Structure of the Catalytic Domain of Human DOT1L, a Non-SET Domain Nucleosomal Histone Methyltransferase-Reference-Cited by-同舟云学术

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

Published:2003-03 Issue:5 Volume:112 Page:711-723
ISSN:0092-8674
Container-title:Cell
language:en
Short-container-title:Cell

Author:

Min Jinrong,Feng Qin,Li Zhizhong,Zhang Yi,Xu Rui-Ming

Publisher

Elsevier BV

Subject

General Biochemistry, Genetics and Molecular Biology

Reference45 articles.

1. Gene silencing;Briggs;Nature,2002

2. Crystallography & NMR system;Brunger;Acta Crystallogr. D,1998

3. Ribbons;Carson;Methods Enzymol.,1997

4. AdoMet-dependent methylation, DNA methyltransferases and base flipping;Cheng;Nucleic Acids Res.,2001

5. Chromatin silencing protein and pachytene checkpoint regulator Dot1p has a methyltransferase fold;Dlakic;Trends Biochem. Sci.,2001

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1. Biological Relevance of Dual Lysine and N-Terminal Methyltransferase METTL13;Biomolecules;2024-09-03

2. Design, synthesis, and biological evaluation of adenosine derivatives targeting DOT1L and HATs as anti-leukemia agents;Bioorganic Chemistry;2024-09

3. DOT1L-mediated RAP80 methylation promotes BRCA1 recruitment to elicit DNA repair;Proceedings of the National Academy of Sciences;2024-08-22

4. Discovery of first-in-class DOT1L inhibitors against the R231Q gain-of-function mutation in the catalytic domain with therapeutic potential of lung cancer;Acta Pharmaceutica Sinica B;2024-08

5. Pharmacological targeting of the cancer epigenome;Nature Cancer;2024-06-27

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