| http://purl.uniprot.org/citations/15972449 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15972449 | http://www.w3.org/2000/01/rdf-schema#comment | "The zeta-associated protein of 70 kDa (ZAP-70) is expressed in patients with aggressive chronic lymphocytic leukemia (CLL). We found that ZAP-70+ CLL cells expressed activated heat-shock protein 90 (Hsp90) with high binding affinity for Hsp90 inhibitors, such as 17-allyl-amino-demethoxy-geldanamycin (17-AAG), whereas normal lymphocytes or ZAP-70-CLL cells expressed nonactivated Hsp90. Activated Hsp90 bound and stabilized ZAP-70, which behaved like an Hsp90 client protein only in CLL cells. Treatment with Hsp90 inhibitors such as 17-AAG and 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG) induced ZAP-70 degradation and apoptosis in CLL cells but not in T cells, and also impaired B-cell receptor signaling in leukemia cells. Transduction of ZAP-70-CLL cells with an adenovirus encoding ZAP-70 activated Hsp90 and specifically rendered the leukemia cells sensitive to 17-AAG. These data indicate that Hsp90 is necessary for ZAP-70 expression and activity; that ZAP-70 is unique among Hsp90 clients, in that its chaperone-dependency is conditional on the cell type in which it is expressed; and also that ZAP-70 is required for cell survival and signaling in CLL. Additionally, ZAP-70 expression in CLL cells confers markedly heightened sensitivity to 17-AAG or 17-DMAG, suggesting that these or other Hsp90 inhibitors could be valuable therapeutically in patients with aggressive CLL."xsd:string |
| http://purl.uniprot.org/citations/15972449 | http://purl.org/dc/terms/identifier | "doi:10.1182/blood-2005-03-1099"xsd:string |
| http://purl.uniprot.org/citations/15972449 | http://purl.uniprot.org/core/author | "Chen L."xsd:string |
| http://purl.uniprot.org/citations/15972449 | http://purl.uniprot.org/core/author | "Kamal A."xsd:string |
| http://purl.uniprot.org/citations/15972449 | http://purl.uniprot.org/core/author | "Prada C.E."xsd:string |
| http://purl.uniprot.org/citations/15972449 | http://purl.uniprot.org/core/author | "Burrows F.J."xsd:string |
| http://purl.uniprot.org/citations/15972449 | http://purl.uniprot.org/core/author | "Kipps T.J."xsd:string |
| http://purl.uniprot.org/citations/15972449 | http://purl.uniprot.org/core/author | "Castro J.E."xsd:string |
| http://purl.uniprot.org/citations/15972449 | http://purl.uniprot.org/core/author | "Loria O."xsd:string |
| http://purl.uniprot.org/citations/15972449 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/15972449 | http://purl.uniprot.org/core/name | "Blood"xsd:string |
| http://purl.uniprot.org/citations/15972449 | http://purl.uniprot.org/core/pages | "2506-2512"xsd:string |
| http://purl.uniprot.org/citations/15972449 | http://purl.uniprot.org/core/title | "ZAP-70 is a novel conditional heat shock protein 90 (Hsp90) client: inhibition of Hsp90 leads to ZAP-70 degradation, apoptosis, and impaired signaling in chronic lymphocytic leukemia."xsd:string |
| http://purl.uniprot.org/citations/15972449 | http://purl.uniprot.org/core/volume | "106"xsd:string |
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