@article{8927,
  abstract     = {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.},
  author       = {Nardo, Alexander D. and Schneeweiss-Gleixner, Mathias and Bakail, May M and Dixon, Emmanuel D. and Lax, Sigurd F. and Trauner, Michael},
  issn         = {14783231},
  journal      = {Liver International},
  number       = {1},
  pages        = {20--32},
  publisher    = {Wiley},
  title        = {{Pathophysiological mechanisms of liver injury in COVID-19}},
  doi          = {10.1111/liv.14730},
  volume       = {41},
  year         = {2021},
}

@article{9262,
  abstract     = {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.},
  author       = {Mbianda, Johanne and Bakail, May M and André, Christophe and Moal, Gwenaëlle and Perrin, Marie E. and Pinna, Guillaume and Guerois, Raphaël and Becher, Francois and Legrand, Pierre and Traoré, Seydou and Douat, Céline and Guichard, Gilles and Ochsenbein, Françoise},
  issn         = {2375-2548},
  journal      = {Science Advances},
  number       = {12},
  publisher    = {American Association for the Advancement of Science},
  title        = {{Optimal anchoring of a foldamer inhibitor of ASF1 histone chaperone through backbone plasticity}},
  doi          = {10.1126/sciadv.abd9153},
  volume       = {7},
  year         = {2021},
}

@article{9016,
  abstract     = {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.},
  author       = {Bakail, May M and Rodriguez‐Marin, Silvia and Hegedüs, Zsófia and Perrin, Marie E. and Ochsenbein, Françoise and Wilson, Andrew J.},
  issn         = {1439-4227},
  journal      = {ChemBioChem},
  number       = {7},
  pages        = {891--895},
  publisher    = {Wiley},
  title        = {{Recognition of ASF1 by using hydrocarbon‐constrained peptides}},
  doi          = {10.1002/cbic.201800633},
  volume       = {20},
  year         = {2019},
}

@article{9018,
  abstract     = {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.},
  author       = {Bakail, May M and Gaubert, Albane and Andreani, Jessica and Moal, Gwenaëlle and Pinna, Guillaume and Boyarchuk, Ekaterina and Gaillard, Marie-Cécile and Courbeyrette, Regis and Mann, Carl and Thuret, Jean-Yves and Guichard, Bérengère and Murciano, Brice and Richet, Nicolas and Poitou, Adeline and Frederic, Claire and Le Du, Marie-Hélène and Agez, Morgane and Roelants, Caroline and Gurard-Levin, Zachary A. and Almouzni, Geneviève and Cherradi, Nadia and Guerois, Raphael and Ochsenbein, Françoise},
  issn         = {2451-9456},
  journal      = {Cell Chemical Biology},
  keywords     = {Clinical Biochemistry, Molecular Medicine, Biochemistry, Molecular Biology, Pharmacology, Drug Discovery},
  number       = {11},
  pages        = {1573--1585.e10},
  publisher    = {Elsevier},
  title        = {{Design on a rational basis of high-affinity peptides inhibiting the histone chaperone ASF1}},
  doi          = {10.1016/j.chembiol.2019.09.002},
  volume       = {26},
  year         = {2019},
}

@article{9019,
  abstract     = {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.},
  author       = {Bakail, May M and Ochsenbein, Francoise},
  issn         = {1631-0748},
  journal      = {Comptes Rendus Chimie},
  keywords     = {General Chemistry, General Chemical Engineering},
  number       = {1-2},
  pages        = {19--27},
  publisher    = {Elsevier},
  title        = {{Targeting protein–protein interactions, a wide open field for drug design}},
  doi          = {10.1016/j.crci.2015.12.004},
  volume       = {19},
  year         = {2016},
}

@article{9017,
  abstract     = {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.},
  author       = {Richet, Nicolas and Liu, Danni and Legrand, Pierre and Velours, Christophe and Corpet, Armelle and Gaubert, Albane and Bakail, May M and Moal-Raisin, Gwenaelle and Guerois, Raphael and Compper, Christel and Besle, Arthur and Guichard, Berengère and Almouzni, Genevieve and Ochsenbein, Françoise},
  issn         = {1362-4962},
  journal      = {Nucleic Acids Research},
  number       = {3},
  pages        = {1905--1917},
  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}},
  doi          = {10.1093/nar/gkv021},
  volume       = {43},
  year         = {2015},
}