Results 41 to 50 of about 1,793 (163)

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

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

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

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

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

Journal of Virology
Christopher H Douse, Yorgo Modis
exaly   +2 more sources

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

A family of macrodomain proteins reverses cellular mono-ADP-ribosylation [PDF]

Nature Structural & Molecular Biology, 2013
ADP-ribosylation is a reversible post-translational modification with wide-ranging biological functions in all kingdoms of life. A variety of enzymes use NAD(+) to transfer either single or multiple ADP-ribose (ADPr) moieties onto distinct amino acid substrates, often in response to DNA damage or other stresses.
Jankevicius, Gytis, Hassler, Markus, Golia, Barbara, Rybin, Vladimir, Zacharias, Martin, Timinszky, Gyula, Ladurner, Andreas G   +6 more
openaire   +2 more sources

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

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

Characterization of Brucella abortus lipopolysaccharide macrodomains as mega rafts

Cellular Microbiology, 2006
The lipopolysaccharides (LPS) of intracellular Proteobacteria such as Brucella, Chlamydia, Legionella and Rickettsia, have properties distinct from enterobacterial LPSs. These properties include deficient LPS induction of host cell activation, low endotoxicity and resistance to macrophage degradation.
Lapaque, N., Forquet, F., de Chastellier, C., Mishal, Z., Jolly, G., Moreno, E., Moriyon, I., Heuser, J.E., He, H.T., Gorvel, J.P.   +9 more
openaire   +5 more sources