[{"issue":"1","language":[{"iso":"eng"}],"isi":1,"publication_identifier":{"eissn":["14783231"],"issn":["14783223"]},"quality_controlled":"1","doi":"10.1111/liv.14730","department":[{"_id":"CampIT"}],"publisher":"Wiley","user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","article_type":"original","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"scopus_import":"1","article_processing_charge":"No","publication":"Liver International","day":"01","file":[{"checksum":"6e4f21b77ef22c854e016240974fc473","file_id":"9091","date_updated":"2021-02-04T12:01:45Z","access_level":"open_access","date_created":"2021-02-04T12:01:45Z","file_name":"2021_Liver_Nardo.pdf","success":1,"creator":"dernst","file_size":930414,"relation":"main_file","content_type":"application/pdf"}],"author":[{"full_name":"Nardo, Alexander D.","first_name":"Alexander D.","last_name":"Nardo"},{"last_name":"Schneeweiss-Gleixner","first_name":"Mathias","full_name":"Schneeweiss-Gleixner, Mathias"},{"full_name":"Bakail, May M","id":"FB3C3F8E-522F-11EA-B186-22963DDC885E","orcid":"0000-0002-9592-1587","first_name":"May M","last_name":"Bakail"},{"full_name":"Dixon, Emmanuel D.","last_name":"Dixon","first_name":"Emmanuel D."},{"full_name":"Lax, Sigurd F.","last_name":"Lax","first_name":"Sigurd F."},{"first_name":"Michael","last_name":"Trauner","full_name":"Trauner, Michael"}],"title":"Pathophysiological mechanisms of liver injury in COVID-19","status":"public","external_id":{"isi":["000594239200001"]},"citation":{"ama":"Nardo AD, Schneeweiss-Gleixner M, Bakail MM, Dixon ED, Lax SF, Trauner M. Pathophysiological mechanisms of liver injury in COVID-19. <i>Liver International</i>. 2021;41(1):20-32. doi:<a href=\"https://doi.org/10.1111/liv.14730\">10.1111/liv.14730</a>","apa":"Nardo, A. D., Schneeweiss-Gleixner, M., Bakail, M. M., Dixon, E. D., Lax, S. F., &#38; Trauner, M. (2021). Pathophysiological mechanisms of liver injury in COVID-19. <i>Liver International</i>. Wiley. <a href=\"https://doi.org/10.1111/liv.14730\">https://doi.org/10.1111/liv.14730</a>","mla":"Nardo, Alexander D., et al. “Pathophysiological Mechanisms of Liver Injury in COVID-19.” <i>Liver International</i>, vol. 41, no. 1, Wiley, 2021, pp. 20–32, doi:<a href=\"https://doi.org/10.1111/liv.14730\">10.1111/liv.14730</a>.","ista":"Nardo AD, Schneeweiss-Gleixner M, Bakail MM, Dixon ED, Lax SF, Trauner M. 2021. Pathophysiological mechanisms of liver injury in COVID-19. Liver International. 41(1), 20–32.","chicago":"Nardo, Alexander D., Mathias Schneeweiss-Gleixner, May M Bakail, Emmanuel D. Dixon, Sigurd F. Lax, and Michael Trauner. “Pathophysiological Mechanisms of Liver Injury in COVID-19.” <i>Liver International</i>. Wiley, 2021. <a href=\"https://doi.org/10.1111/liv.14730\">https://doi.org/10.1111/liv.14730</a>.","ieee":"A. D. Nardo, M. Schneeweiss-Gleixner, M. M. Bakail, E. D. Dixon, S. F. Lax, and M. Trauner, “Pathophysiological mechanisms of liver injury in COVID-19,” <i>Liver International</i>, vol. 41, no. 1. Wiley, pp. 20–32, 2021.","short":"A.D. Nardo, M. Schneeweiss-Gleixner, M.M. Bakail, E.D. Dixon, S.F. Lax, M. Trauner, Liver International 41 (2021) 20–32."},"intvolume":"        41","has_accepted_license":"1","publication_status":"published","oa":1,"ddc":["570"],"date_published":"2021-01-01T00:00:00Z","year":"2021","acknowledgement":"This work was supported by grant F7310‐B21 from the Austrian Science Foundation (to MT). We thank Jelena Remetic, Claudia D. Fuchs, Veronika Mlitz and Daniel Steinacher, for their valuable input and discussion. Figure 1 and Figure 2 have been created with BioRender.com.","_id":"8927","month":"01","type":"journal_article","oa_version":"Published Version","date_updated":"2023-08-04T11:19:51Z","abstract":[{"text":"The recent outbreak of coronavirus disease 2019 (COVID‐19), caused by the Severe Acute Respiratory Syndrome Coronavirus‐2 (SARS‐CoV‐2) has resulted in a world‐wide pandemic. Disseminated lung injury with the development of acute respiratory distress syndrome (ARDS) is the main cause of mortality in COVID‐19. Although liver failure does not seem to occur in the absence of pre‐existing liver disease, hepatic involvement in COVID‐19 may correlate with overall disease severity and serve as a prognostic factor for the development of ARDS. The spectrum of liver injury in COVID‐19 may range from direct infection by SARS‐CoV‐2, indirect involvement by systemic inflammation, hypoxic changes, iatrogenic causes such as drugs and ventilation to exacerbation of underlying liver disease. This concise review discusses the potential pathophysiological mechanisms for SARS‐CoV‐2 hepatic tropism as well as acute and possibly long‐term liver injury in COVID‐19.","lang":"eng"}],"page":"20-32","date_created":"2020-12-06T23:01:16Z","file_date_updated":"2021-02-04T12:01:45Z","volume":41},{"status":"public","external_id":{"pmid":["33741589"],"isi":["000633443000011"]},"intvolume":"         7","citation":{"mla":"Mbianda, Johanne, et al. “Optimal Anchoring of a Foldamer Inhibitor of ASF1 Histone Chaperone through Backbone Plasticity.” <i>Science Advances</i>, vol. 7, no. 12, eabd9153, American Association for the Advancement of Science, 2021, doi:<a href=\"https://doi.org/10.1126/sciadv.abd9153\">10.1126/sciadv.abd9153</a>.","ista":"Mbianda J, Bakail MM, André C, Moal G, Perrin ME, Pinna G, Guerois R, Becher F, Legrand P, Traoré S, Douat C, Guichard G, Ochsenbein F. 2021. Optimal anchoring of a foldamer inhibitor of ASF1 histone chaperone through backbone plasticity. Science Advances. 7(12), eabd9153.","apa":"Mbianda, J., Bakail, M. M., André, C., Moal, G., Perrin, M. E., Pinna, G., … Ochsenbein, F. (2021). Optimal anchoring of a foldamer inhibitor of ASF1 histone chaperone through backbone plasticity. <i>Science Advances</i>. American Association for the Advancement of Science. <a href=\"https://doi.org/10.1126/sciadv.abd9153\">https://doi.org/10.1126/sciadv.abd9153</a>","ama":"Mbianda J, Bakail MM, André C, et al. Optimal anchoring of a foldamer inhibitor of ASF1 histone chaperone through backbone plasticity. <i>Science Advances</i>. 2021;7(12). doi:<a href=\"https://doi.org/10.1126/sciadv.abd9153\">10.1126/sciadv.abd9153</a>","short":"J. Mbianda, M.M. Bakail, C. André, G. Moal, M.E. Perrin, G. Pinna, R. Guerois, F. Becher, P. Legrand, S. Traoré, C. Douat, G. Guichard, F. Ochsenbein, Science Advances 7 (2021).","ieee":"J. Mbianda <i>et al.</i>, “Optimal anchoring of a foldamer inhibitor of ASF1 histone chaperone through backbone plasticity,” <i>Science Advances</i>, vol. 7, no. 12. American Association for the Advancement of Science, 2021.","chicago":"Mbianda, Johanne, May M Bakail, Christophe André, Gwenaëlle Moal, Marie E. Perrin, Guillaume Pinna, Raphaël Guerois, et al. “Optimal Anchoring of a Foldamer Inhibitor of ASF1 Histone Chaperone through Backbone Plasticity.” <i>Science Advances</i>. American Association for the Advancement of Science, 2021. <a href=\"https://doi.org/10.1126/sciadv.abd9153\">https://doi.org/10.1126/sciadv.abd9153</a>."},"oa":1,"publication_status":"published","has_accepted_license":"1","date_published":"2021-03-19T00:00:00Z","ddc":["570"],"acknowledgement":"We thank the Synchrotron SOLEIL, the European Synchrotron Radiation Facility (ESRF), and the French Infrastructure for Integrated Structural Biology (FRISBI) ANR-10-INBS-05. We are particularly grateful to A. Clavier and A. Campalans for help in setting up and performing the cell penetration assays. Funding: Research was funded by the French Centre National de Recherche Scientifique (CNRS), the Commissariat à l’Energie Atomique (CEA), University of Bordeaux, University Paris-Saclay, and the Synchrotron Soleil. The project was supported by the ANR 2007 BREAKABOUND (JC-07-216078), 2011 BIPBIP (ANR-10-BINF-0003), 2012 CHAPINHIB (ANR-12-BSV5-0022-01), 2015 CHIPSET (ANR-15-CE11-008-01), 2015 HIMPP2I (ANR-15-CE07-0010), and the program labeled by the ARC foundation 2016 PGA1*20160203953). M.B. was supported by Canceropole (Paris, France) and a grant for young researchers from La Ligue contre le Cancer. J.M. was supported by La Ligue contre le Cancer.","year":"2021","_id":"9262","date_updated":"2023-08-07T14:20:26Z","abstract":[{"lang":"eng","text":"Sequence-specific oligomers with predictable folding patterns, i.e., foldamers, provide new opportunities to mimic α-helical peptides and design inhibitors of protein-protein interactions. One major hurdle of this strategy is to retain the correct orientation of key side chains involved in protein surface recognition. Here, we show that the structural plasticity of a foldamer backbone may notably contribute to the required spatial adjustment for optimal interaction with the protein surface. By using oligoureas as α helix mimics, we designed a foldamer/peptide hybrid inhibitor of histone chaperone ASF1, a key regulator of chromatin dynamics. The crystal structure of its complex with ASF1 reveals a notable plasticity of the urea backbone, which adapts to the ASF1 surface to maintain the same binding interface. One additional benefit of generating ASF1 ligands with nonpeptide oligourea segments is the resistance to proteolysis in human plasma, which was highly improved compared to the cognate α-helical peptide."}],"month":"03","type":"journal_article","oa_version":"Published Version","volume":7,"date_created":"2021-03-22T07:14:03Z","file_date_updated":"2021-03-22T12:49:00Z","isi":1,"language":[{"iso":"eng"}],"issue":"12","publication_identifier":{"issn":["2375-2548"]},"doi":"10.1126/sciadv.abd9153","quality_controlled":"1","user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","publisher":"American Association for the Advancement of Science","pmid":1,"department":[{"_id":"CampIT"}],"publication":"Science Advances","article_processing_charge":"No","tmp":{"name":"Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)","short":"CC BY-NC (4.0)","image":"/images/cc_by_nc.png","legal_code_url":"https://creativecommons.org/licenses/by-nc/4.0/legalcode"},"article_type":"original","author":[{"full_name":"Mbianda, Johanne","last_name":"Mbianda","first_name":"Johanne"},{"first_name":"May M","last_name":"Bakail","full_name":"Bakail, May M","orcid":"0000-0002-9592-1587","id":"FB3C3F8E-522F-11EA-B186-22963DDC885E"},{"last_name":"André","first_name":"Christophe","full_name":"André, Christophe"},{"last_name":"Moal","first_name":"Gwenaëlle","full_name":"Moal, Gwenaëlle"},{"last_name":"Perrin","first_name":"Marie E.","full_name":"Perrin, Marie E."},{"first_name":"Guillaume","last_name":"Pinna","full_name":"Pinna, Guillaume"},{"last_name":"Guerois","first_name":"Raphaël","full_name":"Guerois, Raphaël"},{"full_name":"Becher, Francois","last_name":"Becher","first_name":"Francois"},{"last_name":"Legrand","first_name":"Pierre","full_name":"Legrand, Pierre"},{"full_name":"Traoré, Seydou","first_name":"Seydou","last_name":"Traoré"},{"full_name":"Douat, Céline","first_name":"Céline","last_name":"Douat"},{"last_name":"Guichard","first_name":"Gilles","full_name":"Guichard, Gilles"},{"full_name":"Ochsenbein, Françoise","last_name":"Ochsenbein","first_name":"Françoise"}],"license":"https://creativecommons.org/licenses/by-nc/4.0/","day":"19","file":[{"access_level":"open_access","date_created":"2021-03-22T12:49:00Z","checksum":"737624cd0e630ffa7c52797a690500e3","date_updated":"2021-03-22T12:49:00Z","file_id":"9280","creator":"dernst","relation":"main_file","content_type":"application/pdf","file_size":837156,"success":1,"file_name":"2021_ScienceAdv_Mbianda.pdf"}],"title":"Optimal anchoring of a foldamer inhibitor of ASF1 histone chaperone through backbone plasticity","article_number":"eabd9153"},{"publication_identifier":{"issn":["1439-4227","1439-7633"]},"doi":"10.1002/cbic.201800633","quality_controlled":"1","issue":"7","language":[{"iso":"eng"}],"author":[{"first_name":"May M","last_name":"Bakail","full_name":"Bakail, May M","id":"FB3C3F8E-522F-11EA-B186-22963DDC885E","orcid":"0000-0002-9592-1587"},{"first_name":"Silvia","last_name":"Rodriguez‐Marin","full_name":"Rodriguez‐Marin, Silvia"},{"full_name":"Hegedüs, Zsófia","first_name":"Zsófia","last_name":"Hegedüs"},{"full_name":"Perrin, Marie E.","last_name":"Perrin","first_name":"Marie E."},{"first_name":"Françoise","last_name":"Ochsenbein","full_name":"Ochsenbein, Françoise"},{"full_name":"Wilson, Andrew J.","first_name":"Andrew J.","last_name":"Wilson"}],"day":"01","title":"Recognition of ASF1 by using hydrocarbon‐constrained peptides","publisher":"Wiley","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication":"ChemBioChem","article_type":"original","article_processing_charge":"No","oa":1,"publication_status":"published","date_published":"2019-04-01T00:00:00Z","main_file_link":[{"url":" https://doi.org/10.1002/cbic.201800633","open_access":"1"}],"status":"public","extern":"1","intvolume":"        20","citation":{"chicago":"Bakail, May M, Silvia Rodriguez‐Marin, Zsófia Hegedüs, Marie E. Perrin, Françoise Ochsenbein, and Andrew J. Wilson. “Recognition of ASF1 by Using Hydrocarbon‐constrained Peptides.” <i>ChemBioChem</i>. Wiley, 2019. <a href=\"https://doi.org/10.1002/cbic.201800633\">https://doi.org/10.1002/cbic.201800633</a>.","ieee":"M. M. Bakail, S. Rodriguez‐Marin, Z. Hegedüs, M. E. Perrin, F. Ochsenbein, and A. J. Wilson, “Recognition of ASF1 by using hydrocarbon‐constrained peptides,” <i>ChemBioChem</i>, vol. 20, no. 7. Wiley, pp. 891–895, 2019.","short":"M.M. Bakail, S. Rodriguez‐Marin, Z. Hegedüs, M.E. Perrin, F. Ochsenbein, A.J. Wilson, ChemBioChem 20 (2019) 891–895.","ama":"Bakail MM, Rodriguez‐Marin S, Hegedüs Z, Perrin ME, Ochsenbein F, Wilson AJ. Recognition of ASF1 by using hydrocarbon‐constrained peptides. <i>ChemBioChem</i>. 2019;20(7):891-895. doi:<a href=\"https://doi.org/10.1002/cbic.201800633\">10.1002/cbic.201800633</a>","apa":"Bakail, M. M., Rodriguez‐Marin, S., Hegedüs, Z., Perrin, M. E., Ochsenbein, F., &#38; Wilson, A. J. (2019). Recognition of ASF1 by using hydrocarbon‐constrained peptides. <i>ChemBioChem</i>. Wiley. <a href=\"https://doi.org/10.1002/cbic.201800633\">https://doi.org/10.1002/cbic.201800633</a>","ista":"Bakail MM, Rodriguez‐Marin S, Hegedüs Z, Perrin ME, Ochsenbein F, Wilson AJ. 2019. Recognition of ASF1 by using hydrocarbon‐constrained peptides. ChemBioChem. 20(7), 891–895.","mla":"Bakail, May M., et al. “Recognition of ASF1 by Using Hydrocarbon‐constrained Peptides.” <i>ChemBioChem</i>, vol. 20, no. 7, Wiley, 2019, pp. 891–95, doi:<a href=\"https://doi.org/10.1002/cbic.201800633\">10.1002/cbic.201800633</a>."},"page":"891-895","oa_version":"Published Version","type":"journal_article","month":"04","date_updated":"2023-02-23T13:46:48Z","abstract":[{"text":"Inhibiting the histone H3–ASF1 (anti‐silencing function 1) protein–protein interaction (PPI) represents a potential approach for treating numerous cancers. As an α‐helix‐mediated PPI, constraining the key histone H3 helix (residues 118–135) is a strategy through which chemical probes might be elaborated to test this hypothesis. In this work, variant H3118–135 peptides bearing pentenylglycine residues at the i and i+4 positions were constrained by olefin metathesis. Biophysical analyses revealed that promotion of a bioactive helical conformation depends on the position at which the constraint is introduced, but that the potency of binding towards ASF1 is unaffected by the constraint and instead that enthalpy–entropy compensation occurs.","lang":"eng"}],"volume":20,"date_created":"2021-01-19T10:59:14Z","year":"2019","_id":"9016"},{"citation":{"mla":"Bakail, May M., et al. “Design on a Rational Basis of High-Affinity Peptides Inhibiting the Histone Chaperone ASF1.” <i>Cell Chemical Biology</i>, vol. 26, no. 11, Elsevier, 2019, p. 1573–1585.e10, doi:<a href=\"https://doi.org/10.1016/j.chembiol.2019.09.002\">10.1016/j.chembiol.2019.09.002</a>.","ista":"Bakail MM, Gaubert A, Andreani J, Moal G, Pinna G, Boyarchuk E, Gaillard M-C, Courbeyrette R, Mann C, Thuret J-Y, Guichard B, Murciano B, Richet N, Poitou A, Frederic C, Le Du M-H, Agez M, Roelants C, Gurard-Levin ZA, Almouzni G, Cherradi N, Guerois R, Ochsenbein F. 2019. Design on a rational basis of high-affinity peptides inhibiting the histone chaperone ASF1. Cell Chemical Biology. 26(11), 1573–1585.e10.","apa":"Bakail, M. M., Gaubert, A., Andreani, J., Moal, G., Pinna, G., Boyarchuk, E., … Ochsenbein, F. (2019). Design on a rational basis of high-affinity peptides inhibiting the histone chaperone ASF1. <i>Cell Chemical Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.chembiol.2019.09.002\">https://doi.org/10.1016/j.chembiol.2019.09.002</a>","ama":"Bakail MM, Gaubert A, Andreani J, et al. Design on a rational basis of high-affinity peptides inhibiting the histone chaperone ASF1. <i>Cell Chemical Biology</i>. 2019;26(11):1573-1585.e10. doi:<a href=\"https://doi.org/10.1016/j.chembiol.2019.09.002\">10.1016/j.chembiol.2019.09.002</a>","short":"M.M. Bakail, A. Gaubert, J. Andreani, G. Moal, G. Pinna, E. Boyarchuk, M.-C. Gaillard, R. Courbeyrette, C. Mann, J.-Y. Thuret, B. Guichard, B. Murciano, N. Richet, A. Poitou, C. Frederic, M.-H. Le Du, M. Agez, C. Roelants, Z.A. Gurard-Levin, G. Almouzni, N. Cherradi, R. Guerois, F. Ochsenbein, Cell Chemical Biology 26 (2019) 1573–1585.e10.","ieee":"M. M. Bakail <i>et al.</i>, “Design on a rational basis of high-affinity peptides inhibiting the histone chaperone ASF1,” <i>Cell Chemical Biology</i>, vol. 26, no. 11. Elsevier, p. 1573–1585.e10, 2019.","chicago":"Bakail, May M, Albane Gaubert, Jessica Andreani, Gwenaëlle Moal, Guillaume Pinna, Ekaterina Boyarchuk, Marie-Cécile Gaillard, et al. “Design on a Rational Basis of High-Affinity Peptides Inhibiting the Histone Chaperone ASF1.” <i>Cell Chemical Biology</i>. Elsevier, 2019. <a href=\"https://doi.org/10.1016/j.chembiol.2019.09.002\">https://doi.org/10.1016/j.chembiol.2019.09.002</a>."},"extern":"1","intvolume":"        26","status":"public","external_id":{"pmid":["31543461"]},"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.chembiol.2019.09.002"}],"date_published":"2019-11-21T00:00:00Z","oa":1,"publication_status":"published","_id":"9018","year":"2019","date_created":"2021-01-19T11:04:50Z","volume":26,"month":"11","oa_version":"Published Version","type":"journal_article","date_updated":"2023-02-23T13:46:53Z","abstract":[{"lang":"eng","text":"Anti-silencing function 1 (ASF1) is a conserved H3-H4 histone chaperone involved in histone dynamics during replication, transcription, and DNA repair. Overexpressed in proliferating tissues including many tumors, ASF1 has emerged as a promising therapeutic target. Here, we combine structural, computational, and biochemical approaches to design peptides that inhibit the ASF1-histone interaction. Starting from the structure of the human ASF1-histone complex, we developed a rational design strategy combining epitope tethering and optimization of interface contacts to identify a potent peptide inhibitor with a dissociation constant of 3 nM. When introduced into cultured cells, the inhibitors impair cell proliferation, perturb cell-cycle progression, and reduce cell migration and invasion in a manner commensurate with their affinity for ASF1. Finally, we find that direct injection of the most potent ASF1 peptide inhibitor in mouse allografts reduces tumor growth. Our results open new avenues to use ASF1 inhibitors as promising leads for cancer therapy."}],"page":"1573-1585.e10","issue":"11","language":[{"iso":"eng"}],"keyword":["Clinical Biochemistry","Molecular Medicine","Biochemistry","Molecular Biology","Pharmacology","Drug Discovery"],"quality_controlled":"1","doi":"10.1016/j.chembiol.2019.09.002","publication_identifier":{"issn":["2451-9456"]},"article_type":"original","article_processing_charge":"No","publication":"Cell Chemical Biology","pmid":1,"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publisher":"Elsevier","title":"Design on a rational basis of high-affinity peptides inhibiting the histone chaperone ASF1","day":"21","author":[{"first_name":"May M","last_name":"Bakail","id":"FB3C3F8E-522F-11EA-B186-22963DDC885E","orcid":"0000-0002-9592-1587","full_name":"Bakail, May M"},{"full_name":"Gaubert, Albane","last_name":"Gaubert","first_name":"Albane"},{"full_name":"Andreani, Jessica","last_name":"Andreani","first_name":"Jessica"},{"first_name":"Gwenaëlle","last_name":"Moal","full_name":"Moal, Gwenaëlle"},{"first_name":"Guillaume","last_name":"Pinna","full_name":"Pinna, Guillaume"},{"full_name":"Boyarchuk, Ekaterina","first_name":"Ekaterina","last_name":"Boyarchuk"},{"first_name":"Marie-Cécile","last_name":"Gaillard","full_name":"Gaillard, Marie-Cécile"},{"last_name":"Courbeyrette","first_name":"Regis","full_name":"Courbeyrette, Regis"},{"last_name":"Mann","first_name":"Carl","full_name":"Mann, Carl"},{"first_name":"Jean-Yves","last_name":"Thuret","full_name":"Thuret, Jean-Yves"},{"last_name":"Guichard","first_name":"Bérengère","full_name":"Guichard, Bérengère"},{"full_name":"Murciano, Brice","first_name":"Brice","last_name":"Murciano"},{"last_name":"Richet","first_name":"Nicolas","full_name":"Richet, Nicolas"},{"last_name":"Poitou","first_name":"Adeline","full_name":"Poitou, Adeline"},{"last_name":"Frederic","first_name":"Claire","full_name":"Frederic, Claire"},{"full_name":"Le Du, Marie-Hélène","first_name":"Marie-Hélène","last_name":"Le Du"},{"first_name":"Morgane","last_name":"Agez","full_name":"Agez, Morgane"},{"first_name":"Caroline","last_name":"Roelants","full_name":"Roelants, Caroline"},{"full_name":"Gurard-Levin, Zachary A.","first_name":"Zachary A.","last_name":"Gurard-Levin"},{"full_name":"Almouzni, Geneviève","last_name":"Almouzni","first_name":"Geneviève"},{"full_name":"Cherradi, Nadia","last_name":"Cherradi","first_name":"Nadia"},{"first_name":"Raphael","last_name":"Guerois","full_name":"Guerois, Raphael"},{"last_name":"Ochsenbein","first_name":"Françoise","full_name":"Ochsenbein, Françoise"}]},{"has_accepted_license":"1","oa":1,"publication_status":"published","ddc":["570"],"date_published":"2016-02-06T00:00:00Z","status":"public","citation":{"apa":"Bakail, M. M., &#38; Ochsenbein, F. (2016). Targeting protein–protein interactions, a wide open field for drug design. <i>Comptes Rendus Chimie</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.crci.2015.12.004\">https://doi.org/10.1016/j.crci.2015.12.004</a>","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.","mla":"Bakail, May M., and Francoise Ochsenbein. “Targeting Protein–Protein Interactions, a Wide Open Field for Drug Design.” <i>Comptes Rendus Chimie</i>, vol. 19, no. 1–2, Elsevier, 2016, pp. 19–27, doi:<a href=\"https://doi.org/10.1016/j.crci.2015.12.004\">10.1016/j.crci.2015.12.004</a>.","ama":"Bakail MM, Ochsenbein F. Targeting protein–protein interactions, a wide open field for drug design. <i>Comptes Rendus Chimie</i>. 2016;19(1-2):19-27. doi:<a href=\"https://doi.org/10.1016/j.crci.2015.12.004\">10.1016/j.crci.2015.12.004</a>","short":"M.M. Bakail, F. Ochsenbein, Comptes Rendus Chimie 19 (2016) 19–27.","chicago":"Bakail, May M, and Francoise Ochsenbein. “Targeting Protein–Protein Interactions, a Wide Open Field for Drug Design.” <i>Comptes Rendus Chimie</i>. Elsevier, 2016. <a href=\"https://doi.org/10.1016/j.crci.2015.12.004\">https://doi.org/10.1016/j.crci.2015.12.004</a>.","ieee":"M. M. Bakail and F. Ochsenbein, “Targeting protein–protein interactions, a wide open field for drug design,” <i>Comptes Rendus Chimie</i>, vol. 19, no. 1–2. Elsevier, pp. 19–27, 2016."},"extern":"1","intvolume":"        19","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."},{"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.","lang":"fre"}],"date_updated":"2023-02-23T13:46:55Z","type":"journal_article","month":"02","oa_version":"Published Version","page":"19-27","file_date_updated":"2021-01-22T12:36:52Z","date_created":"2021-01-19T11:11:54Z","volume":19,"year":"2016","_id":"9019","publication_identifier":{"issn":["1631-0748"]},"quality_controlled":"1","doi":"10.1016/j.crci.2015.12.004","language":[{"iso":"eng"}],"issue":"1-2","keyword":["General Chemistry","General Chemical Engineering"],"file":[{"creator":"dernst","file_size":2045260,"relation":"main_file","content_type":"application/pdf","file_name":"2016_ComptesRendueChimie_Bakail.pdf","success":1,"access_level":"open_access","date_created":"2021-01-22T12:36:52Z","checksum":"c262814ffdbfe95900256ab9ff42cdf5","file_id":"9035","date_updated":"2021-01-22T12:36:52Z"}],"license":"https://creativecommons.org/licenses/by-nc-nd/4.0/","day":"06","author":[{"last_name":"Bakail","first_name":"May M","full_name":"Bakail, May M","id":"FB3C3F8E-522F-11EA-B186-22963DDC885E","orcid":"0000-0002-9592-1587"},{"full_name":"Ochsenbein, Francoise","first_name":"Francoise","last_name":"Ochsenbein"}],"title":"Targeting protein–protein interactions, a wide open field for drug design","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publisher":"Elsevier","article_processing_charge":"No","tmp":{"name":"Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)","short":"CC BY-NC-ND (4.0)","image":"/images/cc_by_nc_nd.png","legal_code_url":"https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode"},"article_type":"original","publication":"Comptes Rendus Chimie"},{"issue":"3","language":[{"iso":"eng"}],"quality_controlled":"1","doi":"10.1093/nar/gkv021","publication_identifier":{"issn":["1362-4962","0305-1048"]},"article_type":"original","article_processing_charge":"No","publication":"Nucleic Acids Research","pmid":1,"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publisher":"Oxford University Press","title":"Structural insight into how the human helicase subunit MCM2 may act as a histone chaperone together with ASF1 at the replication fork","day":"18","author":[{"full_name":"Richet, Nicolas","last_name":"Richet","first_name":"Nicolas"},{"full_name":"Liu, Danni","first_name":"Danni","last_name":"Liu"},{"full_name":"Legrand, Pierre","first_name":"Pierre","last_name":"Legrand"},{"first_name":"Christophe","last_name":"Velours","full_name":"Velours, Christophe"},{"last_name":"Corpet","first_name":"Armelle","full_name":"Corpet, Armelle"},{"last_name":"Gaubert","first_name":"Albane","full_name":"Gaubert, Albane"},{"orcid":"0000-0002-9592-1587","id":"FB3C3F8E-522F-11EA-B186-22963DDC885E","full_name":"Bakail, May M","first_name":"May M","last_name":"Bakail"},{"full_name":"Moal-Raisin, Gwenaelle","first_name":"Gwenaelle","last_name":"Moal-Raisin"},{"last_name":"Guerois","first_name":"Raphael","full_name":"Guerois, Raphael"},{"first_name":"Christel","last_name":"Compper","full_name":"Compper, Christel"},{"full_name":"Besle, Arthur","first_name":"Arthur","last_name":"Besle"},{"full_name":"Guichard, Berengère","last_name":"Guichard","first_name":"Berengère"},{"last_name":"Almouzni","first_name":"Genevieve","full_name":"Almouzni, Genevieve"},{"first_name":"Françoise","last_name":"Ochsenbein","full_name":"Ochsenbein, Françoise"}],"citation":{"short":"N. Richet, D. Liu, P. Legrand, C. Velours, A. Corpet, A. Gaubert, M.M. Bakail, G. Moal-Raisin, R. Guerois, C. Compper, A. Besle, B. Guichard, G. Almouzni, F. Ochsenbein, Nucleic Acids Research 43 (2015) 1905–1917.","chicago":"Richet, Nicolas, Danni Liu, Pierre Legrand, Christophe Velours, Armelle Corpet, Albane Gaubert, May M Bakail, et al. “Structural Insight into How the Human Helicase Subunit MCM2 May Act as a Histone Chaperone Together with ASF1 at the Replication Fork.” <i>Nucleic Acids Research</i>. Oxford University Press, 2015. <a href=\"https://doi.org/10.1093/nar/gkv021\">https://doi.org/10.1093/nar/gkv021</a>.","ieee":"N. Richet <i>et al.</i>, “Structural insight into how the human helicase subunit MCM2 may act as a histone chaperone together with ASF1 at the replication fork,” <i>Nucleic Acids Research</i>, vol. 43, no. 3. Oxford University Press, pp. 1905–1917, 2015.","apa":"Richet, N., Liu, D., Legrand, P., Velours, C., Corpet, A., Gaubert, A., … Ochsenbein, F. (2015). Structural insight into how the human helicase subunit MCM2 may act as a histone chaperone together with ASF1 at the replication fork. <i>Nucleic Acids Research</i>. Oxford University Press. <a href=\"https://doi.org/10.1093/nar/gkv021\">https://doi.org/10.1093/nar/gkv021</a>","mla":"Richet, Nicolas, et al. “Structural Insight into How the Human Helicase Subunit MCM2 May Act as a Histone Chaperone Together with ASF1 at the Replication Fork.” <i>Nucleic Acids Research</i>, vol. 43, no. 3, Oxford University Press, 2015, pp. 1905–17, doi:<a href=\"https://doi.org/10.1093/nar/gkv021\">10.1093/nar/gkv021</a>.","ista":"Richet N, Liu D, Legrand P, Velours C, Corpet A, Gaubert A, Bakail MM, Moal-Raisin G, Guerois R, Compper C, Besle A, Guichard B, Almouzni G, Ochsenbein F. 2015. Structural insight into how the human helicase subunit MCM2 may act as a histone chaperone together with ASF1 at the replication fork. Nucleic Acids Research. 43(3), 1905–1917.","ama":"Richet N, Liu D, Legrand P, et al. Structural insight into how the human helicase subunit MCM2 may act as a histone chaperone together with ASF1 at the replication fork. <i>Nucleic Acids Research</i>. 2015;43(3):1905-1917. doi:<a href=\"https://doi.org/10.1093/nar/gkv021\">10.1093/nar/gkv021</a>"},"intvolume":"        43","extern":"1","status":"public","external_id":{"pmid":["25618846"]},"date_published":"2015-02-18T00:00:00Z","publication_status":"published","_id":"9017","year":"2015","date_created":"2021-01-19T11:01:01Z","volume":43,"oa_version":"Published Version","type":"journal_article","month":"02","abstract":[{"lang":"eng","text":"MCM2 is a subunit of the replicative helicase machinery shown to interact with histones H3 and H4 during the replication process through its N-terminal domain. During replication, this interaction has been proposed to assist disassembly and assembly of nucleosomes on DNA. However, how this interaction participates in crosstalk with histone chaperones at the replication fork remains to be elucidated. Here, we solved the crystal structure of the ternary complex between the histone-binding domain of Mcm2 and the histones H3-H4 at 2.9 Å resolution. Histones H3 and H4 assemble as a tetramer in the crystal structure, but MCM2 interacts only with a single molecule of H3-H4. The latter interaction exploits binding surfaces that contact either DNA or H2B when H3-H4 dimers are incorporated in the nucleosome core particle. Upon binding of the ternary complex with the histone chaperone ASF1, the histone tetramer dissociates and both MCM2 and ASF1 interact simultaneously with the histones forming a 1:1:1:1 heteromeric complex. Thermodynamic analysis of the quaternary complex together with structural modeling support that ASF1 and MCM2 could form a chaperoning module for histones H3 and H4 protecting them from promiscuous interactions. This suggests an additional function for MCM2 outside its helicase function as a proper histone chaperone connected to the replication pathway."}],"date_updated":"2023-02-23T13:46:50Z","page":"1905-1917"}]