Publikation:

Cell-Permeable Nicotinamide Adenine Dinucleotides for Exploration of Cellular Protein ADP-Ribosylation

Lade...
Vorschaubild

Dateien

Kasprzyk_2-1eqn1rdx0codc8.pdf
Kasprzyk_2-1eqn1rdx0codc8.pdfGröße: 4.93 MBDownloads: 13

Datum

2024

Herausgeber:innen

Kontakt

ISSN der Zeitschrift

Electronic ISSN

ISBN

Bibliografische Daten

Verlag

Schriftenreihe

Auflagebezeichnung

ArXiv-ID

Internationale Patentnummer

Link zur Lizenz
oops

Angaben zur Forschungsförderung

Deutsche Forschungsgemeinschaft (DFG): 496470458
Deutsche Forschungsgemeinschaft (DFG): MA 2288/21-1

Projekt

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

Gesperrt bis

Titel in einer weiteren Sprache

Publikationstyp
Zeitschriftenartikel
Publikationsstatus
Published

Erschienen in

Angewandte Chemie International Edition. Wiley. 2024, 63(51), e202411203. ISSN 1433-7851. eISSN 1521-3773. Verfügbar unter: doi: 10.1002/anie.202411203

Zusammenfassung

Posttranslational modifications (PTMs) greatly enhance the functional diversity of proteins, surpassing the number of gene‐encoded variations. One intriguing PTM is ADP‐ribosylation, which utilizes nicotinamide adenine dinucleotide (NAD+) as a substrate and is essential in cell signaling pathways regulating cellular responses. Here, we report the first cell‐permeable NAD+ analogs and demonstrate their utility for investigating cellular ADP‐ribosylation. Using a desthiobiotin‐labelled analog for affinity enrichment of proteins that are ADP‐ribosylated in living cells under oxidative stress, we identified protein targets associated with host‐virus interactions, DNA damage and repair, protein biosynthesis, and ribosome biogenesis. Most of these targets have been noted in various literature sources, highlighting the potential of our probes for cellular ADP‐ribosylome studies.

Zusammenfassung in einer weiteren Sprache

Fachgebiet (DDC)
540 Chemie

Schlagwörter

ADP-ribosylation, Drug delivery, NAD+, Nucleotides, Post-translational modifications

Konferenz

Rezension
undefined / . - undefined, undefined

Forschungsvorhaben

Organisationseinheiten

Zeitschriftenheft

Zugehörige Datensätze in KOPS

Zitieren

ISO 690KASPRZYK, Renata, Sonja RIETH, Peter HEID, Florian STENGEL, Andreas MARX, 2024. Cell-Permeable Nicotinamide Adenine Dinucleotides for Exploration of Cellular Protein ADP-Ribosylation. In: Angewandte Chemie International Edition. Wiley. 2024, 63(51), e202411203. ISSN 1433-7851. eISSN 1521-3773. Verfügbar unter: doi: 10.1002/anie.202411203
BibTex
@article{Kasprzyk2024-12-16CellP-70926,
  year={2024},
  doi={10.1002/anie.202411203},
  title={Cell-Permeable Nicotinamide Adenine Dinucleotides for Exploration of Cellular Protein ADP-Ribosylation},
  number={51},
  volume={63},
  issn={1433-7851},
  journal={Angewandte Chemie International Edition},
  author={Kasprzyk, Renata and Rieth, Sonja and Heid, Peter and Stengel, Florian and Marx, Andreas},
  note={Article Number: e202411203}
}
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/123456789/70926">
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:contributor>Marx, Andreas</dc:contributor>
    <dc:contributor>Rieth, Sonja</dc:contributor>
    <dc:creator>Heid, Peter</dc:creator>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dc:creator>Kasprzyk, Renata</dc:creator>
    <dcterms:title>Cell-Permeable Nicotinamide Adenine Dinucleotides for Exploration of Cellular Protein ADP-Ribosylation</dcterms:title>
    <dc:creator>Marx, Andreas</dc:creator>
    <dc:creator>Stengel, Florian</dc:creator>
    <dc:contributor>Heid, Peter</dc:contributor>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2024-10-08T08:00:31Z</dcterms:available>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/70926/1/Kasprzyk_2-1eqn1rdx0codc8.pdf"/>
    <dcterms:issued>2024-12-16</dcterms:issued>
    <dc:creator>Rieth, Sonja</dc:creator>
    <dc:language>eng</dc:language>
    <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/70926"/>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2024-10-08T08:00:31Z</dc:date>
    <dc:contributor>Stengel, Florian</dc:contributor>
    <dc:contributor>Kasprzyk, Renata</dc:contributor>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/70926/1/Kasprzyk_2-1eqn1rdx0codc8.pdf"/>
    <dcterms:abstract>Posttranslational modifications (PTMs) greatly enhance the functional diversity of proteins, surpassing the number of gene‐encoded variations. One intriguing PTM is ADP‐ribosylation, which utilizes nicotinamide adenine dinucleotide (NAD+) as a substrate and is essential in cell signaling pathways regulating cellular responses. Here, we report the first cell‐permeable NAD+ analogs and demonstrate their utility for investigating cellular ADP‐ribosylation. Using a desthiobiotin‐labelled analog for affinity enrichment of proteins that are ADP‐ribosylated in living cells under oxidative stress, we identified protein targets associated with host‐virus interactions, DNA damage and repair, protein biosynthesis, and ribosome biogenesis. Most of these targets have been noted in various literature sources, highlighting the potential of our probes for cellular ADP‐ribosylome studies.</dcterms:abstract>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/>
  </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
Ja
Diese Publikation teilen