Results 1 to 10 of about 1,800 (162)

The Viral Macrodomain Counters Host Antiviral ADP-Ribosylation [PDF]

open access: yesViruses, 2020
Macrodomains, enzymes that remove ADP-ribose from proteins, are encoded by several families of RNA viruses and have recently been shown to counter innate immune responses to virus infection.
Yousef M O Alhammad   +2 more
exaly   +8 more sources

The Conserved Macrodomain Is a Potential Therapeutic Target for Coronaviruses and Alphaviruses [PDF]

open access: yesPathogens, 2022
Emerging and re-emerging viral diseases pose continuous public health threats, and effective control requires a combination of non-pharmacologic interventions, treatment with antivirals, and prevention with vaccines.
Anthony K L Leung   +2 more
exaly   +6 more sources

Recurrent Loss of Macrodomain Activity in Host Immunity and Viral Proteins

open access: yesPathogens, 2023
Protein post-translational modifications (PTMs) are an important battleground in the evolutionary arms races that are waged between the host innate immune system and viruses.
Andrew Ryan, Matthew D Daugherty
exaly   +7 more sources

Screening assay to monitor mono-ADP-ribosylhydrolase activity of viral macrodomains in cells [PDF]

open access: yesCommunications Biology
Mono-ADP-ribosylation, a modification of both proteins and nucleic acids, is implicated in innate immunity. Intracellularly, this modification is catalyzed by PARP enzymes, some induced in response to interferons.
Sarah Knapp   +16 more
doaj   +2 more sources

Discovery and Development Strategies for SARS-CoV-2 NSP3 Macrodomain Inhibitors

open access: yesPathogens, 2023
The worldwide public health and socioeconomic consequences caused by the COVID-19 pandemic highlight the importance of increasing preparedness for viral disease outbreaks by providing rapid disease prevention and treatment strategies.
Tryfon Zarganes - Tzitzikas   +2 more
exaly   +3 more sources

Targeting SARS-CoV-2 Macrodomain-1 to Restore the Innate Immune Response Using In Silico Screening of Medicinal Compounds and Free Energy Calculation Approaches

open access: yesViruses, 2023
Among the different drug targets of SARS-CoV-2, a multi-domain protein known as NSP3 is a critical element of the translational and replication machinery.
Fahd Al-Mulla   +2 more
exaly   +3 more sources

The Mac1 ADP-ribosylhydrolase is a therapeutic target for SARS-CoV-2 [PDF]

open access: yeseLife
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) continues to pose a threat to public health. Current therapeutics remain limited to direct-acting antivirals that lack distinct mechanisms of action and are already showing signs of viral ...
Rahul K Suryawanshi   +30 more
doaj   +2 more sources

Mutations differentially affecting the coronavirus Mac1 ADP-ribose binding and hydrolysis activities indicate that it promotes multiple stages of the viral replication cycle [PDF]

open access: yesJournal of Virology
All coronaviruses (CoVs) encode a conserved macrodomain, termed Mac1, in non-structural protein 3 (nsp3) that binds and hydrolyzes ADP-ribose covalently attached to proteins.
Joseph J. O'Connor   +9 more
doaj   +2 more sources

Streptomyces coelicolor macrodomain hydrolase SCO6735 cleaves thymidine-linked ADP-ribosylation of DNA

open access: yesComputational and Structural Biotechnology Journal, 2022
ADP-ribosylation is an ancient, highly conserved, and reversible covalent modification critical for a variety of endogenous processes in both prokaryotes and eukaryotes.
Johannes Gregor Matthias Rack   +2 more
exaly   +3 more sources

Family-wide analysis of human macrodomains reveals novel activities and identifies PARG as most efficient ADPr-RNA hydrolase [PDF]

open access: yesCommunications Biology
ADP-ribosylation is well-known as protein posttranslational modification and was recently also identified as RNA posttranscriptional modification. When macrodomain proteins were identified as protein ADP-ribosylhydrolases, several ADP-ribosylation ...
Lisa Weixler   +9 more
doaj   +2 more sources

Home - About - Disclaimer - Privacy