78 is a Clp homologue within mitochondria of Saccharomyces cerevisiae. Deletion of HSP78 does not cause any detectable changes in wild type cells, but results in a petite phenotype in the ssc1-3 mutant strain carrying a temperature-sensitive allele of mt-hsp70. When overexpressed in the ssc1-3 mutant strain, hsp78 suppresses the defect in mitochondrial protein import under permissive conditions in vitro and interacts directly with newly imported polypeptide chains. As a molecular chaperone, hsp78 prevents the aggregation of misfolded proteins in the matrix of mitochondria under conditions of impaired mt-hsp70 function. However, unlike misfolded proteins associated with mt-hsp70, hsp78-bound polypeptides are not efficiently degraded by the ATP-dependent PIM1 protease. Thus, hsp78 can partially substitute for mt-hsp70 functions in the assembly of mitochondria and may be part of a salvage pathway if mt-hsp70 is limiting."xsd:string |
| http://purl.uniprot.org/citations/7628444 | http://purl.org/dc/terms/identifier | "doi:10.1002/j.1460-2075.1995.tb07349.x"xsd:string |
| http://purl.uniprot.org/citations/7628444 | http://purl.org/dc/terms/identifier | "doi:10.1002/j.1460-2075.1995.tb07349.x"xsd:string |
| http://purl.uniprot.org/citations/7628444 | http://purl.uniprot.org/core/author | "Schmitt M."xsd:string |
| http://purl.uniprot.org/citations/7628444 | http://purl.uniprot.org/core/author | "Schmitt M."xsd:string |
| http://purl.uniprot.org/citations/7628444 | http://purl.uniprot.org/core/author | "Langer T."xsd:string |
| http://purl.uniprot.org/citations/7628444 | http://purl.uniprot.org/core/author | "Langer T."xsd:string |
| http://purl.uniprot.org/citations/7628444 | http://purl.uniprot.org/core/author | "Neupert W."xsd:string |
| http://purl.uniprot.org/citations/7628444 | http://purl.uniprot.org/core/author | "Neupert W."xsd:string |
| http://purl.uniprot.org/citations/7628444 | http://purl.uniprot.org/core/date | "1995"xsd:gYear |
| http://purl.uniprot.org/citations/7628444 | http://purl.uniprot.org/core/date | "1995"xsd:gYear |
| http://purl.uniprot.org/citations/7628444 | http://purl.uniprot.org/core/name | "EMBO J."xsd:string |
| http://purl.uniprot.org/citations/7628444 | http://purl.uniprot.org/core/name | "EMBO J."xsd:string |
| http://purl.uniprot.org/citations/7628444 | http://purl.uniprot.org/core/pages | "3434-3444"xsd:string |
| http://purl.uniprot.org/citations/7628444 | http://purl.uniprot.org/core/pages | "3434-3444"xsd:string |
| http://purl.uniprot.org/citations/7628444 | http://purl.uniprot.org/core/title | "Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70."xsd:string |
| http://purl.uniprot.org/citations/7628444 | http://purl.uniprot.org/core/title | "Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70."xsd:string |
| http://purl.uniprot.org/citations/7628444 | http://purl.uniprot.org/core/volume | "14"xsd:string |
| http://purl.uniprot.org/citations/7628444 | http://purl.uniprot.org/core/volume | "14"xsd:string |
| http://purl.uniprot.org/citations/7628444 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/7628444 |
| http://purl.uniprot.org/citations/7628444 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/7628444 |
| http://purl.uniprot.org/citations/7628444 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/7628444 |
| http://purl.uniprot.org/citations/7628444 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/7628444 |