| http://purl.uniprot.org/citations/8995684 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8995684 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8995684 | http://www.w3.org/2000/01/rdf-schema#comment | "The adenovirus (Ad) 14.7-kDa E3 protein (E3-14.7K), which can inhibit tumor necrosis factor alpha (TNF-alpha) cytolysis, was used to screen HeLa cell cDNA libraries for interacting proteins in the yeast two-hybrid system. A new member of the low-molecular-weight (LMW) GTP-binding protein family with Ras and ADP-ribosylation factor homology was discovered by this selection and has been named FIP-1 (14.7K-interacting protein). FIP-1 colocalized with Ad E3-14.7K in the cytoplasm especially near the nuclear membrane and in discrete foci on or near the plasma membrane. Its interaction with E3-14.7K was dependent on the FIP-1 GTP-binding domain. The stable expression of FIP-1 antisense message partially protected the cells from TNF-alpha cytolysis. FIP-1 was associated transiently with several unknown phosphorylated cellular proteins within 15 min after treatment with TNF-alpha. FIP-1 mRNA was expressed ubiquitously but at higher levels in human skeletal muscle, heart, and brain. In addition to homology to other LMW GTP-binding proteins, FIP-1 has regions of homology to two prokaryotic metalloproteases. However, there was no homology between FIP-1 and any of the recently isolated death proteins in the TNF-alpha or Fas/APO1 cytolytic pathway and no interaction with several members of the Bcl-2 family of inhibitors of apoptosis. These data suggest that FIP-1, as a cellular target for Ad E3-14.7K, is either a new intermediate on a previously described pathway or part of a novel TNF-alpha-induced cell death pathway. FIP-1 has two consensus sequences for myristoylation which would be expected to facilitate membrane association and also has sequences for Ser/Thr as well as Tyr phosphorylation that could affect its function."xsd:string |
| http://purl.uniprot.org/citations/8995684 | http://purl.org/dc/terms/identifier | "doi:10.1128/jvi.71.2.1576-1582.1997"xsd:string |
| http://purl.uniprot.org/citations/8995684 | http://purl.org/dc/terms/identifier | "doi:10.1128/jvi.71.2.1576-1582.1997"xsd:string |
| http://purl.uniprot.org/citations/8995684 | http://purl.uniprot.org/core/author | "Horwitz M.S."xsd:string |
| http://purl.uniprot.org/citations/8995684 | http://purl.uniprot.org/core/author | "Horwitz M.S."xsd:string |
| http://purl.uniprot.org/citations/8995684 | http://purl.uniprot.org/core/author | "Li Y."xsd:string |
| http://purl.uniprot.org/citations/8995684 | http://purl.uniprot.org/core/author | "Li Y."xsd:string |
| http://purl.uniprot.org/citations/8995684 | http://purl.uniprot.org/core/author | "Kang J."xsd:string |
| http://purl.uniprot.org/citations/8995684 | http://purl.uniprot.org/core/author | "Kang J."xsd:string |
| http://purl.uniprot.org/citations/8995684 | http://purl.uniprot.org/core/date | "1997"xsd:gYear |
| http://purl.uniprot.org/citations/8995684 | http://purl.uniprot.org/core/date | "1997"xsd:gYear |
| http://purl.uniprot.org/citations/8995684 | http://purl.uniprot.org/core/name | "J. Virol."xsd:string |
| http://purl.uniprot.org/citations/8995684 | http://purl.uniprot.org/core/name | "J. Virol."xsd:string |
| http://purl.uniprot.org/citations/8995684 | http://purl.uniprot.org/core/pages | "1576-1582"xsd:string |
| http://purl.uniprot.org/citations/8995684 | http://purl.uniprot.org/core/pages | "1576-1582"xsd:string |
| http://purl.uniprot.org/citations/8995684 | http://purl.uniprot.org/core/title | "Interaction of an adenovirus 14.7-kilodalton protein inhibitor of tumor necrosis factor alpha cytolysis with a new member of the GTPase superfamily of signal transducers."xsd:string |
| http://purl.uniprot.org/citations/8995684 | http://purl.uniprot.org/core/title | "Interaction of an adenovirus 14.7-kilodalton protein inhibitor of tumor necrosis factor alpha cytolysis with a new member of the GTPase superfamily of signal transducers."xsd:string |
| http://purl.uniprot.org/citations/8995684 | http://purl.uniprot.org/core/volume | "71"xsd:string |
| http://purl.uniprot.org/citations/8995684 | http://purl.uniprot.org/core/volume | "71"xsd:string |
| http://purl.uniprot.org/citations/8995684 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/8995684 |
| http://purl.uniprot.org/citations/8995684 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/8995684 |
| http://purl.uniprot.org/citations/8995684 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/8995684 |
| http://purl.uniprot.org/citations/8995684 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/8995684 |