Almac Discovery

Craigavon, United Kingdom

Almac Discovery

Craigavon, United Kingdom

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La kinase Wee-1 est un régulateur clé pour certains points de contrôle du cycle cellulaire, et l'inhibition de Wee-1 empêche les cellules cancéreuses de s'arrêter (pour réparer leur ADN endommagé) et les force à poursuivre leur cycle, les poussant ainsi vers la mort cellulaire. Dans plusieurs modèles de cancer, les inhibiteurs de Wee-1 découverts par Almac Discovery montrent de bonnes propriétés médicamenteuses, une efficacité élevée, une excellente sélectivité et démontre une puissante activité antiproliférative in vitro et in vivo, tant en agents seuls qu'en association avec des génotoxiques. «Nous sommes ravis de poursuivre le travail remarquable d'Almac Discovery sur cette cible prometteuse», a déclaré le Dr. Bertrand Ducrey, CEO de Debiopharm International SA, et d'ajouter: «L'incontestable expertise d'Almac Discovery en matière de chimie médicinale et de découverte de nouveaux médicaments est très complémentaire au modèle d'affaires de Debiopharm, et nous nous réjouissons de développer ces composés afin d'offrir un traitement novateur aux patients présentant un besoin médical élevé.» Le Dr Stephen Barr, directeur général et président d'Almac Discovery a déclaré : «Nous sommes extrêmement heureux d'annoncer cet accord avec Debiopharm qui a démontré son expertise et présente un parcours impressionnant en matière de développement de médicaments. Le professionnalisme, le dévouement et l'engagement de leur équipe correspondent parfaitement à nos propres valeurs fondamentales, ce qui a fait d'eux notre choix numéro un pour développer notre inhibiteur de Wee-1. Ce type d'accord permet aux deux sociétés de continuer leurs efforts pour améliorer la santé humaine dans le monde entier, et nous nous réjouissons de travailler avec eux.» Membre de Debiopharm Group™ - groupe international dont le siège social se trouve en Suisse, composé de cinq sociétés biopharmaceutiques actives dans les domaines des sciences de la vie que sont le développement de médicaments, la fabrication de médicaments exclusifs selon les BPF et les outils de diagnostic, ainsi que dans la gestion des investissements - Debiopharm International SA se concentre sur le développement de médicaments sur ordonnance ciblant des besoins médicaux non satisfaits. La société acquiert des licences puis développe des médicaments candidats prometteurs. Les produits sont commercialisés par l'octroi de licences à des partenaires pharmaceutiques, afin de les rendre accessibles au plus grand nombre possible de patients dans le monde.


CRAIGAVON, Irlanda del Norte y LAUSANA, Suiza, June 20, 2017 /PRNewswire/ -- - Almac Discovery y Debiopharm International SA anuncian un acuerdo de licencia para el desarrollo de un nuevo inhibidor Wee-1 Almac Discovery (http://www.almacgroup.com/discovery), una compañía...


News Article | November 8, 2016
Site: www.newsmaker.com.au

The report provides comprehensive information on the therapeutics under development for Gastric Cancer,complete with analysis by stage of development,drug target,mechanism of action (MoA),route of administration (RoA) and molecule type. The report also coversthe descriptive pharmacological action of the therapeutics,its complete research and development history and latest news and press releases. Additionally,the report provides an overview of key players involved in therapeutic development for Gastric Cancer and features dormant and discontinued projects. The report helps in identifying and tracking emerging players in the market and their portfolios,enhances decision making capabilities and helps to create effective counter strategies to gain competitive advantage. Complete report on Gastric Cancer - Pipeline Review, H2 2016 addition with 196 market data tables and 17 figures, spread across 963 pages is available at http://www.rnrmarketresearch.com/gastric-cancer-pipeline-review-h2-2016-market-report.html This report features investigational drugs from across globe covering over 20 therapy areas and nearly 3,000 indications. The report is built using data and information sourced from Global Markets Direct's proprietary databases,company/university websites,clinical trial registries,conferences,SEC filings,investor presentations and featured press releases from company/university sites and industry-specific third party sources. Drug profiles featured in the report undergoes periodic review following a stringent set of processes to ensure that all the profiles are updated with the latest set of information. Additionally,various dynamic tracking processes ensure that the most recent developments are captured on a real time basis. 3SBio Inc. ,AB Science SA ,AbbVie Inc ,AbGenomics International, Inc. ,ADC Therapeutics Sarl,Advaxis, Inc. ,Advenchen Laboratories, LLC ,Agenus, Inc. ,Almac Discovery Limited ,Alteogen Inc.,Ambrx, Inc.,Amgen Inc. ,arGEN-X BV ,Asana BioSciences, LLC ,Aslan Pharmaceuticals Pte Ltd,Astellas Pharma Inc. ,AstraZeneca Plc ,Atara Biotherapeutics, Inc. ,Athenex, Inc. ,Azaya Therapeutics, Inc. ,Basilea Pharmaceutica Ltd. ,Bayer AG ,BeiGene, Ltd. Inquire before buyinghttp://www.rnrmarketresearch.com/contacts/inquire-before-buying?rname=748025(This is a premium report price at US$2000 for a single user PDF license).


Research and Markets has announced the addition of the "Ubiquitin Enzymes: Key Targets and Future Market Potential, 2016-2030" report to their offering. One of the key objectives of this report was to understand the current activity and the future potential of the market. The study provides a detailed market forecast and opportunity analysis for the period between 2016 and 2030. The research, analysis and insights presented in this report include a detailed description of ubiquitin enzyme inhibitors along with drug classes closely associated with them. To add robustness to our model, we have provided three scenarios for our market forecast, namely the conservative, base and optimistic scenarios, to account for future uncertainties. The opinions and insights presented in this study were influenced by several discussions conducted with experts in this domain. All actual figures have been sourced and analyzed from publicly available information forums and from primary research. All financial figures mentioned in this report are in USD, unless otherwise specified. Key Topics Covered: 1. Preface 1.1. Chapter Overview 1.2. Research Methodology 1.3. Chapter Outlines 2. Executive Summary 3. Introduction 3.1. Chapter Overview 3.2. The Concept of Protein Homeostasis 3.3. Importance of Post Translational Modifications in Cellular Functions 3.4. Discovery of the Ubiquitin/Ubiquitin Proteasome System 3.5. Ubiquitin: Structure and Function 3.6. Fundamentals of the UPS 3.7. Therapeutic Applications of UPS 3.8. Emergence of Ubiquitin Enzyme Inhibitors 4. Ubiquitin Enzyme Inhibitors: Market Overview 4.1. Chapter Overview 4.2. Ubiquitin Enzyme Inhibitors: Development Pipeline 4.3. Ubiquitin Enzyme Inhibitors: Distribution by Phase of Development 4.4. Ubiquitin Enzyme Inhibitors: Distribution by Therapeutic Area 4.5. Ubiquitin Enzyme Inhibitors: Distribution by Target Ubiquitin Enzymes 4.6. Ubiquitin Enzyme Inhibitors: Distribution by Geography 4.7. Ubiquitin Enzyme Inhibitors: Most Active Industry Players 4.8. Ubiquitin Enzyme Inhibitors: Research Tools, Key Technologies and Precursor Compounds 5. Key Insights: Therapeutic Areas and Potential Targets 5.1. Chapter Overview 5.2. Ubiquitin Enzyme Inhibitors Clinical Development Analysis: Therapeutic Areas 5.3. Ubiquitin Enzyme Inhibitors Clinical Development Analysis: Potential Targets 5.4. Ubiquitin Enzyme Inhibitors Clinical Development Analysis: Developer Landscape 5.5. Developers of Ubiquitin Enzyme Inhibitors: Geographical Presence 5.6. Ubiquitin Enzyme Inhibitors and UPS: Recent/Upcoming Conferences 6. E1 and E2 Enzymes as Therapeutic Targets 6.1. Chapter Overview 6.2. E1 Activating Enzymes as Drug Targets 6.3. E2 Conjugating Enzymes as Drug Targets 7. E3 Enzymes as Therapeutic Targets 7.1. Chapter Overview 7.2. E3 Ligases: An Introduction 7.3. E3 Ligases: Mechanism of Action 7.4. E3 Ligases: Important Families 7.5. E3 Ligase Inhibitors: List of Related Targets 7.6. E3 Ligase Inhibitors: Screening Methods 7.7. E3 Ligase Inhibitors: Development Pipeline 7.8. E3 Ligase Inhibitors: Drug Profiles 7.9. E3 Ligase Inhibitors: Challenges and Opportunities 8. DUB Enzymes as Therapeutic Targets 8.1. Chapter Overview 8.2. DUBs: An Introduction 8.3. DUBs: Mechanism of Action 8.4. DUBs: Important Families 8.5. DUB Inhibitors: List of Related Targets 8.6. DUB Inhibitors: Screening Methods 8.7. DUB Inhibitors: Development Pipeline 8.8. DUB Inhibitors: Drug Profiles 8.9. DUB Inhibitors Development: Challenges and Opportunities 9. Associated Drug Classes 9.1. Chapter Overview 9.2. Proteasome Inhibitors 9.3. Immunomodulatory Drugs 9.4. IAP Inhibitors 10. Venture Capital Interest 10.1. Chapter Overview 10.2. Funding Instances: Distribution by Type of Funding 10.3. Funding Instances for Development of Ubiquitin Based Therapeutics 10.4. Rising Venture Capital Interest 10.5. Leading Players: Distribution by Number of Funding Instances 10.6. Most Active Venture Capital Firms/Investors 10.7. Funding Instances: Distribution by Focus Area 11. Recent Collaborations 11.1. Chapter Overview 11.2. Partnership Models/Agreements 11.3. UPS Based Therapeutics: Recent Collaborations 11.4. Recent Collaborations: Distribution by Month/Year 11.5. Recent Collaborations: Distribution by Type of Model 11.6. Recent Collaborations: Distribution by Focus Area 11.7. Recent Collaborations: Most Active Companies 12. Market Forecast and Opportunity Analysis 12.1. Chapter Overview 12.2. Scope and Limitations 12.3. Forecast Methodology 12.4. Overall Ubiquitin Enzyme Inhibitors Market 12.5. Ubiquitin Enzyme Inhibitors Market: Individual Forecasts 13. Conclusion 13.1. Drugs Targeting Protein Modification Pathways Have Emerged as Valuable Therapeutic Options 13.2. Extensive Research is Being Carried Out to Address the Challenges Associated with Drug Discovery 13.3. The Evolving Pipeline Caters to a Wide Spectrum of Disease Indications 13.4. Targeted Therapies are Being Developed by Leveraging Inherent Specificity of Various UPS Components 13.5. Growing Partnerships and VC Support are Indicative of Lucrative Future Potential 13.6. Novel Technology Platforms and Therapeutic Concepts Will Act as Key Enablers to Drive Future Growth 13.7. Once Approved, Ubiquitin Enzyme Inhibitors are Poised to Achieve an Accelerated Growth 14. Interview Transcripts 14.1. Chapter Overview 14.2. Martin Wiles, Vice President Business Development and Licensing, Almac Discovery  Gerald Gavory, Director of Biology, Almac Discovery 14.3. Katrin Rittinger, Research Group Leader, Francis Crick Institute 14.4. Zhihao Zhuang, Associate Professor, Department of Chemistry and Biochemistry, University Of Delaware 15. Appendix 1: Tabulated Data 16. Appendix 2: List Of Companies And Organizations For more information about this report visit http://www.researchandmarkets.com/research/qpzw26/ubiquitin Research and Markets Laura Wood, Senior Manager press@researchandmarkets.com For E.S.T Office Hours Call +1-917-300-0470 For U.S./CAN Toll Free Call +1-800-526-8630 For GMT Office Hours Call +353-1-416-8900 U.S. Fax: 646-607-1907 Fax (outside U.S.): +353-1-481-1716


Higgins C.,Queen's University of Belfast | Bouazzaoui S.,Queen's University of Belfast | Gaddale K.,Queen's University of Belfast | D'Costa Z.,Queen's University of Belfast | And 7 more authors.
Bioorganic and Medicinal Chemistry Letters | Year: 2014

This Letter describes the further development and SAR exploration of a novel series of Legumain inhibitors. Based upon a previously identified Legumain inhibitor from our group, we explored the SAR of the carbamate phenyl ring system to probe the P3 pocket of the enzyme. This led to the identification of a sub-nanomolar inhibitor of Legumain. © 2014 Elsevier Ltd. All rights reserved.


Valentine A.,Queen's University of Belfast | O'Rourke M.,Queen's University of Belfast | Yakkundi A.,Queen's University of Belfast | Worthington J.,University of Ulster | And 15 more authors.
Clinical Cancer Research | Year: 2011

Purpose: Antiangiogenic therapies can be an important adjunct to the management of many malignancies. Here we investigated a novel protein, FKBPL, and peptide derivative for their antiangiogenic activity and mechanism of action. Experimental Design: Recombinant FKBPL (rFKBPL) and its peptide derivative were assessed in a range of human microvascular endothelial cell (HMEC-1) assays in vitro. Their ability to inhibit proliferation, migration, and Matrigel-dependent tubule formation was determined. They were further evaluated in an ex vivo rat model of neovascularization and in two in vivo mouse models of angiogenesis, that is, the sponge implantation and the intravital microscopy models. Antitumor efficacy was determined in two human tumor xenograft models grown in severe compromised immunodeficient (SCID) mice. Finally, the dependence of peptide on CD44 was determined using a CD44-targeted siRNA approach or in cell lines of differing CD44 status. Results: rFKBPL inhibited endothelial cell migration, tubule formation, and microvessel formation in vitro and in vivo. The region responsible for FKBPL's antiangiogenic activity was identified, and a 24-amino acid peptide (AD-01) spanning this sequence was synthesized. It was potently antiangiogenic and inhibited growth in two human tumor xenograft models (DU145 and MDA-231) when administered systemically, either on its own or in combination with docetaxel. The antiangiogenic activity of FKBPL and AD-01 was dependent on the cell-surface receptor CD44, and signaling downstream of this receptor promoted an antimigratory phenotype. Conclusion: FKBPL and its peptide derivative AD-01 have potent antiangiogenic activity. Thus, these agents offer the potential of an attractive new approach to antiangiogenic therapy. ©2011 AACR.


Ness K.A.,Queen's University of Belfast | Eddie S.L.,Queen's University of Belfast | Burton S.,Almac Discovery | Harrison T.,Almac Discovery | And 2 more authors.
Bioorganic and Medicinal Chemistry Letters | Year: 2016

This letter describes the design, development and SAR exploration of a novel series of small legumain inhibitors. The SAR of a new small molecule legumain inhibitor chemotype was explored and found to have improved physiochemical properties compared to previously developed inhibitors within our group. However, further development of this series was found to be limited as the SAR was observed to be relatively flat. © 2015 Elsevier B.V. All rights reserved.


Ness K.A.,Queen's University of Belfast | Eddie S.L.,Queen's University of Belfast | Higgins C.A.,Queen's University of Belfast | Templeman A.,Queen's University of Belfast | And 12 more authors.
Bioorganic and Medicinal Chemistry Letters | Year: 2015

This Letter describes the continued SAR exploration of small molecule Legumain inhibitors with the aim of developing a potent and selective in vitro tool compound. Work continued in this Letter explores the use of alternative P2-P3 linker units and the P3 group SAR which led to the identification of 10t, a potent, selective and cellularly active Legumain inhibitor. We also demonstrate that 10t has activity in both cancer cell viability and colony formation assays. © 2015 Elsevier Ltd. All rights reserved.


PubMed | Queen's University of Belfast and Almac Discovery
Type: Journal Article | Journal: Bioorganic & medicinal chemistry letters | Year: 2015

This Letter describes the continued SAR exploration of small molecule Legumain inhibitors with the aim of developing a potent and selective in vitro tool compound. Work continued in this Letter explores the use of alternative P2-P3 linker units and the P3 group SAR which led to the identification of 10t, a potent, selective and cellularly active Legumain inhibitor. We also demonstrate that 10t has activity in both cancer cell viability and colony formation assays.


PubMed | Queen's University of Belfast and Almac Discovery
Type: Journal Article | Journal: Bioorganic & medicinal chemistry letters | Year: 2014

This Letter describes the further development and SAR exploration of a novel series of Legumain inhibitors. Based upon a previously identified Legumain inhibitor from our group, we explored the SAR of the carbamate phenyl ring system to probe the P3 pocket of the enzyme. This led to the identification of a sub-nanomolar inhibitor of Legumain.

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