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Research Progress of Heat Shock Protein 90 and Hepatocellular Carcinoma

Research Progress of Heat Shock Protein 90 and Hepatocellular Carcinoma
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摘要 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. 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.
出处 《International Journal of Clinical Medicine》 2020年第2期43-52,共10页 临床医学国际期刊(英文)
关键词 LIVER Cancer Heat Shock Protein 90 MOLECULAR CHAPERONE INHIBITOR TARGETED Therapy Liver Cancer Heat Shock Protein 90 Molecular Chaperone Inhibitor Targeted Therapy
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  • 1Yi-FengWu,Ming-FuCao,Yan-PingGao,FeiChen,TaoWang,EdwardP.Zumbika,Kai-XianQian.Down-modulation of heat shock protein 70 and up-modulation of Caspase-3 during schisandrin B-induced apoptosis in human hepatoma SMMC-7721 cells[J].World Journal of Gastroenterology,2004,10(20):2944-2948. 被引量:29
  • 2Xiao-PingWang Guo-ZhenLiu Ai-LiSong Rui-FenChen Hai-YanLi YuLiu.Expression and significance of heat shock protein 70 and glucose-regulated protein 94 in human esophageal carcinoma[J].World Journal of Gastroenterology,2005,11(3):429-432. 被引量:28
  • 3Stechmann A et al. Evolutionary origins of Hsp90 chaperones and a deep paralogy in their bacterial ancestors. J Eukaryot Microbiol, 2004, 51(3): 364-373.
  • 4Jonathan D el al. Immunoelectron microscopy provides evidence that tumor necrosis factor receptor-associated protein 1 (trap-l) is a mitochondrial protein which also localizes at specific extramitochondrial sites. Exp Cell Res, 2000, 260(1): 30-39.
  • 5Monte AA et al. Proof of interaction between Leishmania SIR2RPI deacetylase and chaperone HSP83. Parasitol Res, 2007, 100(4): 811-818.
  • 6Chen Bet al. The HSP90 family of genes in the human genome: Insights into their divergence and evolution. Genomics, 2005, (86): 627-637.
  • 7Schweinfest CW et al. Cloning and sequence analysis of Hsp89alpha DeltaN, a new member of theHsp90 gene family. Biochim Biophys Acta, 1998, 1398(1): 18-24.
  • 8Anna Z et al. Hsp90n An accidental product of a fortuitous chromosomal translocation rather than a regular Hsp90 family member of human proteome. Biochim Biophys Acta, 2008, 1784(11): 1844-1846.
  • 9Takayuki KN et al. Substrate-binding characteristics of proteins in the 90 kDa heat shock protein family. Biochem J, 2001, 354(Pt 3): 663-670.
  • 10Kobayakawa T et al. Substitution of only two residues of human Hsp90α causes impeded dimerization of Hsp90β. Cell Stress Chaperones, 2008, 13(1): 97-104.

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