Fremont, MO, United States
Fremont, MO, United States

DiscoverRx develops, commercializes and manufactures reagents and assay kits for the drug discovery market. Their focus is on lucrative protein target classes, such as G-protein-coupled receptors and kinases.The company is built around a proprietary technology called enzyme fragment complementation or EFC which forms the basis of the assays that they design and market. In EFC, two β-galactosidase fragments are employed which are themselves inactive. One fragment has an inactivating deletion while the second fragment has a complementing fragment; in solution where both EA and ED are present, certain pairs of fragments combine spontaneously to form active complexes. Some pairs of fragments interact only weakly and combine to produce enzyme activity only when forced into close proximity by virtue of their attachment to proteins which bind to each other. This property permits evaluation of intracellular protein interactions for use in high throughput screening of drug candidates for their effect on specific cellular pathways. The company offers a wide variety of cell lines that produce such fusion products. Wikipedia.

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The kinase family of 500 enzymes provides a tremendous opportunity for drug discovery with over 30 inhibitors approved for the treatment of human disease. Development of selective inhibitors to interrogate this important family of proteins is a critical step to better understand the roles they play in human disease. A publicly available KCGS enables the community to openly collaborate on the discovery and development of new therapies. This collaborative project between industrial and academic scientists will continue to expand the KCGS with the goal of full coverage of all human protein kinases. This expansion, combined with the use of the set in varied disease-relevant phenotypic screens and sharing of the resulting data in the public domain, is the best mechanism to ensure that the therapeutic potential of as many protein kinases as possible will be uncovered. David Drewry, Ph.D., a research associate professor at the UNC Eshelman School of Pharmacy, SGC-UNC principal investigator and KCGS project leader, said, "With this publication we are sharing our goals, and announcing to the community our progress towards construction of a comprehensive KCGS. In the paper, we disclose the results of broad kinome screening of a compound set we call Published Kinase Inhibitor Set 2. We are releasing these results into the public domain in keeping with our mission to support the discovery of new medicines through open access science. These results now put us about halfway towards our goal of complete kinome coverage. We sincerely thank all of our co-author partners whose vision, generosity, and hard work makes the construction of this set possible." DiscoverX, through its KINOMEscan offering, is the leading provider of kinase screening services and has successfully partnered with multiple organizations to bring kinase inhibitor programs into the clinic. Todd R. Nelson Ph.D., CEO of DiscoverX, stated, "Through the extension of our work with the SGC and continued expansion of the KCGS, DiscoverX continues to take a leading role supporting the discovery and development of therapeutic molecules, especially in the areas of oncology, immunology, and neuroscience." About DiscoverX DiscoverX Corporation, headquartered in Fremont, CA, USA, is a leader in the design, manufacture and sale of biochemical and cell-based assays for the drug discovery & life science markets. This industry-leading portfolio of products and services, under the KINOMEscan®, PathHunter® and BioMAP® brands, are used to aid life science research and enable rapid development of safe and effective biologic and small molecule drugs, by improving research productivity, effectiveness of screening, lead optimization & bioanalytical campaigns, as well as providing predictive tools that deliver physiologically relevant insights on drug molecules from early discovery through pre-clinical development. DiscoverX embodies a pioneering approach to creating life science tools that have been widely adopted across the globe in pharmaceutical, biotechnology and academic laboratories. Learn more at discoverx.com. About the Structural Genomics Consortium (SGC) The SGC is a pre-competitive public-private partnership that accelerates research in human biology and drug discovery by making all of its research output freely available to the scientific community. To achieve its mission, the organization is building an open and collaborative network of scientists: the SGC has active research facilities at six leading academic institutions across the globe (Toronto-Canada, Oxford-UK, UNICAMP-Brazil, Karolinska-Sweden, UNC Chapel Hill-USA and Frankfurt-Germany), and SGC scientists collaborate with more than 300 researchers in academia and industry. The SGC is a registered charity (number 1097737) that receives funds from AbbVie, Bayer Pharma AG, Boehringer Ingelheim, Canada Foundation for Innovation, Eshelman Institute for Innovation, Genome Canada, Innovative Medicines Initiative (EU/EFPIA), Janssen, Merck & Co., Novartis Pharma AG, Ontario Ministry of Economic Development and Innovation, Pfizer, São Paulo Research Foundation-FAPESP, Takeda, and Wellcome Trust. For more information, visit www.thesgc.org.  PKIS2, a collection of >300 fully annotated kinase inhibitors donated by GSK, Pfizer, and Takeda, is currently available from the SGC UNC by completing an on-line request.


Patent
DiscoveRX | Date: 2017-06-28

Disclosed are methods for detecting and quantitatively measuring a binding property of a compound to a target macromolecule, wherein the target macromolecule is subject to denaturation and is linked to a labeling peptide, such as a short enzyme fragment. The method uses a fluid mixture comprising (i) a chimeric molecule comprising a target macromolecule linked to the labeling peptide and (ii) a compound being measured for binding to the target macromolecule, wherein said target macromolecule is subject to denaturation. After allowing for binding of the compound (e.g. a small molecule inhibitor of the target macromolecule), one detects a signal from the labeling peptide, such as by enzyme fragment complementation. This signal indicates a differential between denatured and non- denatured target macromolecules and thereby indicates a differential between target macromolecules not bound to the compound and target macromolecules bound to the compound, respectively.


Berg E.L.,DiscoveRX
Drug Discovery Today | Year: 2014

The complexity of human biology makes it challenging to develop safe and effective new medicines. Systems biology omics-based efforts have led to an explosion of high-throughput data and focus is now shifting to the integration of diverse data types to connect molecular and pathway information to predict disease outcomes. Better models of human disease biology, including more integrated network-based models that can accommodate multiple omics data types, as well as more relevant experimental systems, will help predict drug effects in patients, enabling personalized medicine, improvement of the success rate of new drugs in the clinic, and the finding of new uses for existing drugs. © 2013 Elsevier Ltd.


Methods and compositions are provided to measure the binding of a test compound to a target peptide by measuring the effect of the compound on the abundance of the target peptide inside a cell. The target peptide may bind the test compound at an active site or an allosteric site, and it has been found that such binding may stabilize the target peptide against cellular degradation. The target peptide will preferably comprise a destabilizing mutation which shortens the half life of the target peptide within the cell, typically a mammalian cell. Test compounds, including small molecules, have been found to stabilize target peptides. Also provided are systems and kits for use in practicing the methods.


Patent
DiscoveRX | Date: 2014-03-18

Agents that inhibit or prevent restenosis are identified by assaying test agents in a battery of assays to measure the effect of the test agent on cell proliferation, thrombosis, tissue modeling, and inflammation. Treatment for restenosis is provided using compositions of the invention.


Patent
DiscoveRX | Date: 2015-07-28

Provided herein are nucleic acid tags that are linked to, or capable of linking to, a protein of interest. In particular, the nucleic acid tags are oligonucleotides comprising a reporter function and a protein tagging function. Also provided herein, are nucleic acid tag compositions, kits and methods of use thereof.


Patent
DiscoveRX | Date: 2014-04-21

Methods and systems for evaluating biological dataset profiles relating to toxic agents including candidate pharmaceuticals, environmental agents, biowarfare and chemical warfare agents are provided, where datasets comprising information for multiple cellular parameters are compared and identified, and used in the evaluation of candidate agents.


Patent
DiscoveRX | Date: 2012-01-11

Provided herein are nucleic acid tags that are linked to, or capable of linking to, a protein of interest. In particular, the nucleic acid tags are oligonucleotides comprising a reporter function and a protein tagging function. Also provided herein, are nucleic acid tag compositions, kits and methods of use thereof.


Patent
DiscoveRX | Date: 2015-08-19

Disclosed are methods for detecting and quantitatively measuring a binding property of a compound to a target macromolecule, wherein the target macromolecule is subject to denaturation and is linked to a labeling peptide, such as a short enzyme fragment. The method uses a fluid mixture comprising (i) a chimeric molecule comprising a target macromolecule linked to the labeling peptide and (ii) a compound being measured for binding to the target macromolecule, wherein said target macromolecule is subject to denaturation. After allowing for binding of the compound (e.g. a small molecule inhibitor of the target macromolecule), one detects a signal from the labeling peptide, such as by enzyme fragment complementation. This signal indicates a differential between denatured and non-denatured target macromolecules and thereby indicates a differential between target macromolecules not bound to the compound and target macromolecules bound to the compound, respectively.


Methods and materials are disclosed for use in an enzyme fragment complementation assay using complementary fragments of -galactosidase to study the trafficking of proteins in a cell. Compounds that bind to a target peptide have been found to affect protein folding and therefore trafficking. -Galactosidase fragments, an enzyme donor (ED) and an enzyme acceptor (EA), are fused to a target peptide and to an intracellular compartment protein, wherein the compartment is involved in intracellular trafficking. Contacting the cell with a compound that binds to the target peptide results in enhanced movement of the protein through the cellular trafficking pathway comprised of the endoplasmic reticulum, Golgi apparatus, the plasma membrane, endosomes, etc. Using this approach, compounds that bind to a target peptide and alter its ability to traffic through the normal cellular pathway can be readily detected.

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