@article{12131,
  abstract     = {Replication-incompetent adenoviral vectors have been extensively used as a platform for vaccine design, with at least four anti-COVID-19 vaccines authorized to date. These vaccines elicit neutralizing antibody responses directed against SARS-CoV-2 Spike protein and confer significant level of protection against SARS-CoV-2 infection. Immunization with adenovirus-vectored vaccines is known to be accompanied by the production of anti-vector antibodies, which may translate into reduced efficacy of booster or repeated rounds of revaccination. Here, we used blood samples from patients who received an adenovirus-based Gam-COVID-Vac vaccine to address the question of whether anti-vector antibodies may influence the magnitude of SARS-CoV-2-specific humoral response after booster vaccination. We observed that rAd26-based prime vaccination with Gam-COVID-Vac induced the development of Ad26-neutralizing antibodies, which persisted in circulation for at least 9 months. Our analysis further indicates that high pre-boost Ad26 neutralizing antibody titers do not appear to affect the humoral immunogenicity of the Gam-COVID-Vac boost. The titers of anti-SARS-CoV-2 RBD IgGs and antibodies, which neutralized both the wild type and the circulating variants of concern of SARS-CoV-2 such as Delta and Omicron, were independent of the pre-boost levels of Ad26-neutralizing antibodies. Thus, our results support the development of repeated immunization schedule with adenovirus-based COVID-19 vaccines.},
  author       = {Byazrova, Maria G. and Astakhova, Ekaterina A. and Minnegalieva, Aygul and Sukhova, Maria M. and Mikhailov, Artem A. and Prilipov, Alexey G. and Gorchakov, Andrey A. and Filatov, Alexander V.},
  issn         = {2059-0105},
  journal      = {npj Vaccines},
  keywords     = {Pharmacology (medical), Infectious Diseases, Pharmacology, Immunology, SARS-COV-2, COVID},
  publisher    = {Springer Nature},
  title        = {{Anti-Ad26 humoral immunity does not compromise SARS-COV-2 neutralizing antibody responses following Gam-COVID-Vac booster vaccination}},
  doi          = {10.1038/s41541-022-00566-x},
  volume       = {7},
  year         = {2022},
}

@article{11447,
  abstract     = {Empirical essays of fitness landscapes suggest that they may be rugged, that is having multiple fitness peaks. Such fitness landscapes, those that have multiple peaks, necessarily have special local structures, called reciprocal sign epistasis (Poelwijk et al. in J Theor Biol 272:141–144, 2011). Here, we investigate the quantitative relationship between the number of fitness peaks and the number of reciprocal sign epistatic interactions. Previously, it has been shown (Poelwijk et al. in J Theor Biol 272:141–144, 2011) that pairwise reciprocal sign epistasis is a necessary but not sufficient condition for the existence of multiple peaks. Applying discrete Morse theory, which to our knowledge has never been used in this context, we extend this result by giving the minimal number of reciprocal sign epistatic interactions required to create a given number of peaks.},
  author       = {Saona Urmeneta, Raimundo J and Kondrashov, Fyodor and Khudiakova, Kseniia},
  issn         = {1522-9602},
  journal      = {Bulletin of Mathematical Biology},
  keywords     = {Computational Theory and Mathematics, General Agricultural and Biological Sciences, Pharmacology, General Environmental Science, General Biochemistry, Genetics and Molecular Biology, General Mathematics, Immunology, General Neuroscience},
  number       = {8},
  publisher    = {Springer Nature},
  title        = {{Relation between the number of peaks and the number of reciprocal sign epistatic interactions}},
  doi          = {10.1007/s11538-022-01029-z},
  volume       = {84},
  year         = {2022},
}

@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{11117,
  abstract     = {Over the last years it has become evident that the nuclear envelope (NE) is more than a passive membrane barrier that separates the nucleus from the cytoplasm. The NE not only controls the trafficking of macromolecules between the nucleoplasm and the cytosol, but also provides anchoring sites for chromosomes and cytoskeleton to the nuclear periphery. Targeting of chromatin to the NE might actually be part of gene expression regulation in eukaryotes. Mutations in certain NE proteins are associated with a diversity of human diseases, including muscular dystrophy, neuropathy, lipodistrophy, torsion dystonia and the premature aging condition progeria. Despite the importance of the NE for cell division and differentiation, relatively little is known about its biogenesis and its role in human diseases. It is our goal to provide a comprehensive view of the NE and to discuss possible implications of NE-associated changes for gene expression, chromatin organization and signal transduction.},
  author       = {D’Angelo, M. A. and HETZER, Martin W},
  issn         = {1420-9071},
  journal      = {Cellular and Molecular Life Sciences},
  keywords     = {Cell Biology, Cellular and Molecular Neuroscience, Pharmacology, Molecular Biology, Molecular Medicine},
  number       = {3},
  pages        = {316--332},
  publisher    = {Springer Nature},
  title        = {{The role of the nuclear envelope in cellular organization}},
  doi          = {10.1007/s00018-005-5361-3},
  volume       = {63},
  year         = {2006},
}