Results 41 to 50 of about 1,800 (162)

Structure of the sirtuin‐linked macrodomain SAV0325 from Staphylococcus aureus [PDF]

Protein Science, 2016
AbstractCells use the post‐translational modification ADP‐ribosylation to control a host of biological activities. In some pathogenic bacteria, an operon‐encoded mono‐ADP‐ribosylation cycle mediates response to host‐induced oxidative stress. In this system, reversible mono ADP‐ribosylation of a lipoylated target protein represses oxidative stress ...
Appel, C. Denise, Feld, Geoffrey K., Wallace, Bret D., Williams, R. Scott   +3 more
openaire   +2 more sources

An MHV macrodomain mutant predicted to lack ADP-ribose binding activity is severely attenuated, indicating multiple roles for the macrodomain in coronavirus replication [PDF]

, 2021
ABSTRACT All coronaviruses (CoVs) contain a macrodomain, also termed Mac1, in non-structural protein 3 (nsp3) which binds and hydrolyzes ADP-ribose covalently attached to proteins. Despite several reports demonstrating that Mac1 is a prominent virulence factor, there is still a limited understanding of its cellular ...
Lynden S. Voth, Joseph J. O’Connor, Catherine M. Kerr, Ethan Doerger, Nancy Schwarting, Parker Sperstad, David K. Johnson, Anthony R. Fehr   +7 more
openaire   +2 more sources

Structure of macrodomain walls in polytwinned magnets

Journal of Applied Physics, 2002
We propose a microscopic approach to the studies of magnetic configurations in hard magnets which may be conveniently used for nanoscale systems; the microstructure of the magnet is easily and naturally included in the calculations. This approach is applied to find the structure of macrodomain walls in polytwinned magnets of the CoPt family ...
Belashchenko, Kirill D., Antropov, Vladimir P.   +1 more
openaire   +2 more sources

Single-nucleotide resolution detection of Topo IV cleavage activity in the Escherichia coli genome with Topo-Seq

Frontiers in Microbiology, 2023
Topoisomerase IV (Topo IV) is the main decatenation enzyme in Escherichia coli; it removes catenation links that are formed during DNA replication. Topo IV binding and cleavage sites were previously identified in the E.
Dmitry Sutormin, Alina Galivondzhyan, Azamat Gafurov, Konstantin Severinov   +3 more
doaj   +1 more source

Recognition of Mono-ADP-Ribosylated ARTD10 Substrates by ARTD8 Macrodomains [PDF]

Structure, 2013
ADP-ribosyltransferases (ARTs) catalyze the transfer of ADP-ribose from NAD(+) onto substrates. Some ARTs generate in an iterative process ADP-ribose polymers that serve as adaptors for distinct protein domains. Other ARTs, exemplified by ARTD10, function as mono-ADP-ribosyltransferases, but it has been unclear whether this modification occurs in cells
Forst, Alexandra H., Karlberg, Tobias, Herzog, Nicolas, Thorsell, Ann-Gerd, Gross, Annika, Feijs, Karla L.H., Verheugd, Patricia, Kursula, Petri, Nijmeijer, Bianca, Kremmer, Elisabeth, Kleine, Henning, Ladurner, Andreas G., Schüler, Herwig, Lüscher, Bernhard   +13 more
openaire   +3 more sources

Computational Investigations of Traditional Chinese Medicinal Compounds against the Omicron Variant of SARS-CoV-2 to Rescue the Host Immune System

Pharmaceuticals, 2022
Macrodomain-I of the NSP3 (non-structural protein 3) is responsible for immune response hijacking in the SARS-CoV-2 infection known as COVID-19. In the omicron variant (B.1.1.529), this domain harbors a new mutation, V1069I, which may increase the ...
Ziad Tareq Naman, Salim Kadhim, Zahraa J. K. Al-Isawi, Christopher J. Butch, Ziyad Tariq Muhseen   +4 more
doaj   +1 more source

Dielectric behavior and phase transition in [111]-oriented PIN–PMN–PT single crystals under dc bias [PDF]

Journal of Advanced Dielectrics, 2014
Temperature and electric field dependences of the dielectric behavior and phase transition for [111]-oriented 0.23PIN–0.52PMN–0.25PT (PIN-PMN–0.25PT) and 0.24PIN–0.43PMN–0.33PT (PIN–PMN–0.33PT) single crystals were investigated over a temperature range ...
Yuhui Wan, Zhenrong Li, Ming Ma, Fei Li, Zhuo Xu, Shiji Fan, Xi Yao   +6 more
doaj   +1 more source

Serine ADP-ribosylation reversal by the hydrolase ARH3

eLife, 2017
ADP-ribosylation (ADPr) is a posttranslational modification (PTM) of proteins that controls many cellular processes, including DNA repair, transcription, chromatin regulation and mitosis. A number of proteins catalyse the transfer and hydrolysis of ADPr,
Pietro Fontana, Juan José Bonfiglio, Luca Palazzo, Edward Bartlett, Ivan Matic, Ivan Ahel   +5 more
doaj   +1 more source

The coronavirus macrodomain is required to prevent PARP-mediated inhibition of virus replication and enhancement of IFN expression.

PLoS Pathogens, 2019
ADP-ribosylation is a ubiquitous post-translational addition of either monomers or polymers of ADP-ribose to target proteins by ADP-ribosyltransferases, usually by interferon-inducible diphtheria toxin-like enzymes known as PARPs.
Matthew E Grunewald, Yating Chen, Chad Kuny, Takashi Maejima, Robert Lease, Dana Ferraris, Masanori Aikawa, Christopher S Sullivan, Stanley Perlman, Anthony R Fehr   +9 more
doaj   +1 more source

Proximal ADP-ribose Hydrolysis in Trypanosomatids is Catalyzed by a Macrodomain

Scientific Reports, 2016
AbstractADP-ribosylation is a ubiquitous protein modification utilized by both prokaryotes and eukaryotes for several cellular functions, such as DNA repair, proliferation and cell signaling. Higher eukaryotes, such as humans, utilize various enzymes to reverse the modification and to regulate ADP-ribose dependent signaling.
Lehtiö Lari, Haikarainen Teemu Johannes
openaire   +2 more sources