Related Experiment Video
Updated: Jul 20, 2026

Intracellular Refolding Assay
Published on: January 24, 2012
The role of heat shock proteins as chaperones on several human diseases
1Department of Biochemistry, Zanjan University of Medical Sciences, Shahrak Karmandan, Zanjan, Iran. mellati3000@yahoo.com
Abstract:
Some heat shock proteins HSPs, act as molecular chaperones. These and other molecular chaperones that are not HSPs, function in a variety of protein biosynthetic event and protect proteins from the deleterious effects of stressors by stabilizing, and refolding proteins. They assist protein folding, assembly, transport and degradation. Several human diseases such as neurodegeneration, cancer, aging, retinal dystrophy, and inflammation arise from defects HSPs and protein folding. This review demonstrates the chaperones such as properties of HSPs in cellular processes and their implication in different kind of human diseases.
Related Concept Videos
Molecular Chaperones and Protein Folding
The...
Molecular Chaperones and Protein Folding
The...
Bacterial Protein Maturation
Other Stress Responses in Bacteria
Diversity of Archaea III
Diversity of Archaea IV

