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1.
Proceedings of the ACM on Human-Computer Interaction ; 7(CSCW1), 2023.
Article in English | Scopus | ID: covidwho-2312121

ABSTRACT

Previous research on employee voice has sought to design technological solutions that address the challenges of speaking up in the workplace. However, effectively embedding employee voice systems in organisations requires designers to engage with the social processes, power relations and contextual factors of individual workplaces. We explore this process within a university workplace through a research project responding to a crisis in educational service delivery arising from the COVID-19 pandemic. Within a successful three-month staff-led engagement, we examined the intricacies of embedding employee voice, exploring how the interactions between existing actors impacted the effectiveness of the process. We sought to identify specific actions to promote employee voice and overcome barriers to its successful establishment in organisational decision-making. We highlight design considerations for an effective employee voice system that facilitates embedding employee voice, including assurance, bounded accountability and bias reflexivity. © 2023 ACM.

2.
STAR Protoc ; 3(1): 101158, 2022 03 18.
Article in English | MEDLINE | ID: covidwho-1650422

ABSTRACT

The SARS-CoV-2 main protease of (Mpro) is an important target for SARS-CoV-2 related drug repurposing and development studies. Here, we describe the steps for structural characterization of SARS-CoV-2 Mpro, starting from plasmid preparation and protein purification. We detail the steps for crystallization using the sitting drop, microbatch (under oil) approach. Finally, we cover data collection and structure determination using serial femtosecond crystallography. For complete details on the use and execution of this protocol, please refer to Durdagi et al. (2021).


Subject(s)
Coronavirus 3C Proteases/chemistry , Models, Molecular , SARS-CoV-2/enzymology , Coronavirus 3C Proteases/genetics , Crystallization , Crystallography, X-Ray , Humans
3.
Structure ; 29(12): 1382-1396.e6, 2021 12 02.
Article in English | MEDLINE | ID: covidwho-1356461

ABSTRACT

The COVID-19 pandemic has resulted in 198 million reported infections and more than 4 million deaths as of July 2021 (covid19.who.int). Research to identify effective therapies for COVID-19 includes: (1) designing a vaccine as future protection; (2) de novo drug discovery; and (3) identifying existing drugs to repurpose them as effective and immediate treatments. To assist in drug repurposing and design, we determine two apo structures of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) main protease at ambient temperature by serial femtosecond X-ray crystallography. We employ detailed molecular simulations of selected known main protease inhibitors with the structures and compare binding modes and energies. The combined structural and molecular modeling studies not only reveal the dynamics of small molecules targeting the main protease but also provide invaluable opportunities for drug repurposing and structure-based drug design strategies against SARS-CoV-2.


Subject(s)
COVID-19 Drug Treatment , Coronavirus 3C Proteases/chemistry , Drug Design , Drug Repositioning , SARS-CoV-2 , Catalytic Domain , Computer Simulation , Crystallography, X-Ray , Dimerization , Molecular Conformation , Molecular Docking Simulation , Principal Component Analysis , Protein Conformation , Recombinant Proteins/chemistry , Temperature
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