Related Experiment Video
Updated: May 5, 2026
Intracellular Refolding Assay
Published on: January 24, 2012
Heat shock protein 110: A novel candidate for disease diagnosis and targeted therapy
Congke Zhao1, Honglin Xiang2, Mengqi Li3
1Key Laboratory of Study and Discovery of Small Targeted Molecules of Hunan Province, Department of Pharmacy, School of Medicine, Hunan Normal University, Changsha 410013, Hunan, China; Department of Medicinal Chemistry, Xiangya School of Pharmaceutical Sciences, Central South University, Changsha 410013, Hunan, China; Hunan Key Laboratory of Diagnostic and Therapeutic Drug Research for Chronic Diseases, Changsha 410013, Hunan, China; Hunan Key Laboratory of Organ Fibrosis, Changsha 410013, Hunan, China.
Abstract:
The heat shock protein 110 (Hsp110) family in eukaryotes plays a pivotal role in maintaining cellular proteostasis. As a unique class of molecular chaperones, Hsp110s act as both independent chaperones and cochaperones for other essential molecular chaperones. Malfunction of Hsp110s is involved in many diseases. Thus targeting Hsp110s or its interactions with client proteins may provide new approaches for developing therapeutics. In this review, we describe the current understanding of the role and molecular mechanism of Hsp110s in disease development, and discuss the recent exploration of Hsp110s as potential targets to provide a novel direction for disease diagnosis and targeted therapy.
