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1.
Social Politics ; : 25, 2022.
Article in English | Web of Science | ID: covidwho-1741019

ABSTRACT

COVID-19 threatens to slow progress on the implementation of peace agreements, and reverse hard-won gains of women peacebuilders' work towards holistic, gender-equal peace, rooted in human security. Through an analysis of in-depth interviews from a purposive sample of women peacebuilders in Colombia, South Sudan, the Philippines, and Ukraine, this article contributes to a greater understanding of the pandemic's impact on women's peace activism, as these peacebuilders adapted to emerging realities and became first responders. We argue that the pandemic has deepened the marginalization of women peacebuilders from formal peace processes, possibly to detriment of both immediate recovery and long-term peacebuilding.

2.
Virologie ; 25(SUPPL 1):S36, 2021.
Article in English | EMBASE | ID: covidwho-1256140

ABSTRACT

The multidomain non-structural protein 3 (Nsp3) is the largest protein encoded by coronavirus (CoV) genomes and several regions of this protein are essential for viral replication. Previously, SARS-CoV Nsp3 has been shown to contain a SARS-Unique Domain (SUD), which can bind Guanine-rich non-canonical nucleic acid structures called G-quadruplexes (G4) and is essential for SARS-CoV replication. In this presentation, we will show that the SARS-CoV-2 Nsp3 protein also contains a SUD domain interacting with G4s. We will present structural models for these interactions that reveal significant differences with the 3D structures of the SARS-CoV SUD/G4 complex. We will show data, obtained by three in vitro assays, characterizing the interactions between the SARSCoV- 2 SUD domain and different DNA and RNA G4s. Interestingly, these interactions can be disrupted by specific ligands of these G4s and some of these molecules can inhibit SARS-CoV-2 replication in human lung epithelial cell lines. Altogether, our results pave the way for further studies on the role of SUD/G4 interactions during SARSCoV- 2 replication and the use of inhibitors of these interactions as potent antiviral agents.

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