{"intvolume":" 19","file":[{"file_size":2045260,"content_type":"application/pdf","creator":"dernst","file_id":"9035","date_updated":"2021-01-22T12:36:52Z","access_level":"open_access","relation":"main_file","success":1,"file_name":"2016_ComptesRendueChimie_Bakail.pdf","date_created":"2021-01-22T12:36:52Z","checksum":"c262814ffdbfe95900256ab9ff42cdf5"}],"language":[{"iso":"eng"}],"title":"Targeting protein–protein interactions, a wide open field for drug design","quality_controlled":"1","issue":"1-2","oa_version":"Published Version","keyword":["General Chemistry","General Chemical Engineering"],"publisher":"Elsevier","article_type":"original","year":"2016","day":"06","tmp":{"image":"/images/cc_by_nc_nd.png","legal_code_url":"https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode","short":"CC BY-NC-ND (4.0)","name":"Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)"},"date_published":"2016-02-06T00:00:00Z","license":"https://creativecommons.org/licenses/by-nc-nd/4.0/","volume":19,"date_updated":"2023-02-23T13:46:55Z","type":"journal_article","has_accepted_license":"1","extern":"1","publication_identifier":{"issn":["1631-0748"]},"doi":"10.1016/j.crci.2015.12.004","author":[{"full_name":"Bakail, May M","first_name":"May M","orcid":"0000-0002-9592-1587","last_name":"Bakail","id":"FB3C3F8E-522F-11EA-B186-22963DDC885E"},{"full_name":"Ochsenbein, Francoise","first_name":"Francoise","last_name":"Ochsenbein"}],"_id":"9019","publication":"Comptes Rendus Chimie","publication_status":"published","abstract":[{"lang":"eng","text":"Targeting protein–protein interactions has long been considered as a very difficult if impossible task, but over the past decade, front lines have moved. The number of successful examples is exponentially growing. This review presents a rapid overview of recent advances in this field considering the strengths and weaknesses of the small molecule approaches and alternative strategies such as the selection or design of artificial antibodies, peptides or peptidomimetics."},{"lang":"fre","text":"Cibler les interactions protéine–protéine a longtemps été considéré comme une tâche très difficile, voire impossible, mais, depuis les dix dernières années, les lignes ont bougé. Le nombre d’exemples de réussites s’accroît exponentiellement. Cette revue présente un rapide panorama des avancées récentes dans ce domaine, considérant les forces et les faiblesses de l’approche « petite molécule » ainsi que des stratégies alternatives comme la sélection ou le design d’anticorps artificiels, de peptides ou de peptidomimétiques."}],"article_processing_charge":"No","citation":{"apa":"Bakail, M. M., & Ochsenbein, F. (2016). Targeting protein–protein interactions, a wide open field for drug design. Comptes Rendus Chimie. Elsevier. https://doi.org/10.1016/j.crci.2015.12.004","ista":"Bakail MM, Ochsenbein F. 2016. Targeting protein–protein interactions, a wide open field for drug design. Comptes Rendus Chimie. 19(1–2), 19–27.","chicago":"Bakail, May M, and Francoise Ochsenbein. “Targeting Protein–Protein Interactions, a Wide Open Field for Drug Design.” Comptes Rendus Chimie. Elsevier, 2016. https://doi.org/10.1016/j.crci.2015.12.004.","ieee":"M. M. Bakail and F. Ochsenbein, “Targeting protein–protein interactions, a wide open field for drug design,” Comptes Rendus Chimie, vol. 19, no. 1–2. Elsevier, pp. 19–27, 2016.","short":"M.M. Bakail, F. Ochsenbein, Comptes Rendus Chimie 19 (2016) 19–27.","ama":"Bakail MM, Ochsenbein F. Targeting protein–protein interactions, a wide open field for drug design. Comptes Rendus Chimie. 2016;19(1-2):19-27. doi:10.1016/j.crci.2015.12.004","mla":"Bakail, May M., and Francoise Ochsenbein. “Targeting Protein–Protein Interactions, a Wide Open Field for Drug Design.” Comptes Rendus Chimie, vol. 19, no. 1–2, Elsevier, 2016, pp. 19–27, doi:10.1016/j.crci.2015.12.004."},"date_created":"2021-01-19T11:11:54Z","month":"02","page":"19-27","status":"public","ddc":["570"],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","file_date_updated":"2021-01-22T12:36:52Z","oa":1}