Lee, C.H., et al. (2012) Inhibition of Heat Shock Protein (Hsp) 27 Potentiates the Suppressive Effect of Hsp90 Inhibitors in Targeting Breast Cancer Stem-Like Cells. Biochimie, 6, 1382-1389.
https://doi.org/10.1016/j.biochi.2012.02.034

has been cited by the following article:

• TITLE: Research Progress of Heat Shock Protein 90 and Hepatocellular Carcinoma

  AUTHORS: Qiyu Jiang, Xiongshan Shen

  KEYWORDS: Liver Cancer, Heat Shock Protein 90, Molecular Chaperone, Inhibitor, Targeted Therapy

  JOURNAL NAME: International Journal of Clinical Medicine, Vol.11 No.2, February 13, 2020

  ABSTRACT: Heat shock protein (HSP) is a kind of protein that mainly acts as a molecular chaperone to participate in the synthesis and folding of proteins, maintain the spatial conformation of proteins and protect cells from damage and other important biological functions. HSP90 plays an important role in maintaining molecular chaperone structure, regulating cell cycle and apoptosis, coordinating hormone signal transduction and promoting wound healing. And HSP90 also plays an important role in the occurrence and progression of tumors. In recent years, HSP90 inhibitors have made some achievements in molecular targeted therapy for malignant tumors, but further research is needed in clinical application. In this paper, the research status of the relationship between hepatocellular carcinoma targeted by heat shock protein 90 was reviewed.