http://purl.uniprot.org/citations/19349277 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/19349277 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/19349277 | http://www.w3.org/2000/01/rdf-schema#comment | "The 26 S proteasome is a large proteolytic machine, which degrades most intracellular proteins. We found that thioredoxin, Txnl1/TRP32, binds to Rpn11, a subunit of the regulatory complex of the human 26 S proteasome. Txnl1 is abundant, metabolically stable, and widely expressed and is present in the cytoplasm and nucleus. Txnl1 has thioredoxin activity with a redox potential of about -250 mV. Mutant Txnl1 with one active site cysteine replaced by serine formed disulfide bonds to eEF1A1, a substrate-recruiting factor of the 26 S proteasome. eEF1A1 is therefore a likely physiological substrate. In response to knockdown of Txnl1, ubiquitin-protein conjugates were moderately stabilized. Hence, Txnl1 is the first example of a direct connection between protein reduction and proteolysis, two major intracellular protein quality control mechanisms."xsd:string |
http://purl.uniprot.org/citations/19349277 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m900016200"xsd:string |
http://purl.uniprot.org/citations/19349277 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m900016200"xsd:string |
http://purl.uniprot.org/citations/19349277 | http://purl.uniprot.org/core/author | "Semple C.A."xsd:string |
http://purl.uniprot.org/citations/19349277 | http://purl.uniprot.org/core/author | "Semple C.A."xsd:string |
http://purl.uniprot.org/citations/19349277 | http://purl.uniprot.org/core/author | "Madsen L."xsd:string |
http://purl.uniprot.org/citations/19349277 | http://purl.uniprot.org/core/author | "Madsen L."xsd:string |
http://purl.uniprot.org/citations/19349277 | http://purl.uniprot.org/core/author | "Johnsen A.H."xsd:string |
http://purl.uniprot.org/citations/19349277 | http://purl.uniprot.org/core/author | "Johnsen A.H."xsd:string |
http://purl.uniprot.org/citations/19349277 | http://purl.uniprot.org/core/author | "Hartmann-Petersen R."xsd:string |
http://purl.uniprot.org/citations/19349277 | http://purl.uniprot.org/core/author | "Hartmann-Petersen R."xsd:string |
http://purl.uniprot.org/citations/19349277 | http://purl.uniprot.org/core/author | "Hendil K.B."xsd:string |
http://purl.uniprot.org/citations/19349277 | http://purl.uniprot.org/core/author | "Hendil K.B."xsd:string |
http://purl.uniprot.org/citations/19349277 | http://purl.uniprot.org/core/author | "Andersen K.M."xsd:string |
http://purl.uniprot.org/citations/19349277 | http://purl.uniprot.org/core/author | "Andersen K.M."xsd:string |
http://purl.uniprot.org/citations/19349277 | http://purl.uniprot.org/core/author | "Prag S."xsd:string |
http://purl.uniprot.org/citations/19349277 | http://purl.uniprot.org/core/author | "Prag S."xsd:string |
http://purl.uniprot.org/citations/19349277 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
http://purl.uniprot.org/citations/19349277 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
http://purl.uniprot.org/citations/19349277 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/19349277 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/19349277 | http://purl.uniprot.org/core/pages | "15246-15254"xsd:string |
http://purl.uniprot.org/citations/19349277 | http://purl.uniprot.org/core/pages | "15246-15254"xsd:string |