{"product_id":"hiv-1-integrase-mechanism-and-inhibitor-design-hardback-9780470184745","title":"HIV-1 Integrase; Mechanism and Inhibitor Design (Hardback) 9780470184745","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eHIV-1 Integrase\u003c\/font\u003e\u003cbr\u003e\r\n\u003cfont size=\"5\"\u003eMechanism and Inhibitor Design\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eNouri Neamati (Edited by), N Neamati (Author), Binghe Wang (Series edited by)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780470184745, Wiley\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 28 October 2011\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e528 pages\u003cbr\u003e28.7 x 22.2 x 3.3 cm, 1.465 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cem\u003e\u003cfont size=\"3\"\u003e\u003cp\u003e“This book will be certainly a valuable reference source for all those who are interested in antiviral drug discovery. All of the information contained in this text offers a rich scientific support for researchers in academia and industry at any level who are interested in enhancing their knowledge on a very fascinating scientific topic.”  (\u003ci\u003eChemMedChem\u003c\/i\u003e, 2012)\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\u003c\/font\u003e\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003eThis book comprehensively covers the mechanisms of action and inhibitor design for HIV-1 integrase. It serves as a resource for scientists facing challenging drug design issues and researchers in antiviral drug discovery. Despite numerous review articles and isolated book chapters dealing with HIV-1 integrase, there has not been a single source for those working to devise anti-AIDS drugs against this promising target. But this book fills that gap and offers a valuable introduction to the field for the interdisciplinary scientists who will need to work together to design drugs that target HIV-1 integrase.\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eChapter 1. HIV life cycle: Targets for anti-HIV agents (\u003ci\u003eErik De Clercq (Rega Institute)\u003c\/i\u003e).  \u003cp\u003eChapter 2. PP32 is hot (\u003ci\u003eDuane P. Grandgenett (SLU)\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003eChapter 3. Integrase mechanism and function (\u003ci\u003eRobert Craigie (NIDDK, NIH)\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003eChapter 4. Structural studies of retroviral integrases (\u003ci\u003eMariusz Jaskolski, Jerry N. Alexandratos, Grzegorz Bujacz and Alexander Wlodawer (NIDDK, NCI, NIH)\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003eChapter 5. Retroviral integration target site selection (\u003ci\u003eAngela Ciuffi and Frederick Bushman (U. Penn)\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003eChapter 6. The pleiotropic nature of human immunodeficiency virus type 1 integrase mutations (\u003ci\u003eAlan Engelman (Harvard)\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003eChapter 7. Insights into HIV-1 integrase-DNA interaction (\u003ci\u003eAllison Johnson, Christopse Marchand, and Yves Pommier (NCI, NIH)\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003eChapter 8. Functional interaction between human immunodeficiency virus type 1 reverse transcriptase and integrase (\u003ci\u003eThomas Wilkinson and Samson A. Chow (UCLA)\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003eChapter 9. Cellular cofactors of HIV integration (\u003ci\u003eWannes Thys, Koen Bartholomeeusen, Zeger Debyser and Jan De Rijck (KULeuven)\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003eChapter 10. Structural aspects of the lentiviral integrase - LEDGF interaction (\u003ci\u003eSteve Hare, Alan Engelman and Peter Cherepanov (Imperial College London and Harvard)\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003eChapter 11. Host factors that affect provirus stability and silencing (\u003ci\u003eRichard A. Katz, René Daniel and Anna Marie Skalka (Fox Chase)\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003eChapter 12. Assays for the evaluation of HIV-1 integrase enzymatic activity, DNA-binding and co-factor interaction (\u003ci\u003eFrauke Christ, Katrien Busschots, Jelle Hendrix, Melissa McNeely, Yves Engelborghs, Zeger Debyser (KU Leuven, Belgium)\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003eChapter 13. HIV-1 integrase inhibitor design: Overview and historical perspectives (\u003ci\u003eNouri Neamati (USC)\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003eChapter 14. HIV integrase inhibitors: from diketoacids to heterocyclic templates: A history of HIV integrase medicinal chemistry at Merck West Point and Merck Rome (IRBM) leading to the discovery of raltegravir (\u003ci\u003eMelissa S. Egbertson, Neville J. Anthony and Vincenzo Summa\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003eChapter 15. Elvitegravir, a novel quinolone HIV-1 integrase strand transfer inhibitor (\u003ci\u003eHisashi Shinkai, Motohide Sato, and Yuji Matsuzaki, Central Pharmaceutical Research Institute, JT Inc., Takatsuki, Japan\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003eChapter 16. Conformationally constrained tricyclic HIV integrase inhibitors (\u003ci\u003eMaria Fardis, Haolun Jin, Xiaowu Chen, Manuel Tsiang, James Chen, Choung Kim, Matthew Wright (Gilead)\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003eChapter 17. Slow onset kinetics of HIV integrase inhibitors and proposed molecular model (\u003ci\u003eEdward P. Garvey and Benjamin Schwartz\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003eChapter 18. Azaindole hydroxamic acids are hiv-1 integrase inhibitors (\u003ci\u003eMichael B. Plewe, Ted W. Johnson\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003eChapter 19. A simple and accurate in vitro method for predicting serum protein binding of hiv integrase strand transfer inhibitors (\u003ci\u003eIra B. Dicker, Michael A. Walker, Zeyu Lin, Brian Terry, Lori Pajor, Ming Zheng, B. Narasimhulu Naidu, Jacques Banville, Nicholas A. Meanwell and Mark Krystal (BMS)).\u003cbr\u003e Chapter 20. Role of metals in HIV-1 integrase inhibitor design (Mario Sechi, Mauro Carcelli, Dominga Rogolino and Nouri Neamati\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003eChapter 21. Discovery and development of natural product inhibitors of HIV-1 integrase (\u003ci\u003eSheo B. Singh (Merck)\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003eChapter 22. Development of styrylquinoline integrase inhibitors (\u003ci\u003eJean-Francois Mouscadet, Eric Deprez, Didier Desmaele, Jean d'Angelo (CNRS, France)\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003eChapter 23. Dicaffeoyltartaric acid and dicaffeoylquinic acid HIV integrase inhibitors (\u003ci\u003eDavid c. Crosby and W. Edward Robinson, Jr. (UCI)\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003eChapter 24. Design and discovery of peptide-based inhibitors (\u003ci\u003eYa-Qiu Long and Nouri Neamati (Shanghai \u0026amp; USC)\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003eChapter 25. Nucleotide-Based Inhibitors of HIV Integrase (\u003ci\u003eVasu Nair and Guochen Chi (U. Georgia)\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003eChapter 26. Design of HIV-1 Integrase Inhibitors Using Computer-aided techniques (\u003ci\u003eErik Serrao, Rambabu Gundla, Jinxia Deng, Srinivas Odde, Nouri Neamati (USC)\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003eChapter 27. Application of protein covalent modification to studying the structure and function of HIV-1 integrase and its inhibitors (\u003ci\u003eXue Zhi Zhao and Terrence R. Burke, Jr.\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003eChapter 28. HIV-1 intergase-DNA models (\u003ci\u003eChenzhong Liao, Marc C. Nicklaus (NCI)\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003eChapter 29. A new paradigm for integrase inhibition: blocking enzyme function without directly targeting the active site (\u003ci\u003eLaith Q. Al-Mawsawi and Nouri Neamati\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003eChapter 30. Resistance to integrase inhibitors (\u003ci\u003eLeen Hombrouck, Zeger Debyser and Myriam Witvrouw (KU Leuven, Belgium)\u003c\/i\u003e).\u003c\/p\u003e\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Chemistry [\u003ca title=\"See our other books on Chemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Chemistry%20%5BPN%5D%22\"\u003ePN\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Wiley","offers":[{"title":"Brand New","offer_id":52257151680792,"sku":"9780470184745","price":106.29,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/files\/9780470184745.jpg?v=1781277659","url":"https:\/\/freshlyprintedbooks.co.uk\/products\/hiv-1-integrase-mechanism-and-inhibitor-design-hardback-9780470184745","provider":"Freshly Printed Books","version":"1.0","type":"link"}