Cambridge, MA, United States
Cambridge, MA, United States
SEARCH FILTERS
Time filter
Source Type

Patent
Epizyme | Date: 2017-04-05

The present invention relates to aryl- or heteroaryl-substituted benzene compounds (I). The present invention also relates to pharmaceutical compositions containing these compounds and methods of treating cancer by administering these compounds and pharmaceutical compositions to subjects in need thereof. The present invention also relates to the use of such compounds for research or other non-therapeutic purposes.


The present invention relates to substituted benzene compounds and bicyclic heteroaryl compounds. The present invention also relates to pharmaceutical compositions containing these compounds and methods of treating cancer by administering these compounds and pharmaceutical compositions to subjects in need thereof. The present invention also relates to the use of such compounds for research or other non-therapeutic purposes.


Provided herein is N-((4,6-dimethyl-2-oxo-1,2-dihydropyridin-3-yl)methyl)-5-(ethyl (tetrahydro-2H-pyran-4-yl)amino)-4-methyl-4-(morpholinomethyl)-[1,1-biphenyl]-3-carboxamide hydrobromideAlso provided herein is a particular polymorph form of this compound and its use.


Patent
Epizyme and Eisai R&D Management Co. | Date: 2017-04-26

The present invention relates to methods of treating cancer by administering an EZH2 inhibitor or a pharmaceutical composition thereof to the subject in need thereof. The present claims define methods for treating specific subtypes of non-Hodgkins lymphoma comprising the administration to a subject of EZH2 inhibitors. Preferred EZH2 inhibitors include tazemetostat (EPZ-6438 E7438) and other compounds. Dosage amounts and regimes are also defined.


Patent
Epizyme | Date: 2017-05-03

Described herein are compounds of Formula (I)-(XIII), pharmaceutically acceptable salts thereof, and pharmaceutical compositions thereof. Compounds of the present invention are useful for inhibiting PRMT5 activity. Methods of using the compounds for treating PRMT5-mediated disorders are also described.


Patent
Epizyme and Celgene | Date: 2017-06-21

The disclosure relates to combinations comprising inhibitors of human histone methyltransferase DOT1L and one or more therapeutic agents, particularly anticancer agents, and methods of combination therapy for administering to subjects in need thereof for the treatment of cancer.


Patent
Epizyme and Glaxosmithkline | Date: 2017-06-14

Described herein are methods of treating cancer using one or more PRMT5 inhibitors, for example using one or more compounds of Formulae (1-5) or (A-F), pharmaceutically acceptable salts thereof, and/or pharmaceutical compositions thereof. Described herein are methods of treating cancer using one or more PRMT5 inhibitors, for example using one or more compounds of Formulae (1-5) or (A-F), pharmaceutically acceptable salts thereof, and/or pharmaceutical compositions thereof.


Patent
Epizyme | Date: 2017-05-10

The present invention relates to substituted benzene compounds. The present invention also relates to pharmaceutical compositions containing these compounds and such compounds for use in treating cancer. The present invention also relates to the use of such compounds for research or other non-therapeutic purposes.


Copeland R.A.,Epizyme
Nature Reviews Drug Discovery | Year: 2016

The drug-target residence time model was first introduced in 2006 and has been broadly adopted across the chemical biology, biotechnology and pharmaceutical communities. While traditional in vitro methods view drug-target interactions exclusively in terms of equilibrium affinity, the residence time model takes into account the conformational dynamics of target macromolecules that affect drug binding and dissociation. The key tenet of this model is that the lifetime (or residence time) of the binary drug-target complex, and not the binding affinity per se, dictates much of the in vivo pharmacological activity. Here, this model is revisited and key applications of it over the past 10 years are highlighted. © 2016 Macmillan Publishers Limited.


Copeland R.A.,Epizyme
Clinical Cancer Research | Year: 2013

The protein methyltransferases (PMT) constitute a large and important class of enzymes that catalyze sitespecific methylation of lysine or arginine residues on histones and other proteins. Site-specific histone methylation is a critical component of chromatin regulation of gene transcription-a pathway that is often genetically altered in human cancers. Oncogenic alterations (e.g., mutations, chromosomal translocations, and others) of PMTs, or of associated proteins, have been found to confer unique dependencies of cancer cells on the activity of specific PMTs. Examples of potent, selective small-molecule inhibitors of specific PMTs are reviewed that have been shown to kill cancers cells bearing such oncogenic alterations, while having minimal effect on proliferation of nonaltered cells. Selective inhibitors of the PMTs, DOT1L and EZH2, have entered phase I clinical studies and additional examples of selective PMT inhibitors are likely to enter the clinic soon. The current state of efforts toward clinical testing of selective PMT inhibitors as personalized cancer therapeutics is reviewed here. © 2013 American Association for Cancer Research.

Loading Epizyme collaborators
Loading Epizyme collaborators