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http://purl.uniprot.org/citations/7621825http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7621825http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7621825http://www.w3.org/2000/01/rdf-schema#comment"The nin1-1 mutant of Saccharomyces cerevisiae cannot perform the G1/S and G2/M transitions at restrictive temperatures. At such temperatures, nin1-1 strains fail to activate histone H1 kinase after release from alpha factor-imposed G1 block and after release from hydroxyurea-imposed S block. The nin1-1 mutation shows synthetic lethality with certain cdc28 mutant alleles such as cdc28-IN. Two lines of evidence indicate that Nin1p is a component of the 26S proteasome complex: (i) Nin1p, as well as the known component of the 26S proteasome, shifted to the 26S proteasome peak in the glycerol density gradient after preincubation of crude extract with ATP-Mg2+, and (ii) nin1-1 cells accumulated polyubiquitinated proteins under restrictive conditions. These results suggest that activation of Cdc28p kinase requires proteolysis. We have cloned a human cDNA encoding a regulatory subunit of the 26S proteasome, p31, which was found to be a homolog of Nin1p."xsd:string
http://purl.uniprot.org/citations/7621825http://purl.org/dc/terms/identifier"doi:10.1002/j.1460-2075.1995.tb07313.x"xsd:string
http://purl.uniprot.org/citations/7621825http://purl.org/dc/terms/identifier"doi:10.1002/j.1460-2075.1995.tb07313.x"xsd:string
http://purl.uniprot.org/citations/7621825http://purl.uniprot.org/core/author"Tanaka K."xsd:string
http://purl.uniprot.org/citations/7621825http://purl.uniprot.org/core/author"Tanaka K."xsd:string
http://purl.uniprot.org/citations/7621825http://purl.uniprot.org/core/author"Toh-e A."xsd:string
http://purl.uniprot.org/citations/7621825http://purl.uniprot.org/core/author"Toh-e A."xsd:string
http://purl.uniprot.org/citations/7621825http://purl.uniprot.org/core/author"Shimizu Y."xsd:string
http://purl.uniprot.org/citations/7621825http://purl.uniprot.org/core/author"Shimizu Y."xsd:string
http://purl.uniprot.org/citations/7621825http://purl.uniprot.org/core/author"Fujimuro M."xsd:string
http://purl.uniprot.org/citations/7621825http://purl.uniprot.org/core/author"Fujimuro M."xsd:string
http://purl.uniprot.org/citations/7621825http://purl.uniprot.org/core/author"Moomaw C."xsd:string
http://purl.uniprot.org/citations/7621825http://purl.uniprot.org/core/author"Moomaw C."xsd:string
http://purl.uniprot.org/citations/7621825http://purl.uniprot.org/core/author"Slaughter C.A."xsd:string
http://purl.uniprot.org/citations/7621825http://purl.uniprot.org/core/author"Slaughter C.A."xsd:string
http://purl.uniprot.org/citations/7621825http://purl.uniprot.org/core/author"DeMartino G.N."xsd:string
http://purl.uniprot.org/citations/7621825http://purl.uniprot.org/core/author"DeMartino G.N."xsd:string
http://purl.uniprot.org/citations/7621825http://purl.uniprot.org/core/author"Kominami K."xsd:string
http://purl.uniprot.org/citations/7621825http://purl.uniprot.org/core/author"Kominami K."xsd:string
http://purl.uniprot.org/citations/7621825http://purl.uniprot.org/core/author"Tanahashi N."xsd:string
http://purl.uniprot.org/citations/7621825http://purl.uniprot.org/core/author"Tanahashi N."xsd:string
http://purl.uniprot.org/citations/7621825http://purl.uniprot.org/core/author"Yokosawa H."xsd:string
http://purl.uniprot.org/citations/7621825http://purl.uniprot.org/core/author"Yokosawa H."xsd:string