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Pramod K. Srivastava

Researcher at University of Connecticut

Publications -  405
Citations -  29058

Pramod K. Srivastava is an academic researcher from University of Connecticut. The author has contributed to research in topics: Heat shock protein & Antigen. The author has an hindex of 79, co-authored 390 publications receiving 27330 citations. Previous affiliations of Pramod K. Srivastava include Gujarat University & Memorial Sloan Kettering Cancer Center.

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Clinical impact of COVID-19 on patients with cancer (CCC19): a cohort study.

Nicole M. Kuderer, +239 more
- 20 Jun 2020 - 
TL;DR: The outcomes of a cohort of patients with cancer and COVID-19 are characterised and potential prognostic factors for mortality and severe illness are identified and race and ethnicity, obesity status, cancer type, type of anticancer therapy, and recent surgery were not associated with mortality.
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Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the NF-κB pathway

TL;DR: It is reported here that heat shock proteins (HSP), the most abundant and conserved mammalian molecules, constitute such an internal signal that provides a unified mechanism for response to internal and external stimuli.
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CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin.

TL;DR: It is shown here that complexes of peptides with heat shock proteins hsp90, calreticulin, and hsp70 are also taken up by macrophages and dendritic cells and re-presented by MHC class I molecules.
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Roles of heat-shock proteins in innate and adaptive immunity

TL;DR: The immunological properties of HSPs enable them to be used in new immunotherapies of cancers and infections and make them uniquely suited to an important role in organismal survival by their participation in innate and adaptive immune responses.
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A Mechanism for the Specific Immunogenicity of Heat Shock Protein-Chaperoned Peptides

TL;DR: It is shown that exogenous antigens chaperoned by a heat shockprotein can be channeled into the endogenous pathway, presented by MHC class I molecules, and recognized by CD8+ T lymphocytes, which provides a basis for the tumor-specific and virus-specific immunogenicity of cognate heat shock protein preparations and offer a mechanism for the classical phenomenon of cross-priming.