SUV39H1 is a New Client Protein of Hsp90 Degradated by Chaetocin as a Novel C-Terminal Inhibitor of Hsp90-Reference-Cited by-同舟云学术

SUV39H1 is a New Client Protein of Hsp90 Degradated by Chaetocin as a Novel C-Terminal Inhibitor of Hsp90

Published:2021-01-01 Issue:1 Volume:29 Page:73-82
ISSN:1976-9148
Container-title:Biomolecules & Therapeutics
language:en
Short-container-title:Biomolecules & Therapeutics

Author:

Lian Bin¹,Lin Qian¹,Tang Wei¹,Qi Xin¹,Li Jing¹²³

Affiliation:

1. Key Laboratory of Marine Drugs, Chinese Ministry of Education, School of Medicine and Pharmacy, Ocean University of China, Qingdao 266003, China

2. Laboratory for Marine Drugs and Bioproducts of Qingdao National Laboratory for Marine Science and Technology, Qingdao 266237, China

3. Open Studio for Drugability Research of Marine Natural Products, Pilot National Laboratory for Marine Science and Technology, Qingdao 266000, China

Funder

National Natural Science Foundation of China

NSFC Shandong Joint Fund

Qingdao National Laboratory

Central Universities

National Science and Technology Major Project for Significant New Drugs Development

Publisher

The Korean Society of Applied Pharmacology

Subject

Drug Discovery,Pharmacology,Molecular Medicine,Biochemistry

Link

http://pdf.medrang.co.kr/BT2/2021/029/BT029-01-09.pdf

Reference48 articles.

1. The Histone Methyltransferase SUV39H1 Suppresses Embryonal Rhabdomyosarcoma Formation in Zebrafish

2. Modulation of Chaperone Function and Cochaperone Interaction by Novobiocin in the C-terminal Domain of Hsp90

3. HSP90 inhibitors in the clinic: what have we learnt?

4. Recruitment of the Histone Methyltransferase SUV39H1 and Its Role in the Oncogenic Properties of the Leukemia-Associated PML-Retinoic Acid Receptor Fusion Protein

5. Anti-leukemia activity of chaetocin via death receptor-dependent apoptosis and dual modulation of the histone methyl-transferase SUV39H1

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