GS-441524-Diphosphate-Ribose Derivatives as Nanomolar Binders and Fluorescence Polarization Tracers for SARS-CoV-2 and Other Viral Macrodomains-Reference-Cited by-同舟云学术

GS-441524-Diphosphate-Ribose Derivatives as Nanomolar Binders and Fluorescence Polarization Tracers for SARS-CoV-2 and Other Viral Macrodomains

Published:2024-04-22 Issue:5 Volume:19 Page:1093-1105
ISSN:1554-8929
Container-title:ACS Chemical Biology
language:en
Short-container-title:ACS Chem. Biol.

Author:

Peng Kewen¹,Wallace Shamar D.²,Bagde Saket R.²^ORCID,Shang Jialin¹,Anmangandla Ananya¹^ORCID,Jana Sadhan¹,Fromme J. Christopher²,Lin Hening³^ORCID

Affiliation:

1. Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, United States

2. Department of Molecular Biology and Genetics, Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, New York 14853, United States

3. Howard Hughes Medical Institute, Department of Chemistry and Chemical Biology, Department of Molecular Biology and Genetics, Cornell University, Ithaca, New York 14853, United States

Funder

National Institute of Arthritis and Musculoskeletal and Skin Diseases

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Link

https://pubs.acs.org/doi/pdf/10.1021/acschembio.4c00027

Reference42 articles.

1. Macrodomains: Structure, Function, Evolution, and Catalytic Activities

2. Macrodomain-containing proteins: regulating new intracellular functions of mono(ADP-ribosyl)ation

3. The mechanisms of catalysis and ligand binding for the SARS-CoV-2 NSP3 macrodomain from neutron and x-ray diffraction at room temperature

4. The Viral Macrodomain Counters Host Antiviral ADP-Ribosylation

5. Viral macrodomains: a structural and evolutionary assessment of the pharmacological potential

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