Menin-MLL inhibitors block oncogenic transformation by MLL-fusion proteins in a fusion partner-independent manner

Leukemia. 2016 Feb;30(2):508-13. doi: 10.1038/leu.2015.144. Epub 2015 Jun 18.

Authors

S He¹, B Malik¹, D Borkin¹, H Miao¹, S Shukla¹, K Kempinska¹, T Purohit¹, J Wang¹, L Chen¹, B Parkin², S N Malek², G Danet-Desnoyers³, A G Muntean¹, T Cierpicki¹, J Grembecka¹

Affiliations

¹ Department of Pathology, University of Michigan, Ann Arbor MI, USA.
² Division of Hematology and Oncology, Department of Internal Medicine, University of Michigan, Ann Arbor MI, USA.
³ Division of Hematology-Oncology, Department of Medicine, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.

No abstract available

Publication types

Letter
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't

MeSH terms

Animals
Cell Line, Tumor
Cell Transformation, Neoplastic / drug effects*
Histone-Lysine N-Methyltransferase / antagonists & inhibitors*
Humans
Leukemia, Biphenotypic, Acute / drug therapy*
Leukemia, Biphenotypic, Acute / pathology
Mice
Myeloid-Lymphoid Leukemia Protein / antagonists & inhibitors*
Myeloid-Lymphoid Leukemia Protein / physiology*
Oncogene Proteins, Fusion / physiology*
Proto-Oncogene Proteins / antagonists & inhibitors*

Substances

KMT2A protein, human
MEN1 protein, human
MLL-AF4 fusion protein, human
MLL-AF9 fusion protein, human
Oncogene Proteins, Fusion
Proto-Oncogene Proteins
Myeloid-Lymphoid Leukemia Protein
Histone-Lysine N-Methyltransferase

Grants and funding