Publikation:

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

Lade...
Vorschaubild

Dateien

Wallrodt_0-405693.pdf
Wallrodt_0-405693.pdfGröße: 2.61 MBDownloads: 455

Datum

2017

Autor:innen

Herausgeber:innen

Kontakt

ISSN der Zeitschrift

Electronic ISSN

ISBN

Bibliografische Daten

Verlag

Schriftenreihe

Auflagebezeichnung

DOI (zitierfähiger Link)
ArXiv-ID

Internationale Patentnummer

Link zur Lizenz

Angaben zur Forschungsförderung

Projekt

Open Access-Veröffentlichung
Open Access Gold
Core Facility der Universität Konstanz

Gesperrt bis

Titel in einer weiteren Sprache

Publikationstyp
Zeitschriftenartikel
Publikationsstatus
Published

Erschienen in

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

Konferenz

Rezension
undefined / . - undefined, undefined

Forschungsvorhaben

Organisationseinheiten

Zeitschriftenheft

Verknüpfte Datensätze

Zitieren

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}
}
RDF
<rdf:RDF
    xmlns:dcterms="http://purl.org/dc/terms/"
    xmlns:dc="http://purl.org/dc/elements/1.1/"
    xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#"
    xmlns:bibo="http://purl.org/ontology/bibo/"
    xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#"
    xmlns:foaf="http://xmlns.com/foaf/0.1/"
    xmlns:void="http://rdfs.org/ns/void#"
    xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > 
  <rdf:Description rdf:about="https://kops.uni-konstanz.de/server/rdf/resource/123456789/38625">
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/>
    <dcterms:rights rdf:resource="http://creativecommons.org/licenses/by/4.0/"/>
    <dcterms:abstract xml:lang="eng">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&lt;sup&gt;+&lt;/sup&gt; 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&lt;sup&gt;+&lt;/sup&gt; analogues for the investigation of the polymer-synthesising enzymes ARTD1, ARTD2, ARTD5 and ARTD6. By varying the site and size of the NAD&lt;sup&gt;+&lt;/sup&gt; modification, suitable probes were identified for each enzyme. This report provides guidelines for choosing analogues for studying poly(ADP-ribose)-synthesising enzymes.</dcterms:abstract>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-04-27T06:03:57Z</dcterms:available>
    <dc:creator>Wallrodt, Sarah</dc:creator>
    <dcterms:issued>2017-03-10</dcterms:issued>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/38625/3/Wallrodt_0-405693.pdf"/>
    <dcterms:title>Investigation of the action of poly(ADP-ribose)-synthesising enzymes on NAD&lt;sup&gt;+&lt;/sup&gt; analogues</dcterms:title>
    <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/38625"/>
    <dc:contributor>Simpson, Edward L.</dc:contributor>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:contributor>Wallrodt, Sarah</dc:contributor>
    <dc:language>eng</dc:language>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/38625/3/Wallrodt_0-405693.pdf"/>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dc:rights>Attribution 4.0 International</dc:rights>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dc:creator>Marx, Andreas</dc:creator>
    <dc:creator>Simpson, Edward L.</dc:creator>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-04-27T06:03:57Z</dc:date>
    <dc:contributor>Marx, Andreas</dc:contributor>
  </rdf:Description>
</rdf:RDF>

Interner Vermerk

xmlui.Submission.submit.DescribeStep.inputForms.label.kops_note_fromSubmitter

Kontakt
URL der Originalveröffentl.

Prüfdatum der URL

Prüfungsdatum der Dissertation

Finanzierungsart

Kommentar zur Publikation

Allianzlizenz
Corresponding Authors der Uni Konstanz vorhanden
Internationale Co-Autor:innen
Universitätsbibliographie
Ja
Begutachtet
Diese Publikation teilen