Therapeutic strategies for COVID-19: progress and lessons learned
G Li, R Hilgenfeld, R Whitley, E De Clercq - Nature Reviews Drug …, 2023 - nature.com
Abstract The coronavirus disease 2019 (COVID-19) pandemic has stimulated tremendous
efforts to develop therapeutic strategies that target severe acute respiratory syndrome …
efforts to develop therapeutic strategies that target severe acute respiratory syndrome …
Accelerating antiviral drug discovery: lessons from COVID-19
During the coronavirus disease 2019 (COVID-19) pandemic, a wave of rapid and
collaborative drug discovery efforts took place in academia and industry, culminating in …
collaborative drug discovery efforts took place in academia and industry, culminating in …
Iterative computational design and crystallographic screening identifies potent inhibitors targeting the Nsp3 macrodomain of SARS-CoV-2
S Gahbauer, GJ Correy, M Schuller… - Proceedings of the …, 2023 - National Acad Sciences
The nonstructural protein 3 (NSP3) of the severe acute respiratory syndrome-coronavirus-2
(SARS-CoV-2) contains a conserved macrodomain enzyme (Mac1) that is critical for …
(SARS-CoV-2) contains a conserved macrodomain enzyme (Mac1) that is critical for …
PARP14 and PARP9/DTX3L regulate interferon-induced ADP-ribosylation
P Kar, C Chatrin, N Đukić, O Suyari, M Schuller… - The EMBO …, 2024 - embopress.org
PARP-catalysed ADP-ribosylation (ADPr) is important in regulating various cellular
pathways. Until recently, PARP-dependent mono-ADP-ribosylation has been poorly …
pathways. Until recently, PARP-dependent mono-ADP-ribosylation has been poorly …
A single inactivating amino acid change in the SARS-CoV-2 NSP3 Mac1 domain attenuates viral replication in vivo
Despite unprecedented efforts, our therapeutic arsenal against SARS-CoV-2 remains
limited. The conserved macrodomain 1 (Mac1) in NSP3 is an enzyme exhibiting ADP …
limited. The conserved macrodomain 1 (Mac1) in NSP3 is an enzyme exhibiting ADP …
PARP14 is a writer, reader, and eraser of mono-ADP-ribosylation
A Torretta, C Chatzicharalampous… - Journal of Biological …, 2023 - ASBMB
PARP14/BAL2 is a large multidomain enzyme involved in signaling pathways with
relevance to cancer, inflammation, and infection. Inhibition of its mono-ADP-ribosylating …
relevance to cancer, inflammation, and infection. Inhibition of its mono-ADP-ribosylating …
Targeting SARS-CoV-2 nonstructural protein 3: Function, structure, inhibition, and perspective in drug discovery
As a highly contagious human pathogen, severe acute respiratory syndrome-associated
coronavirus-2 (SARS-CoV-2) has infected billions of people worldwide with more than 6 …
coronavirus-2 (SARS-CoV-2) has infected billions of people worldwide with more than 6 …
Mutation of a highly conserved isoleucine residue in loop 2 of several β-coronavirus macrodomains indicates that enhanced ADP-ribose binding is detrimental for …
CM Kerr, JJ Pfannenstiel, YM Alhammad… - Journal of …, 2024 - journals.asm.org
All coronaviruses (CoVs) encode for a conserved macrodomain (Mac1) located in non-
structural protein 3. Mac1 is an ADP-ribosylhydrolase that binds and hydrolyzes mono-ADP …
structural protein 3. Mac1 is an ADP-ribosylhydrolase that binds and hydrolyzes mono-ADP …
An update on the current state of SARS-CoV-2 Mac1 inhibitors
JJ O'Connor, D Ferraris, AR Fehr - Pathogens, 2023 - mdpi.com
Non-structural protein 3 (nsp3) from all coronaviruses (CoVs) contains a conserved
macrodomain, known as Mac1, that has been proposed as a potential therapeutic target for …
macrodomain, known as Mac1, that has been proposed as a potential therapeutic target for …
A Fluorescence Polarization Assay for Macrodomains Facilitates the Identification of Potent Inhibitors of the SARS-CoV-2 Macrodomain
A Anmangandla, S Jana, K Peng… - ACS chemical …, 2023 - ACS Publications
Viral macrodomains, which can bind to and/or hydrolyze adenine diphosphate ribose (ADP-
ribose or ADPr) from proteins, have been suggested to counteract host immune response …
ribose or ADPr) from proteins, have been suggested to counteract host immune response …