Publikation:

Investigation of the action of poly(ADP-ribose)-synthesising enzymes on NAD+ analogues

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2017

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Simpson, Edward L.

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http://nbn-resolving.de/urn:nbn:de:bsz:352-0-405693
DOI (zitierfähiger Link)
https://doi.org/10.3762/bjoc.13.49
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CC BY 4.0

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Published

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Beilstein Journal of Organic Chemistry. 2017, 13, pp. 495-501. eISSN 1860-5397. Available under: doi: 10.3762/bjoc.13.49

Zusammenfassung

ADP-ribosyl transferases with diphtheria toxin homology (ARTDs) catalyse the covalent addition of ADP-ribose onto different acceptors forming mono- or poly(ADP-ribos)ylated proteins. Out of the 18 members identified, only four are known to synthesise the complex poly(ADP-ribose) biopolymer. The investigation of this posttranslational modification is important due to its involvement in cancer and other diseases. Lately, metabolic labelling approaches comprising different reporter-modified NAD+ building blocks have stimulated and enriched proteomic studies and imaging applications of ADP-ribosylation processes. Herein, we compare the substrate scope and applicability of different NAD+ analogues for the investigation of the polymer-synthesising enzymes ARTD1, ARTD2, ARTD5 and ARTD6. By varying the site and size of the NAD+ modification, suitable probes were identified for each enzyme. This report provides guidelines for choosing analogues for studying poly(ADP-ribose)-synthesising enzymes.

Zusammenfassung in einer weiteren Sprache

Fachgebiet (DDC)
540 Chemie

Schlagwörter

ARTD; click chemistry; NAD+; poly(ADP-ribose); posttranslational modification

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ISO 690WALLRODT, Sarah, Edward L. SIMPSON, Andreas MARX, 2017. Investigation of the action of poly(ADP-ribose)-synthesising enzymes on NAD+ analogues. In: Beilstein Journal of Organic Chemistry. 2017, 13, pp. 495-501. eISSN 1860-5397. Available under: doi: 10.3762/bjoc.13.49
BibTex
@article{Wallrodt2017-03-10Inves-38625,
  year={2017},
  doi={10.3762/bjoc.13.49},
  title={Investigation of the action of poly(ADP-ribose)-synthesising enzymes on NAD<sup>+</sup> analogues},
  volume={13},
  journal={Beilstein Journal of Organic Chemistry},
  pages={495--501},
  author={Wallrodt, Sarah and Simpson, Edward L. and Marx, Andreas}
}
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