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http://purl.uniprot.org/citations/10558878http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10558878http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10558878http://www.w3.org/2000/01/rdf-schema#comment"DNase II is a well-known deoxyribonuclease (DNase) that catalyzes the hydrolysis of DNA into oligonucleotides under acidic conditions. We have identified a novel DNase that shows homology to DNase II, named DLAD, from a search of an expressed sequence tag data base. The full-length cDNA for rat DLAD cloned by polymerase chain reaction encodes a 356-amino acid polypeptide containing a putative N-terminal signal peptide and 5 potential N-glycosylation sites; there is a predicted catalytic domain resemblance to rat DNase II. The predicted DLAD translation product shares 32.9% identity with DNase II. Interestingly, expression of the DRAD mRNA is highly restricted to the liver. A Myc-His tagged recombinant DLAD recovered mainly from the cytoplasm of transfected HeLa S3 cells has a divalent cation-independent DNase activity. The DLAD activity prefers acidic conditions to neutral. The recombinant protein expressed in HeLa S3 cells inhibits the expression of GFP- and lac Z-expression vectors, suggesting that DLAD may play a role in elimination of exogenous DNA. Identification of the full-length cDNA for DLAD would lead to an understanding of the physiology of this DNase II-like molecule."xsd:string
http://purl.uniprot.org/citations/10558878http://purl.org/dc/terms/identifier"doi:10.1006/bbrc.1999.1699"xsd:string
http://purl.uniprot.org/citations/10558878http://purl.org/dc/terms/identifier"doi:10.1006/bbrc.1999.1699"xsd:string
http://purl.uniprot.org/citations/10558878http://purl.uniprot.org/core/author"Tanuma S."xsd:string
http://purl.uniprot.org/citations/10558878http://purl.uniprot.org/core/author"Tanuma S."xsd:string
http://purl.uniprot.org/citations/10558878http://purl.uniprot.org/core/author"Shiokawa D."xsd:string
http://purl.uniprot.org/citations/10558878http://purl.uniprot.org/core/author"Shiokawa D."xsd:string
http://purl.uniprot.org/citations/10558878http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10558878http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10558878http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/10558878http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/10558878http://purl.uniprot.org/core/pages"395-399"xsd:string
http://purl.uniprot.org/citations/10558878http://purl.uniprot.org/core/pages"395-399"xsd:string
http://purl.uniprot.org/citations/10558878http://purl.uniprot.org/core/title"Cloning of a cDNA encoding a rat DNase II-like acid DNase."xsd:string
http://purl.uniprot.org/citations/10558878http://purl.uniprot.org/core/title"Cloning of a cDNA encoding a rat DNase II-like acid DNase."xsd:string
http://purl.uniprot.org/citations/10558878http://purl.uniprot.org/core/volume"265"xsd:string
http://purl.uniprot.org/citations/10558878http://purl.uniprot.org/core/volume"265"xsd:string
http://purl.uniprot.org/citations/10558878http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10558878
http://purl.uniprot.org/citations/10558878http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10558878
http://purl.uniprot.org/citations/10558878http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10558878
http://purl.uniprot.org/citations/10558878http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10558878
http://purl.uniprot.org/uniprot/Q9QZK8http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/10558878
http://purl.uniprot.org/uniprot/Q9QZK9http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/10558878