Download 4461-4469 November 29, 2012

Survey
yes no Was this document useful for you?
   Thank you for your participation!

* Your assessment is very important for improving the workof artificial intelligence, which forms the content of this project

page
1
page
2
page
3
page
4
page
5
page
6
page
7
Document related concepts
no text concepts found
Transcript 
Structural insights into inhibition of the bivalent meninMLL interaction by small molecules in leukemia
by Aibin Shi, Marcelo J. Murai, Shihan He, George Lund, Thomas Hartley, Trupta
Purohit, Gireesh Reddy, Maksymilian Chruszcz, Jolanta Grembecka, and Tomasz
Cierpicki
Blood
Volume 120(23):4461-4469
November 29, 2012
©2012 by American Society of Hematology
Structure of the menin-MLL complex.
Aibin Shi et al. Blood 2012;120:4461-4469
©2012 by American Society of Hematology
Crystal structure of the menin–MI-2 complex.
Aibin Shi et al. Blood 2012;120:4461-4469
©2012 by American Society of Hematology
Development of second-generation menin-MLL inhibitors.
Aibin Shi et al. Blood 2012;120:4461-4469
©2012 by American Society of Hematology
Small molecules targeting the MBM1 site efficiently disrupt bivalent menin-MLL interaction.
Aibin Shi et al. Blood 2012;120:4461-4469
©2012 by American Society of Hematology
Second-generation inhibitor MI-2-2 exhibits strongly enhanced cellular activities compared with
MI-2.
Aibin Shi et al. Blood 2012;120:4461-4469
©2012 by American Society of Hematology
MI-2-2 exhibits pronounced activity in MV4;11 human leukemia cells with MLL-AF4 translocation.
Aibin Shi et al. Blood 2012;120:4461-4469
©2012 by American Society of Hematology
Related documents