Related Experiment Video
Updated: Jul 29, 2026

Intracellular Refolding Assay
Published on: January 24, 2012
Molecular chaperones and cancer immunotherapy
X Y Wang1, J G Facciponte, J R Subjeck
1Department of Cellular Stress Biology and Urologic Oncology, Roswell Park Cancer Institute, Buffalo, NY 14263, USA. xiang-yang.wang@roswellpark.org
Abstract:
As one of the most abundant and evolutionally conserved intracellular proteins, heat shock proteins, also known as stress proteins or molecular chaperones, perform critical functions in maintaining cell homeostasis under physiological as well as stress conditions. Certain chaperones in extracellular milieu are also capable of modulating innate and adaptive immunity due to their ability to chaperone polypeptides and to interact with the host's immune system, particularly professional antigen-presenting cells. The immunomodulating properties of chaperones have been exploited for cancer immunotherapy. Clinical trials using chaperone-based vaccines to treat various malignancies are ongoing.
Related Concept Videos
Molecular Chaperones and Protein Folding
The...
Cancer Therapies
However, cancer treatments can pose several challenges, as therapies used to kill cancer cells are generally also toxic to normal cells. Moreover, cancer cells mutate rapidly and can develop resistance to chemical agents or radiation therapy. Besides, all types of cancer cells may not respond to the same therapy. Some cancer cells respond to one...
Targeted Cancer Therapies
There are several types of targeted therapies against specific...
Molecular Chaperones and Protein Folding
The...
Targeted Cancer Therapies
There are several types of targeted therapies against specific...
Tumor Immunotherapy

