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Stuart K. Calderwood

Researcher at Beth Israel Deaconess Medical Center

Publications -  273
Citations -  21191

Stuart K. Calderwood is an academic researcher from Beth Israel Deaconess Medical Center. The author has contributed to research in topics: Heat shock protein & HSF1. The author has an hindex of 74, co-authored 262 publications receiving 19626 citations. Previous affiliations of Stuart K. Calderwood include University of Queensland & Royal Victoria Infirmary.

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HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine.

TL;DR: Findings indicate that CD14 is a co-receptor for HSP70-mediated signaling in human monocytes and are indicative of an previously unrecognized function for H SP70 as an extracellular protein with regulatory effects on human monocyte, having a dual role as chaperone and cytokine.
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Novel signal transduction pathway utilized by extracellular HSP70: role of toll-like receptor (TLR) 2 and TLR4.

TL;DR: It is demonstrated that exogenously added HSP70 possesses potent cytokine activity, with the ability to bind with high affinity to the plasma membrane, elicit a rapid intracellular Ca2+ flux, activate NF-κB, and up-regulate the expression of pro-inflammatory cytokines in human monocytes.
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Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications

TL;DR: Although Hsp levels are not informative at the diagnostic level, they are useful biomarkers for carcinogenesis in some tissues and signal the degree of differentiation and the aggressiveness of some cancers.
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Heat shock proteins in cancer: chaperones of tumorigenesis.

TL;DR: The heat shock proteins have thus become targets for rational anti-cancer drug design: HSP90 inhibitors are currently showing much promise in clinical trials, whereas the increased expression of HSPs in tumors is forming the basis of chaperone-based immunotherapy.
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Sequential Phosphorylation by Mitogen-activated Protein Kinase and Glycogen Synthase Kinase 3 Represses Transcriptional Activation by Heat Shock Factor-1

TL;DR: Experiments indicate that MAPK is a potent inhibitor of HSF-1 function and may be involved in repressing the heat shock response during normal growth and development and deactivating the heatshock response during recovery from stress.