Results 21 to 30 of about 4,884 (228)

Structural Insights into Plasticity and Discovery of Remdesivir Metabolite GS-441524 Binding in SARS-CoV-2 Macrodomain

ACS Medicinal Chemistry Letters, 2021
The nsP3 macrodomain is a conserved protein interaction module that plays essential regulatory roles in host immune response by recognizing and removing posttranslational ADP-ribosylation sites during SARS-CoV-2 infection.
Xiaomin Ni, Martin Schröder, Victor Hernandez-Olmos   +2 more
exaly   +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]

Journal 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, Anuradha Roy, Reem Khattabi, Catherine Kerr, Nancy Schwarting, Yousef M. Alhammad, Philip Gao, Xiaoming Zhang, Xufang Deng, Anthony R. Fehr   +9 more
doaj   +2 more sources

Crystal structure and biochemical activity of the macrodomain from rubella virus p150. [PDF]

J Virol
Rubella virus encodes a nonstructural polyprotein with RNA polymerase, methyltransferase, and papain-like cysteine protease activities, along with a putative macrodomain of unknown function.
Stoll GA, Nikolopoulos N, Zhai H, Zhang L, Douse CH, Modis Y.   +5 more
europepmc   +2 more sources

CACHE Challenge #3: Targeting the Nsp3 Macrodomain of SARS-CoV-2. [PDF]

J Chem Inf Model
The third Critical Assessment of Computational Hit-finding Experiments (CACHE) challenged computational teams to identify chemically novel ligands targeting the macrodomain 1 of SARS-CoV-2 Nsp3, a promising coronavirus drug target.
Herasymenko O, Silva M, Correy GJ, Abu-Saleh AAA, Ackloo S, Arrowsmith C, Ashworth A, Ban F, Beck H, Bishop KP, Bohórquez HJ, Bolotokova A, Breznik M, Chau I, Chen Y, Cherkasov A, Dehaen W, Della Corte D, Denzinger K, Doering NP, Edfeldt K, Edwards A, Fayne D, Gentile F, Gibson E, Gokdemir O, Gunnarsson A, Günther J, Irwin JJ, Jensen JH, Harding RJ, Hillisch A, Hoffer L, Hogner A, Hutchinson A, Kandwal S, Karlova A, Koirala K, Kotelnikov S, Kozakov D, Lee J, Lee S, Lessel U, Liu S, Liu X, Loppnau P, Meiler J, Moretti R, Moroz YS, Muvva C, Oprea TI, Paige B, Pandit A, Park K, Poda G, Protopopov MV, Pütter V, Ravichandran R, Rognan D, Rosta E, Sabnis Y, Scott T, Seitova A, Sharma P, Sindt F, Song M, Steinmann C, Stevens R, Talagayev V, Tararina VV, Tarkhanova O, Tingey D, Trant JF, Treleaven D, Tropsha A, Walters P, Wells J, Westermaier Y, Wolber G, Wortmann L, Zheng S, Fraser JS, Schapira M.   +82 more
europepmc   +2 more sources

Both ADP-Ribosyl-Binding and Hydrolase Activities of the Alphavirus nsP3 Macrodomain Affect Neurovirulence in Mice

mBio, 2020
Macrodomain (MD), a highly conserved protein fold present in a subset of plus-strand RNA viruses, binds to and hydrolyzes ADP-ribose (ADPr) from ADP-ribosylated proteins.
Rachy Abraham, Robert L. McPherson, Morgan Dasovich, Mohsen Badiee, Anthony K. L. Leung, Diane E. Griffin   +5 more
doaj   +2 more sources

Pyrimidone inhibitors targeting Chikungunya Virus nsP3 macrodomain by fragment-based drug design.

PLoS ONE, 2021
The macrodomain of nsP3 (nsP3MD) is highly conserved among the alphaviruses and ADP-ribosylhydrolase activity of Chikungunya Virus (CHIKV) nsP3MD is critical for CHIKV viral replication and virulence.
Sixue Zhang, Atefeh Garzan, Nicole Haese, Robert Bostwick, Yohanka Martinez-Gzegozewska, Lynn Rasmussen, Daniel N Streblow, Mark T Haise, Ashish K Pathak, Corinne E Augelli-Szafran, Mousheng Wu   +10 more
doaj   +2 more sources

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

Communications 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, Roko Žaja, Nonso J. Ikenga, Jonas Siefert, Ganga Mohan, Gülcan Aydin, Sven Wijngaarden, Dmitri V. Filippov, Bernhard Lüscher, Karla L. H. Feijs-Žaja   +9 more
doaj   +2 more sources

The SARS-CoV-2 Conserved Macrodomain Is a Mono-ADP-Ribosylhydrolase [PDF]

Journal of Virology, 2020
SARS-CoV-2 has recently emerged into the human population and has led to a worldwide pandemic of COVID-19 that has caused more than 1.2 million deaths worldwide.
Yousef M. O. Alhammad, M. Kashipathy, Anuradha Roy, J. Gagné, Peter McDonald, Philip Gao, Louis Nonfoux, K. Battaile, David K. Johnson, Erik D. Holmstrom, G. Poirier, S. Lovell, Anthony R. Fehr   +12 more
semanticscholar   +4 more sources

Synthesis and Macrodomain Binding of Gln‐carba‐ADPr‐peptide

ChemBioChem
Mono‐ADP‐ribosylation is a dynamic post‐translational modification (PTM) with important roles in cell signalling. This modification occurs on a wide variety of amino acids, and one of the canonical modification sites within proteins is the side chain of ...
Sander B. Engelsma, A. Nardozza, Pieter Saint Aulaire, H. Overkleeft, G. A. Marel, A. Ladurner, D. Filippov   +6 more
semanticscholar   +3 more sources

PARP14 is regulated by the PARP9/DTX3L complex and promotes interferon γ-induced ADP-ribosylation [PDF]

The EMBO Journal
Protein ADP-ribosylation plays important but ill-defined roles in antiviral signalling cascades such as the interferon response. Several viruses of clinical interest, including coronaviruses, express hydrolases that reverse ADP-ribosylation catalysed by ...
Victoria Chaves Ribeiro, Lilian Cristina Russo, Nícolas Carlos Hoch   +2 more
doaj   +2 more sources