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http://purl.uniprot.org/citations/7479976http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7479976http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7479976http://www.w3.org/2000/01/rdf-schema#comment"The inhibitor protein I kappa B alpha controls the nuclear import of the transcription factor NF-kappa B. The inhibitory activity of I kappa B alpha is regulated from the cytoplasmic compartment by signal-induced proteolysis. Previous studies have shown that signal-dependent phosphorylation of serine residues 32 and 36 targets I kappa B alpha to the ubiquitin-proteasome pathway. Here we provide evidence that lysine residues 21 and 22 serve as the primary sites for signal-induced ubiquitination of I kappa B alpha. Conservative Lys-->Arg substitutions at both Lys-21 and Lys-22 produce dominant-negative mutants of I kappa B alpha in vivo. These constitutive inhibitors are appropriately phosphorylated but fail to release NF-kappa B in response to multiple inducers, including viral proteins, cytokines, and agents that mimic antigenic stimulation through the T-cell receptor. Moreover, these Lys-->Arg mutations prevent signal-dependent degradation of I kappa B alpha in vivo and ubiquitin conjugation in vitro. We conclude that site-specific ubiquitination of phosphorylated I kappa B alpha at Lys-21 and/or Lys-22 is an obligatory step in the activation of NF-kappa B."xsd:string
http://purl.uniprot.org/citations/7479976http://purl.org/dc/terms/identifier"doi:10.1073/pnas.92.24.11259"xsd:string
http://purl.uniprot.org/citations/7479976http://purl.org/dc/terms/identifier"doi:10.1073/pnas.92.24.11259"xsd:string
http://purl.uniprot.org/citations/7479976http://purl.uniprot.org/core/author"Chen Z."xsd:string
http://purl.uniprot.org/citations/7479976http://purl.uniprot.org/core/author"Chen Z."xsd:string
http://purl.uniprot.org/citations/7479976http://purl.uniprot.org/core/author"Maniatis T."xsd:string
http://purl.uniprot.org/citations/7479976http://purl.uniprot.org/core/author"Maniatis T."xsd:string
http://purl.uniprot.org/citations/7479976http://purl.uniprot.org/core/author"Scherer D.C."xsd:string
http://purl.uniprot.org/citations/7479976http://purl.uniprot.org/core/author"Scherer D.C."xsd:string
http://purl.uniprot.org/citations/7479976http://purl.uniprot.org/core/author"Ballard D.W."xsd:string
http://purl.uniprot.org/citations/7479976http://purl.uniprot.org/core/author"Ballard D.W."xsd:string
http://purl.uniprot.org/citations/7479976http://purl.uniprot.org/core/author"Brockman J.A."xsd:string
http://purl.uniprot.org/citations/7479976http://purl.uniprot.org/core/author"Brockman J.A."xsd:string
http://purl.uniprot.org/citations/7479976http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7479976http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7479976http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/7479976http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/7479976http://purl.uniprot.org/core/pages"11259-11263"xsd:string
http://purl.uniprot.org/citations/7479976http://purl.uniprot.org/core/pages"11259-11263"xsd:string
http://purl.uniprot.org/citations/7479976http://purl.uniprot.org/core/title"Signal-induced degradation of IkappaB alpha requires site-specific ubiquitination."xsd:string
http://purl.uniprot.org/citations/7479976http://purl.uniprot.org/core/title"Signal-induced degradation of IkappaB alpha requires site-specific ubiquitination."xsd:string
http://purl.uniprot.org/citations/7479976http://purl.uniprot.org/core/volume"92"xsd:string
http://purl.uniprot.org/citations/7479976http://purl.uniprot.org/core/volume"92"xsd:string