Results 11 to 20 of about 1,793 (163)
The Conserved Macrodomain Is a Potential Therapeutic Target for Coronaviruses and Alphaviruses [PDF]
Pathogens, 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 +3 more
doaj +4 more sources
The Viral Macrodomain Counters Host Antiviral ADP-Ribosylation [PDF]
Viruses, 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, Anthony R. Fehr
doaj +6 more sources
Viral macrodomains: a structural and evolutionary assessment of the pharmacological potential [PDF]
Open Biology, 2020 Viral macrodomains possess the ability to counteract host ADP-ribosylation, a post-translational modification implicated in the creation of an antiviral environment via immune response regulation.
Johannes Gregor Matthias Rack +5 more
doaj +6 more sources
Mitochondrial ceramide-rich macrodomains functionalize Bax upon irradiation. [PDF]
PLoS ONE, 2011 BACKGROUND:Evidence indicates that Bax functions as a "lipidic" pore to regulate mitochondrial outer membrane permeabilization (MOMP), the apoptosis commitment step, through unknown membrane elements.
Hyunmi Lee +14 more
doaj +4 more sources
Macrodomain ADP-ribosylhydrolase and the pathogenesis of infectious diseases. [PDF]
PLoS Pathogens, 2018 Anthony K L Leung +2 more
doaj +4 more sources
Structure-Based Rational Design of a Selective Hydrolase Inhibitor of the Severe Acute Respiratory Syndrome Coronavirus-2 Nsp3 Macrodomain. [PDF]
ChembiochemStructure‐guided design of a sulfamoyl‐modified analog of GS‐441524 yielded a selective, high‐affinity inhibitor of the SARS‐CoV‐2 macrodomain Nsp3b. The compound occupies the phosphate‐binding pocket, forming a stabilizing hydrogen‐bond network that enhances binding affinity (K_D = 0.86 μM).
Krishnathas R +13 more
europepmc +2 more sources
Macrodomains: Structure, Function, Evolution, and Catalytic Activities [PDF]
Annual Review of Biochemistry, 2016 Recent developments indicate that macrodomains, an ancient and diverse protein domain family, are key players in the recognition, interpretation, and turnover of ADP-ribose (ADPr) signaling. Crucial to this is the ability of macrodomains to recognize ADPr either directly, in the form of a metabolic derivative, or as a modification covalently bound to ...
Johannes Gregor Matthias Rack +2 more
+5 more sources
ACS Chemical Biology, 2023 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 and be viable targets for the development of antiviral drugs. Therefore, developing high-throughput screening (HTS) techniques for macrodomain inhibitors is of great interest ...
Ananya Anmangandla +9 more
openaire +2 more sources
PARG: A Macrodomain in Disguise [PDF]
Structure, 2011 Our understanding of poly-ADP-ribosylation as a posttranslational modification was limited by the lack of structural information on poly-ADP-ribose (PAR) hydrolysing enzymes. A recent study in Nature (Slade et al., 2011) reports the structure of PAR glycohydrolase (PARG), revealing unexpected similarity to the ubiquitous ADP-ribose-binding macrodomains.
Markus Hassler +2 more
openaire +2 more sources
Viruses, 2023 Since the emergence of SARS-CoV-2, many genetic variations within its genome have been identified, but only a few mutations have been found in nonstructural proteins (NSPs).
Behnaz Yazdani +3 more
doaj +1 more source