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• W2770683693 startingPage "345" @default.
• W2770683693 abstract "Large heat shock proteins (HSPs) or stress proteins, including Hsp110 and Grp170, are unique molecular chaperones with superior capability of shuttling tumor protein antigens into professional antigen-presenting cells, such as dendritic cells, for highly efficient cross-presentation and T cell priming. Reconstituted chaperone complexes of large HSP and tumor protein antigen have been demonstrated to generate a robust antigen-specific T lymphocyte response with therapeutic potency against multiple cancer types in preclinical models. Here, we describe the methods for preparing this recombinant chaperone complex vaccine and analyzing the vaccine-induced activation of antigen-specific T cells using in vitro and in vivo systems." @default.
• W2770683693 created "2017-12-04" @default.
• W2770683693 creator A5016166287 @default.
• W2770683693 creator A5042783365 @default.
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• W2770683693 date "2017-11-26" @default.
• W2770683693 modified "2023-10-03" @default.
• W2770683693 title "Creation of Recombinant Chaperone Vaccine Using Large Heat Shock Protein for Antigen-Targeted Cancer Immunotherapy" @default.
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• W2770683693 doi "https://doi.org/10.1007/978-1-4939-7477-1_25" @default.
• W2770683693 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5812279" @default.
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• W2770683693 hasPublicationYear "2017" @default.
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