Search Results - "Feijs, Karla Lh"
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Dynamic subcellular localization of the mono-ADP-ribosyltransferase ARTD10 and interaction with the ubiquitin receptor p62
Published in Cell communication and signaling (20-09-2012)“…ADP-ribosylation is a posttranslational modification catalyzed in cells by ADP-ribosyltransferases (ARTD or PARP enzymes). The ARTD family consists of 17…”
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Are PARPs promiscuous?
Published in Bioscience reports (27-05-2022)“…Post-translational modifications exist in different varieties to regulate diverse characteristics of their substrates, ultimately leading to maintenance of…”
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ARTD10 substrate identification on protein microarrays: regulation of GSK3β by mono-ADP-ribosylation
Published in Cell communication and signaling (19-01-2013)“…Although ADP-ribosylation has been described five decades ago, only recently a distinction has been made between eukaryotic intracellular poly- and…”
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Recognition of Mono-ADP-Ribosylated ARTD10 Substrates by ARTD8 Macrodomains
Published in Structure (London) (05-03-2013)“…ADP-ribosyltransferases (ARTs) catalyze the transfer of ADP-ribose from NAD+ onto substrates. Some ARTs generate in an iterative process ADP-ribose polymers…”
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Protein and RNA ADP-ribosylation detection is influenced by sample preparation and reagents used
Published in Life science alliance (01-01-2023)“…The modification of substrates with ADP-ribose (ADPr) is important in, for example, antiviral immunity and cancer. Recently, several reagents were developed to…”
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ARTD10 substrate identification on protein microarrays: regulation of GSK3[beta] by mono-ADP-ribosylation
Published in Cell communication and signaling (19-01-2013)“…Although ADP-ribosylation has been described five decades ago, only recently a distinction has been made between eukaryotic intracellular poly- and…”
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Regulation of NF-[kappa]B signalling by the mono-ADP-ribosyltransferase ARTD10
Published in Nature communications (01-04-2013)“…Adenosine diphosphate-ribosylation is a post-translational modification mediated by intracellular and membrane-associated extracellular enzymes and many…”
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