http://purl.uniprot.org/citations/9683573 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/9683573 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/9683573 | http://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/9683573 | http://purl.org/dc/terms/identifier | "doi:10.1006/viro.1998.9220"xsd:string |
http://purl.uniprot.org/citations/9683573 | http://purl.org/dc/terms/identifier | "doi:10.1006/viro.1998.9220"xsd:string |
http://purl.uniprot.org/citations/9683573 | http://purl.uniprot.org/core/author | "Schilling B."xsd:string |
http://purl.uniprot.org/citations/9683573 | http://purl.uniprot.org/core/author | "Schilling B."xsd:string |
http://purl.uniprot.org/citations/9683573 | http://purl.uniprot.org/core/author | "Vidal M."xsd:string |
http://purl.uniprot.org/citations/9683573 | http://purl.uniprot.org/core/author | "Vidal M."xsd:string |
http://purl.uniprot.org/citations/9683573 | http://purl.uniprot.org/core/author | "Munger K."xsd:string |
http://purl.uniprot.org/citations/9683573 | http://purl.uniprot.org/core/author | "Munger K."xsd:string |
http://purl.uniprot.org/citations/9683573 | http://purl.uniprot.org/core/author | "De-Medina T."xsd:string |
http://purl.uniprot.org/citations/9683573 | http://purl.uniprot.org/core/author | "De-Medina T."xsd:string |
http://purl.uniprot.org/citations/9683573 | http://purl.uniprot.org/core/author | "Syken J."xsd:string |
http://purl.uniprot.org/citations/9683573 | http://purl.uniprot.org/core/author | "Syken J."xsd:string |
http://purl.uniprot.org/citations/9683573 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
http://purl.uniprot.org/citations/9683573 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
http://purl.uniprot.org/citations/9683573 | http://purl.uniprot.org/core/name | "Virology"xsd:string |
http://purl.uniprot.org/citations/9683573 | http://purl.uniprot.org/core/name | "Virology"xsd:string |
http://purl.uniprot.org/citations/9683573 | http://purl.uniprot.org/core/pages | "74-85"xsd:string |
http://purl.uniprot.org/citations/9683573 | http://purl.uniprot.org/core/pages | "74-85"xsd:string |
http://purl.uniprot.org/citations/9683573 | http://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/9683573 | http://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/9683573 | http://purl.uniprot.org/core/volume | "247"xsd:string |
http://purl.uniprot.org/citations/9683573 | http://purl.uniprot.org/core/volume | "247"xsd:string |