An iridium(iii)-based irreversible protein–protein interaction inhibitor of BRD4 as a potent anticancer agent-Reference-Cited by-同舟云学术

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An iridium(iii)-based irreversible protein–protein interaction inhibitor of BRD4 as a potent anticancer agent

Published:2015 Issue:10 Volume:6 Page:5400-5408
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Zhong Hai-Jing¹²³⁴⁵,Lu Lihua⁶⁷⁸⁵,Leung Ka-Ho⁶⁷⁸⁵,Wong Catherine C. L.⁹¹⁰¹¹¹²¹³,Peng Chao⁹¹⁰¹¹¹²¹³,Yan Siu-Cheong¹⁴¹⁵¹⁶⁵,Ma Dik-Lung⁶⁷⁸⁵^ORCID,Cai Zongwei¹⁷⁶⁷⁸¹⁸,David Wang Hui-Min¹⁹²⁰²¹²²²³,Leung Chung-Hang¹²³⁴⁵

Affiliation:

1. State Key Laboratory of Quality Research in Chinese Medicine

2. Institute of Chinese Medical Sciences

3. University of Macau

4. Macao

5. China

6. Department of Chemistry

7. Hong Kong Baptist University

8. Kowloon Tong

9. National Center for Protein Science Shanghai

10. State Key Laboratory of Cell Biology

11. Institute of Biochemistry and Cell Biology

12. Shanghai Institutes for Biological Sciences

13. Chinese Academy of Sciences

14. Department of Applied Biology and Chemical Technology

15. The Hong Kong Polytechnic University

16. Hung Hom, Kowloon

17. Partner State Key Laboratory of Environmental and Biological Analysis

18. P. R. China

19. Department of Fragrance and Cosmetic Science

20. Kaohsiung Medical University

21. Kaohsiung 807

22. Republic of China

23. Graduate Institute of Natural Products

Abstract

This is the first report of a metal complex that targets the BRD4-acylated histone protein-protein interaction (PPI).

Funder

Hong Kong Baptist University

Health and Medical Research Fund

Science and Technology Development Fund

Universidade de Macau

The Research Grants Council, University Grants Committee, Hong Kong

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2015/SC/C5SC02321A

Reference60 articles.

1. The Role of Chromatin during Transcription

2. Regulation of nucleosome dynamics by histone modifications

3. Multivalent engagement of chromatin modifications by linked binding modules

4. Epigenetic protein families: a new frontier for drug discovery

5. How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers

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