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- W2410130676 abstract "Cellular stress proteins like the classical heat-shock proteins (HSPs) hsp70 (, , ), hsp90 () and hsp110 (); the glucose-regulated proteins gp96/GRP94 (,) and grp170 (); as well as the endoplasmic chaperone calreticulin (,) have been shown to induce cytotoxic T-cell responses and protective immunity when isolated from tumor or infected cells and used to vaccinate animals (, , ; reviewed in refs. 11–17). The specificity of the immune responses is owing to antigenic peptides associated with the HSPs (, , , , , , , , ). The HSP-peptide complexes are taken up by professional antigen-presenting cells (APCs) for effective presentation of the peptides to T cells (,, , , , , , ). The extensively studied endoplasmic reticulum-resident chaperone gp96 is most efficient and promising in this regard (, , , , , ); encouraging clinical studies with human cancer patients ()." @default.
- W2410130676 created "2016-06-24" @default.
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- W2410130676 date "2003-11-21" @default.
- W2410130676 modified "2023-10-16" @default.
- W2410130676 title "Single-Chain Fv-Based Affinity Purification of the Cellular Stress Protein gp96 for Vaccine Development" @default.
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- W2410130676 doi "https://doi.org/10.1385/1-59259-334-8:393" @default.
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