In Situ Proteome Profiling and Bioimaging Applications of Small-Molecule Affinity-Based Probes Derived From DOT1L Inhibitors-Reference-Cited by-同舟云学术

In Situ Proteome Profiling and Bioimaging Applications of Small-Molecule Affinity-Based Probes Derived From DOT1L Inhibitors

Published:2016-04-26 Issue:23 Volume:22 Page:7824-7836
ISSN:0947-6539
Container-title:Chemistry - A European Journal
language:en
Short-container-title:Chem. Eur. J.

Author:

Zhu Biwei¹,Zhang Hailong¹,Pan Sijun¹,Wang Chenyu¹,Ge Jingyan²,Lee Jun-Seok³,Yao Shao Q.¹

Affiliation:

1. Department of Chemistry; National University of Singapore; 3 Science drive 3 Singapore 117543 Singapore

2. Institute of Bioengineering; Zhejiang University of Technology; Hangzhou 310014 P.R. China

3. Molecular Recognition Research Center; Korea Institute of Science and Technology (KIST) and Department of Biological Chemistry; University of Science & Technology; Republic of Korea

Funder

National Medical Research Council

Ministry of Education

Publisher

Wiley

Subject

General Chemistry,Catalysis,Organic Chemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/chem.201600259/fullpdf

Reference54 articles.

1. Catalytic site remodelling of the DOT1L methyltransferase by selective inhibitors

2. Structure of the Catalytic Domain of Human DOT1L, a Non-SET Domain Nucleosomal Histone Methyltransferase

3. hDOT1L Links Histone Methylation to Leukemogenesis

4. Dot1p Modulates Silencing in Yeast by Methylation of the Nucleosome Core

5. Methylation of H3-Lysine 79 Is Mediated by a New Family of HMTases without a SET Domain

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