Mimicking H3 Substrate Arginine in the Design of G9a Lysine Methyltransferase Inhibitors for Cancer Therapy: A Computational Study for Structure-Based Drug Design-Reference-Cited by-同舟云学术

Mimicking H3 Substrate Arginine in the Design of G9a Lysine Methyltransferase Inhibitors for Cancer Therapy: A Computational Study for Structure-Based Drug Design

Published:2021-02-22 Issue:9 Volume:6 Page:6100-6111
ISSN:2470-1343
Container-title:ACS Omega
language:en
Short-container-title:ACS Omega

Author:

Chandar Charles M. Ramya¹,Li Mu-Chun²³^ORCID,Hsieh Hsing-Pang²³⁴^ORCID,Coumar Mohane Selvaraj¹^ORCID

Affiliation:

1. Centre for Bioinformatics, School of Life Sciences, Pondicherry University, Kalapet, Puducherry 605014, India

2. Institute of Biotechnology and Pharmaceutical Research, National Health Research Institutes, 35 Keyan Road, Zhunan, Miaoli County, Taiwan 350, ROC

3. Department of Chemistry, National Tsing Hua University, No. 101, Section 2, Kuang-Fu Road, Hsinchu 300, Taiwan

4. Biomedical Translation Research Center, Academia Sinica, Taipei 115, Taiwan

Funder

Ministry of Education

National Health Research Institutes

Department of Biotechnology , Ministry of Science and Technology

National Cheng Kung University

Ministry of Science and Technology, Taiwan

Publisher

American Chemical Society (ACS)

Subject

General Chemical Engineering,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acsomega.0c04710

Reference63 articles.

1. SET Domain-containing Protein, G9a, Is a Novel Lysine-preferring Mammalian Histone Methyltransferase with Hyperactivity and Specific Selectivity to Lysines 9 and 27 of Histone H3

2. A Complex with Chromatin Modifiers That Occupies E2F- and Myc-Responsive Genes in G 0 Cells

3. G9a, a multipotent regulator of gene expression

4. Histone methyltransferases G9a and GLP form heteromeric complexes and are both crucial for methylation of euchromatin at H3-K9

5. Partitioning and Plasticity of Repressive Histone Methylation States in Mammalian Chromatin

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