Results 141 to 150 of about 1,793 (163)

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

A macrodomain-linked immunosorbent assay (MLISA) for mono-ADP-ribosyltransferases [PDF]

Analytical Biochemistry, 2018
ADP-ribosyltransferases (ARTs) catalyze reversible additions of mono- and poly-ADP-ribose onto diverse types of proteins by using nicotinamide adenine dinucleotide (NAD+) as a cosubstrate. In the human ART superfamily, 14 out of 20 members are shown to catalyze endogenous protein mono-ADP-ribosylation and play important roles in regulating various ...
Yong Zhang
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

Macrodomain-containing proteins are new mono-ADP-ribosylhydrolases

Nature Structural & 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.
Rosenthal Florian, Feijs Karla L H, Frugier Emilie, Bonalli Mario, Forst Alexandra H, Imhof Ralph, Winkler Hans C, Fischer David, Caflisch Amedeo, Hassa Paul O, Lüscher Bernhard, Hottiger Michael O   +11 more
openaire   +2 more sources

Observation of the magnetic vector potential in the classical macrodomain

Physics Letters A, 2002
zbMATH Open Web Interface contents unavailable due to conflicting licenses.
Varma, Ram K., Punithavelu, A. M., Banerjee, S. B.   +2 more
openaire   +1 more source

Expanding the functional repertoire of macrodomains

Nature Structural & Molecular Biology, 2013
Macrodomains are conserved globular domains that can interact with, and in some cases modify, ADP-ribose–based molecules. In this issue, two reports add to the functional repertoire of this domain, by demonstrating that a subset of macrodomain-containing proteins functions to catalyze the removal of protein-proximal ADP-ribose.
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Dynamics on Microdomain-Macrodomain Transition of Relaxor Ferroelectrics [PDF]

Wuli Huaxue Xuebao/ Acta Physico - Chimica Sinica, 2004
Zhang Dong-Jie, Yao Xi
exaly   +2 more sources

Polarized raman spectroscopy of oriented macrodomain of phospholipids containing amphotericin

Biochemical and Biophysical Research Communications, 1982
Abstract A new method for preparing oriented macrodomains of phospholipid multilayers is described: it consists of controlled evaporation of solutions of phospholipid vesicles on specially prepared glass slides. The polarized Raman spectra, as well as the observation between crossed polarizers, show that the phospholipid molecules are oriented: the ...
M, Harrand, W L, Peticolas, R, Dupeyrat
openaire   +2 more sources

Migrasome formation is mediated by assembly of micron-scale tetraspanin macrodomains

Nature Cell Biology, 2019
Migrasomes are recently discovered cellular organelles that form as large vesicle-like structures on retraction fibres of migrating cells. While the process of migrasome formation has been described before, the molecular mechanism underlying migrasome biogenesis remains unclear. Here, we propose that the mechanism of migrasome formation consists of the
Yuwei Huang, Ben Zucker, Shaojin Zhang, Sharon Elias, Yun Zhu, Hui Chen, Tianlun Ding, Ying Li, Yujie Sun, Jizhong Lou, Michael M. Kozlov, Li Yu   +11 more
openaire   +2 more sources

Perfectness of Macrodomains of BaTiO₃ Crystals

Journal of the Physical Society of Japan, 1961
Statistico-thermodynamical investigation is made on the size and density of reversely-polarized microdomains contained within a unidomain c -plate (or a macrodomain of a multidomain c -plate) of BaTiO 3 in thermal equilibrium at room temperature, with or without constant electric field applied.
Kêitsirô Aizu, Osamu Nakada
openaire   +1 more source