Emerald Bio

Bainbridge Island, WA, United States

Emerald Bio

Bainbridge Island, WA, United States

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Protein Engineering Market by Technologies, End Uses, Trends and Forecast to 2021, Upcoming Report by iHealthcareAnalyst, Inc. Protein Engineering Market by Technology (Rational Product Design, Directed Evolution), and End User (Academic Research Institutes, Biotechnology Companies, Contract Research Organizations, Pharmaceutical Enterprises) and Forecast 2017-2021. Maryland Heights, MO, May 17, 2017 --( Visit Protein Engineering Market by Technology (Rational Product Design, Directed Evolution), and End User (Academic Research Institutes, Biotechnology Companies, Contract Research Organizations, Pharmaceutical Enterprises) and Forecast 2017-2021 at https://www.ihealthcareanalyst.com/report/protein-engineering-market/ The global protein (antibody) engineering market segmentation is based on technology (rational product design, directed evolution), and end user (academic research institutes, biotechnology and pharmaceutical companies, contract research organizations). The global protein (antibody) engineering market report provides market size (Revenue USD Million 2014 to 2021), market share, trends and forecasts growth trends (CAGR%, 2017 to 2021). The global protein (antibody) engineering market research report is further segmented by geography into North America (U.S., Canada), Latin America (Brazil, Mexico, Rest of LA), Europe (U.K., Germany, France, Italy, Spain, Rest of EU), Asia Pacific (Japan, China, India, Rest of APAC), and Rest of the World. The global protein (antibody) market report also provides the detailed market landscape (market drivers, restraints, opportunities), market attractiveness analysis and also tracks the major competitors operating in the market by company overview, financial snapshot, key products, technologies and services offered, market share analysis and recent trends in the global market. Major players operating in the global protein (antibody) engineering market and included in this report are BioXcell, Covalab, Emerald Bio, Fusion Antibodies, GenTarget, Inc., IBL International, ImaginAb, Precision Antibody, and ProSci, Inc. 1. Technology 1.1. Rational Product Design 1.2. Directed Evolution 2. End User 2.1. Academic Research Institutes 2.2. Biotechnology and Pharmaceutical Companies 2.3. Contract Research Organizations 3. Company Profiles 3.1. BioXcell 3.2. Covalab 3.3. Emerald Bio 3.4. Fusion Antibodies 3.5. GenTarget, Inc. 3.6. IBL International 3.7. ImaginAb 3.8. Precision Antibody 3.9. ProSci, Inc. To request Table of Contents and Sample Pages of this report visit: https://www.ihealthcareanalyst.com/report/protein-engineering-market/ About Us iHealthcareAnalyst, Inc. is a global healthcare market research and consulting company providing market analysis, and competitive intelligence services to global clients. The company publishes syndicate, custom and consulting grade healthcare reports covering animal healthcare, biotechnology, clinical diagnostics, healthcare informatics, healthcare services, medical devices, medical equipment, and pharmaceuticals. In addition to multi-client studies, we offer creative consulting services and conduct proprietary single-client assignments targeted at client’s specific business objectives, information needs, time frame and budget. Please contact us to receive a proposal for a proprietary single-client study. Contact Us iHealthcareAnalyst, Inc. 2109, Mckelvey Hill Drive, Maryland Heights, MO 63043 United States Email: sales@ihealthcareanalyst.com Website: https://www.ihealthcareanalyst.com Maryland Heights, MO, May 17, 2017 --( PR.com )-- Protein engineering is the design of new enzymes or proteins with new or desirable functions. It is the conception and production of unnatural polypeptides, often through modification of amino acid sequences that are found in nature. Synthetic protein structures and functions can now be designed entirely on a computer or produced through directed evolution in the laboratory. In rational protein design, the scientist uses detailed knowledge of the structure and function of the protein to make desired changes. In general, this has the advantage of being inexpensive and technically easy, since site-directed mutagenesis techniques are well-developed. In directed evolution, random mutagenesis is applied to a protein, and a selection regime is used to pick out variants that have the desired qualities, where further rounds of mutation and selection are then applied. This method mimics natural evolution and, in general, may produce superior results to rational design.Visit Protein Engineering Market by Technology (Rational Product Design, Directed Evolution), and End User (Academic Research Institutes, Biotechnology Companies, Contract Research Organizations, Pharmaceutical Enterprises) and Forecast 2017-2021 at https://www.ihealthcareanalyst.com/report/protein-engineering-market/The global protein (antibody) engineering market segmentation is based on technology (rational product design, directed evolution), and end user (academic research institutes, biotechnology and pharmaceutical companies, contract research organizations).The global protein (antibody) engineering market report provides market size (Revenue USD Million 2014 to 2021), market share, trends and forecasts growth trends (CAGR%, 2017 to 2021). The global protein (antibody) engineering market research report is further segmented by geography into North America (U.S., Canada), Latin America (Brazil, Mexico, Rest of LA), Europe (U.K., Germany, France, Italy, Spain, Rest of EU), Asia Pacific (Japan, China, India, Rest of APAC), and Rest of the World. The global protein (antibody) market report also provides the detailed market landscape (market drivers, restraints, opportunities), market attractiveness analysis and also tracks the major competitors operating in the market by company overview, financial snapshot, key products, technologies and services offered, market share analysis and recent trends in the global market.Major players operating in the global protein (antibody) engineering market and included in this report are BioXcell, Covalab, Emerald Bio, Fusion Antibodies, GenTarget, Inc., IBL International, ImaginAb, Precision Antibody, and ProSci, Inc.1. Technology1.1. Rational Product Design1.2. Directed Evolution2. End User2.1. Academic Research Institutes2.2. Biotechnology and Pharmaceutical Companies2.3. Contract Research Organizations3. Company Profiles3.1. BioXcell3.2. Covalab3.3. Emerald Bio3.4. Fusion Antibodies3.5. GenTarget, Inc.3.6. IBL International3.7. ImaginAb3.8. Precision Antibody3.9. ProSci, Inc.To request Table of Contents and Sample Pages of this report visit:https://www.ihealthcareanalyst.com/report/protein-engineering-market/About UsiHealthcareAnalyst, Inc. is a global healthcare market research and consulting company providing market analysis, and competitive intelligence services to global clients. The company publishes syndicate, custom and consulting grade healthcare reports covering animal healthcare, biotechnology, clinical diagnostics, healthcare informatics, healthcare services, medical devices, medical equipment, and pharmaceuticals.In addition to multi-client studies, we offer creative consulting services and conduct proprietary single-client assignments targeted at client’s specific business objectives, information needs, time frame and budget. Please contact us to receive a proposal for a proprietary single-client study.Contact UsiHealthcareAnalyst, Inc.2109, Mckelvey Hill Drive,Maryland Heights, MO 63043United StatesEmail: sales@ihealthcareanalyst.comWebsite: https://www.ihealthcareanalyst.com


Terry-Lorenzo R.T.,Sunovion Pharmaceuticals | Chun L.E.,Emerald Bio | Brown S.P.,Sunovion Pharmaceuticals | Heffernan M.L.R.,Sunovion Pharmaceuticals | And 7 more authors.
Bioscience Reports | Year: 2014

The NMDAR (N-methyl-D-aspartate receptor) is a central regulator of synaptic plasticity and learning and memory. hDAAO (human D-amino acid oxidase) indirectly reduces NMDAR activity by degrading the NMDAR co-agonist D-serine. Since NMDAR hypofunction is thought to be a foundational defect in schizophrenia, hDAAO inhibitors have potential as treatments for schizophrenia and other nervous system disorders. Here, we sought to identify novel chemicals that inhibit hDAAO activity. We used computational tools to design a focused, purchasable library of compounds. After screening this library for hDAAO inhibition, we identified the structurally novel compound, 'compound 2' [3-(7-hydroxy-2-oxo-4-phenyl-2H-chromen-6-yl)propanoic acid], which displayed low nM hDAAO inhibitory potency (Ki = 7 nM). Although the library was expected to enrich for compounds that were competitive for both D-serine and FAD, compound 2 actually was FAD uncompetitive, much like canonical hDAAO inhibitors such as benzoic acid. Compound 2 and an analog were independently co-crystalized with hDAAO. These compounds stabilized a novel conformation of hDAAO in which the active-site lid was in an open position. These results confirm previous hypotheses regarding active-site lid flexibility of mammalian D-amino acid oxidases and could assist in the design of the next generation of hDAAO inhibitors. © 2014 The Author(s).


PubMed | Emerald Bio and Deciphera Pharmaceuticals
Type: Journal Article | Journal: Molecular cancer therapeutics | Year: 2015

Altiratinib (DCC-2701) was designed based on the rationale of engineering a single therapeutic agent able to address multiple hallmarks of cancer (1). Specifically, altiratinib inhibits not only mechanisms of tumor initiation and progression, but also drug resistance mechanisms in the tumor and microenvironment through balanced inhibition of MET, TIE2 (TEK), and VEGFR2 (KDR) kinases. This profile was achieved by optimizing binding into the switch control pocket of all three kinases, inducing type II inactive conformations. Altiratinib durably inhibits MET, both wild-type and mutated forms, in vitro and in vivo. Through its balanced inhibitory potency versus MET, TIE2, and VEGFR2, altiratinib provides an agent that inhibits three major evasive (re)vascularization and resistance pathways (HGF, ANG, and VEGF) and blocks tumor invasion and metastasis. Altiratinib exhibits properties amenable to oral administration and exhibits substantial blood-brain barrier penetration, an attribute of significance for eventual treatment of brain cancers and brain metastases.


PubMed | University of Minnesota and Emerald Bio
Type: Journal Article | Journal: PLoS pathogens | Year: 2015

Anaplasma phagocytophilum, the causative agent of Human Granulocytic Anaplasmosis (HGA), is an obligately intracellular -proteobacterium that is transmitted by Ixodes spp ticks. However, the pathogen is not transovarially transmitted between tick generations and therefore needs to survive in both a mammalian host and the arthropod vector to complete its life cycle. To adapt to different environments, pathogens rely on differential gene expression as well as the modification of proteins and other molecules. Random transposon mutagenesis of A. phagocytophilum resulted in an insertion within the coding region of an o-methyltransferase (omt) family 3 gene. In wild-type bacteria, expression of omt was up-regulated during binding to tick cells (ISE6) at 2 hr post-inoculation, but nearly absent by 4 hr p.i. Gene disruption reduced bacterial binding to ISE6 cells, and the mutant bacteria that were able to enter the cells were arrested in their replication and development. Analyses of the proteomes of wild-type versus mutant bacteria during binding to ISE6 cells identified Major Surface Protein 4 (Msp4), but also hypothetical protein APH_0406, as the most differentially methylated. Importantly, two glutamic acid residues (the targets of the OMT) were methyl-modified in wild-type Msp4, whereas a single asparagine (not a target of the OMT) was methylated in APH_0406. In vitro methylation assays demonstrated that recombinant OMT specifically methylated Msp4. Towards a greater understanding of the overall structure and catalytic activity of the OMT, we solved the apo (PDB_ID:4OA8), the S-adenosine homocystein-bound (PDB_ID:4OA5), the SAH-Mn2+ bound (PDB_ID:4PCA), and SAM- Mn2+ bound (PDB_ID:4PCL) X-ray crystal structures of the enzyme. Here, we characterized a mutation in A. phagocytophilum that affected the ability of the bacteria to productively infect cells from its natural vector. Nevertheless, due to the lack of complementation, we cannot rule out secondary mutations.


Fox D.,Emerald Bio | Burgin A.B.,Emerald Bio | Gurney M.E.,Tetra Discovery Partners, Llc | Gurney M.E.,West Virginia University
Cellular Signalling | Year: 2014

Phosphodiesterase-4B (PDE4B) regulates the pro-inflammatory Toll Receptor -Tumor Necrosis Factor α (TNFα) pathway in monocytes, macrophages and microglial cells. As such, it is an important, although under-exploited molecular target for anti-inflammatory drugs. This is due in part to the difficulty of developing selective PDE4B inhibitors as the amino acid sequence of the PDE4 active site is identical in all PDE4 subtypes (PDE4A-D). We show that highly selective PDE4B inhibitors can be designed by exploiting sequence differences outside the active site. Specifically, PDE4B selectivity can be achieved by capture of a C-terminal regulatory helix, now termed CR3 (Control Region 3), across the active site in a conformation that closes access by cAMP. PDE4B selectivity is driven by a single amino acid polymorphism in CR3 (Leu674 in PDE4B1 versus Gln594 in PDE4D). The reciprocal mutations in PDE4B and PDE4D cause a 70-80 fold shift in selectivity. Our structural studies show that CR3 is flexible and can adopt multiple orientations and multiple registries in the closed conformation. The new co-crystal structure with bound ligand provides a guide map for the design of PDE4B selective anti-inflammatory drugs. © 2013 The Authors.


Elliman S.J.,Orbsen Therapeutics Ltd. | Howley B.V.,National University of Ireland | Mehta D.S.,Biogen Idec | Fearnhead H.O.,National University of Ireland | And 2 more authors.
Oncogenesis | Year: 2014

MicroRNAs (miRNAs) are deregulated in cancer and have been shown to exhibit both oncogenic and tumor suppressive functions. Although the functional effects of several miRNAs have been elucidated, those of many remain to be discovered. In silico analysis identified microRNA-206 (miR-206) binding sites in the 3′-untranslated regions (3′-UTR) of both the mouse and human CCND1 gene. Cyclin D1 is a recognized oncogene involved in direct phosphorylation of the retinoblastoma (Rb) protein and promoting cell cycle transition from G1 to S. miR-206 specifically binds to the CCND1 3′-UTR and mediates reduction of both cyclin D1 protein and mRNA. Expression of miR-206 induced a G1 arrest and a decrease in cell proliferation in breast cancer cells. Ectopic expression of miRNA-resistant cyclin D1 was able to reverse the miR-206-induced decrease in cell proliferation. Therefore, we identified miR-206 as an activator of cell cycle arrest resulting in a decrease in cell proliferation that is dependent on the inhibition of cyclin D1. Interestingly, prostatic cancer (PCa) cells express low levels of miR-206 resulting in deregulated cyclin D1 expression compared with non-transformed primary prostatic epithelial cells (PrEC). Finally, we demonstrate that cyclin D1 is regulated by miR-206 in PrEC but not in PCa cells and this is due to the absence of a CCND1 3'-UTR in these cells. This suggests that miR-206-based anti-cyclin D1 targeted therapy would be beneficial in cancers where cyclin D1 is overexpressed and contains a 3′-UTR. © 2014 Macmillan Publishers Limited All rights reserved.


PubMed | Orbsen Therapeutics Ltd, National University of Ireland, Biogen Idec and Emerald Bio
Type: | Journal: Oncogenesis | Year: 2014

MicroRNAs (miRNAs) are deregulated in cancer and have been shown to exhibit both oncogenic and tumor suppressive functions. Although the functional effects of several miRNAs have been elucidated, those of many remain to be discovered. In silico analysis identified microRNA-206 (miR-206) binding sites in the 3-untranslated regions (3-UTR) of both the mouse and human CCND1 gene. Cyclin D1 is a recognized oncogene involved in direct phosphorylation of the retinoblastoma (Rb) protein and promoting cell cycle transition from G1 to S. miR-206 specifically binds to the CCND1 3-UTR and mediates reduction of both cyclin D1 protein and mRNA. Expression of miR-206 induced a G1 arrest and a decrease in cell proliferation in breast cancer cells. Ectopic expression of miRNA-resistant cyclin D1 was able to reverse the miR-206-induced decrease in cell proliferation. Therefore, we identified miR-206 as an activator of cell cycle arrest resulting in a decrease in cell proliferation that is dependent on the inhibition of cyclin D1. Interestingly, prostatic cancer (PCa) cells express low levels of miR-206 resulting in deregulated cyclin D1 expression compared with non-transformed primary prostatic epithelial cells (PrEC). Finally, we demonstrate that cyclin D1 is regulated by miR-206 in PrEC but not in PCa cells and this is due to the absence of a CCND1 3-UTR in these cells. This suggests that miR-206-based anti-cyclin D1 targeted therapy would be beneficial in cancers where cyclin D1 is overexpressed and contains a 3-UTR.


PubMed | Emerald Bio and West Virginia University
Type: Journal Article | Journal: Cellular signalling | Year: 2014

Phosphodiesterase-4B (PDE4B) regulates the pro-inflammatory Toll Receptor -Tumor Necrosis Factor (TNF) pathway in monocytes, macrophages and microglial cells. As such, it is an important, although under-exploited molecular target for anti-inflammatory drugs. This is due in part to the difficulty of developing selective PDE4B inhibitors as the amino acid sequence of the PDE4 active site is identical in all PDE4 subtypes (PDE4A-D). We show that highly selective PDE4B inhibitors can be designed by exploiting sequence differences outside the active site. Specifically, PDE4B selectivity can be achieved by capture of a C-terminal regulatory helix, now termed CR3 (Control Region 3), across the active site in a conformation that closes access by cAMP. PDE4B selectivity is driven by a single amino acid polymorphism in CR3 (Leu674 in PDE4B1 versus Gln594 in PDE4D). The reciprocal mutations in PDE4B and PDE4D cause a 70-80 fold shift in selectivity. Our structural studies show that CR3 is flexible and can adopt multiple orientations and multiple registries in the closed conformation. The new co-crystal structure with bound ligand provides a guide map for the design of PDE4B selective anti-inflammatory drugs.

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