| http://purl.uniprot.org/citations/9872961 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9872961 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9872961 | http://www.w3.org/2000/01/rdf-schema#comment | "Proteasomes are multicatalytic complexes that function as the major proteolytic machinery in regulated protein degradation. The eukaryotic 20S proteasome proteolytic core structure comprises 14 different subunits: 7 alpha-type and 7 beta-type. DTS7 is a dominant temperature-sensitive (DTS) lethal mutation at 29 degrees that also acts as a recessive lethal at ambient temperatures. DTS7 maps to cytological position 71AB. Molecular characterization of DTS7 reveals that this is caused by a missense mutation in a beta-type subunit gene, beta2. A previously characterized DTS mutant, l(3)73Ai1, results from a missense mutation in another beta-type subunit gene, beta6. These two mutants share a very similar phenotype, show a strong allele-specific genetic interaction, and are rescued by the same extragenic suppressor, Su(DTS)-1. We propose that these mutants might act as "poison subunits," disrupting proteasome function in a dosage-dependent manner, and suggest how they may interact on the basis of the structure of the yeast 20S proteasome."xsd:string |
| http://purl.uniprot.org/citations/9872961 | http://purl.org/dc/terms/identifier | "doi:10.1093/genetics/151.1.211"xsd:string |
| http://purl.uniprot.org/citations/9872961 | http://purl.org/dc/terms/identifier | "doi:10.1093/genetics/151.1.211"xsd:string |
| http://purl.uniprot.org/citations/9872961 | http://purl.uniprot.org/core/author | "Belote J.M."xsd:string |
| http://purl.uniprot.org/citations/9872961 | http://purl.uniprot.org/core/author | "Belote J.M."xsd:string |
| http://purl.uniprot.org/citations/9872961 | http://purl.uniprot.org/core/author | "Smyth K.A."xsd:string |
| http://purl.uniprot.org/citations/9872961 | http://purl.uniprot.org/core/author | "Smyth K.A."xsd:string |
| http://purl.uniprot.org/citations/9872961 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/9872961 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/9872961 | http://purl.uniprot.org/core/name | "Genetics"xsd:string |
| http://purl.uniprot.org/citations/9872961 | http://purl.uniprot.org/core/name | "Genetics"xsd:string |
| http://purl.uniprot.org/citations/9872961 | http://purl.uniprot.org/core/pages | "211-220"xsd:string |
| http://purl.uniprot.org/citations/9872961 | http://purl.uniprot.org/core/pages | "211-220"xsd:string |
| http://purl.uniprot.org/citations/9872961 | http://purl.uniprot.org/core/title | "The dominant temperature-sensitive lethal DTS7 of Drosophila melanogaster encodes an altered 20S proteasome beta-type subunit."xsd:string |
| http://purl.uniprot.org/citations/9872961 | http://purl.uniprot.org/core/title | "The dominant temperature-sensitive lethal DTS7 of Drosophila melanogaster encodes an altered 20S proteasome beta-type subunit."xsd:string |
| http://purl.uniprot.org/citations/9872961 | http://purl.uniprot.org/core/volume | "151"xsd:string |
| http://purl.uniprot.org/citations/9872961 | http://purl.uniprot.org/core/volume | "151"xsd:string |
| http://purl.uniprot.org/citations/9872961 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/9872961 |
| http://purl.uniprot.org/citations/9872961 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/9872961 |
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| http://purl.uniprot.org/citations/9872961 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/9872961 |
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| http://purl.uniprot.org/uniprot/O17311 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9872961 |