Results 191 to 200 of about 4,884 (228)

PARP12-mediated mono-ADP-ribosylation as a checkpoint for necroptosis and apoptosis. [PDF]

Proc Natl Acad Sci U S A
Huang X, Li F, Liu L, Li Y, Zhang M, Ma G, Gao Y, Shan B, Liang X, Yuan J, Pan H.   +10 more
europepmc   +1 more source

Macrodomain organization of the Escherichia coli chromosome [PDF]

EMBO Journal, 2004
We have explored the Escherichia coli chromosome architecture by genetic dissection, using a site-specific recombination system that reveals the spatial proximity of distant DNA sites and records interactions. By analysing the percentages of recombination between pairs of sites scattered over the chromosome, we observed that DNA interactions were ...
Francois Cornet, Frederic Boccard
exaly   +3 more sources

Unique Mutations in the Murine Hepatitis Virus Macrodomain Differentially Attenuate Virus Replication, Indicating Multiple Roles for the Macrodomain in Coronavirus Replication

Journal of Virology, 2021
In the wake of the COVID-19 epidemic, there has been a surge to better understand how CoVs replicate and to identify potential therapeutic targets that could mitigate disease caused by SARS-CoV-2 and other prominent CoVs. The highly conserved macrodomain, also termed Mac1, is a small domain within nonstructural protein 3.
Lynden S Voth, David K Johnson, Anthony R Fehr   +2 more
exaly   +4 more sources

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Macrodomain-containing proteins are new mono-ADP-ribosylhydrolases

Nature Structural and Molecular Biology, 2013
ADP-ribosylation is an important post-translational protein modification (PTM) that regulates diverse biological processes. ADP-ribosyltransferase diphtheria toxin-like 10 (ARTD10, also known as PARP10) mono-ADP-ribosylates acidic side chains and is one of eighteen ADP-ribosyltransferases that catalyze mono- or poly-ADP-ribosylation of target proteins.
Karla L H Feijs, Hans Winkler, Amedeo Caflisch   +2 more
exaly   +3 more sources

Hydrolysis of ADP-Ribosylation by Macrodomains

2018
ADP-ribosylation is the process of transferring the ADP-ribose moiety from NAD+ to a substrate. While a number of proteins represent well described substrates accepting ADP-ribose modification, a recent report demonstrated biological role for DNA ADP-ribosylation as well.
Melanija, Posavec Marjanovic, Gytis, Jankevicius, Ivan, Ahel   +2 more
openaire   +2 more sources

Synthesis and Macrodomain Binding of Mono‐ADP‐Ribosylated Peptides

Angewandte Chemie, 2016
AbstractMono‐ADP‐ribosylation is a dynamic posttranslational modification (PTM) with important roles in signaling. Mammalian proteins that recognize or hydrolyze mono‐ADP‐ribosylated proteins have been described. We report the synthesis of ADP‐ribosylated peptides from the proteins histone H2B, RhoA and, HNP‐1.
Kistemaker, H.A., Nardozza, A.P., Overkleeft, H.S., Marel, G.A. van der, Ladurner, A.G., Filippov, D.V.   +5 more
openaire   +3 more sources

In silico-based screening of natural products as potential inhibitors of SARS-CoV-2 macrodomain 1

Journal of Biomolecular Structure and Dynamics, 2023
The rapid spread of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) worldwide has led to over 600 million cases of coronavirus disease 2019 (COVID-19). Identifying effective molecules that can counteract the virus is imperative.
Song-Yi Xie, Shoujing Cao, Juhong Wu, Zhinuo Xie, Yu-Tsen Liu, Wei Fu, Qianqian Zhao, Lin Liu, Lin Yang, Jinyu Li   +9 more
semanticscholar   +1 more source

A macrodomain-containing histone rearranges chromatin upon sensing PARP1 activation

Nature Structural and Molecular Biology, 2009
Poly-ADP-ribosylation is a post-translational modification catalyzed by PARP enzymes with roles in transcription and chromatin biology. Here we show that distinct macrodomains, including those of histone macroH2A1.1, are recruited to sites of PARP1 activation induced by laser-generated DNA damage. Chemical PARP1 inhibitors, PARP1 knockdown and mutation
Gyula Timinszky, Georg Kustatscher, Bianca Nijmeijer   +2 more
exaly   +4 more sources