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http://purl.uniprot.org/citations/9404889http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9404889http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9404889http://www.w3.org/2000/01/rdf-schema#comment"We have purified three new human U4/U6-snRNP proteins from HeLa cells. The three proteins formed a tightly bound complex and behaved as a single species throughout the purification. All three proteins have been identified by peptide sequencing, and full-length cDNA sequences have been obtained for all of them. Two of the proteins are homologues of the Saccharomyces cerevisiae splicing factors Prp3 and Prp4, and the third protein is a cyclophilin. Both the human and S. cerevisiae Prp4 proteins have seven repeats of the WD motif and likely fold into structures very similar to those of the beta subunits of G proteins. The human Prp3 protein is highly basic and is closely related to S. cerevisiae Prp3 only in its carboxyl-terminal half. The human homologues of Prp3 and Prp4 are part of a stable complex in the absence of RNA. The third protein in the complex is a new cyclophilin. Cyclophilins have been proposed to act as chaperones in a variety of cellular processes, and we discuss some possible roles of this U4/U6 snRNP-associated cyclophilin."xsd:string
http://purl.uniprot.org/citations/9404889http://purl.uniprot.org/core/author"Kobayashi R."xsd:string
http://purl.uniprot.org/citations/9404889http://purl.uniprot.org/core/author"Kobayashi R."xsd:string
http://purl.uniprot.org/citations/9404889http://purl.uniprot.org/core/author"Krainer A.R."xsd:string
http://purl.uniprot.org/citations/9404889http://purl.uniprot.org/core/author"Krainer A.R."xsd:string
http://purl.uniprot.org/citations/9404889http://purl.uniprot.org/core/author"Horowitz D.S."xsd:string
http://purl.uniprot.org/citations/9404889http://purl.uniprot.org/core/author"Horowitz D.S."xsd:string
http://purl.uniprot.org/citations/9404889http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9404889http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9404889http://purl.uniprot.org/core/name"RNA"xsd:string
http://purl.uniprot.org/citations/9404889http://purl.uniprot.org/core/name"RNA"xsd:string
http://purl.uniprot.org/citations/9404889http://purl.uniprot.org/core/pages"1374-1387"xsd:string
http://purl.uniprot.org/citations/9404889http://purl.uniprot.org/core/pages"1374-1387"xsd:string
http://purl.uniprot.org/citations/9404889http://purl.uniprot.org/core/title"A new cyclophilin and the human homologues of yeast Prp3 and Prp4 form a complex associated with U4/U6 snRNPs."xsd:string
http://purl.uniprot.org/citations/9404889http://purl.uniprot.org/core/title"A new cyclophilin and the human homologues of yeast Prp3 and Prp4 form a complex associated with U4/U6 snRNPs."xsd:string
http://purl.uniprot.org/citations/9404889http://purl.uniprot.org/core/volume"3"xsd:string
http://purl.uniprot.org/citations/9404889http://purl.uniprot.org/core/volume"3"xsd:string
http://purl.uniprot.org/citations/9404889http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9404889
http://purl.uniprot.org/citations/9404889http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9404889
http://purl.uniprot.org/citations/9404889http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9404889
http://purl.uniprot.org/citations/9404889http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9404889
http://purl.uniprot.org/uniprot/O43395http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9404889
http://purl.uniprot.org/uniprot/O43172http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9404889