scholarly journals The Role of Nuclear Receptor–Binding SET Domain Family Histone Lysine Methyltransferases in Cancer

2017 ◽  
Vol 7 (6) ◽  
pp. a026708 ◽  
Author(s):  
Richard L. Bennett ◽  
Alok Swaroop ◽  
Catalina Troche ◽  
Jonathan D. Licht
Keyword(s):  
Nuclear Receptor ◽  
Receptor Binding ◽  
Set Domain ◽  
Domain Family ◽  
Histone Lysine ◽  
Lysine Methyltransferases ◽  
Histone Lysine Methyltransferases

Role of Histone Lysine Methyltransferases SUV39H1 and SETDB1 in Gliomagenesis: Modulation of Cell Proliferation, Migration, and Colony Formation

2013 ◽  
Vol 16 (1) ◽  
pp. 70-82 ◽  
Author(s):  
Anastasia Spyropoulou ◽  
Antonios Gargalionis ◽  
Georgia Dalagiorgou ◽  
Christos Adamopoulos ◽  
Kostas A. Papavassiliou ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Colony Formation ◽  
Histone Lysine ◽  
Lysine Methyltransferases ◽  
Histone Lysine Methyltransferases

scholarly journals Role of several histone lysine methyltransferases in tumor development

2016 ◽  
Vol 4 (3) ◽  
pp. 293-299 ◽  
Author(s):  
JIFU LI ◽  
SHUNQIN ZHU ◽  
XIAO-XUE KE ◽  
HONGJUAN CUI
Keyword(s):  
Tumor Development ◽  
Histone Lysine ◽  
Lysine Methyltransferases ◽  
Histone Lysine Methyltransferases

The Arabidopsis thaliana SET-domain-containing protein ASHH1/SDG26 interacts with itself and with distinct histone lysine methyltransferases

2012 ◽  
Vol 125 (5) ◽  
pp. 679-692 ◽  
Author(s):  
María del Pilar Valencia-Morales ◽  
José Alberto Camas-Reyes ◽  
José Luis Cabrera-Ponce ◽  
Raúl Alvarez-Venegas
Keyword(s):  
Arabidopsis Thaliana ◽  
Set Domain ◽  
Histone Lysine ◽  
Lysine Methyltransferases ◽  
Histone Lysine Methyltransferases

The role of NSD2 (Nuclear receptor‐binding SET domain‐containing protein) in AR‐mediated transcriptional regulation

2008 ◽  
Vol 22 (S2) ◽  
pp. 202-202
Author(s):  
Hee‐Bum Kang ◽  
Hyo‐Kyoung Choi ◽  
Kyung‐Chul Choi ◽  
Yoo‐Hyun Lee ◽  
Jung‐Yoon Yoo ◽  
...  
Keyword(s):  
Transcriptional Regulation ◽  
Nuclear Receptor ◽  
Receptor Binding ◽  
Set Domain

scholarly journals Methylation of geometrically constrained lysine analogues by histone lysine methyltransferases

2020 ◽  
Vol 56 (20) ◽  
pp. 3039-3042 ◽  
Author(s):  
Abbas H. K. Al Temimi ◽  
Paul B. White ◽  
Marcus J. M. Mulders ◽  
Nicole G. A. van der Linden ◽  
Richard H. Blaauw ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Histone Lysine ◽  
Lysine Methyltransferases ◽  
Geometrically Constrained ◽  
Histone Lysine Methyltransferases

Histone lysine methyltransferases (KMTs) exhibit substrate specificity for lysine and its geometrically constrained mimics.

scholarly journals Lysine Ethylation by Histone Lysine Methyltransferases

ChemBioChem ◽  
2019 ◽  
Vol 21 (3) ◽  
pp. 392-400 ◽  
Author(s):  
Abbas H. K. Al Temimi ◽  
Michael Martin ◽  
Qingxi Meng ◽  
Danny C. Lenstra ◽  
Ping Qian ◽  
...  
Keyword(s):  
Histone Lysine ◽  
Lysine Methyltransferases ◽  
Histone Lysine Methyltransferases
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