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Targeting the Hsp90-Cdc37-client protein interaction to disrupt Hsp90 chaperone machinery
Li, Ting1; Jiang, Hu-Lin2; Tong, Yun-Guang3,4; Lu, Jin-Jian1
2018-04-27
Source PublicationJOURNAL OF HEMATOLOGY & ONCOLOGY
ISSN1756-8722
Volume11
Abstract

Heat shock protein 90 (Hsp90) is a critical molecular chaperone protein that regulates the folding, maturation, and stability of a wide variety of proteins. In recent years, the development of Hsp90-directed inhibitors has grown rapidly, and many of these inhibitors have entered clinical trials. In parallel, the functional dissection of the Hsp90 chaperone machinery has highlighted the activity disruption of Hsp90 co-chaperone as a potential target. With the roles of Hsp90 co-chaperones being elucidated, cell division cycle 37 (Cdc37), a ubiquitous co-chaperone of Hsp90 that directs the selective client proteins into the Hsp90 chaperone cycle, shows great promise. Moreover, the Hsp90-Cdc37-client interaction contributes to the regulation of cellular response and cellular growth and is more essential to tumor tissues than normal tissues. Herein, we discuss the current understanding of the clients of Hsp90-Cdc37, the interaction of Hsp90-Cdc37-client protein, and the therapeutic possibilities of targeting Hsp90-Cdc37-client protein interaction as a strategy to inhibit Hsp90 chaperone machinery to present new insights on alternative ways of inhibiting Hsp90 chaperone machinery.

KeywordHsp90 Chaperone Machinery Cdc37 Kinase Client Protein Interaction
DOI10.1186/s13045-018-0602-8
URLView the original
Indexed BySCI
Language英语
WOS Research AreaOncology ; Hematology
WOS SubjectOncology ; Hematology
WOS IDWOS:000431301500001
PublisherBIOMED CENTRAL LTD
The Source to ArticleWOS
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Cited Times [WOS]:3   [WOS Record]     [Related Records in WOS]
Document TypeJournal article
CollectionInstitute of Chinese Medical Sciences
Affiliation1.State Key Laboratory of Quality Research in Chinese Medicine, Institute of Chinese Medical Sciences, University of Macau, Avenida da Universidade, Taipa, Macau China
2.State Key Laboratory of Natural Medicines, China Pharmaceutical University, Nanjing, China
3.Department of Pathology, Xinxiang Medical University, 601 East Jinsui Ave, Xinxiang, Henan China
4.Omigen, Inc., 15375 Barranca Pkwy, Irvine, CA H106 USA
First Author AffilicationInstitute of Chinese Medical Sciences
Recommended Citation
GB/T 7714
Li, Ting,Jiang, Hu-Lin,Tong, Yun-Guang,et al. Targeting the Hsp90-Cdc37-client protein interaction to disrupt Hsp90 chaperone machinery[J]. JOURNAL OF HEMATOLOGY & ONCOLOGY,2018,11.
APA Li, Ting,Jiang, Hu-Lin,Tong, Yun-Guang,&Lu, Jin-Jian.(2018).Targeting the Hsp90-Cdc37-client protein interaction to disrupt Hsp90 chaperone machinery.JOURNAL OF HEMATOLOGY & ONCOLOGY,11.
MLA Li, Ting,et al."Targeting the Hsp90-Cdc37-client protein interaction to disrupt Hsp90 chaperone machinery".JOURNAL OF HEMATOLOGY & ONCOLOGY 11(2018).
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