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http://purl.uniprot.org/citations/9683573http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9683573http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9683573http://www.w3.org/2000/01/rdf-schema#comment"We have cloned hTid-1, a human homolog of the Drosophila tumor suppressor protein Tid56, by virtue of its ability to form complexes with the human papillomavirus E7 oncoprotein. The carboxyl terminal cysteine-rich metal binding domain of E7 is the major determinant for interaction with hTid-1. The carboxyl terminus of E7 is essential for the functional and structural integrity of E7 and has previously been shown to function as a multimerization domain. The hTid-1 protein is a member of the DnaJ-family of chaperones. Its mRNA is widely expressed in human tissues, including the HPV-18-positive cervical carcinoma cell line HeLa and human genital keratinocytes, the normal host cells of the HPVs. The hTid-1 gene has been mapped to the short arm of chromosome 16. The large tumor antigens of polyomaviruses encode functional J-domains that are important for viral replication as well as cellular transformation. The ability of HPV E7 to interact with a cellular DnaJ protein suggests that these two viral oncoproteins may target common regulatory pathways through J-domains."xsd:string
http://purl.uniprot.org/citations/9683573http://purl.org/dc/terms/identifier"doi:10.1006/viro.1998.9220"xsd:string
http://purl.uniprot.org/citations/9683573http://purl.org/dc/terms/identifier"doi:10.1006/viro.1998.9220"xsd:string
http://purl.uniprot.org/citations/9683573http://purl.uniprot.org/core/author"Schilling B."xsd:string
http://purl.uniprot.org/citations/9683573http://purl.uniprot.org/core/author"Schilling B."xsd:string
http://purl.uniprot.org/citations/9683573http://purl.uniprot.org/core/author"Vidal M."xsd:string
http://purl.uniprot.org/citations/9683573http://purl.uniprot.org/core/author"Vidal M."xsd:string
http://purl.uniprot.org/citations/9683573http://purl.uniprot.org/core/author"Munger K."xsd:string
http://purl.uniprot.org/citations/9683573http://purl.uniprot.org/core/author"Munger K."xsd:string
http://purl.uniprot.org/citations/9683573http://purl.uniprot.org/core/author"De-Medina T."xsd:string
http://purl.uniprot.org/citations/9683573http://purl.uniprot.org/core/author"De-Medina T."xsd:string
http://purl.uniprot.org/citations/9683573http://purl.uniprot.org/core/author"Syken J."xsd:string
http://purl.uniprot.org/citations/9683573http://purl.uniprot.org/core/author"Syken J."xsd:string
http://purl.uniprot.org/citations/9683573http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9683573http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9683573http://purl.uniprot.org/core/name"Virology"xsd:string
http://purl.uniprot.org/citations/9683573http://purl.uniprot.org/core/name"Virology"xsd:string
http://purl.uniprot.org/citations/9683573http://purl.uniprot.org/core/pages"74-85"xsd:string
http://purl.uniprot.org/citations/9683573http://purl.uniprot.org/core/pages"74-85"xsd:string
http://purl.uniprot.org/citations/9683573http://purl.uniprot.org/core/title"A novel human DnaJ protein, hTid-1, a homolog of the Drosophila tumor suppressor protein Tid56, can interact with the human papillomavirus type 16 E7 oncoprotein."xsd:string
http://purl.uniprot.org/citations/9683573http://purl.uniprot.org/core/title"A novel human DnaJ protein, hTid-1, a homolog of the Drosophila tumor suppressor protein Tid56, can interact with the human papillomavirus type 16 E7 oncoprotein."xsd:string
http://purl.uniprot.org/citations/9683573http://purl.uniprot.org/core/volume"247"xsd:string
http://purl.uniprot.org/citations/9683573http://purl.uniprot.org/core/volume"247"xsd:string